|
Enzyme 1
[top]
|
| Enzyme 1 ID |
5246 |
| Enzyme 1 Name |
5-aminolevulinate synthase, erythroid-specific, mitochondrial |
| Enzyme 1 Synonyms |
- ALAS-E
- 5-aminolevulinic acid synthase 2
- Delta-ALA synthase 2
- Delta-aminolevulinate synthase 2
|
| Enzyme 1 Gene Name |
ALAS2 |
| Enzyme 1 Protein Sequence |
>5-aminolevulinate synthase, erythroid-specific, mitochondrial
MVTAAMLLQCCPVLARGPTSLLGKVVKTHQFLFGIGRCPILATQGPNCSQIHLKATKAGG
DSPSWAKGHCPFMLSELQDGKSKIVQKAAPEVQEDVKAFKTDLPSSLVSVSLRKPFSGPQ
EQEQISGKVTHLIQNNMPGNYVFSYDQFFRDKIMEKKQDHTYRVFKTVNRWADAYPFAQH
FSEASVASKDVSVWCSNDYLGMSRHPQVLQATQETLQRHGAGAGGTRNISGTSKFHVELE
QELAELHQKDSALLFSSCFVANDSTLFTLAKILPGCEIYSDAGNHASMIQGIRNSGAAKF
VFRHNDPDHLKKLLEKSNPKIPKIVAFETVHSMDGAICPLEELCDVSHQYGALTFVDEVH
AVGLYGSRGAGIGERDGIMHKIDIISGTLGKAFGCVGGYIASTRDLVDMVRSYAAGFIFT
TSLPPMVLSGALESVRLLKGEEGQALRRAHQRNVKHMRQLLMDRGLPVIPCPSHIIPIRV
GNAALNSKLCDLLLSKHGIYVQAINYPTVPRGEELLRLAPSPHHSPQMMEDFVEKLLLAW
TAVGLPLQDVSVAACNFCRRPVHFELMSEWERSYFGNMGPQYVTTYA
|
| Enzyme 1 Number of Residues |
587 |
| Enzyme 1 Molecular Weight |
64632.9 |
| Enzyme 1 Theoretical pI |
8.19 |
| Enzyme 1 GO Classification |
| Function |
- 5-aminolevulinate synthase activity
- N-acyltransferase activity
- N-succinyltransferase activity
- acyltransferase activity
- binding
- catalytic activity
- cofactor binding
- pyridoxal phosphate binding
- transferase activity
- transferase activity, transferring acyl groups
- transferase activity, transferring acyl groups other than amino-acyl groups
- transferase activity, transferring nitrogenous groups
|
| Process |
- biosynthetic process
- cellular biosynthetic process
- heterocycle biosynthetic process
- metabolic process
- nitrogen compound metabolic process
- porphyrin metabolic process
- tetrapyrrole biosynthetic process
- tetrapyrrole metabolic process
|
| Component |
- cell part
- cytoplasmic part
- intracellular part
- mitochondrial matrix
- mitochondrial part
|
|
| Enzyme 1 General Function |
Involved in 5-aminolevulinate synthase activity |
| Enzyme 1 Specific Function |
Succinyl-CoA + glycine = 5-aminolevulinate + CoA + CO(2) |
| Enzyme 1 Pathways |
- Glycine, Serine and Threonine Metabolism (map00260
)
|
| Enzyme 1 Reactions |
- succinyl-CoA + glycine = 5-aminolevulinate + CoA + CO2 [RN:R00830]
|
| Enzyme 1 Pfam Domain Function |
|
| Enzyme 1 Signals |
|
| Enzyme 1 Transmembrane Regions |
|
| Enzyme 1 Essentiality |
Not Available |
| Enzyme 1 GenBank ID Protein |
3220249  |
| Enzyme 1 UniProtKB/Swiss-Prot ID |
P22557  |
| Enzyme 1 UniProtKB/Swiss-Prot Entry Name |
HEM0_HUMAN  |
| Enzyme 1 PDB ID |
Not Available |
| Enzyme 1 Cellular Location |
Not Available |
| Enzyme 1 Gene Sequence |
>1764 bp
ATGGTGACTGCAGCCATGCTGCTACAGTGCTGCCCAGTGCTTGCCCGGGGCCCCACAAGC
CTCCTAGGCAAGGTGGTTAAGACTCACCAGTTCCTGTTTGGTATTGGACGCTGTCCCATC
CTGGCTACCCAAGGACCAAACTGTTCTCAAATCCACCTTAAGGCAACAAAGGCTGGAGGA
GATTCTCCATCTTGGGCGAAGGGCCACTGTCCCTTCATGCTGTCGGAACTCCAGGATGGG
AAGAGCAAGATTGTGCAGAAGGCAGCCCCAGAAGTCCAGGAAGATGTGAAGGCTTTCAAG
ACAGATCTGCCTAGCTCCCTGGTCTCAGTCAGCCTAAGGAAGCCATTTTCCGGTCCCCAG
GAGCAGGAGCAGATCTCTGGGAAGGTCACACACCTGATTCAGAACAATATGCCTGGAAAC
TATGTCTTCAGTTATGACCAGTTTTTCAGGGACAAGATCATGGAGAAGAAACAGGATCAC
ACCTACCGTGTGTTCAAGACTGTGAACCGCTGGGCTGATGCATATCCCTTTGCCCAACAT
TTCTCTGAGGCATCTGTGGCCTCAAAGGATGTGTCCGTCTGGTGTAGTAATGATTACCTG
GGCATGAGCCGACACCCTCAGGTCTTGCAAGCCACACAGGAGACCCTGCAGCGTCATGGT
GCTGGAGCTGGTGGCACCCGCAACATCTCAGGCACCAGTAAGTTTCATGTGGAGCTTGAG
CAGGAGCTGGCTGAGCTGCACCAGAAGGACTCAGCCCTGCTCTTCTCCTCCTGCTTTGTT
GCCAATGACTCTACTCTCTTCACCTTGGCCAAGATCCTGCCAGGGTGCGAGATTTACTCA
GACGCAGGCAACCATGCTTCCATGATCCAAGGTATCCGTAACAGTGGAGCAGCCAAGTTT
GTCTTCAGGCACAATGACCCTGACCACCTAAAGAAACTTCTAGAGAAGTCTAACCCTAAG
ATACCCAAAATTGTGGCCTTTGAGACTGTCCACTCCATGGATGGTGCCATCTGTCCCCTC
GAGGAGTTGTGTGATGTGTCCCACCAGTATGGGGCCCTGACCTTCGTGGATGAGGTCCAT
GCTGTAGGACTGTATGGGTCCCGGGGCGCTGGGATTGGGGAGCGTGATGGAATTATGCAT
AAGATTGACATCATCTCTGGAACTCTTGGCAAGGCCTTTGGCTGTGTGGGCGGCTACATT
GCCAGCACCCGTGACTTGGTGGACATGGTGCGCTCCTATGCTGCAGGCTTCATCTTTACC
ACTTCTCTGCCCCCCATGGTGCTCTCTGGAGCTCTAGAATCTGTGCGGCTGCTCAAGGGA
GAGGAGGGCCAAGCCCTGAGGCGAGCCCACCAGCGCAATGTCAAGCACATGCGCCAGCTA
CTCATGGACAGGGGCCTTCCTGTCATCCCCTGCCCCAGCCACATCATCCCCATCCGGGTG
GGCAATGCAGCACTCAACAGCAAGCTCTGTGATCTCCTGCTCTCCAAGCATGGCATCTAT
GTGCAGGCCATCAACTACCCAACTGTCCCCCGGGGTGAAGAGCTCCTGCGCTTGGCACCC
TCCCCCCACCACAGCCCTCAGATGATGGAAGATTTTGTGGAGAAGCTGCTGCTGGCTTGG
ACTGCGGTGGGGCTGCCCCTCCAGGATGTGTCTGTGGCTGCCTGCAATTTCTGTCGCCGT
CCTGTACACTTTGAGCTCATGAGTGAGTGGGAACGTTCCTACTTCGGGAACATGGGGCCC
CAGTATGTCACCACCTATGCCTGA
|
| Enzyme 1 GenBank Gene ID |
AF068624  |
| Enzyme 1 GeneCard ID |
ALAS2  |
| Enzyme 1 GenAtlas ID |
ALAS2  |
| Enzyme 1 HGNC ID |
HGNC:397  |
| Enzyme 1 Chromosome Location |
Not Available |
| Enzyme 1 Locus |
Not Available |
| Enzyme 1 SNPs |
SNPJam Report  |
| Enzyme 1 General References |
- Bishop DF: Two different genes encode delta-aminolevulinate synthase in humans: nucleotide sequences of cDNAs for the housekeeping and erythroid genes. Nucleic Acids Res. 1990 Dec 11;18(23):7187-8. [PubMed
]
- Cox TC, Bawden MJ, Martin A, May BK: Human erythroid 5-aminolevulinate synthase: promoter analysis and identification of an iron-responsive element in the mRNA. EMBO J. 1991 Jul;10(7):1891-902. [PubMed
]
- Surinya KH, Cox TC, May BK: Identification and characterization of a conserved erythroid-specific enhancer located in intron 8 of the human 5-aminolevulinate synthase 2 gene. J Biol Chem. 1998 Jul 3;273(27):16798-809. [PubMed
]
- Ross MT, Grafham DV, Coffey AJ, Scherer S, McLay K, Muzny D, Platzer M, Howell GR, Burrows C, Bird CP, Frankish A, Lovell FL, Howe KL, Ashurst JL, Fulton RS, Sudbrak R, Wen G, Jones MC, Hurles ME, Andrews TD, Scott CE, Searle S, Ramser J, Whittaker A, Deadman R, Carter NP, Hunt SE, Chen R, Cree A, Gunaratne P, Havlak P, Hodgson A, Metzker ML, Richards S, Scott G, Steffen D, Sodergren E, Wheeler DA, Worley KC, Ainscough R, Ambrose KD, Ansari-Lari MA, Aradhya S, Ashwell RI, Babbage AK, Bagguley CL, Ballabio A, Banerjee R, Barker GE, Barlow KF, Barrett IP, Bates KN, Beare DM, Beasley H, Beasley O, Beck A, Bethel G, Blechschmidt K, Brady N, Bray-Allen S, Bridgeman AM, Brown AJ, Brown MJ, Bonnin D, Bruford EA, Buhay C, Burch P, Burford D, Burgess J, Burrill W, Burton J, Bye JM, Carder C, Carrel L, Chako J, Chapman JC, Chavez D, Chen E, Chen G, Chen Y, Chen Z, Chinault C, Ciccodicola A, Clark SY, Clarke G, Clee CM, Clegg S, Clerc-Blankenburg K, Clifford K, Cobley V, Cole CG, Conquer JS, Corby N, Connor RE, David R, Davies J, Davis C, Davis J, Delgado O, Deshazo D, Dhami P, Ding Y, Dinh H, Dodsworth S, Draper H, Dugan-Rocha S, Dunham A, Dunn M, Durbin KJ, Dutta I, Eades T, Ellwood M, Emery-Cohen A, Errington H, Evans KL, Faulkner L, Francis F, Frankland J, Fraser AE, Galgoczy P, Gilbert J, Gill R, Glockner G, Gregory SG, Gribble S, Griffiths C, Grocock R, Gu Y, Gwilliam R, Hamilton C, Hart EA, Hawes A, Heath PD, Heitmann K, Hennig S, Hernandez J, Hinzmann B, Ho S, Hoffs M, Howden PJ, Huckle EJ, Hume J, Hunt PJ, Hunt AR, Isherwood J, Jacob L, Johnson D, Jones S, de Jong PJ, Joseph SS, Keenan S, Kelly S, Kershaw JK, Khan Z, Kioschis P, Klages S, Knights AJ, Kosiura A, Kovar-Smith C, Laird GK, Langford C, Lawlor S, Leversha M, Lewis L, Liu W, Lloyd C, Lloyd DM, Loulseged H, Loveland JE, Lovell JD, Lozado R, Lu J, Lyne R, Ma J, Maheshwari M, Matthews LH, McDowall J, McLaren S, McMurray A, Meidl P, Meitinger T, Milne S, Miner G, Mistry SL, Morgan M, Morris S, Muller I, Mullikin JC, Nguyen N, Nordsiek G, Nyakatura G, O'Dell CN, Okwuonu G, Palmer S, Pandian R, Parker D, Parrish J, Pasternak S, Patel D, Pearce AV, Pearson DM, Pelan SE, Perez L, Porter KM, Ramsey Y, Reichwald K, Rhodes S, Ridler KA, Schlessinger D, Schueler MG, Sehra HK, Shaw-Smith C, Shen H, Sheridan EM, Shownkeen R, Skuce CD, Smith ML, Sotheran EC, Steingruber HE, Steward CA, Storey R, Swann RM, Swarbreck D, Tabor PE, Taudien S, Taylor T, Teague B, Thomas K, Thorpe A, Timms K, Tracey A, Trevanion S, Tromans AC, d'Urso M, Verduzco D, Villasana D, Waldron L, Wall M, Wang Q, Warren J, Warry GL, Wei X, West A, Whitehead SL, Whiteley MN, Wilkinson JE, Willey DL, Williams G, Williams L, Williamson A, Williamson H, Wilming L, Woodmansey RL, Wray PW, Yen J, Zhang J, Zhou J, Zoghbi H, Zorilla S, Buck D, Reinhardt R, Poustka A, Rosenthal A, Lehrach H, Meindl A, Minx PJ, Hillier LW, Willard HF, Wilson RK, Waterston RH, Rice CM, Vaudin M, Coulson A, Nelson DL, Weinstock G, Sulston JE, Durbin R, Hubbard T, Gibbs RA, Beck S, Rogers J, Bentley DR: The DNA sequence of the human X chromosome. Nature. 2005 Mar 17;434(7031):325-37. [PubMed
]
- Cox TC, Bottomley SS, Wiley JS, Bawden MJ, Matthews CS, May BK: X-linked pyridoxine-responsive sideroblastic anemia due to a Thr388-to-Ser substitution in erythroid 5-aminolevulinate synthase. N Engl J Med. 1994 Mar 10;330(10):675-9. [PubMed
]
- Cotter PD, Baumann M, Bishop DF: Enzymatic defect in "X-linked" sideroblastic anemia: molecular evidence for erythroid delta-aminolevulinate synthase deficiency. Proc Natl Acad Sci U S A. 1992 May 1;89(9):4028-32. [PubMed
]
- Furuyama K, Uno R, Urabe A, Hayashi N, Fujita H, Kondo M, Sassa S, Yamamoto M: R411C mutation of the ALAS2 gene encodes a pyridoxine-responsive enzyme with low activity. Br J Haematol. 1998 Dec;103(3):839-41. [PubMed
]
- Harigae H, Furuyama K, Kudo K, Hayashi N, Yamamoto M, Sassa S, Sasaki T: A novel mutation of the erythroid-specific gamma-Aminolevulinate synthase gene in a patient with non-inherited pyridoxine-responsive sideroblastic anemia. Am J Hematol. 1999 Oct;62(2):112-4. [PubMed
]
- Cotter PD, May A, Li L, Al-Sabah AI, Fitzsimons EJ, Cazzola M, Bishop DF: Four new mutations in the erythroid-specific 5-aminolevulinate synthase (ALAS2) gene causing X-linked sideroblastic anemia: increased pyridoxine responsiveness after removal of iron overload by phlebotomy and coinheritance of hereditary hemochromatosis. Blood. 1999 Mar 1;93(5):1757-69. [PubMed
]
- Cazzola M, May A, Bergamaschi G, Cerani P, Ferrillo S, Bishop DF: Absent phenotypic expression of X-linked sideroblastic anemia in one of 2 brothers with a novel ALAS2 mutation. Blood. 2002 Dec 1;100(12):4236-8. Epub 2002 Aug 8. [PubMed
]
- Hurford MT, Marshall-Taylor C, Vicki SL, Zhou JZ, Silverman LM, Rezuke WN, Altman A, Tsongalis GJ: A novel mutation in exon 5 of the ALAS2 gene results in X-linked sideroblastic anemia. Clin Chim Acta. 2002 Jul;321(1-2):49-53. [PubMed
]
- Whatley SD, Ducamp S, Gouya L, Grandchamp B, Beaumont C, Badminton MN, Elder GH, Holme SA, Anstey AV, Parker M, Corrigall AV, Meissner PN, Hift RJ, Marsden JT, Ma Y, Mieli-Vergani G, Deybach JC, Puy H: C-terminal deletions in the ALAS2 gene lead to gain of function and cause X-linked dominant protoporphyria without anemia or iron overload. Am J Hum Genet. 2008 Sep;83(3):408-14. Epub 2008 Sep 4. [PubMed
]
|
| Enzyme 1 Metabolite References |
Not Available |
|
Enzyme 2
[top]
|
| Enzyme 2 ID |
5251 |
| Enzyme 2 Name |
5-aminolevulinate synthase, nonspecific, mitochondrial |
| Enzyme 2 Synonyms |
- ALAS-H
- 5-aminolevulinic acid synthase 1
- Delta-ALA synthase 1
- Delta-aminolevulinate synthase 1
|
| Enzyme 2 Gene Name |
ALAS1 |
| Enzyme 2 Protein Sequence |
>5-aminolevulinate synthase, nonspecific, mitochondrial
MESVVRRCPFLSRVPQAFLQKAGKSLLFYAQNCPKMMEVGAKPAPRALSTAAVHYQQIKE
TPPASEKDKTAKAKVQQTPDGSQQSPDGTQLPSGHPLPATSQGTASKCPFLAAQMNQRGS
SVFCKASLELQEDVQEMNAVRKEVAETSAGPSVVSVKTDGGDPSGLLKNFQDIMQKQRPE
RVSHLLQDNLPKSVSTFQYDRFFEKKIDEKKNDHTYRVFKTVNRRAHIFPMADDYSDSLI
TKKQVSVWCSNDYLGMSRHPRVCGAVMDTLKQHGAGAGGTRNISGTSKFHVDLERELADL
HGKDAALLFSSCFVANDSTLFTLAKMMPGCEIYSDSGNHASMIQGIRNSRVPKYIFRHND
VSHLRELLQRSDPSVPKIVAFETVHSMDGAVCPLEELCDVAHEFGAITFVDEVHAVGLYG
ARGGGIGDRDGVMPKMDIISGTLGKAFGCVGGYIASTSSLIDTVRSYAAGFIFTTSLPPM
LLAGALESVRILKSAEGRVLRRQHQRNVKLMRQMLMDAGLPVVHCPSHIIPVRVADAAKN
TEVCDELMSRHNIYVQAINYPTVPRGEELLRIAPTPHHTPQMMNYFLENLLVTWKQVGLE
LKPHSSAECNFCRRPLHFEVMSEREKSYFSGLSKLVSAQA
|
| Enzyme 2 Number of Residues |
640 |
| Enzyme 2 Molecular Weight |
70580.3 |
| Enzyme 2 Theoretical pI |
8.57 |
| Enzyme 2 GO Classification |
| Function |
- 5-aminolevulinate synthase activity
- N-acyltransferase activity
- N-succinyltransferase activity
- acyltransferase activity
- binding
- catalytic activity
- cofactor binding
- pyridoxal phosphate binding
- transferase activity
- transferase activity, transferring acyl groups
- transferase activity, transferring acyl groups other than amino-acyl groups
- transferase activity, transferring nitrogenous groups
|
| Process |
- biosynthetic process
- cellular biosynthetic process
- heterocycle biosynthetic process
- metabolic process
- nitrogen compound metabolic process
- porphyrin metabolic process
- tetrapyrrole biosynthetic process
- tetrapyrrole metabolic process
|
| Component |
- cell part
- cytoplasmic part
- intracellular part
- mitochondrial matrix
- mitochondrial part
|
|
| Enzyme 2 General Function |
Involved in 5-aminolevulinate synthase activity |
| Enzyme 2 Specific Function |
Succinyl-CoA + glycine = 5-aminolevulinate + CoA + CO(2) |
| Enzyme 2 Pathways |
- Glycine, Serine and Threonine Metabolism (map00260
)
|
| Enzyme 2 Reactions |
- succinyl-CoA + glycine = 5-aminolevulinate + CoA + CO2 [RN:R00830]
|
| Enzyme 2 Pfam Domain Function |
|
| Enzyme 2 Signals |
|
| Enzyme 2 Transmembrane Regions |
|
| Enzyme 2 Essentiality |
Not Available |
| Enzyme 2 GenBank ID Protein |
28583  |
| Enzyme 2 UniProtKB/Swiss-Prot ID |
P13196  |
| Enzyme 2 UniProtKB/Swiss-Prot Entry Name |
HEM1_HUMAN  |
| Enzyme 2 PDB ID |
Not Available |
| Enzyme 2 Cellular Location |
Not Available |
| Enzyme 2 Gene Sequence |
>1923 bp
ATGGAGAGTGTTGTTCGCCGCTGCCCATTCTTATCCCGAGTCCCCCAGGCCTTTCTGCAG
AAAGCAGGCAAATCTCTGTTGTTCTATGCCCAAAACTGCCCCAAGATGATGGAAGTTGGG
GCCAAGCCAGCCCCTCGGGCATTGTCCACTGCAGCAGTACACTACCAACAGATCAAAGAA
ACCCCTCCGGCCAGTGAGAAAGACAAAACTGCTAAGGCCAAGGTCCAACAGACTCCTGAT
GGATCCCAGCAGAGTCCAGATGGCACACAGCTTCCGTCTGGACACCCCTTGCCTGCCACA
AGCCAGGGCACTGCAAGCAAATGCCCTTTCCTGGCAGCACAGATGAATCAGAGAGGCAGC
AGTGTCTTCTGCAAAGCCAGTCTTGAGCTTCAGGAGGATGTGCAGGAAATGAATGCCGTG
AGGAAAGAGGTTGCTGAAACCTCAGCAGGCCCCAGTGTGGTTAGTGTGAAAACCGATGGA
GGGGATCCCAGTGGACTGCTGAAGAACTTCCAGGACATTATGCAAAAGCAAAGACCAGAA
AGAGTGTCTCATCTTCTTCAAGATAACTTGCCAAAATCTGTTTCCACTTTTCAGTATGAT
CGTTTCTTTGAGAAAAAAATTGATGAGAAAAAGAATGACCACACCTATCGAGTTTTTAAA
ACTGTGAACCGGCGAGCACACATCTTCCCCATGGCAGATGACTATTCAGACTCCCTCATC
ACCAAAAAGCAAGTGTCAGTCTGGTGCAGTAATGACTACCTAGGAATGAGTCGCCACCCA
CGGGTGTGTGGGGCAGTTATGGACACTTTGAAACAACATGGTGCTGGGGCAGGTGGTACT
AGAAATATTTCTGGAACTAGTAAATTCCATGTGGACTTAGAGCGGGAGCTGGCAGACCTC
CATGGGAAAGATGCCGCACTCTTGTTTTCCTCGTGCTTTGTGGCCAATGACTCAACCCTC
TTCACCCTGGCTAAGATGATGCCAGGCTGTGAGATTTACTCTGATTCTGGGAACCATGCC
TCCATGATCCAAGGGATTCGAAACAGCCGAGTGCCAAAGTACATCTTCCGCCACAATGAT
GTCAGCCACCTCAGAGAACTGCTGCAAAGATCTGACCCCTCAGTCCCCAAGATTGTGGCA
TTTGAAACTGTCCATTCAATGGATGGGGCGGTGTGCCCACTGGAAGAGCTGTGTGATGTG
GCCCATGAGTTTGGAGCAATCACCTTCGTGGATGAGGTCCACGCAGTGGGGCTTTATGGG
GCTCGAGGCGGAGGGATTGGGGATCGGGATGGAGTCATGCCAAAAATGGACATCATTTCT
GGAACACTTGGCAAAGCCTTTGGTTGTGTTGGAGGGTACATCGCCAGCACGAGTTCTCTG
ATTGACACCGTACGGTCCTATGCTGCTGGCTTCATCTTCACCACCTCTCTGCCACCCATG
CTGCTGGCTGGAGCCCTGGAGTCTGTGCGGATCCTGAAGAGCGCTGAGGGACGGGTGCTT
CGCCGCCAGCACCAGCGCAACGTCAAACTCATGAGACAGATGCTAATGGATGCCGGCCTC
CCTGTTGTCCACTGCCCCAGCCACATCATCCCTGTGCGGGTTGCAGATGCTGCTAAAAAC
ACAGAAGTCTGTGATGAACTAATGAGCAGACATAACATCTACGTGCAAGCAATCAATTAC
CCTACGGTGCCCCGGGGAGAAGAGCTCCTACGGATTGCCCCCACCCCTCACCACACACCC
CAGATGATGAACTACTTCCTTGAGAATCTGCTAGTCACATGGAAGCAAGTGGGGCTGGAA
CTGAAGCCTCATTCCTCAGCTGAGTGCAACTTCTGCAGGAGGCCACTGCATTTTGAAGTG
ATGAGTGAAAGAGAGAAGTCCTATTTCTCAGGCTTGAGCAAGTTGGTATCTGCTCAGGCC
TGA
|
| Enzyme 2 GenBank Gene ID |
X56351  |
| Enzyme 2 GeneCard ID |
ALAS1  |
| Enzyme 2 GenAtlas ID |
ALAS1  |
| Enzyme 2 HGNC ID |
HGNC:396  |
| Enzyme 2 Chromosome Location |
3 |
| Enzyme 2 Locus |
3p21.1 |
| Enzyme 2 SNPs |
SNPJam Report  |
| Enzyme 2 General References |
- Bishop DF: Two different genes encode delta-aminolevulinate synthase in humans: nucleotide sequences of cDNAs for the housekeeping and erythroid genes. Nucleic Acids Res. 1990 Dec 11;18(23):7187-8. [PubMed
]
- Bawden MJ, Borthwick IA, Healy HM, Morris CP, May BK, Elliott WH: Sequence of human 5-aminolevulinate synthase cDNA. Nucleic Acids Res. 1987 Oct 26;15(20):8563. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
|
| Enzyme 2 Metabolite References |
Not Available |
|
Enzyme 3
[top]
|
| Enzyme 3 ID |
5278 |
| Enzyme 3 Name |
2-amino-3-ketobutyrate coenzyme A ligase, mitochondrial |
| Enzyme 3 Synonyms |
- AKB ligase
- Aminoacetone synthase
- Glycine acetyltransferase
|
| Enzyme 3 Gene Name |
GCAT |
| Enzyme 3 Protein Sequence |
>2-amino-3-ketobutyrate coenzyme A ligase, mitochondrial
MWPGNAWRAALFWVPRGRRAQSALAQLRGILEGELEGIRGAGTWKSERVITSRQGPHIRV
DGVSGGILNFCANNYLGLSSHPEVIQAGLQALEEFGAGLSSVRFICGTQSIHKNLEAKIA
RFHQREDAILYPSCYDANAGLFEALLTPEDAVLSDELNHASIIDGIRLCKAHKYRYRHLD
MADLEAKLQEAQKHRLRLVATDGAFSMDGDIAPLQEICCLASRYGALVFMDECHATGFLG
PTGRGTDELLGVMDQVTIINSTLGKALGGASGGYTTGPGPLVSLLRQRARPYLFSNSLPP
AVVGCASKALDLLMGSNTIVQSMAAKTQRFRSKMEAAGFTISGASHPICPVMLGDARLAS
RMADDMLKRGIFVIGFSYPVVPKGKARIRVQISAVHSEEDIDRCVEAFVEVGRLHGALP
|
| Enzyme 3 Number of Residues |
419 |
| Enzyme 3 Molecular Weight |
45284.6 |
| Enzyme 3 Theoretical pI |
8.11 |
| Enzyme 3 GO Classification |
| Function |
- C-acetyltransferase activity
- acetyltransferase activity
- acyltransferase activity
- binding
- catalytic activity
- cofactor binding
- glycine C-acetyltransferase activity
- pyridoxal phosphate binding
- transferase activity
- transferase activity, transferring acyl groups
- transferase activity, transferring acyl groups other than amino-acyl groups
- transferase activity, transferring nitrogenous groups
|
| Process |
- biosynthetic process
- metabolic process
|
| Component |
| — |
|
| Enzyme 3 General Function |
Involved in glycine C-acetyltransferase activity |
| Enzyme 3 Specific Function |
Acetyl-CoA + glycine = CoA + 2-amino-3- oxobutanoate |
| Enzyme 3 Pathways |
- Glycine, Serine and Threonine Metabolism (map00260
)
|
| Enzyme 3 Reactions |
- acetyl-CoA + glycine = CoA + L-2-amino-3-oxobutanoate [RN:R00371]
|
| Enzyme 3 Pfam Domain Function |
|
| Enzyme 3 Signals |
|
| Enzyme 3 Transmembrane Regions |
|
| Enzyme 3 Essentiality |
Not Available |
| Enzyme 3 GenBank ID Protein |
Not Available |
| Enzyme 3 UniProtKB/Swiss-Prot ID |
O75600  |
| Enzyme 3 UniProtKB/Swiss-Prot Entry Name |
KBL_HUMAN  |
| Enzyme 3 PDB ID |
Not Available |
| Enzyme 3 Cellular Location |
Not Available |
| Enzyme 3 Gene Sequence |
>1260 bp
ATGTGGCCTGGGAACGCCTGGCGCGCCGCACTCTTCTGGGTGCCCCGCGGCCGCCGCGCA
CAGTCAGCGCTGGCCCAGCTGCGTGGCATTCTGGAGGGGGAGCTGGAAGGCATCCGCGGA
GCTGGCACTTGGAAGAGTGAGCGGGTCATCACGTCCCGTCAGGGGCCGCACATCCGCGTG
GACGGCGTCTCCGGAGGAATCCTCAACTTCTGTGCCAACAACTACCTGGGCCTGAGCAGC
CACCCTGAGGTGATTCAGGCAGGTCTGCAGGCTCTGGAGGAGTTTGGAGCTGGCCTTAGC
TCGGTCCGCTTCATCTGTGGAACCCAGAGCATCCACAAGAATCTAGAAGCAAAAATAGCC
CGCTTCCACCAGCGGGAGGATGCCATCCTCTATCCCAGCTGTTATGACGCCAACGCCGGC
CTCTTTGAGGCCCTGCTGACCCCAGAGGACGCAGTCCTGTCGGACGAGCTGAACCATGCC
TCCATCATCGACGGCATCCGGCTGTGCAAGGCCCACAAGTACCGCTATCGCCACCTGGAC
ATGGCCGACCTAGAAGCCAAGCTGCAGGAGGCCCAGAAGCATCGGCTGCGCCTGGTGGCC
ACCGATGGGGCCTTTTCCATGGATGGCGACATCGCACCCCTGCAGGAGATCTGCTGCCTC
GCCTCTAGATATGGTGCCCTGGTCTTCATGGATGAATGCCATGCCACTGGTTTCCTGGGG
CCCACAGGACGGGGCACAGATGAGCTGCTGGGTGTGATGGACCAGGTCACCATCATCAAC
TCCACCCTGGGGAAGGCCCTGGGTGGAGCATCAGGGGGCTACACGACAGGGCCTGGGCCC
CTGGTGTCACTGCTGCGGCAGCGCGCCCGGCCATACCTCTTCTCCAACAGTCTGCCACCT
GCTGTCGTTGGCTGCGCCTCCAAGGCCCTAGATCTGCTGATGGGGAGTAACACCATTGTC
CAGTCTATGGCTGCCAAGACCCAGAGGTTCCGTAGTAAGATGGAAGCTGCTGGCTTCACT
ATCTCAGGAGCCAGTCACCCCATCTGCCCTGTGATGCTGGGTGATGCCCGGCTGGCCTCT
CGCATGGCGGATGACATGCTGAAGAGAGGCATCTTTGTCATCGGGTTCAGCTACCCCGTG
GTCCCCAAGGGCAAGGCCCGGATCCGGGTACAGATCTCAGCAGTGCATAGCGAGGAAGAC
ATTGACCGCTGCGTGGAGGCCTTCGTGGAAGTGGGGCGACTGCACGGGGCACTGCCCTGA
|
| Enzyme 3 GenBank Gene ID |
AF077740  |
| Enzyme 3 GeneCard ID |
GCAT  |
| Enzyme 3 GenAtlas ID |
GCAT  |
| Enzyme 3 HGNC ID |
HGNC:4188  |
| Enzyme 3 Chromosome Location |
2 |
| Enzyme 3 Locus |
22q13.1 |
| Enzyme 3 SNPs |
SNPJam Report  |
| Enzyme 3 General References |
- Edgar AJ, Polak JM: Molecular cloning of the human and murine 2-amino-3-ketobutyrate coenzyme A ligase cDNAs. Eur J Biochem. 2000 Mar;267(6):1805-12. [PubMed
]
- Dunham I, Shimizu N, Roe BA, Chissoe S, Hunt AR, Collins JE, Bruskiewich R, Beare DM, Clamp M, Smink LJ, Ainscough R, Almeida JP, Babbage A, Bagguley C, Bailey J, Barlow K, Bates KN, Beasley O, Bird CP, Blakey S, Bridgeman AM, Buck D, Burgess J, Burrill WD, O'Brien KP, et al.: The DNA sequence of human chromosome 22. Nature. 1999 Dec 2;402(6761):489-95. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
|
| Enzyme 3 Metabolite References |
Not Available |
|
Enzyme 4
[top]
|
| Enzyme 4 ID |
5420 |
| Enzyme 4 Name |
Methylenetetrahydrofolate reductase |
| Enzyme 4 Synonyms |
Not Available |
| Enzyme 4 Gene Name |
MTHFR |
| Enzyme 4 Protein Sequence |
>Methylenetetrahydrofolate reductase
MVNEARGNSSLNPCLEGSASSGSESSKDSSRCSTPGLDPERHERLREKMRRRLESGDKWF
SLEFFPPRTAEGAVNLISRFDRMAAGGPLYIDVTWHPAGDPGSDKETSSMMIASTAVNYC
GLETILHMTCCRQRLEEITGHLHKAKQLGLKNIMALRGDPIGDQWEEEEGGFNYAVDLVK
HIRSEFGDYFDICVAGYPKGHPEAGSFEADLKHLKEKVSAGADFIITQLFFEADTFFRFV
KACTDMGITCPIVPGIFPIQGYHSLRQLVKLSKLEVPQEIKDVIEPIKDNDAAIRNYGIE
LAVSLCQELLASGLVPGLHFYTLNREMATTEVLKRLGMWTEDPRRPLPWALSAHPKRREE
DVRPIFWASRPKSYIYRTQEWDEFPNGRWGNSSSPAFGELKDYYLFYLKSKSPKEELLKM
WGEELTSEESVFEVFVLYLSGEPNRNGHKVTCLPWNDEPLAAETSLLKEELLRVNRQGIL
TINSQPNINGKPSSDPIVGWGPSGGYVFQKAYLEFFTSRETAEALLQVLKKYELRVNYHL
VNVKGENITNAPELQPNAVTWGIFPGREIIQPTVVDPVSFMFWKDEAFALWIERWGKLYE
EESPSRTIIQYIHDNYFLVNLVDNDFPLDNCLWQVVEDTLELLNRPTQNARETEAP
|
| Enzyme 4 Number of Residues |
656 |
| Enzyme 4 Molecular Weight |
74595.9 |
| Enzyme 4 Theoretical pI |
5.00 |
| Enzyme 4 GO Classification |
| Function |
- catalytic activity
- methylenetetrahydrofolate reductase (NADPH) activity
- methylenetetrahydrofolate reductase (NADPH) activity
- oxidoreductase activity
- oxidoreductase activity, acting on the CH-NH group of donors
- oxidoreductase activity, acting on the CH-NH group of donors, NAD or NADP as acceptor
|
| Process |
- cellular amino acid and derivative metabolic process
- cellular amino acid metabolic process
- cellular metabolic process
- metabolic process
- methionine metabolic process
- oxidation reduction
- sulfur amino acid metabolic process
|
| Component |
| — |
|
| Enzyme 4 General Function |
Involved in methylenetetrahydrofolate reductase (NADPH) activity |
| Enzyme 4 Specific Function |
Catalyzes the conversion of 5,10- methylenetetrahydrofolate to 5-methyltetrahydrofolate, a co- substrate for homocysteine remethylation to methionine |
| Enzyme 4 Pathways |
|
| Enzyme 4 Reactions |
- 5-methyltetrahydrofolate + NAD(P)+ = 5,10-methylenetetrahydrofolate + NAD(P)H + H+ [RN:R01224 R07168]
|
| Enzyme 4 Pfam Domain Function |
|
| Enzyme 4 Signals |
|
| Enzyme 4 Transmembrane Regions |
|
| Enzyme 4 Essentiality |
Not Available |
| Enzyme 4 GenBank ID Protein |
6139053  |
| Enzyme 4 UniProtKB/Swiss-Prot ID |
P42898  |
| Enzyme 4 UniProtKB/Swiss-Prot Entry Name |
MTHR_HUMAN  |
| Enzyme 4 PDB ID |
Not Available |
| Enzyme 4 Cellular Location |
Not Available |
| Enzyme 4 Gene Sequence |
>1971 bp
ATGGTGAACGAAGCCAGAGGAAACAGCAGCCTCAACCCCTGCTTGGAGGGCAGTGCCAGC
AGTGGCAGTGAGAGCTCCAAAGATAGTTCGAGATGTTCCACCCCGGGCCTGGACCCTGAG
CGGCATGAGAGACTCCGGGAGAAGATGAGGCGGCGATTGGAATCTGGTGACAAGTGGTTC
TCCCTGGAATTCTTCCCTCCTCGAACTGCTGAGGGAGCTGTCAATCTCATCTCAAGGTTT
GACCGGATGGCAGCAGGTGGCCCCCTCTACATAGACGTGACCTGGCACCCAGCAGGTGAC
CCTGGCTCAGACAAGGAGACCTCCTCCATGATGATCGCCAGCACCGCCGTGAACTACTGT
GGCCTGGAGACCATCCTGCACATGACCTGCTGCCGTCAGCGCCTGGAGGAGATCACGGGC
CATCTGCACAAAGCTAAGCAGCTGGGCCTGAAGAACATCATGGCGCTGCGGGGAGACCCA
ATAGGTGACCAGTGGGAAGAGGAGGAGGGAGGCTTCAACTACGCAGTGGACCTGGTGAAG
CACATCCGAAGTGAGTTTGGTGACTACTTTGACATCTGTGTGGCAGGTTACCCCAAAGGC
CACCCCGAAGCAGGGAGCTTTGAGGCTGACCTGAAGCACTTGAAGGAGAAGGTGTCTGCG
GGAGCCGATTTCATCATCACGCAGCTTTTCTTTGAGGCTGACACATTCTTCCGCTTTGTG
AAGGCATGCACCGACATGGGCATCACTTGCCCCATCGTCCCCGGGATCTTTCCCATCCAG
GGCTACCACTCCCTTCGGCAGCTTGTGAAGCTGTCCAAGCTGGAGGTGCCACAGGAGATC
AAGGACGTGATTGAGCCAATCAAAGACAACGATGCTGCCATCCGCAACTATGGCATCGAG
CTGGCCGTGAGCCTGTGCCAGGAGCTTCTGGCCAGTGGCTTGGTGCCAGGCCTCCACTTC
TACACCCTCAACCGCGAGATGGCTACCACAGAGGTGCTGAAGCGCCTGGGGATGTGGACT
GAGGACCCCAGGCGTCCCCTACCCTGGGCTCTCAGTGCCCACCCCAAGCGCCGAGAGGAA
GATGTACGTCCCATCTTCTGGGCCTCCAGACCAAAGAGTTACATCTACCGTACCCAGGAG
TGGGACGAGTTCCCTAACGGCCGCTGGGGCAATTCCTCTTCCCCTGCCTTTGGGGAGCTG
AAGGACTACTACCTCTTCTACCTGAAGAGCAAGTCCCCCAAGGAGGAGCTGCTGAAGATG
TGGGGGGAGGAGCTGACCAGTGAAGCAAGTGTCTTTGAAGTCTTTGTTCTTTACCTCTCG
GGAGAACCAAACCGGAATGGTCACAAAGTGACTTGCCTGCCCTGGAACGATGAGCCCCTG
GCGGCTGAGACCAGCCTGCTGAAGGAGGAGCTGCTGCGGGTGAACCGCCAGGGCATCCTC
ACCATCAACTCACAGCCCAACATCAACGGGAAGCCGTCCTCCGACCCCATCGTGGGCTGG
GGCCCCAGCGGGGGCTATGTCTTCCAGAAGGCCTACTTAGAGTTTTTCACTTCCCGCGAG
ACAGCGGAAGCACTTCTGCAAGTGCTGAAGAAGTACGAGCTCCGGGTTAATTACCACCTT
GTCAATGTGAAGGGTGAAAACATCACCAATGCCCCTGAACTGCAGCCGAATGCTGTCACT
TGGGGCATCTTCCCTGGGCGAGAGATCATCCAGCCCACCGTAGTGGATCCCGTCAGCTTC
ATGTTCTGGAAGGACGAGGCCTTTGCCCTGTGGATTGAGCGGTGGGGAAAGCTGTATGAG
GAGGAGTCCCCGTCCCGCACCATCATCCAGTACATCCACGACAACTACTTCCTGGTCAAC
CTGGTGGACAATGACTTCCCACTGGACAACTGCCTCTGGCAGGTGGTGGAAGACACATTG
GAGCTTCTCAACAGGCCCACCCAGAATGCGAGAGAAACGGAGGCTCCATGA
|
| Enzyme 4 GenBank Gene ID |
U09806  |
| Enzyme 4 GeneCard ID |
MTHFR  |
| Enzyme 4 GenAtlas ID |
MTHFR  |
| Enzyme 4 HGNC ID |
HGNC:7436  |
| Enzyme 4 Chromosome Location |
1 |
| Enzyme 4 Locus |
1p36.3 |
| Enzyme 4 SNPs |
SNPJam Report  |
| Enzyme 4 General References |
- Goyette P, Pai A, Milos R, Frosst P, Tran P, Chen Z, Chan M, Rozen R: Gene structure of human and mouse methylenetetrahydrofolate reductase (MTHFR) Mamm Genome. 1998 Aug;9(8):652-6. [PubMed
]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
- Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Goyette P, Sumner JS, Milos R, Duncan AM, Rosenblatt DS, Matthews RG, Rozen R: Human methylenetetrahydrofolate reductase: isolation of cDNA, mapping and mutation identification. Nat Genet. 1994 Jun;7(2):195-200. [PubMed
]
- Goyette P, Sumner JS, Milos R, Duncan AM, Rosenblatt DS, Matthews RG, Rozen R: Human methylenetetrahydrofolate reductase: isolation of cDNA mapping and mutation identification. Nat Genet. 1994 Aug;7(4):551. [PubMed
]
- Goyette P, Frosst P, Rosenblatt DS, Rozen R: Seven novel mutations in the methylenetetrahydrofolate reductase gene and genotype/phenotype correlations in severe methylenetetrahydrofolate reductase deficiency. Am J Hum Genet. 1995 May;56(5):1052-9. [PubMed
]
- van der Put NM, Steegers-Theunissen RP, Frosst P, Trijbels FJ, Eskes TK, van den Heuvel LP, Mariman EC, den Heyer M, Rozen R, Blom HJ: Mutated methylenetetrahydrofolate reductase as a risk factor for spina bifida. Lancet. 1995 Oct 21;346(8982):1070-1. [PubMed
]
- Frosst P, Blom HJ, Milos R, Goyette P, Sheppard CA, Matthews RG, Boers GJ, den Heijer M, Kluijtmans LA, van den Heuvel LP, et al.: A candidate genetic risk factor for vascular disease: a common mutation in methylenetetrahydrofolate reductase. Nat Genet. 1995 May;10(1):111-3. [PubMed
]
- Ou CY, Stevenson RE, Brown VK, Schwartz CE, Allen WP, Khoury MJ, Rozen R, Oakley GP Jr, Adams MJ Jr: 5,10 Methylenetetrahydrofolate reductase genetic polymorphism as a risk factor for neural tube defects. Am J Med Genet. 1996 Jun 28;63(4):610-4. [PubMed
]
- Goyette P, Christensen B, Rosenblatt DS, Rozen R: Severe and mild mutations in cis for the methylenetetrahydrofolate reductase (MTHFR) gene, and description of five novel mutations in MTHFR. Am J Hum Genet. 1996 Dec;59(6):1268-75. [PubMed
]
- Chen J, Giovannucci E, Kelsey K, Rimm EB, Stampfer MJ, Colditz GA, Spiegelman D, Willett WC, Hunter DJ: A methylenetetrahydrofolate reductase polymorphism and the risk of colorectal cancer. Cancer Res. 1996 Nov 1;56(21):4862-4. [PubMed
]
- Schneider JA, Rees DC, Liu YT, Clegg JB: Worldwide distribution of a common methylenetetrahydrofolate reductase mutation. Am J Hum Genet. 1998 May;62(5):1258-60. [PubMed
]
- van der Put NM, Gabreels F, Stevens EM, Smeitink JA, Trijbels FJ, Eskes TK, van den Heuvel LP, Blom HJ: A second common mutation in the methylenetetrahydrofolate reductase gene: an additional risk factor for neural-tube defects? Am J Hum Genet. 1998 May;62(5):1044-51. [PubMed
]
- Kluijtmans LA, Wendel U, Stevens EM, van den Heuvel LP, Trijbels FJ, Blom HJ: Identification of four novel mutations in severe methylenetetrahydrofolate reductase deficiency. Eur J Hum Genet. 1998 May-Jun;6(3):257-65. [PubMed
]
- Weisberg I, Tran P, Christensen B, Sibani S, Rozen R: A second genetic polymorphism in methylenetetrahydrofolate reductase (MTHFR) associated with decreased enzyme activity. Mol Genet Metab. 1998 Jul;64(3):169-72. [PubMed
]
- Christensen B, Arbour L, Tran P, Leclerc D, Sabbaghian N, Platt R, Gilfix BM, Rosenblatt DS, Gravel RA, Forbes P, Rozen R: Genetic polymorphisms in methylenetetrahydrofolate reductase and methionine synthase, folate levels in red blood cells, and risk of neural tube defects. Am J Med Genet. 1999 May 21;84(2):151-7. [PubMed
]
- Skibola CF, Smith MT, Kane E, Roman E, Rollinson S, Cartwright RA, Morgan G: Polymorphisms in the methylenetetrahydrofolate reductase gene are associated with susceptibility to acute leukemia in adults. Proc Natl Acad Sci U S A. 1999 Oct 26;96(22):12810-5. [PubMed
]
- Sibani S, Christensen B, O'Ferrall E, Saadi I, Hiou-Tim F, Rosenblatt DS, Rozen R: Characterization of six novel mutations in the methylenetetrahydrofolate reductase (MTHFR) gene in patients with homocystinuria. Hum Mutat. 2000;15(3):280-7. [PubMed
]
- Casas JP, Hingorani AD, Bautista LE, Sharma P: Meta-analysis of genetic studies in ischemic stroke: thirty-two genes involving approximately 18,000 cases and 58,000 controls. Arch Neurol. 2004 Nov;61(11):1652-61. [PubMed
]
- Ley TJ, Mardis ER, Ding L, Fulton B, McLellan MD, Chen K, Dooling D, Dunford-Shore BH, McGrath S, Hickenbotham M, Cook L, Abbott R, Larson DE, Koboldt DC, Pohl C, Smith S, Hawkins A, Abbott S, Locke D, Hillier LW, Miner T, Fulton L, Magrini V, Wylie T, Glasscock J, Conyers J, Sander N, Shi X, Osborne JR, Minx P, Gordon D, Chinwalla A, Zhao Y, Ries RE, Payton JE, Westervelt P, Tomasson MH, Watson M, Baty J, Ivanovich J, Heath S, Shannon WD, Nagarajan R, Walter MJ, Link DC, Graubert TA, DiPersio JF, Wilson RK: DNA sequencing of a cytogenetically normal acute myeloid leukaemia genome. Nature. 2008 Nov 6;456(7218):66-72. [PubMed
]
|
| Enzyme 4 Metabolite References |
Not Available |
|
Enzyme 5
[top]
|
| Enzyme 5 ID |
5480 |
| Enzyme 5 Name |
4-aminobutyrate aminotransferase, mitochondrial |
| Enzyme 5 Synonyms |
- (S)-3-amino-2-methylpropionate transaminase
- GABA aminotransferase
- GABA-AT
- Gamma-amino-N-butyrate transaminase
- GABA transaminase
- GABA-T
- L-AIBAT
|
| Enzyme 5 Gene Name |
ABAT |
| Enzyme 5 Protein Sequence |
>4-aminobutyrate aminotransferase, mitochondrial
MASMLLAQRLACSFQHSYRLLVPGSRHISQAAAKVDVEFDYDGPLMKTEVPGPRSQELMK
QLNIIQNAEAVHFFCNYEESRGNYLVDVDGNRMLDLYSQISSVPIGYSHPALLKLIQQPQ
NASMFVNRPALGILPPENFVEKLRQSLLSVAPKGMSQLITMACGSCSNENALKTIFMWYR
SKERGQRGFSQEELETCMINQAPGCPDYSILSFMGAFHGRTMGCLATTHSKAIHKIDIPS
FDWPIAPFPRLKYPLEEFVKENQQEEARCLEEVEDLIVKYRKKKKTVAGIIVEPIQSEGG
DNHASDDFFRKLRDIARKHGCAFLVDEVQTGGGCTGKFWAHEHWGLDDPADVMTFSKKMM
TGGFFHKEEFRPNAPYRIFNTWLGDPSKNLLLAEVINIIKREDLLNNAAHAGKALLTGLL
DLQARYPQFISRVRGRGTFCSFDTPDDSIRNKLILIARNKGVVLGGCGDKSIRFRPTLVF
RDHHAHLFLNIFSDILADFK
|
| Enzyme 5 Number of Residues |
500 |
| Enzyme 5 Molecular Weight |
56438.4 |
| Enzyme 5 Theoretical pI |
8.04 |
| Enzyme 5 GO Classification |
| Function |
- 4-aminobutyrate transaminase activity
- binding
- catalytic activity
- cofactor binding
- pyridoxal phosphate binding
- transaminase activity
- transferase activity
- transferase activity, transferring nitrogenous groups
|
| Process |
- cellular amino acid and derivative metabolic process
- cellular amino acid derivative metabolic process
- cellular metabolic process
- gamma-aminobutyric acid metabolic process
- metabolic process
|
| Component |
| — |
|
| Enzyme 5 General Function |
Involved in 4-aminobutyrate transaminase activity |
| Enzyme 5 Specific Function |
Catalyzes the conversion of gamma-aminobutyrate and L- beta-aminoisobutyrate to succinate semialdehyde and methylmalonate semialdehyde, respectively. Can also convert delta-aminovalerate and beta-alanine |
| Enzyme 5 Pathways |
- Valine, Leucine and Isoleucine Degradation (map00280
)
|
| Enzyme 5 Reactions |
- (S)-3-amino-2-methylpropanoate + 2-oxoglutarate = 2-methyl-3-oxopropanoate + L-glutamate
|
| Enzyme 5 Pfam Domain Function |
|
| Enzyme 5 Signals |
|
| Enzyme 5 Transmembrane Regions |
|
| Enzyme 5 Essentiality |
Not Available |
| Enzyme 5 GenBank ID Protein |
158254434  |
| Enzyme 5 UniProtKB/Swiss-Prot ID |
P80404  |
| Enzyme 5 UniProtKB/Swiss-Prot Entry Name |
GABT_HUMAN  |
| Enzyme 5 PDB ID |
1OHY  |
| Enzyme 5 PDB File |
Show |
| Enzyme 5 3D Structure |
|
| Enzyme 5 Cellular Location |
Not Available |
| Enzyme 5 Gene Sequence |
>1503 bp
ATGGCCTCCATGTTGCTCGCCCAGCGCCTGGCCTGCAGCTTCCAGCACAGCTACCGCCTG
CTGGTGCCTGGATCCAGACACATTAGTCAAGCTGCAGCCAAAGTCGACGTTGAATTTGAT
TATGATGGGCCTCTGATGAAGACGGAAGTCCCAGGGCCTAGATCTCAGGAGTTAATGAAA
CAGCTGAATATAATTCAGAATGCAGAGGCTGTGCATTTTTTCTGCAATTACGAAGAGAGC
CGAGGCAATTACCTGGTTGATGTGGACGGCAACCGAATGCTGGATCTTTATTCCCAGATC
TCCTCTGTTCCCATAGGTTACAGCCACCCCGCCCTGCTGAAACTCATCCAACAGCCTCAA
AATGCGAGCATGTTTGTCAACAGACCCGCCCTCGGAATCCTGCCTCCGGAGAACTTTGTG
GAGAAGCTCCGGCAGTCCTTGCTCTCGGTGGCTCCCAAAGGGATGTCCCAGCTCATCACC
ATGGCCTGCGGCTCCTGCTCCAATGAAAACGCCTTAAAGACCATCTTCATGTGGTACCGG
AGCAAGGAAAGAGGGCAGAGGGGCTTCTCCCAGGAGGAGCTGGAGACGTGCATGATTAAC
CAGGCCCCTGGCTGCCCCGACTACAGCATCCTCTCCTTCATGGGCGCGTTCCATGGGAGG
ACCATGGGTTGCTTAGCGACCACGCACTCTAAAGCCATTCACAAGATCGACATCCCTTCC
TTTGACTGGCCCATCGCACCGTTCCCACGGCTGAAATACCCTCTGGAAGAGTTTGTGAAA
GAGAACCAACAGGAGGAGGCCCGCTGTCTGGAAGAGGTGGAGGATCTGATTGTGAAATAT
CGGAAAAAGAAGAAGACGGTGGCCGGGATCATCGTGGAGCCCATCCAGTCCGAGGGTGGA
GACAACCACGCATCCGATGACTTCTTTCGGAAGCTGAGAGACATCGCCAGGAAGCATGGC
TGCGCCTTCTTGGTGGACGAGGTACAGACCGGAGGAGGCTGCACGGGCAAGTTCTGGGCC
CATGAGCACTGGGGCCTGGATGACCCAGCAGACGTGATGACCTTCAGCAAGAAGATGATG
ACTGGGGGCTTCTTCCACAAGGAGGAGTTCAGGCCTAATGCTCCCTACCGGATCTTCAAC
ACCTGGCTGGGGGACCCGTCCAAGAACCTGTTGCTGGCTGAGGTCATCAACATCATCAAG
CGGGAGGACCTGCTAAATAATGCAGCCCATGCCGGGAAGGCCCTGCTCACAGGACTGCTG
GACCTCCAGGCCCGGTACCCCCAGTTCATCAGCAGGGTGAGAGGACGAGGCACCTTTTGC
TCCTTCGATACTCCCGATGATTCCATACGGAATAAGCTCATTTTAATTGCCAGAAACAAA
GGTGTGGTGTTGGGTGGCTGTGGTGACAAATCCATTCGTTTCCGTCCCACGCTGGTCTTC
AGGGATCACCACGCTCACCTGTTCCTCAATATTTTCAGTGACATCTTAGCAGACTTCAAG
TAA
|
| Enzyme 5 GenBank Gene ID |
AK290501  |
| Enzyme 5 GeneCard ID |
ABAT  |
| Enzyme 5 GenAtlas ID |
ABAT  |
| Enzyme 5 HGNC ID |
HGNC:23  |
| Enzyme 5 Chromosome Location |
1 |
| Enzyme 5 Locus |
16p13.2 |
| Enzyme 5 SNPs |
SNPJam Report  |
| Enzyme 5 General References |
- Osei YD, Churchich JE: Screening and sequence determination of a cDNA encoding the human brain 4-aminobutyrate aminotransferase. Gene. 1995 Apr 3;155(2):185-7. [PubMed
]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- De Biase D, Barra D, Simmaco M, John RA, Bossa F: Primary structure and tissue distribution of human 4-aminobutyrate aminotransferase. Eur J Biochem. 1995 Jan 15;227(1-2):476-80. [PubMed
]
- Medina-Kauwe LK, Tobin AJ, De Meirleir L, Jaeken J, Jakobs C, Nyhan WL, Gibson KM: 4-Aminobutyrate aminotransferase (GABA-transaminase) deficiency. J Inherit Metab Dis. 1999 Jun;22(4):414-27. [PubMed
]
|
| Enzyme 5 Metabolite References |
Not Available |
|
Enzyme 6
[top]
|
| Enzyme 6 ID |
5509 |
| Enzyme 6 Name |
Tyrosine aminotransferase |
| Enzyme 6 Synonyms |
- TAT
- L-tyrosine:2-oxoglutarate aminotransferase
|
| Enzyme 6 Gene Name |
TAT |
| Enzyme 6 Protein Sequence |
>Tyrosine aminotransferase
MDPYMIQMSSKGNLPSILDVHVNVGGRSSVPGKMKGRKARWSVRPSDMAKKTFNPIRAIV
DNMKVKPNPNKTMISLSIGDPTVFGNLPTDPEVTQAMKDALDSGKYNGYAPSIGFLSSRE
EIASYYHCPEAPLEAKDVILTSGCSQAIDLCLAVLANPGQNILVPRPGFSLYKTLAESMG
IEVKLYNLLPEKSWEIDLKQLEYLIDEKTACLIVNNPSNPCGSVFSKRHLQKILAVAARQ
CVPILADEIYGDMVFSDCKYEPLATLSTDVPILSCGGLAKRWLVPGWRLGWILIHDRRDI
FGNEIRDGLVKLSQRILGPCTIVQGALKSILCRTPGEFYHNTLSFLKSNADLCYGALAAI
PGLRPVRPSGAMYLMVGIEMEHFPEFENDVEFTERLVAEQSVHCLPATCFEYPNFIRVVI
TVPEVMMLEACSRIQEFCEQHYHCAEGSQEECDK
|
| Enzyme 6 Number of Residues |
454 |
| Enzyme 6 Molecular Weight |
50398.9 |
| Enzyme 6 Theoretical pI |
6.24 |
| Enzyme 6 GO Classification |
| Function |
- 1-aminocyclopropane-1-carboxylate synthase activity
- L-tyrosine aminotransferase activity
- L-tyrosine:2-oxoglutarate aminotransferase activity
- binding
- carbon-sulfur lyase activity
- catalytic activity
- cofactor binding
- lyase activity
- pyridoxal phosphate binding
- transaminase activity
- transferase activity
- transferase activity, transferring nitrogenous groups
|
| Process |
- aromatic amino acid family catabolic process
- aromatic amino acid family metabolic process
- biosynthetic process
- cellular amino acid and derivative metabolic process
- cellular amino acid catabolic process
- cellular amino acid metabolic process
- cellular metabolic process
- metabolic process
|
| Component |
| — |
|
| Enzyme 6 General Function |
Involved in 1-aminocyclopropane-1-carboxylate synthase activity |
| Enzyme 6 Specific Function |
Transaminase involved in tyrosine breakdown. Converts tyrosine to p-hydroxyphenylpyruvate. Can catalyze the reverse reaction, using glutamic acid, with 2-oxoglutarate as cosubstrate (in vitro). Has no transaminase activity towards phenylalanine |
| Enzyme 6 Pathways |
|
| Enzyme 6 Reactions |
- L-tyrosine + 2-oxoglutarate = 4-hydroxyphenylpyruvate + L-glutamate [RN:R00734]
|
| Enzyme 6 Pfam Domain Function |
|
| Enzyme 6 Signals |
|
| Enzyme 6 Transmembrane Regions |
|
| Enzyme 6 Essentiality |
Not Available |
| Enzyme 6 GenBank ID Protein |
36713  |
| Enzyme 6 UniProtKB/Swiss-Prot ID |
P17735  |
| Enzyme 6 UniProtKB/Swiss-Prot Entry Name |
ATTY_HUMAN  |
| Enzyme 6 PDB ID |
Not Available |
| Enzyme 6 Cellular Location |
Not Available |
| Enzyme 6 Gene Sequence |
>1365 bp
ATGGACCCATACATGATTCAGATGAGCAGCAAAGGCAACCTCCCCTCAATTCTGGACGTG
CATGTCAACGTTGGTGGGAGAAGCTCTGTGCCGGGAAAAATGAAAGGCAGAAAGGCCAGG
TGGTCTGTGAGGCCCTCAGACATGGCCAAGAAAACTTTCAACCCCATCCGAGCCATTGTG
GACAACATGAAGGTGAAACCAAATCCAAACAAAACCATGATTTCCCTGTCCATTGGGGAC
CCTACTGTGTTTGGAAACCTGCCTACAGACCCTGAAGTTACCCAGGCAATGAAAGATGCC
CTGGACTCGGGCAAATATAATGGCTATGCCCCATCCATCGGCTTCCTATCCAGTCGGGAG
GAGATTGCTTCTTATTACCACTGTCCTGAGGCACCCCTAGAAGCTAAGGACGTCATTCTG
ACAAGTGGCTGCAGCCAAGCTATTGACCTTTGTTTAGCTGTGTTGGCCAACCCAGGGCAG
AACATCCTGGTTCCAAGACCTGGTTTCTCTCTCTACAAGACTCTGGCTGAGTCTATGGGA
ATTGAGGTCAAACTCTACAATTTGTTGCCAGAGAAATCTTGGGAAATTGACCTGAAACAA
CTGGAATATCTAATTGATGAAAAGACAGCTTGTCTCATTGTCAATAATCCATCAAACCCC
TGTGGGTCAGTGTTCAGCAAACGTCATCTTCAGAAGATTCTGGCAGTGGCTGCACGGCAG
TGTGTCCCCATCTTAGCTGATGAGATCTATGGAGACATGGTGTTTTCGGATTGCAAATAT
GAACCACTGGCCACCCTCAGCACCGATGTCCCCATCCTGTCCTGTGGAGGGCTGGCCAAG
CGCTGGCTGGTTCCTGGCTGGAGGTTGGGCTGGATCCTCATTCATGACCGAAGAGACATT
TTTGGCAATGAGATCCGAGATGGGCTGGTGAAGCTGAGTCAGCGCATTTTGGGACCCTGT
ACCATTGTCCAGGGAGCTCTGAAAAGCATCCTATGTCGCACCCCGGGAGAGTTTTACCAC
AACACTCTGAGCTTCCTCAAGTCCAATGCTGATCTCTGTTATGGGGCGTTGGCTGCCATC
CCTGGACTCCGGCCAGTCCGCCCTTCTGGGGCTATGTACCTCATGGTTGGAATTGAGATG
GAACATTTCCCAGAATTTGAGAACGATGTGGAGTTCACGGAGCGGTTAGTTGCTGAGCAG
TCTGTCCACTGCCTCCCAGCAACGTGCTTTGAGTACCCGAATTTCATCCGAGTGGTCATC
ACAGTCCCCGAGGTGATGATGCTGGAGGCGTGCAGCCGGATCCAGGAGTTCTGTGAGCAG
CACTACCATTGTGCTGAAGGCAGCCAGGAGGAGTGTGATAAATAG
|
| Enzyme 6 GenBank Gene ID |
X52520  |
| Enzyme 6 GeneCard ID |
TAT  |
| Enzyme 6 GenAtlas ID |
TAT  |
| Enzyme 6 HGNC ID |
HGNC:11573  |
| Enzyme 6 Chromosome Location |
1 |
| Enzyme 6 Locus |
16q22.1 |
| Enzyme 6 SNPs |
SNPJam Report  |
| Enzyme 6 General References |
- Rettenmeier R, Natt E, Zentgraf H, Scherer G: Isolation and characterization of the human tyrosine aminotransferase gene. Nucleic Acids Res. 1990 Jul 11;18(13):3853-61. [PubMed
]
- Zelenin SM, Mertvetsov NP: [Nucleotide sequence of the human tyrosine aminotransferase gene] Bioorg Khim. 1994 Feb;20(2):196-204. [PubMed
]
- Seralini GE, Luu-The V, Labrie F: Cloning and expression of human tyrosine aminotransferase cDNA. Biochim Biophys Acta. 1995 Jan 2;1260(1):97-101. [PubMed
]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
- Sivaraman S, Kirsch JF: The narrow substrate specificity of human tyrosine aminotransferase--the enzyme deficient in tyrosinemia type II. FEBS J. 2006 May;273(9):1920-9. [PubMed
]
- Natt E, Kida K, Odievre M, Di Rocco M, Scherer G: Point mutations in the tyrosine aminotransferase gene in tyrosinemia type II. Proc Natl Acad Sci U S A. 1992 Oct 1;89(19):9297-301. [PubMed
]
|
| Enzyme 6 Metabolite References |
Not Available |
|
Enzyme 7
[top]
|
| Enzyme 7 ID |
5510 |
| Enzyme 7 Name |
Aromatic-L-amino-acid decarboxylase |
| Enzyme 7 Synonyms |
- AADC
- DOPA decarboxylase
- DDC
|
| Enzyme 7 Gene Name |
DDC |
| Enzyme 7 Protein Sequence |
>Aromatic-L-amino-acid decarboxylase
MNASEFRRRGKEMVDYVANYMEGIEGRQVYPDVEPGYLRPLIPAAAPQEPDTFEDIINDV
EKIIMPGVTHWHSPYFFAYFPTASSYPAMLADMLCGAIGCIGFSWAASPACTELETVMMD
WLGKMLELPKAFLNEKAGEGGGVIQGSASEATLVALLAARTKVIHRLQAASPELTQAAIM
EKLVAYSSDQAHSSVERAGLIGGVKLKAIPSDGNFAMRASALQEALERDKAAGLIPFFMV
ATLGTTTCCSFDNLLEVGPICNKEDIWLHVDAAYAGSAFICPEFRHLLNGVEFADSFNFN
PHKWLLVNFDCSAMWVKKRTDLTGAFRLDPTYLKHSHQDSGLITDYRHWQIPLGRRFRSL
KMWFVFRMYGVKGLQAYIRKHVQLSHEFESLVRQDPRFEICVEVILGLVCFRLKGSNKVN
EALLQRINSAKKIHLVPCHLRDKFVLRFAICSRTVESAHVQRAWEHIKELAADVLRAERE
|
| Enzyme 7 Number of Residues |
480 |
| Enzyme 7 Molecular Weight |
53893.8 |
| Enzyme 7 Theoretical pI |
7.21 |
| Enzyme 7 GO Classification |
| Function |
- binding
- carbon-carbon lyase activity
- carboxy-lyase activity
- catalytic activity
- cofactor binding
- lyase activity
- pyridoxal phosphate binding
|
| Process |
- carboxylic acid metabolic process
- cellular amino acid and derivative metabolic process
- cellular metabolic process
- metabolic process
- organic acid metabolic process
- oxoacid metabolic process
|
| Component |
| — |
|
| Enzyme 7 General Function |
Involved in carboxy-lyase activity |
| Enzyme 7 Specific Function |
Catalyzes the decarboxylation of L-3,4- dihydroxyphenylalanine (DOPA) to dopamine, L-5-hydroxytryptophan to serotonin and L-tryptophan to tryptamine |
| Enzyme 7 Pathways |
|
| Enzyme 7 Reactions |
- (1) 3,4-dihydroxy-L-phenylalanine = dopamine + CO2 [RN:R02080]
- (2) 5-hydroxy-L-tryptophan = 5-hydroxytryptamine + CO2 [RN:R02701]
|
| Enzyme 7 Pfam Domain Function |
|
| Enzyme 7 Signals |
|
| Enzyme 7 Transmembrane Regions |
|
| Enzyme 7 Essentiality |
Not Available |
| Enzyme 7 GenBank ID Protein |
Not Available |
| Enzyme 7 UniProtKB/Swiss-Prot ID |
P20711  |
| Enzyme 7 UniProtKB/Swiss-Prot Entry Name |
DDC_HUMAN  |
| Enzyme 7 PDB ID |
1JS3  |
| Enzyme 7 PDB File |
Show |
| Enzyme 7 3D Structure |
|
| Enzyme 7 Cellular Location |
Not Available |
| Enzyme 7 Gene Sequence |
>1443 bp
ATGAACGCAAGTGAATTCCGAAGGAGAGGGAAGGAGATGGTGGATTACGTGGCCAACTAC
ATGGAAGGCATTGAGGGACGCCAGGTCTACCCTGACGTGGAGCCCGGGTACCTGCGGCCG
CTGATCCCTGCCGCTGCCCCTCAGGAGCCAGACACGTTTGAGGACATCATCAACGACGTT
GAGAAGATAATCATGCCTGGGGTGACGCACTGGCACAGCCCCTACTTCTTCGCCTACTTC
CCCACTGCCAGCTCGTACCCGGCCATGCTTGCGGACATGCTGTGCGGGGCCATTGGCTGC
ATCGGCTTCTCCTGGGCGGCAAGCCCAGCATGCACAGAGCTGGAGACTGTGATGATGGAC
TGGCTCGGGAAGATGCTGGAACTACCAAAGGCATTTTTGAATGAGAAAGCTGGAGAAGGG
GGAGGAGTGATCCAGGGAAGTGCCAGTGAAGCCACCCTGGTGGCCCTGCTGGCCGCTCGG
ACCAAAGTGATCCATCGGCTGCAGGCAGCGTCCCCAGAGCTCACACAGGCCGCTATCATG
GAGAAGCTGGTGGCTTACTCATCCGATCAGGCACACTCCTCAGTGGAAAGAGCTGGGTTA
ATTGGTGGAGTGAAATTAAAAGCCATCCCCTCAGATGGCAACTTCGCCATGCGTGCGTCT
GCCCTGCAGGAAGCCCTGGAGAGAGACAAAGCGGCTGGCCTGATTCCTTTCTTTATGGTT
GCCACCCTGGGGACCACAACATGCTGCTCCTTTGACAATCTCTTAGAAGTCGGTCCTATC
TGCAACAAGGAAGACATATGGCTGCACGTTGATGCAGCCTACGCAGGCAGTGCATTCATC
TGCCCTGAGTTCCGGCACCTTCTGAATGGAGTGGAGTTTGCAGATTCATTCAACTTTAAT
CCCCACAAATGGCTATTGGTGAATTTTGACTGTTCTGCCATGTGGGTGAAAAAGAGAACA
GACTTAACGGGAGCCTTTAGACTGGACCCCACTTACCTGAAGCACAGCCATCAGGATTCA
GGGCTTATCACTGACTACCGGCATTGGCAGATACCACTGGGCAGAAGATTTCGCTCTTTG
AAAATGTGGTTTGTATTTAGGATGTATGGAGTCAAAGGACTGCAGGCTTATATCCGCAAG
CATGTCCAGCTGTCCCATGAGTTTGAGTCACTGGTGCGCCAGGATCCCCGCTTTGAAATC
TGTGTGGAAGTCATTCTGGGGCTTGTCTGCTTTCGGCTAAAGGGTTCCAACAAAGTGAAT
GAAGCTCTTCTGCAAAGAATAAACAGTGCCAAAAAAATCCACTTGGTTCCATGTCACCTC
AGGGACAAGTTTGTCCTGCGCTTTGCCATCTGTTCTCGCACGGTGGAATCTGCCCATGTG
CAGCGGGCCTGGGAACACATCAAAGAGCTGGCGGCCGACGTGCTGCGAGCAGAGAGGGAG
TAG
|
| Enzyme 7 GenBank Gene ID |
M76180  |
| Enzyme 7 GeneCard ID |
DDC  |
| Enzyme 7 GenAtlas ID |
DDC  |
| Enzyme 7 HGNC ID |
HGNC:2719  |
| Enzyme 7 Chromosome Location |
7 |
| Enzyme 7 Locus |
7p12.2 |
| Enzyme 7 SNPs |
SNPJam Report  |
| Enzyme 7 General References |
- Ichinose H, Kurosawa Y, Titani K, Fujita K, Nagatsu T: Isolation and characterization of a cDNA clone encoding human aromatic L-amino acid decarboxylase. Biochem Biophys Res Commun. 1989 Nov 15;164(3):1024-30. [PubMed
]
- Scherer LJ, McPherson JD, Wasmuth JJ, Marsh JL: Human dopa decarboxylase: localization to human chromosome 7p11 and characterization of hepatic cDNAs. Genomics. 1992 Jun;13(2):469-71. [PubMed
]
- Sumi-Ichinose C, Ichinose H, Takahashi E, Hori T, Nagatsu T: Molecular cloning of genomic DNA and chromosomal assignment of the gene for human aromatic L-amino acid decarboxylase, the enzyme for catecholamine and serotonin biosynthesis. Biochemistry. 1992 Mar 3;31(8):2229-38. [PubMed
]
- Hillier LW, Fulton RS, Fulton LA, Graves TA, Pepin KH, Wagner-McPherson C, Layman D, Maas J, Jaeger S, Walker R, Wylie K, Sekhon M, Becker MC, O'Laughlin MD, Schaller ME, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Cordes M, Du H, Sun H, Edwards J, Bradshaw-Cordum H, Ali J, Andrews S, Isak A, Vanbrunt A, Nguyen C, Du F, Lamar B, Courtney L, Kalicki J, Ozersky P, Bielicki L, Scott K, Holmes A, Harkins R, Harris A, Strong CM, Hou S, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Leonard S, Rohlfing T, Rock SM, Tin-Wollam AM, Abbott A, Minx P, Maupin R, Strowmatt C, Latreille P, Miller N, Johnson D, Murray J, Woessner JP, Wendl MC, Yang SP, Schultz BR, Wallis JW, Spieth J, Bieri TA, Nelson JO, Berkowicz N, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Bedell JA, Mardis ER, Clifton SW, Chissoe SL, Marra MA, Raymond C, Haugen E, Gillett W, Zhou Y, James R, Phelps K, Iadanoto S, Bubb K, Simms E, Levy R, Clendenning J, Kaul R, Kent WJ, Furey TS, Baertsch RA, Brent MR, Keibler E, Flicek P, Bork P, Suyama M, Bailey JA, Portnoy ME, Torrents D, Chinwalla AT, Gish WR, Eddy SR, McPherson JD, Olson MV, Eichler EE, Green ED, Waterston RH, Wilson RK: The DNA sequence of human chromosome 7. Nature. 2003 Jul 10;424(6945):157-64. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Le Van Thai A, Coste E, Allen JM, Palmiter RD, Weber MJ: Identification of a neuron-specific promoter of human aromatic L-amino acid decarboxylase gene. Brain Res Mol Brain Res. 1993 Mar;17(3-4):227-38. [PubMed
]
- Craig SP, Thai AL, Weber M, Craig IW: Localisation of the gene for human aromatic L-amino acid decarboxylase (DDC) to chromosome 7p13-->p11 by in situ hybridisation. Cytogenet Cell Genet. 1992;61(2):114-6. [PubMed
]
- Cargill M, Altshuler D, Ireland J, Sklar P, Ardlie K, Patil N, Shaw N, Lane CR, Lim EP, Kalyanaraman N, Nemesh J, Ziaugra L, Friedland L, Rolfe A, Warrington J, Lipshutz R, Daley GQ, Lander ES: Characterization of single-nucleotide polymorphisms in coding regions of human genes. Nat Genet. 1999 Jul;22(3):231-8. [PubMed
]
- Chang YT, Sharma R, Marsh JL, McPherson JD, Bedell JA, Knust A, Brautigam C, Hoffmann GF, Hyland K: Levodopa-responsive aromatic L-amino acid decarboxylase deficiency. Ann Neurol. 2004 Mar;55(3):435-8. [PubMed
]
- Pons R, Ford B, Chiriboga CA, Clayton PT, Hinton V, Hyland K, Sharma R, De Vivo DC: Aromatic L-amino acid decarboxylase deficiency: clinical features, treatment, and prognosis. Neurology. 2004 Apr 13;62(7):1058-65. [PubMed
]
|
| Enzyme 7 Metabolite References |
Not Available |
|
Enzyme 8
[top]
|
| Enzyme 8 ID |
5515 |
| Enzyme 8 Name |
Aspartate aminotransferase, cytoplasmic |
| Enzyme 8 Synonyms |
- Glutamate oxaloacetate transaminase 1
- Transaminase A
|
| Enzyme 8 Gene Name |
GOT1 |
| Enzyme 8 Protein Sequence |
>Aspartate aminotransferase, cytoplasmic
MAPPSVFAEVPQAQPVLVFKLTADFREDPDPRKVNLGVGAYRTDDCHPWVLPVVKKVEQK
IANDNSLNHEYLPILGLAEFRSCASRLALGDDSPALKEKRVGGVQSLGGTGALRIGADFL
ARWYNGTNNKNTPVYVSSPTWENHNAVFSAAGFKDIRSYRYWDAEKRGLDLQGFLNDLEN
APEFSIVVLHACAHNPTGIDPTPEQWKQIASVMKHRFLFPFFDSAYQGFASGNLERDAWA
IRYFVSEGFEFFCAQSFSKNFGLYNERVGNLTVVGKEPESILQVLSQMEKIVRITWSNPP
AQGARIVASTLSNPELFEEWTGNVKTMADRILTMRSELRARLEALKTPGTWNHITDQIGM
FSFTGLNPKQVEYLVNEKHIYLLPSGRINVSGLTTKNLDYVATSIHEAVTKIQ
|
| Enzyme 8 Number of Residues |
413 |
| Enzyme 8 Molecular Weight |
46247.1 |
| Enzyme 8 Theoretical pI |
7.01 |
| Enzyme 8 GO Classification |
| Function |
- binding
- catalytic activity
- cofactor binding
- pyridoxal phosphate binding
- transaminase activity
- transferase activity
- transferase activity, transferring nitrogenous groups
|
| Process |
- biosynthetic process
- cellular amino acid and derivative metabolic process
- cellular amino acid metabolic process
- cellular metabolic process
- metabolic process
|
| Component |
| — |
|
| Enzyme 8 General Function |
Involved in transferase activity, transferring nitrogenous groups |
| Enzyme 8 Specific Function |
Plays a key role in amino acid metabolism |
| Enzyme 8 Pathways |
|
| Enzyme 8 Reactions |
- L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate [RN:R00355]
|
| Enzyme 8 Pfam Domain Function |
|
| Enzyme 8 Signals |
|
| Enzyme 8 Transmembrane Regions |
|
| Enzyme 8 Essentiality |
Not Available |
| Enzyme 8 GenBank ID Protein |
Not Available |
| Enzyme 8 UniProtKB/Swiss-Prot ID |
P17174  |
| Enzyme 8 UniProtKB/Swiss-Prot Entry Name |
AATC_HUMAN  |
| Enzyme 8 PDB ID |
1AJS  |
| Enzyme 8 PDB File |
Show |
| Enzyme 8 3D Structure |
|
| Enzyme 8 Cellular Location |
Not Available |
| Enzyme 8 Gene Sequence |
>1242 bp
ATGGCACCTCCGTCAGTCTTTGCCGAGGTTCCGCAGGCCCAGCCTGTCCTGGTCTTCAAG
CTCACTGCCGACTTCAGGGAGGATCCGGACCCCCGCAAGGTCAACCTGGGAGTGGGAGCA
TATCGCACGGATGACTGCCATCCCTGGGTTTTGCCAGTAGTGAAGAAAGTGGAGCAGAAG
ATTGCTAATGACAATAGCCTAAATCACGAGTATCTGCCAATCCTGGGCCTGGCTGAGTTC
CGGAGCTGTGCTTCTCGTCTTGCCCTTGGGGATGACAGCCCAGCACTCAAGGAGAAGCGG
GTAGGAGGTGTGCAATCTTTGGGGGGAACAGGTGCACTTCGAATTGGAGCTGATTTCTTA
GCGCGTTGGTACAATGGAACAAACAACAAGAACACACCTGTCTATGTGTCCTCACCAACC
TGGGAGAATCACAATGCTGTGTTTTCCGCTGCTGGTTTTAAAGACATTCGGTCCTATCGC
TACTGGGATGCAGAGAAGAGAGGATTGGACCTCCAGGGCTTCCTGAATGATCTGGAGAAT
GCTCCTGAGTTCTCCATTGTTGTCCTCCACGCCTGTGCACACAACCCAACTGGGATTGAC
CCAACTCCGGAGCAGTGGAAGCAGATTGCTTCTGTCATGAAGCACCGGTTTCTGTTCCCC
TTCTTTGACTCAGCCTATCAGGGCTTCGCATCTGGAAACCTGGAGAGAGATGCCTGGGCC
ATTCGCTATTTTGTGTCTGAAGGCTTCGAGTTCTTCTGTGCCCAGTCCTTCTCCAAGAAC
TTCGGGCTCTACAATGAGAGAGTCGGGAATCTGACTGTGGTTGGAAAAGAACCTGAGAGC
ATCCTGCAAGTCCTTTCCCAGATGGAGAAGATCGTGCGGATTACTTGGTCCAATCCCCCC
GCCCAGGGAGCACGAATTGTGGCCAGCACCCTCTCTAACCCTGAGCTCTTTGAGGAATGG
ACAGGTAATGTGAAGACAATGGCTGACCGGATTCTGACCATGAGATCTGAACTCAGGGCA
CGACTAGAAGCCCTCAAAACCCCTGGGACCTGGAACCACATCACTGATCAAATTGGCATG
TTCAGCTTCACTGGGTTGAACCCCAAGCAGGTTGAGTATCTGGTCAATGAAAAGCACATC
TACCTGCTGCCAAGTGGTCGAATCAACGTGAGTGGCTTAACCACCAAAAATCTAGATTAC
GTGGCCACCTCCATCCATGAAGCAGTCACCAAAATCCAGTGA
|
| Enzyme 8 GenBank Gene ID |
M37400  |
| Enzyme 8 GeneCard ID |
GOT1  |
| Enzyme 8 GenAtlas ID |
GOT1  |
| Enzyme 8 HGNC ID |
HGNC:4432  |
| Enzyme 8 Chromosome Location |
1 |
| Enzyme 8 Locus |
10q24.1-q25.1 |
| Enzyme 8 SNPs |
SNPJam Report  |
| Enzyme 8 General References |
- Bousquet-Lemercier B, Pol S, Pave-Preux M, Hanoune J, Barouki R: Properties of human liver cytosolic aspartate aminotransferase mRNAs generated by alternative polyadenylation site selection. Biochemistry. 1990 Jun 5;29(22):5293-9. [PubMed
]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
- Deloukas P, Earthrowl ME, Grafham DV, Rubenfield M, French L, Steward CA, Sims SK, Jones MC, Searle S, Scott C, Howe K, Hunt SE, Andrews TD, Gilbert JG, Swarbreck D, Ashurst JL, Taylor A, Battles J, Bird CP, Ainscough R, Almeida JP, Ashwell RI, Ambrose KD, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Bates K, Beasley H, Bray-Allen S, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Cahill P, Camire D, Carter NP, Chapman JC, Clark SY, Clarke G, Clee CM, Clegg S, Corby N, Coulson A, Dhami P, Dutta I, Dunn M, Faulkner L, Frankish A, Frankland JA, Garner P, Garnett J, Gribble S, Griffiths C, Grocock R, Gustafson E, Hammond S, Harley JL, Hart E, Heath PD, Ho TP, Hopkins B, Horne J, Howden PJ, Huckle E, Hynds C, Johnson C, Johnson D, Kana A, Kay M, Kimberley AM, Kershaw JK, Kokkinaki M, Laird GK, Lawlor S, Lee HM, Leongamornlert DA, Laird G, Lloyd C, Lloyd DM, Loveland J, Lovell J, McLaren S, McLay KE, McMurray A, Mashreghi-Mohammadi M, Matthews L, Milne S, Nickerson T, Nguyen M, Overton-Larty E, Palmer SA, Pearce AV, Peck AI, Pelan S, Phillimore B, Porter K, Rice CM, Rogosin A, Ross MT, Sarafidou T, Sehra HK, Shownkeen R, Skuce CD, Smith M, Standring L, Sycamore N, Tester J, Thorpe A, Torcasso W, Tracey A, Tromans A, Tsolas J, Wall M, Walsh J, Wang H, Weinstock K, West AP, Willey DL, Whitehead SL, Wilming L, Wray PW, Young L, Chen Y, Lovering RC, Moschonas NK, Siebert R, Fechtel K, Bentley D, Durbin R, Hubbard T, Doucette-Stamm L, Beck S, Smith DR, Rogers J: The DNA sequence and comparative analysis of human chromosome 10. Nature. 2004 May 27;429(6990):375-81. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Doyle JM, Schinina ME, Bossa F, Doonan S: The amino acid sequence of cytosolic aspartate aminotransferase from human liver. Biochem J. 1990 Sep 15;270(3):651-7. [PubMed
]
- Rikova K, Guo A, Zeng Q, Possemato A, Yu J, Haack H, Nardone J, Lee K, Reeves C, Li Y, Hu Y, Tan Z, Stokes M, Sullivan L, Mitchell J, Wetzel R, Macneill J, Ren JM, Yuan J, Bakalarski CE, Villen J, Kornhauser JM, Smith B, Li D, Zhou X, Gygi SP, Gu TL, Polakiewicz RD, Rush J, Comb MJ: Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer. Cell. 2007 Dec 14;131(6):1190-203. [PubMed
]
|
| Enzyme 8 Metabolite References |
Not Available |
|
Enzyme 9
[top]
|
| Enzyme 9 ID |
5516 |
| Enzyme 9 Name |
Aspartate aminotransferase, mitochondrial |
| Enzyme 9 Synonyms |
- mAspAT
- Fatty acid-binding protein
- FABP-1
- Glutamate oxaloacetate transaminase 2
- Plasma membrane-associated fatty acid-binding protein
- FABPpm
- Transaminase A
|
| Enzyme 9 Gene Name |
GOT2 |
| Enzyme 9 Protein Sequence |
>Aspartate aminotransferase, mitochondrial
MALLHSGRVLPGIAAAFHPGLAAAASARASSWWTHVEMGPPDPILGVTEAFKRDTNSKKM
NLGVGAYRDDNGKPYVLPSVRKAEAQIAAKNLDKEYLPIGGLAEFCKASAELALGENSEV
LKSGRFVTVQTISGTGALRIGASFLQRFFKFSRDVFLPKPTWGNHTPIFRDAGMQLQGYR
YYDPKTCGFDFTGAVEDISKIPEQSVLLLHACAHNPTGVDPRPEQWKEIATVVKKRNLFA
FFDMAYQGFASGDGDKDAWAVRHFIEQGINVCLCQSYAKNMGLYGERVGAFTMVCKDADE
AKRVESQLKILIRPMYSNPPLNGARIAAAILNTPDLRKQWLQEVKVMADRIIGMRTQLVS
NLKKEGSTHNWQHITDQIGMFCFTGLKPEQVERLIKEFSIYMTKDGRISVAGVTSSNVGY
LAHAIHQVTK
|
| Enzyme 9 Number of Residues |
430 |
| Enzyme 9 Molecular Weight |
47517.3 |
| Enzyme 9 Theoretical pI |
9.38 |
| Enzyme 9 GO Classification |
| Function |
- binding
- catalytic activity
- cofactor binding
- pyridoxal phosphate binding
- transaminase activity
- transferase activity
- transferase activity, transferring nitrogenous groups
|
| Process |
- biosynthetic process
- cellular amino acid and derivative metabolic process
- cellular amino acid metabolic process
- cellular metabolic process
- metabolic process
|
| Component |
| — |
|
| Enzyme 9 General Function |
Involved in transferase activity, transferring nitrogenous groups |
| Enzyme 9 Specific Function |
Plays a key role in amino acid metabolism. Important for metabolite exchange between mitochondria and cytosol. Facilitates cellular uptake of long-chain free fatty acids |
| Enzyme 9 Pathways |
|
| Enzyme 9 Reactions |
- L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate [RN:R00355]
|
| Enzyme 9 Pfam Domain Function |
|
| Enzyme 9 Signals |
|
| Enzyme 9 Transmembrane Regions |
|
| Enzyme 9 Essentiality |
Not Available |
| Enzyme 9 GenBank ID Protein |
62898103  |
| Enzyme 9 UniProtKB/Swiss-Prot ID |
P00505  |
| Enzyme 9 UniProtKB/Swiss-Prot Entry Name |
AATM_HUMAN  |
| Enzyme 9 PDB ID |
Not Available |
| Enzyme 9 Cellular Location |
Not Available |
| Enzyme 9 Gene Sequence |
>1293 bp
ATGGCCCTGCTGCATTCCGGCCGCGTCCTCCCCGGGATCGCCGCCGCCTTCCACCCGGGC
CTCGCCGCCGCGGCCTCTGCCAGAGCCAGCTCCTGGTGGACCCATGTGGAAATGGGACCT
CCAGATCCCATTCTGGGAGTCACTGAAGCCTTTAAGAGGGACACCAATAGCAAAAAGATG
AATCTGGGAGTTGGTGCCTACCGGGATGATAATGGAAAGCCTTACGTTCTGCCTAGCGTC
CGCAAGGCAGAGGCCCAGATTGCCGCAAAAAATTTGGACAAGGAATACCTGCCCATTGGG
GGACTGGCTGAATTTTGCAAGGCATCTGCAGAACTAGCCCTGGGTGAGAACAGCGAAGTC
TTGAAGAGTGGCCGGTTTGTCACTGTGCAGACCATTTCTGGAACTGGAGCCTTAAGGATC
GGAGCCAGTTTTCTGCAAAGATTTTTTAAGTTCAGCCGAGATGTCTTTCTGCCCAAACCA
ACCTGGGGAAACCACACACCCATCTTCAGGGATGCTGGCATGCAGCTACAAGGTTATCGG
TATTATGACCCCAAGACTTGCGGTTTTGACTTCACAGGCGCTGTGGAGGATATTTCAAAA
ATACCAGAGCAGAGTGTTCTTCTTCTGCATGCCTGCGCCCACAATCCCACGGGAGTGGAC
CCGCGTCCGGAACAGTGGAAGGAAATAGCAACAGTGGTGAAGAAAAGGAATCTCTTTGCG
TTCTTTGACATGGCCTACCAAGGCTTTGCCAGTGGTGATGGTGATAAGGATACCTGGGCT
GTGCGCCACTTCATCGAACAGGGCATTAATGTTTGCCTCTGCCAATCATATGCCAAGAAC
ATGGGCTTATATGGTGAGCGTGTAGGAGCCTTCACTATGGTCTGCAAAGATGCGGATGAA
GCCAAAAGGGTAGAGTCACAGTTGAAGATCTTGATCCGTCCCATGTATTCCAACCCTCCC
CTCAATGGGGCCCGGATTGCTGCTGCCATTCTGAACACCCCAGATTTGCGAAAACAATGG
CTGCAAGAAGTGAAAGTCATGGCTGACCGCATCATTGGCATGCGGACTCAACTGGTCTCC
AACCTCAAGAAGGAGGGTTCCACCCACAATTGGCAACACATCACCGACCAAATTGGCATG
TTCTGTTTCACAGGGCTAAAGCCTGAACAGGTGGAGCGGCTGATCAAGGAGTTCTCCATC
TACATGACAAAAGATGGCCGCATCTCTGTGGCAGGGGTCACCTCCAGCAACGTGGGCTAC
CTTGCCCATGCCATTCACCAGGTCACCAAGTAA
|
| Enzyme 9 GenBank Gene ID |
AK223271  |
| Enzyme 9 GeneCard ID |
GOT2  |
| Enzyme 9 GenAtlas ID |
GOT2  |
| Enzyme 9 HGNC ID |
HGNC:4433  |
| Enzyme 9 Chromosome Location |
1 |
| Enzyme 9 Locus |
16q21 |
| Enzyme 9 SNPs |
SNPJam Report  |
| Enzyme 9 General References |
- Pol S, Bousquet-Lemercier B, Pave-Preux M, Pawlak A, Nalpas B, Berthelot P, Hanoune J, Barouki R: Nucleotide sequence and tissue distribution of the human mitochondrial aspartate aminotransferase mRNA. Biochem Biophys Res Commun. 1988 Dec 30;157(3):1309-15. [PubMed
]
- Martin J, Han C, Gordon LA, Terry A, Prabhakar S, She X, Xie G, Hellsten U, Chan YM, Altherr M, Couronne O, Aerts A, Bajorek E, Black S, Blumer H, Branscomb E, Brown NC, Bruno WJ, Buckingham JM, Callen DF, Campbell CS, Campbell ML, Campbell EW, Caoile C, Challacombe JF, Chasteen LA, Chertkov O, Chi HC, Christensen M, Clark LM, Cohn JD, Denys M, Detter JC, Dickson M, Dimitrijevic-Bussod M, Escobar J, Fawcett JJ, Flowers D, Fotopulos D, Glavina T, Gomez M, Gonzales E, Goodstein D, Goodwin LA, Grady DL, Grigoriev I, Groza M, Hammon N, Hawkins T, Haydu L, Hildebrand CE, Huang W, Israni S, Jett J, Jewett PB, Kadner K, Kimball H, Kobayashi A, Krawczyk MC, Leyba T, Longmire JL, Lopez F, Lou Y, Lowry S, Ludeman T, Manohar CF, Mark GA, McMurray KL, Meincke LJ, Morgan J, Moyzis RK, Mundt MO, Munk AC, Nandkeshwar RD, Pitluck S, Pollard M, Predki P, Parson-Quintana B, Ramirez L, Rash S, Retterer J, Ricke DO, Robinson DL, Rodriguez A, Salamov A, Saunders EH, Scott D, Shough T, Stallings RL, Stalvey M, Sutherland RD, Tapia R, Tesmer JG, Thayer N, Thompson LS, Tice H, Torney DC, Tran-Gyamfi M, Tsai M, Ulanovsky LE, Ustaszewska A, Vo N, White PS, Williams AL, Wills PL, Wu JR, Wu K, Yang J, Dejong P, Bruce D, Doggett NA, Deaven L, Schmutz J, Grimwood J, Richardson P, Rokhsar DS, Eichler EE, Gilna P, Lucas SM, Myers RM, Rubin EM, Pennacchio LA: The sequence and analysis of duplication-rich human chromosome 16. Nature. 2004 Dec 23;432(7020):988-94. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Martini F, Angelaccio S, Barra D, Pascarella S, Maras B, Doonan S, Bossa F: The primary structure of mitochondrial aspartate aminotransferase from human heart. Biochim Biophys Acta. 1985 Nov 8;832(1):46-51. [PubMed
]
- Zhou SL, Gordon RE, Bradbury M, Stump D, Kiang CL, Berk PD: Ethanol up-regulates fatty acid uptake and plasma membrane expression and export of mitochondrial aspartate aminotransferase in HepG2 cells. Hepatology. 1998 Apr;27(4):1064-74. [PubMed
]
- Amanchy R, Kalume DE, Iwahori A, Zhong J, Pandey A: Phosphoproteome analysis of HeLa cells using stable isotope labeling with amino acids in cell culture (SILAC). J Proteome Res. 2005 Sep-Oct;4(5):1661-71. [PubMed
]
- Rikova K, Guo A, Zeng Q, Possemato A, Yu J, Haack H, Nardone J, Lee K, Reeves C, Li Y, Hu Y, Tan Z, Stokes M, Sullivan L, Mitchell J, Wetzel R, Macneill J, Ren JM, Yuan J, Bakalarski CE, Villen J, Kornhauser JM, Smith B, Li D, Zhou X, Gygi SP, Gu TL, Polakiewicz RD, Rush J, Comb MJ: Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer. Cell. 2007 Dec 14;131(6):1190-203. [PubMed
]
- Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed
]
|
| Enzyme 9 Metabolite References |
Not Available |
|
Enzyme 10
[top]
|
| Enzyme 10 ID |
5536 |
| Enzyme 10 Name |
Branched-chain-amino-acid aminotransferase, cytosolic |
| Enzyme 10 Synonyms |
- BCAT(c)
- Protein ECA39
|
| Enzyme 10 Gene Name |
BCAT1 |
| Enzyme 10 Protein Sequence |
>Branched-chain-amino-acid aminotransferase, cytosolic
MKDCSNGCSAECTGEGGSKEVVGTFKAKDLIVTPATILKEKPDPNNLVFGTVFTDHMLTV
EWSSEFGWEKPHIKPLQNLSLHPGSSALHYAVELFEGLKAFRGVDNKIRLFQPNLNMDRM
YRSAVRATLPVFDKEELLECIQQLVKLDQEWVPYSTSASLYIRPTFIGTEPSLGVKKPTK
ALLFVLLSPVGPYFSSGTFNPVSLWANPKYVRAWKGGTGDCKMGGNYGSSLFAQCEAVDN
GCQQVLWLYGEDHQITEVGTMNLFLYWINEDGEEELATPPLDGIILPGVTRRCILDLAHQ
WGEFKVSERYLTMDDLTTALEGNRVREMFGSGTACVVCPVSDILYKGETIHIPTMENGPK
LASRILSKLTDIQYGREESDWTIVLS
|
| Enzyme 10 Number of Residues |
386 |
| Enzyme 10 Molecular Weight |
42965.8 |
| Enzyme 10 Theoretical pI |
4.95 |
| Enzyme 10 GO Classification |
| Function |
- branched-chain-amino-acid transaminase activity
- catalytic activity
- transaminase activity
- transferase activity
- transferase activity, transferring nitrogenous groups
|
| Process |
- branched chain family amino acid metabolic process
- cellular amino acid and derivative metabolic process
- cellular amino acid metabolic process
- cellular metabolic process
- metabolic process
|
| Component |
| — |
|
| Enzyme 10 General Function |
Involved in catalytic activity |
| Enzyme 10 Specific Function |
Catalyzes the first reaction in the catabolism of the essential branched chain amino acids leucine, isoleucine, and valine |
| Enzyme 10 Pathways |
- Pantothenate and CoA Biosynthesis (map00770
)
- Valine, Leucine and Isoleucine Degradation (map00280
)
|
| Enzyme 10 Reactions |
- L-leucine + 2-oxoglutarate = 4-methyl-2-oxopentanoate + L-glutamate [RN:R01090]
|
| Enzyme 10 Pfam Domain Function |
|
| Enzyme 10 Signals |
|
| Enzyme 10 Transmembrane Regions |
|
| Enzyme 10 Essentiality |
Not Available |
| Enzyme 10 GenBank ID Protein |
38176287  |
| Enzyme 10 UniProtKB/Swiss-Prot ID |
P54687  |
| Enzyme 10 UniProtKB/Swiss-Prot Entry Name |
BCAT1_HUMAN  |
| Enzyme 10 PDB ID |
Not Available |
| Enzyme 10 Cellular Location |
Not Available |
| Enzyme 10 Gene Sequence |
>1161 bp
ATGAAGGATTGCAGTAACGGATGCTCCGCAGAGTGTACCGGAGAAGGAGGATCAAAAGAG
GTGGTGGGGACTTTTAAGGCTAAAGACCTAATAGTCACACCAGCTACCATTTTAAAGGAA
AAACCAGACCCCAATAATCTGGTTTTTGGAACTGTGTTCACGGATCATATGCTGACGGTG
GAGTGGTCCTCAGAGTTTGGATGGGAGAAACCTCATATCAAGCCTCTTCAGAACCTGTCA
TTGCACCCTGGCTCATCAGCTTTGCACTATGCAGTGGAATTATTTGAAGGATTGAAGGCA
TTTCGAGGAGTAGATAATAAAATTCGACTGTTTCAGCCAAACCTCAACATGGATAGAATG
TATCGCTCTGCTGTGAGGGCAACTCTGCCGGTATTTGACAAAGAAGAGCTCTTAGAGTGT
ATTCAACAGCTTGTGAAATTGGATCAAGAATGGGTCCCATATTCAACATCTGCTAGTCTG
TATATTCGTCCTACATTCATTGGAACTGAGCCTTCTCTTGGAGTCAAGAAGCCTACCAAA
GCCCTGCTCTTTGTACTCTTGAGCCCAGTGGGACCTTATTTTTCAAGTGGAACCTTTAAT
CCAGTGTCCCTGTGGGCCAATCCCAAGTATGTAAGAGCCTGGAAAGGTGGAACTGGGGAC
TGCAAGATGGGAGGGAATTACGGCTCATCTCTTTTTGCCCAATGTGAAGCAGTAGATAAT
GGGTGTCAGCAGGTCCTGTGGCTCTATGGAGAGGACCATCAGATCACTGAAGTGGGAACT
ATGAATCTTTTTCTTTACTGGATAAATGAAGATGGAGAAGAAGAACTGGCAACTCCTCCA
CTAGATGGCATCATTCTTCCAGGAGTGACAAGGCGGTGCATTCTGGACCTGGCACATCAG
TGGGGTGAATTTAAGGTGTCAGAGAGATACCTCACCATGGATGACTTGACAACAGCCCTG
GAGGGGAACAGAGTGAGAGAGATGTTTGGCTCTGGTACAGCCTGTGTTGTTTGCCCAGTT
TCTGATATACTGTACAAAGGCGAGACAATACACATTCCAACTATGGAGAATGGTCCTAAG
CTGGCAAGCCGCATCTTGAGCAAATTAACTGATATCCAGTATGGAAGAGAAGAGAGCGAC
TGGACAATTGTGCTATCCTGA
|
| Enzyme 10 GenBank Gene ID |
NM_005504.6  |
| Enzyme 10 GeneCard ID |
BCAT1  |
| Enzyme 10 GenAtlas ID |
BCAT1  |
| Enzyme 10 HGNC ID |
HGNC:976  |
| Enzyme 10 Chromosome Location |
1 |
| Enzyme 10 Locus |
12p12.1 |
| Enzyme 10 SNPs |
SNPJam Report  |
| Enzyme 10 General References |
- Schuldiner O, Eden A, Ben-Yosef T, Yanuka O, Simchen G, Benvenisty N: ECA39, a conserved gene regulated by c-Myc in mice, is involved in G1/S cell cycle regulation in yeast. Proc Natl Acad Sci U S A. 1996 Jul 9;93(14):7143-8. [PubMed
]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
- Scherer SE, Muzny DM, Buhay CJ, Chen R, Cree A, Ding Y, Dugan-Rocha S, Gill R, Gunaratne P, Harris RA, Hawes AC, Hernandez J, Hodgson AV, Hume J, Jackson A, Khan ZM, Kovar-Smith C, Lewis LR, Lozado RJ, Metzker ML, Milosavljevic A, Miner GR, Montgomery KT, Morgan MB, Nazareth LV, Scott G, Sodergren E, Song XZ, Steffen D, Lovering RC, Wheeler DA, Worley KC, Yuan Y, Zhang Z, Adams CQ, Ansari-Lari MA, Ayele M, Brown MJ, Chen G, Chen Z, Clerc-Blankenburg KP, Davis C, Delgado O, Dinh HH, Draper H, Gonzalez-Garay ML, Havlak P, Jackson LR, Jacob LS, Kelly SH, Li L, Li Z, Liu J, Liu W, Lu J, Maheshwari M, Nguyen BV, Okwuonu GO, Pasternak S, Perez LM, Plopper FJ, Santibanez J, Shen H, Tabor PE, Verduzco D, Waldron L, Wang Q, Williams GA, Zhang J, Zhou J, Allen CC, Amin AG, Anyalebechi V, Bailey M, Barbaria JA, Bimage KE, Bryant NP, Burch PE, Burkett CE, Burrell KL, Calderon E, Cardenas V, Carter K, Casias K, Cavazos I, Cavazos SR, Ceasar H, Chacko J, Chan SN, Chavez D, Christopoulos C, Chu J, Cockrell R, Cox CD, Dang M, Dathorne SR, David R, Davis CM, Davy-Carroll L, Deshazo DR, Donlin JE, D'Souza L, Eaves KA, Egan A, Emery-Cohen AJ, Escotto M, Flagg N, Forbes LD, Gabisi AM, Garza M, Hamilton C, Henderson N, Hernandez O, Hines S, Hogues ME, Huang M, Idlebird DG, Johnson R, Jolivet A, Jones S, Kagan R, King LM, Leal B, Lebow H, Lee S, LeVan JM, Lewis LC, London P, Lorensuhewa LM, Loulseged H, Lovett DA, Lucier A, Lucier RL, Ma J, Madu RC, Mapua P, Martindale AD, Martinez E, Massey E, Mawhiney S, Meador MG, Mendez S, Mercado C, Mercado IC, Merritt CE, Miner ZL, Minja E, Mitchell T, Mohabbat F, Mohabbat K, Montgomery B, Moore N, Morris S, Munidasa M, Ngo RN, Nguyen NB, Nickerson E, Nwaokelemeh OO, Nwokenkwo S, Obregon M, Oguh M, Oragunye N, Oviedo RJ, Parish BJ, Parker DN, Parrish J, Parks KL, Paul HA, Payton BA, Perez A, Perrin W, Pickens A, Primus EL, Pu LL, Puazo M, Quiles MM, Quiroz JB, Rabata D, Reeves K, Ruiz SJ, Shao H, Sisson I, Sonaike T, Sorelle RP, Sutton AE, Svatek AF, Svetz LA, Tamerisa KS, Taylor TR, Teague B, Thomas N, Thorn RD, Trejos ZY, Trevino BK, Ukegbu ON, Urban JB, Vasquez LI, Vera VA, Villasana DM, Wang L, Ward-Moore S, Warren JT, Wei X, White F, Williamson AL, Wleczyk R, Wooden HS, Wooden SH, Yen J, Yoon L, Yoon V, Zorrilla SE, Nelson D, Kucherlapati R, Weinstock G, Gibbs RA: The finished DNA sequence of human chromosome 12. Nature. 2006 Mar 16;440(7082):346-51. [PubMed
]
- Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed
]
- Goto M, Miyahara I, Hirotsu K, Conway M, Yennawar N, Islam MM, Hutson SM: Structural determinants for branched-chain aminotransferase isozyme-specific inhibition by the anticonvulsant drug gabapentin. J Biol Chem. 2005 Nov 4;280(44):37246-56. Epub 2005 Sep 1. [PubMed
]
|
| Enzyme 10 Metabolite References |
Not Available |
|
Enzyme 11
[top]
|
| Enzyme 11 ID |
5561 |
| Enzyme 11 Name |
Kynureninase |
| Enzyme 11 Synonyms |
- L-kynurenine hydrolase
|
| Enzyme 11 Gene Name |
KYNU |
| Enzyme 11 Protein Sequence |
>Kynureninase
MEPSSLELPADTVQRIAAELKCHPTDERVALHLDEEDKLRHFRECFYIPKIQDLPPVDLS
LVNKDENAIYFLGNSLGLQPKMVKTYLEEELDKWAKIAAYGHEVGKRPWITGDESIVGLM
KDIVGANEKEIALMNALTVNLHLLMLSFFKPTPKRYKILLEAKAFPSDHYAIESQLQLHG
LNIEESMRMIKPREGEETLRIEDILEVIEKEGDSIAVILFSGVHFYTGQHFNIPAITKAG
QAKGCYVGFDLAHAVGNVELYLHDWGVDFACWCSYKYLNAGAGGIAGAFIHEKHAHTIKP
ALVGWFGHELSTRFKMDNKLQLIPGVCGFRISNPPILLVCSLHASLEIFKQATMKALRKK
SVLLTGYLEYLIKHNYGKDKAATKKPVVNIITPSHVEERGCQLTITFSVPNKDVFQELEK
RGVVCDKRNPNGIRVAPVPLYNSFHDVYKFTNLLTSILDSAETKN
|
| Enzyme 11 Number of Residues |
465 |
| Enzyme 11 Molecular Weight |
52351.1 |
| Enzyme 11 Theoretical pI |
7.04 |
| Enzyme 11 GO Classification |
| Function |
- binding
- catalytic activity
- cofactor binding
- hydrolase activity
- hydrolase activity, acting on acid carbon-carbon bonds
- hydrolase activity, acting on acid carbon-carbon bonds, in ketonic substances
- kynureninase activity
- pyridoxal phosphate binding
|
| Process |
- NAD biosynthetic process
- cellular amino acid and derivative metabolic process
- cellular amino acid derivative metabolic process
- cellular biogenic amine metabolic process
- cellular metabolic process
- coenzyme biosynthetic process
- coenzyme metabolic process
- cofactor metabolic process
- indolalkylamine metabolic process
- metabolic process
- nicotinamide nucleotide biosynthetic process
- pyridine nucleotide biosynthetic process
- tryptophan catabolic process
- tryptophan metabolic process
|
| Component |
- cell part
- cytoplasm
- intracellular part
|
|
| Enzyme 11 General Function |
Involved in metabolic process |
| Enzyme 11 Specific Function |
Catalyzes the cleavage of L-kynurenine (L-Kyn) and L-3- hydroxykynurenine (L-3OHKyn) into anthranilic acid (AA) and 3- hydroxyanthranilic acid (3-OHAA), respectively. Has a preference for the L-3-hydroxy form. Also has cysteine-conjugate-beta-lyase activity |
| Enzyme 11 Pathways |
|
| Enzyme 11 Reactions |
- L-kynurenine + H2O = anthranilate + L-alanine [RN:R00987]
|
| Enzyme 11 Pfam Domain Function |
|
| Enzyme 11 Signals |
|
| Enzyme 11 Transmembrane Regions |
|
| Enzyme 11 Essentiality |
Not Available |
| Enzyme 11 GenBank ID Protein |
Not Available |
| Enzyme 11 UniProtKB/Swiss-Prot ID |
Q16719  |
| Enzyme 11 UniProtKB/Swiss-Prot Entry Name |
KYNU_HUMAN  |
| Enzyme 11 PDB ID |
Not Available |
| Enzyme 11 Cellular Location |
Not Available |
| Enzyme 11 Gene Sequence |
>1398 bp
ATGGAGCCTTCATCTCTTGAGCTGCCGGCTGACACAGTGCAGCGCATTGCGGCTGAACTC
AAATGCCACCCAACGGATGAGAGGGTGGCTCTCCACCTAGATGAGGAAGATAAGCTGAGG
CACTTCAGGGAGTGCTTTTATATTCCCAAAATACAGGATCTGCCTCCAGTTGATTTATCA
TTAGTGAATAAAGATGAAAATGCCATCTATTTCTTGGGAAATTCTCTTGGCCTTCAACCA
AAAATGGTTAAAACATATCTTGAAGAAGAACTAGATAAGTGGGCCAAAATAGCAGCCTAT
GGTCATGAAGTGGGGAAGCGTCCTTGGATTACAGGAGATGAGAGTATTGTAGGCCTTATG
AAGGACATTGTAGGAGCCAATGAGAAAGAAATAGCCCTAATGAATGCTTTGACTGTAAAT
TTACATCTTCTAATGTTATCATTTTTTAAGCCTACGCCAAAACGATATAAAATTCTTCTA
GAAGCCAAAGCCTTCCCTTCTGATCATTATGCTATTGAGTCACAACTACAACTTCACGGA
CTTAACATTGAAGAAAGTATGCGGATGATAAAGCCAAGAGAGGGGGAAGAAACCTTAAGA
ATAGAGGATATCCTTGAAGTAATTGAGAAGGAAGGAGACTCAATTGCAGTGATCCTGTTC
AGTGGGGTGCATTTTTACACTGGACAGCACTTTAATATTCCTGCCATCACAAAAGCTGGA
CAAGCGAAGGGTTGTTATGTTGGCTTTGATCTAGCACATGCAGTTGGAAATGTTGAACTC
TACTTACATGACTGGGGAGTTGATTTTGCCTGCTGGTGTTCCTACAAGTATTTAAATGCA
GGAGCAGGAGGAATTGCTGGTGCCTTCATTCATGAAAAGCATGCCCATACGATTAAACCT
GCATTAGTGGGATGGTTTGGCCATGAACTCAGCACCAGATTTAAGATGGATAACAAACTG
CAGTTAATCCCTGGGGTCTGTGGATTCCGAATTTCAAATCCTCCCATTTTGTTGGTCTGT
TCCTTGCATGCTAGTTTAGAGATCTTTAAGCAAGCGACAATGAAGGCATTGCGGAAAAAA
TCTGTTTTGCTAACTGGCTATCTGGAATACCTGATCAAGCATAACTATGGCAAAGATAAA
GCAGCAACCAAGAAACCAGTTGTGAACATAATTACTCCGTCTCATGTAGAGGAGCGGGGG
TGCCAGCTAACAATAACATTTTCTGTTCCAAACAAAGATGTTTTCCAAGAACTAGAAAAA
AGAGGAGTGGTTTGTGACAAGCGGAATCCAAATGGCATTCGAGTGGCTCCAGTTCCTCTC
TATAATTCTTTCCATGATGTTTATAAATTTACCAATCTGCTCACTTCTATACTTGACTCT
GCAGAAACAAAAAATTAG
|
| Enzyme 11 GenBank Gene ID |
U57721  |
| Enzyme 11 GeneCard ID |
KYNU  |
| Enzyme 11 GenAtlas ID |
KYNU  |
| Enzyme 11 HGNC ID |
HGNC:6469  |
| Enzyme 11 Chromosome Location |
2 |
| Enzyme 11 Locus |
2q22.2 |
| Enzyme 11 SNPs |
SNPJam Report  |
| Enzyme 11 General References |
- Alberati-Giani D, Buchli R, Malherbe P, Broger C, Lang G, Kohler C, Lahm HW, Cesura AM: Isolation and expression of a cDNA clone encoding human kynureninase. Eur J Biochem. 1996 Jul 15;239(2):460-8. [PubMed
]
- Toma S, Nakamura M, Tone S, Okuno E, Kido R, Breton J, Avanzi N, Cozzi L, Speciale C, Mostardini M, Gatti S, Benatti L: Cloning and recombinant expression of rat and human kynureninase. FEBS Lett. 1997 May 12;408(1):5-10. [PubMed
]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
- Walsh HA, Botting NP: Purification and biochemical characterization of some of the properties of recombinant human kynureninase. Eur J Biochem. 2002 Apr;269(8):2069-74. [PubMed
]
- Lima S, Khristoforov R, Momany C, Phillips RS: Crystal structure of Homo sapiens kynureninase. Biochemistry. 2007 Mar 13;46(10):2735-44. Epub 2007 Feb 15. [PubMed
]
- Christensen M, Duno M, Lund AM, Skovby F, Christensen E: Xanthurenic aciduria due to a mutation in KYNU encoding kynureninase. J Inherit Metab Dis. 2007 Apr;30(2):248-55. Epub 2007 Mar 1. [PubMed
]
|
| Enzyme 11 Metabolite References |
Not Available |
|
Enzyme 12
[top]
|
| Enzyme 12 ID |
5564 |
| Enzyme 12 Name |
Glucose-6-phosphate 1-dehydrogenase |
| Enzyme 12 Synonyms |
- G6PD
|
| Enzyme 12 Gene Name |
G6PD |
| Enzyme 12 Protein Sequence |
>Glucose-6-phosphate 1-dehydrogenase
MAEQVALSRTQVCGILREELFQGDAFHQSDTHIFIIMGASGDLAKKKIYPTIWWLFRDGL
LPENTFIVGYARSRLTVADIRKQSEPFFKATPEEKLKLEDFFARNSYVAGQYDDAASYQR
LNSHMNALHLGSQANRLFYLALPPTVYEAVTKNIHESCMSQIGWNRIIVEKPFGRDLQSS
DRLSNHISSLFREDQIYRIDHYLGKEMVQNLMVLRFANRIFGPIWNRDNIACVILTFKEP
FGTEGRGGYFDEFGIIRDVMQNHLLQMLCLVAMEKPASTNSDDVRDEKVKVLKCISEVQA
NNVVLGQYVGNPDGEGEATKGYLDDPTVPRGSTTATFAAVVLYVENERWDGVPFILRCGK
ALNERKAEVRLQFHDVAGDIFHQQCKRNELVIRVQPNEAVYTKMMTKKPGMFFNPEESEL
DLTYGNRYKNVKLPDAYERLILDVFCGSQMHFVRSDELREAWRIFTPLLHQIELEKPKPI
PYIYGSRGPTEADELMKRVGFQYEGTYKWVNPHKL
|
| Enzyme 12 Number of Residues |
515 |
| Enzyme 12 Molecular Weight |
59256.3 |
| Enzyme 12 Theoretical pI |
6.84 |
| Enzyme 12 GO Classification |
| Function |
- NADP or NADPH binding
- binding
- catalytic activity
- glucose-6-phosphate dehydrogenase activity
- nucleotide binding
- oxidoreductase activity
- oxidoreductase activity, acting on CH-OH group of donors
- oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
|
| Process |
- alcohol metabolic process
- glucose metabolic process
- hexose metabolic process
- metabolic process
- monosaccharide metabolic process
- oxidation reduction
- small molecule metabolic process
|
| Component |
| — |
|
| Enzyme 12 General Function |
Involved in glucose-6-phosphate dehydrogenase activity |
| Enzyme 12 Specific Function |
Produces pentose sugars for nucleic acid synthesis and main producer of NADPH reducing power |
| Enzyme 12 Pathways |
|
| Enzyme 12 Reactions |
- D-glucose 6-phosphate + NADP+ = D-glucono-1,5-lactone 6-phosphate + NADPH + H+ [RN:R00835]
|
| Enzyme 12 Pfam Domain Function |
|
| Enzyme 12 Signals |
|
| Enzyme 12 Transmembrane Regions |
|
| Enzyme 12 Essentiality |
Not Available |
| Enzyme 12 GenBank ID Protein |
31543  |
| Enzyme 12 UniProtKB/Swiss-Prot ID |
P11413  |
| Enzyme 12 UniProtKB/Swiss-Prot Entry Name |
G6PD_HUMAN  |
| Enzyme 12 PDB ID |
1QKI  |
| Enzyme 12 PDB File |
Show |
| Enzyme 12 3D Structure |
|
| Enzyme 12 Cellular Location |
Not Available |
| Enzyme 12 Gene Sequence |
>1548 bp
ATGGCAGAGCAGGTGGCCCTGAGCCGGACCCACGTGTGCGGGATCCTGCGGGAAGAGCTT
TTCCAGGGCGATGCCTTCCATCAGTCGGATACACACATATTCATCATCATGGGTGCATCG
GGTGACCTGGCCAAGAAGAAGATCTACCCCACCATCTGGTGGCTGTTCCGGGATGGCCTT
CTGCCCGAAAACACCTTCATCGTGGGCTATGCCCGTTCCCGCCTCACAGTGGCTGACATC
CGCAAACAGAGTGAGCCCTTCTTCAAGGCCACCCCAGAGGAGAAGCTCAAGCTGGAGGAC
TTCTTTGCCCGCAACTCCTATGTGGCTGGCCAGTACGATGATGCAGCCTCCTACCAGCGC
CTCAACAGCCACATGAATGCCCTCCACCTGGGGTCACAGGCCAACCGCCTCTTCTACCTG
GCCTTGCCCCCGACCGTCTACGAGGCCGTCACCAAGAACATTCACGAGTCCTGCATGAGC
CAGATAGGCTGGAACCGCATCATCGTGGAGAAGCCCTTCGGGAGGGACCTGCAGAGCTCT
GACCGGCTGTCCAACCACATCTCCTCCCTGTTCCGTGAGGACCAGATCTACCGCATCGAC
CACTACCTGGGCAAGGAGATGGTGCAGAACCTCATGGTGCTGAGATTTGCCAACAGGATC
TTCGGCCCCATCTGGAACCGGGACAACATCGCCTGCGTTATCCTCACCTTCAAGGAGCCC
TTTGGCACTGAGGGTCGCGGGGGCTATTTCGATGAATTTGGGATCATCCGGGACGTGATG
CAGAACCACCTACTGCAGATGCTGTGTCTGGTGGCCATGGAGAAGCCCGCCTCCACCAAC
TCAGATGACGTCCGTGATGAGAAGGTCAAGGTGTTGAAATGCATCTCAGAGGTGCAGGCC
AACAATGTGGTCCTGGGCCAGTACGTGGGGAACCCCGATGGAGAGGGCGAGGCCACCAAA
GGGTACCTGGACGACCCCACGGTGCCCCGCGGGTCCACCACCGCCACTTTTGCAGCCGTC
GTCCTCTATGTGGAGAATGAGAGGTGGGATGGGGTGCCCTTCATCCTGCGCTGCGGCAAG
GCCCTGAACGAGCGCAAGGCCGAGGTGAGGCTGCAGTTCCATGATGTGGCCGGCGACATC
TTCCACCAGCAGTGCAAGCGCAACGAGCTGGTGATCCGCGTGCAGCCCAACGAGGCCGTG
TACACCAAGATGATGACCAAGAAGCCGGGCATGTTCTTCAACCCCGAGGAGTCGGAGCTG
GACCTGACCTACGGCAACAGATACAAGAACGTGAAGCTCCCTGACGCCTACGAGCGCCTC
ATCCTGGACGTCTTCTGCGGGAGCCAGATGCACTTCGTGCGCAGCGACGAGCTCCGTGAG
GCCTGGCGTATTTTCACCCCACTGCTGCACCAGATTGAGCTGGAGAAGCCCAAGCCCATC
CCCTATATTTATGGCAGCCGAGGCCCCACGGAGGCAGACGAGCTGATGAAGAGAGTGGGT
TTCCAGTATGAGGGCACCTACAAGTGGGTGAACCCCCACAAGCTCTGA
|
| Enzyme 12 GenBank Gene ID |
X03674  |
| Enzyme 12 GeneCard ID |
G6PD  |
| Enzyme 12 GenAtlas ID |
G6PD  |
| Enzyme 12 HGNC ID |
HGNC:4057  |
| Enzyme 12 Chromosome Location |
Not Available |
| Enzyme 12 Locus |
Not Available |
| Enzyme 12 SNPs |
SNPJam Report  |
| Enzyme 12 General References |
- Persico MG, Viglietto G, Martini G, Toniolo D, Paonessa G, Moscatelli C, Dono R, Vulliamy T, Luzzatto L, D'Urso M: Isolation of human glucose-6-phosphate dehydrogenase (G6PD) cDNA clones: primary structure of the protein and unusual 5' non-coding region. Nucleic Acids Res. 1986 Mar 25;14(6):2511-22. [PubMed
]
- Martini G, Toniolo D, Vulliamy T, Luzzatto L, Dono R, Viglietto G, Paonessa G, D'Urso M, Persico MG: Structural analysis of the X-linked gene encoding human glucose 6-phosphate dehydrogenase. EMBO J. 1986 Aug;5(8):1849-55. [PubMed
]
- Hirono A, Beutler E: Molecular cloning and nucleotide sequence of cDNA for human glucose-6-phosphate dehydrogenase variant A(-). Proc Natl Acad Sci U S A. 1988 Jun;85(11):3951-4. [PubMed
]
- Chen EY, Cheng A, Lee A, Kuang WJ, Hillier L, Green P, Schlessinger D, Ciccodicola A, D'Urso M: Sequence of human glucose-6-phosphate dehydrogenase cloned in plasmids and a yeast artificial chromosome. Genomics. 1991 Jul;10(3):792-800. [PubMed
]
- Chen EY, Zollo M, Mazzarella R, Ciccodicola A, Chen CN, Zuo L, Heiner C, Burough F, Repetto M, Schlessinger D, D'Urso M: Long-range sequence analysis in Xq28: thirteen known and six candidate genes in 219.4 kb of high GC DNA between the RCP/GCP and G6PD loci. Hum Mol Genet. 1996 May;5(5):659-68. [PubMed
]
- Ross MT, Grafham DV, Coffey AJ, Scherer S, McLay K, Muzny D, Platzer M, Howell GR, Burrows C, Bird CP, Frankish A, Lovell FL, Howe KL, Ashurst JL, Fulton RS, Sudbrak R, Wen G, Jones MC, Hurles ME, Andrews TD, Scott CE, Searle S, Ramser J, Whittaker A, Deadman R, Carter NP, Hunt SE, Chen R, Cree A, Gunaratne P, Havlak P, Hodgson A, Metzker ML, Richards S, Scott G, Steffen D, Sodergren E, Wheeler DA, Worley KC, Ainscough R, Ambrose KD, Ansari-Lari MA, Aradhya S, Ashwell RI, Babbage AK, Bagguley CL, Ballabio A, Banerjee R, Barker GE, Barlow KF, Barrett IP, Bates KN, Beare DM, Beasley H, Beasley O, Beck A, Bethel G, Blechschmidt K, Brady N, Bray-Allen S, Bridgeman AM, Brown AJ, Brown MJ, Bonnin D, Bruford EA, Buhay C, Burch P, Burford D, Burgess J, Burrill W, Burton J, Bye JM, Carder C, Carrel L, Chako J, Chapman JC, Chavez D, Chen E, Chen G, Chen Y, Chen Z, Chinault C, Ciccodicola A, Clark SY, Clarke G, Clee CM, Clegg S, Clerc-Blankenburg K, Clifford K, Cobley V, Cole CG, Conquer JS, Corby N, Connor RE, David R, Davies J, Davis C, Davis J, Delgado O, Deshazo D, Dhami P, Ding Y, Dinh H, Dodsworth S, Draper H, Dugan-Rocha S, Dunham A, Dunn M, Durbin KJ, Dutta I, Eades T, Ellwood M, Emery-Cohen A, Errington H, Evans KL, Faulkner L, Francis F, Frankland J, Fraser AE, Galgoczy P, Gilbert J, Gill R, Glockner G, Gregory SG, Gribble S, Griffiths C, Grocock R, Gu Y, Gwilliam R, Hamilton C, Hart EA, Hawes A, Heath PD, Heitmann K, Hennig S, Hernandez J, Hinzmann B, Ho S, Hoffs M, Howden PJ, Huckle EJ, Hume J, Hunt PJ, Hunt AR, Isherwood J, Jacob L, Johnson D, Jones S, de Jong PJ, Joseph SS, Keenan S, Kelly S, Kershaw JK, Khan Z, Kioschis P, Klages S, Knights AJ, Kosiura A, Kovar-Smith C, Laird GK, Langford C, Lawlor S, Leversha M, Lewis L, Liu W, Lloyd C, Lloyd DM, Loulseged H, Loveland JE, Lovell JD, Lozado R, Lu J, Lyne R, Ma J, Maheshwari M, Matthews LH, McDowall J, McLaren S, McMurray A, Meidl P, Meitinger T, Milne S, Miner G, Mistry SL, Morgan M, Morris S, Muller I, Mullikin JC, Nguyen N, Nordsiek G, Nyakatura G, O'Dell CN, Okwuonu G, Palmer S, Pandian R, Parker D, Parrish J, Pasternak S, Patel D, Pearce AV, Pearson DM, Pelan SE, Perez L, Porter KM, Ramsey Y, Reichwald K, Rhodes S, Ridler KA, Schlessinger D, Schueler MG, Sehra HK, Shaw-Smith C, Shen H, Sheridan EM, Shownkeen R, Skuce CD, Smith ML, Sotheran EC, Steingruber HE, Steward CA, Storey R, Swann RM, Swarbreck D, Tabor PE, Taudien S, Taylor T, Teague B, Thomas K, Thorpe A, Timms K, Tracey A, Trevanion S, Tromans AC, d'Urso M, Verduzco D, Villasana D, Waldron L, Wall M, Wang Q, Warren J, Warry GL, Wei X, West A, Whitehead SL, Whiteley MN, Wilkinson JE, Willey DL, Williams G, Williams L, Williamson A, Williamson H, Wilming L, Woodmansey RL, Wray PW, Yen J, Zhang J, Zhou J, Zoghbi H, Zorilla S, Buck D, Reinhardt R, Poustka A, Rosenthal A, Lehrach H, Meindl A, Minx PJ, Hillier LW, Willard HF, Wilson RK, Waterston RH, Rice CM, Vaudin M, Coulson A, Nelson DL, Weinstock G, Sulston JE, Durbin R, Hubbard T, Gibbs RA, Beck S, Rogers J, Bentley DR: The DNA sequence of the human X chromosome. Nature. 2005 Mar 17;434(7031):325-37. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Kanno H, Huang IY, Kan YW, Yoshida A: Two structural genes on different chromosomes are required for encoding the major subunit of human red cell glucose-6-phosphate dehydrogenase. Cell. 1989 Aug 11;58(3):595-606. [PubMed
]
- Kanno H, Kondoh T, Yoshida A: 5' structure and expression of human glucose-6-phosphate dehydrogenase mRNA. DNA Cell Biol. 1993 Apr;12(3):209-15. [PubMed
]
- Toniolo D, Filippi M, Dono R, Lettieri T, Martini G: The CpG island in the 5' region of the G6PD gene of man and mouse. Gene. 1991 Jun 30;102(2):197-203. [PubMed
]
- Gevaert K, Goethals M, Martens L, Van Damme J, Staes A, Thomas GR, Vandekerckhove J: Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides. Nat Biotechnol. 2003 May;21(5):566-9. Epub 2003 Mar 31. [PubMed
]
- Chao LT, Du CS, Louie E, Zuo L, Chen E, Lubin B, Chiu DT: A to G substitution identified in exon 2 of the G6PD gene among G6PD deficient Chinese. Nucleic Acids Res. 1991 Nov 11;19(21):6056. [PubMed
]
- Saunders MA, Hammer MF, Nachman MW: Nucleotide variability at G6pd and the signature of malarial selection in humans. Genetics. 2002 Dec;162(4):1849-61. [PubMed
]
- Takizawa T, Huang IY, Ikuta T, Yoshida A: Human glucose-6-phosphate dehydrogenase: primary structure and cDNA cloning. Proc Natl Acad Sci U S A. 1986 Jun;83(12):4157-61. [PubMed
]
- Camardella L, Caruso C, Rutigliano B, Romano M, Di Prisco G, Descalzi-Cancedda F: Human erythrocyte glucose-6-phosphate dehydrogenase. Identification of a reactive lysyl residue labelled with pyridoxal 5'-phosphate. Eur J Biochem. 1988 Feb 1;171(3):485-9. [PubMed
]
- Descalzi-Cancedda F, Caruso C, Romano M, di Prisco G, Camardella L: Amino acid sequence of the carboxy-terminal end of human erythrocyte glucose-6-phosphate dehydrogenase. Biochem Biophys Res Commun. 1984 Jan 13;118(1):332-8. [PubMed
]
- Hirono A, Beutler E: Alternative splicing of human glucose-6-phosphate dehydrogenase messenger RNA in different tissues. J Clin Invest. 1989 Jan;83(1):343-6. [PubMed
]
- Camardella L, Damonte G, Carratore V, Benatti U, Tonetti M, Moneti G: Glucose 6-phosphate dehydrogenase from human erythrocytes: identification of N-acetyl-alanine at the N-terminus of the mature protein. Biochem Biophys Res Commun. 1995 Feb 6;207(1):331-8. [PubMed
]
- Zhang Y, Wolf-Yadlin A, Ross PL, Pappin DJ, Rush J, Lauffenburger DA, White FM: Time-resolved mass spectrometry of tyrosine phosphorylation sites in the epidermal growth factor receptor signaling network reveals dynamic modules. Mol Cell Proteomics. 2005 Sep;4(9):1240-50. Epub 2005 Jun 11. [PubMed
]
- Rush J, Moritz A, Lee KA, Guo A, Goss VL, Spek EJ, Zhang H, Zha XM, Polakiewicz RD, Comb MJ: Immunoaffinity profiling of tyrosine phosphorylation in cancer cells. Nat Biotechnol. 2005 Jan;23(1):94-101. Epub 2004 Dec 12. [PubMed
]
- Rikova K, Guo A, Zeng Q, Possemato A, Yu J, Haack H, Nardone J, Lee K, Reeves C, Li Y, Hu Y, Tan Z, Stokes M, Sullivan L, Mitchell J, Wetzel R, Macneill J, Ren JM, Yuan J, Bakalarski CE, Villen J, Kornhauser JM, Smith B, Li D, Zhou X, Gygi SP, Gu TL, Polakiewicz RD, Rush J, Comb MJ: Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer. Cell. 2007 Dec 14;131(6):1190-203. [PubMed
]
- Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed
]
- Heibeck TH, Ding SJ, Opresko LK, Zhao R, Schepmoes AA, Yang F, Tolmachev AV, Monroe ME, Camp DG 2nd, Smith RD, Wiley HS, Qian WJ: An extensive survey of tyrosine phosphorylation revealing new sites in human mammary epithelial cells. J Proteome Res. 2009 Aug;8(8):3852-61. [PubMed
]
- Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed
]
- Au SW, Gover S, Lam VM, Adams MJ: Human glucose-6-phosphate dehydrogenase: the crystal structure reveals a structural NADP(+) molecule and provides insights into enzyme deficiency. Structure. 2000 Mar 15;8(3):293-303. [PubMed
]
- Vulliamy T, Beutler E, Luzzatto L: Variants of glucose-6-phosphate dehydrogenase are due to missense mutations spread throughout the coding region of the gene. Hum Mutat. 1993;2(3):159-67. [PubMed
]
- Kwok CJ, Martin AC, Au SW, Lam VM: G6PDdb, an integrated database of glucose-6-phosphate dehydrogenase (G6PD) mutations. Hum Mutat. 2002 Mar;19(3):217-24. [PubMed
]
- Takizawa T, Yoneyama Y, Miwa S, Yoshida A: A single nucleotide base transition is the basis of the common human glucose-6-phosphate dehydrogenase variant A (+). Genomics. 1987 Nov;1(3):228-31. [PubMed
]
- Vulliamy TJ, D'Urso M, Battistuzzi G, Estrada M, Foulkes NS, Martini G, Calabro V, Poggi V, Giordano R, Town M, et al.: Diverse point mutations in the human glucose-6-phosphate dehydrogenase gene cause enzyme deficiency and mild or severe hemolytic anemia. Proc Natl Acad Sci U S A. 1988 Jul;85(14):5171-5. [PubMed
]
- De Vita G, Alcalay M, Sampietro M, Cappelini MD, Fiorelli G, Toniolo D: Two point mutations are responsible for G6PD polymorphism in Sardinia. Am J Hum Genet. 1989 Feb;44(2):233-40. [PubMed
]
- Beutler E, Westwood B, Prchal JT, Vaca G, Bartsocas CS, Baronciani L: New glucose-6-phosphate dehydrogenase mutations from various ethnic groups. Blood. 1992 Jul 1;80(1):255-6. [PubMed
]
- Filosa S, Calabro V, Vallone D, Poggi V, Mason P, Pagnini D, Alfinito F, Rotoli B, Martini G, Luzzatto L, et al.: Molecular basis of chronic non-spherocytic haemolytic anaemia: a new G6PD variant (393 Arg----His) with abnormal KmG6P and marked in vivo instability. Br J Haematol. 1992 Jan;80(1):111-6. [PubMed
]
- Perng LI, Chiou SS, Liu TC, Chang JG: A novel C to T substitution at nucleotide 1360 of cDNA which abolishes a natural Hha I site accounts for a new G6PD deficiency gene in Chinese. Hum Mol Genet. 1992 Jun;1(3):205. [PubMed
]
- Ahluwalia A, Corcoran CM, Vulliamy TJ, Ishwad CS, Naidu JM, Argusti A, Stevens DJ, Mason PJ, Luzzatto L: G6PD Kalyan and G6PD Kerala; two deficient variants in India caused by the same 317 Glu-->Lys mutation. Hum Mol Genet. 1992 Jun;1(3):209-10. [PubMed
]
- Nafa K, Reghis A, Osmani N, Baghli L, Benabadji M, Kaplan JC, Vulliamy TJ, Luzzatto L: G6PD Aures: a new mutation (48 Ile-->Thr) causing mild G6PD deficiency is associated with favism. Hum Mol Genet. 1993 Jan;2(1):81-2. [PubMed
]
- Hirono A, Miwa S, Fujii H, Ishida F, Yamada K, Kubota K: Molecular study of eight Japanese cases of glucose-6-phosphate dehydrogenase deficiency by nonradioisotopic single-strand conformation polymorphism analysis. Blood. 1994 Jun 1;83(11):3363-8. [PubMed
]
- Filosa S, Cai W, Galanello R, Cao A, de Mattia D, Schettini F, Martini G: A novel single-base mutation in the glucose 6-phosphate dehydrogenase gene is associated with chronic non-spherocytic haemolytic anaemia. Hum Genet. 1994 Nov;94(5):560-2. [PubMed
]
- Ganczakowski M, Town M, Bowden DK, Vulliamy TJ, Kaneko A, Clegg JB, Weatherall DJ, Luzzatto L: Multiple glucose 6-phosphate dehydrogenase-deficient variants correlate with malaria endemicity in the Vanuatu archipelago (southwestern Pacific). Am J Hum Genet. 1995 Jan;56(1):294-301. [PubMed
]
- Kaeda JS, Chhotray GP, Ranjit MR, Bautista JM, Reddy PH, Stevens D, Naidu JM, Britt RP, Vulliamy TJ, Luzzatto L, et al.: A new glucose-6-phosphate dehydrogenase variant, G6PD Orissa (44 Ala-->Gly), is the major polymorphic variant in tribal populations in India. Am J Hum Genet. 1995 Dec;57(6):1335-41. [PubMed
]
- Mason PJ, Sonati MF, MacDonald D, Lanza C, Busutil D, Town M, Corcoran CM, Kaeda JS, Stevens DJ, al-Ismail S, et al.: New glucose-6-phosphate dehydrogenase mutations associated with chronic anemia. Blood. 1995 Mar 1;85(5):1377-80. [PubMed
]
- Vlachos A, Westwood B, Lipton JM, Beutler E: G6PD Mount Sinai: a new severe hemolytic variant characterized by dual mutations at nucleotides 376G and 1159T (N126D). Hum Mutat. 1998;Suppl 1:S154-5. [PubMed
]
- Galanello R, Loi D, Sollaino C, Dessi S, Cao A, Melis MA: A new glucose 6 phosphate dehydrogenase variant G6PD Sinnai (34 G-->T). Mutations in brief no. 156. Online. Hum Mutat. 1998;12(1):72-3. [PubMed
]
- Iancovici-Kidon M, Sthoeger D, Abrahamov A, Wolach B, Beutler E, Gelbart T, Barak Y: A new exon 9 glucose-6-phosphate dehydrogenase mutation (G6PD "Rehovot") in a Jewish Ethiopian family with variable phenotypes. Blood Cells Mol Dis. 2000 Dec;26(6):567-71. [PubMed
]
- Louicharoen C, Patin E, Paul R, Nuchprayoon I, Witoonpanich B, Peerapittayamongkol C, Casademont I, Sura T, Laird NM, Singhasivanon P, Quintana-Murci L, Sakuntabhai A: Positively selected G6PD-Mahidol mutation reduces Plasmodium vivax density in Southeast Asians. Science. 2009 Dec 11;326(5959):1546-9. [PubMed
]
|
| Enzyme 12 Metabolite References |
Not Available |
|
Enzyme 13
[top]
|
| Enzyme 13 ID |
5606 |
| Enzyme 13 Name |
Glycogen phosphorylase, liver form |
| Enzyme 13 Synonyms |
Not Available |
| Enzyme 13 Gene Name |
PYGL |
| Enzyme 13 Protein Sequence |
>Glycogen phosphorylase, liver form
MAKPLTDQEKRRQISIRGIVGVENVAELKKSFNRHLHFTLVKDRNVATTRDYYFALAHTV
RDHLVGRWIRTQQHYYDKCPKRVYYLSLEFYMGRTLQNTMINLGLQNACDEAIYQLGLDI
EELEEIEEDAGLGNGGLGRLAACFLDSMATLGLAAYGYGIRYEYGIFNQKIRDGWQVEEA
DDWLRYGNPWEKSRPEFMLPVHFYGKVEHTNTGTKWIDTQVVLALPYDTPVPGYMNNTVN
TMRLWSARAPNDFNLRDFNVGDYIQAVLDRNLAENISRVLYPNDNFFEGKELRLKQEYFV
VAATLQDIIRRFKASKFGSTRGAGTVFDAFPDQVAIQLNDTHPALAIPELMRIFVDIEKL
PWSKAWELTQKTFAYTNHTVLPEALERWPVDLVEKLLPRHLEIIYEINQKHLDRIVALFP
KDVDRLRRMSLIEEEGSKRINMAHLCIVGSHAVNGVAKIHSDIVKTKVFKDFSELEPDKF
QNKTNGITPRRWLLLCNPGLAELIAEKIGEDYVKDLSQLTKLHSFLGDDVFLRELAKVKQ
ENKLKFSQFLETEYKVKINPSSMFDVQVKRIHEYKRQLLNCLHVITMYNRIKKDPKKLFV
PRTVIIGGKAAPGYHMAKMIIKLITSVADVVNNDPMVGSKLKVIFLENYRVSLAEKVIPA
TDLSEQISTAGTEASGTGNMKFMLNGALTIGTMDGANVEMAEEAGEENLFIFGMRIDDVA
ALDKKGYEAKEYYEALPELKLVIDQIDNGFFSPKQPDLFKDIINMLFYHDRFKVFADYEA
YVKCQDKVSQLYMNPKAWNTMVLKNIAASGKFSSDRTIKEYAQNIWNVEPSDLKISLSNE
SNKVNGN
|
| Enzyme 13 Number of Residues |
847 |
| Enzyme 13 Molecular Weight |
97147.8 |
| Enzyme 13 Theoretical pI |
7.17 |
| Enzyme 13 GO Classification |
| Function |
- binding
- catalytic activity
- cofactor binding
- phosphorylase activity
- pyridoxal phosphate binding
- transferase activity
- transferase activity, transferring glycosyl groups
- transferase activity, transferring hexosyl groups
|
| Process |
- carbohydrate metabolic process
- metabolic process
- primary metabolic process
|
| Component |
| — |
|
| Enzyme 13 General Function |
Involved in phosphorylase activity |
| Enzyme 13 Specific Function |
Phosphorylase is an important allosteric enzyme in carbohydrate metabolism. Enzymes from different sources differ in their regulatory mechanisms and in their natural substrates. However, all known phosphorylases share catalytic and structural properties |
| Enzyme 13 Pathways |
- Starch and Sucrose Metabolism (map00500
)
|
| Enzyme 13 Reactions |
- [(1->4)-alpha-D-glucosyl]n + phosphate = [(1->4)-alpha-D-glucosyl]n-1 + alpha-D-glucose 1-phosphate [RN:R01821 R06050]
|
| Enzyme 13 Pfam Domain Function |
|
| Enzyme 13 Signals |
|
| Enzyme 13 Transmembrane Regions |
|
| Enzyme 13 Essentiality |
Not Available |
| Enzyme 13 GenBank ID Protein |
183353  |
| Enzyme 13 UniProtKB/Swiss-Prot ID |
P06737  |
| Enzyme 13 UniProtKB/Swiss-Prot Entry Name |
PYGL_HUMAN  |
| Enzyme 13 PDB ID |
1L7X  |
| Enzyme 13 PDB File |
Show |
| Enzyme 13 3D Structure |
|
| Enzyme 13 Cellular Location |
Not Available |
| Enzyme 13 Gene Sequence |
>2544 bp
ATGGGCGAACCGCTGACAGACCAGGAGAAGCGGCGGCAGATCAGCATCCGCGGCATCGTG
GGCGTGGAGAACGTGGCAGAGCTGAAGAAGAGTTTCAACCGGCACCTGCACTTCACGCTG
GTCAAGGACCGCAACGTGGCCACCACCCGCGACTACTACTTCGCGCTGGCGCACACGGTG
CGGGACCACCTGGTGGGGCGCTGGATCCGCACGCAGCAGCACTACTACGACAAGTGCCCC
AAGAGGGAATATTACCTCTCTCTGGAATTTTACATGGGCCGAACATTACAGAACACCATG
ATCAACCTCGGTCTGCAAAATGCCTGTGATGAGGCCATTTACCAGCTTGGATTGGATATA
GAAGAGTTAGAAGAAATTGAAGAAGATGCTGGACTTGGCAATGGTGGTCTTGGGAGACTT
GCTGCCTGCTTCTTGGATTCCATGGCAACCCTGGGACTTGCAGCCTATGGATACGGCATT
CGGTATGAATATGGGATTTTCAATCAGAAGATCCGAGATGGATGGCAGGTAGAAGAAGCA
GATGATTGGCTCAGATATGGAAACCCTTGGGAGAAGTCCCGCCCAGAATTCATGCTGCCT
GTGCACTTCTATGGAAAAGTAGAACACACCAACACCGGGACCAAGTGGATTGACACTCAA
GTGGTCCTGGCTCTGCCATATGACACCCCCGAGCCCGGCTACATGAATAACACTGTCAAC
ACCATGCGCCTCTGGTCTGCTCGGGCACCAAATGACTTTAACCTCAGAGACTTTAATGTT
GGAGACTACATTCAGGCTGTGCTGGACCGAAACCTGGCCGAGAACATCTCCCGGGTCCTC
TATCCCAATGACAATTTTTTTGAAGGGAAGGAGCTAAGATTGAAGCAGGAATACTTTGTG
GTGGCTGCAACCTTGCAAGATATCATCCGCCGTTTCAAAGCCTCCAAGTTTGGCTCCACC
CGTGGTCAAGGAACTGTGTTTGATGCCTTCCCGGATCAGGTGGCCATCCAGCTGAATGAT
ACTCACCCTCGCATCGCGATCCCTGAGCTGATGAGGATTTTTGTGGATATTGAAAAACTG
CCCTGGTCCAAGGCATGGGAGCTCAACCAGAAGACCTTCGCCTACACCAACCACACAGTG
CTCCCGGAAGCCCTGGAGCGCTGGCCCGTGGACCTGGTGGAGAAGCTGCTCCCTCGACAT
TTGGAAATCATTTATGAGATAAATCAGAAGCATTTAGATAGAATTGTGGCCTTGTTTCCT
AAAGATGTGGACCCTCTGAGAAGGATGTCTCTGATAGAAGAGGAAGGAAGCAAAAGGATC
AACATGGCCCATCTCTGCATTGTCGGTTCCCATGCTGTGAATGGCGTGGCTAAAATCCAC
TCAGACATCGTGAAGACTAAAGTATTCAAGGACTTCAGTGAGCTAGAACCTGACAAGTTT
CAGAATAAAACCAATGGGATCACTCCAAGGCGCTGGCTCCTACTCTGCAACCCAGGACTT
GCAGAGCTCATAGCAGAGAAAATTGGAGAAGACTATGTGAAAGACCTGAGCCAGCTGACG
AAGCTCCACAGCTTCCTGGGTGATGATGTCTTCCTCCGGGAACTCGCCAAGGTGAAGCAG
GAGAATAAGCTGAAGTTTTCTCAGTTCCTGGAGACGGAGTACAAAGTGAAGATCAACCCA
TCCTCCATGTTTGATGTCCAGGTGAAGAGGATACATGAGTACAAGCGACAGCTCTTGAAC
TGTCTGCATGTGATCACGATGTACAACCGCATTAAGAAAGACCCTAAGAAGTTATTCGTG
CCAAGGACAGTTATCATTGGTGGTAAAGCTGCCCCAGGATATCACATGGCCAAAATGATC
ATAAAGCTGATCACTTCAGTGGCAGATGTGGTGAACAATGACCCTATGGTTGGAAGCAAG
TTGAAAGTCATCTTCTTGGAGAACTACAGAGTATCTCTTGCTGAAAAAGTCATTCCAGCC
ACAGATCTGTCAGAGCAGATTTCCACTGCAGGCACCGAAGCCTCGGGGACAGGCAATATG
AAGTTCATGCTAAATGGGGCCCTAACTATCGGGACCATGGATGGGGCCAATGTGGAAATG
GCAGAAGAAGCTGGGGAAGAGAACCTGTTCATCTTTGGCATGAGCATAGATGATGTGGCT
GCTTTGGACAAGAAAGGGTACGAGGCAAAAGAATACTATGAGGCACTTCCAGAGCTGAAG
CTGGTCATTGATCAAATTGACAATGGCTTTTTTTCTCCCAAGCAGCCTGACCTCTTCAAA
GATATCATCAACATGCTATTTTATCATGACAGGTTTAAAGTCTTTGCAGACTACGAAGCC
TATGTCAAGTGTCAAGATAAAGTGAGTCAGCTGTACATGAATCCAAAGGCCTGGAACACA
ATGGTACTCAAAAACATAGCTGCCTCGGGGAAATTCTCCAGTGACCGAACAATTAAAGAA
TATGCCCAAAACATCTGGAACGTGGAACCTTCAGATCTAAAGATTTCTCTATCCAATGAA
TCTAACAAAGTCAATGGAAATTGA
|
| Enzyme 13 GenBank Gene ID |
M14636  |
| Enzyme 13 GeneCard ID |
PYGL  |
| Enzyme 13 GenAtlas ID |
PYGL  |
| Enzyme 13 HGNC ID |
HGNC:9725  |
| Enzyme 13 Chromosome Location |
1 |
| Enzyme 13 Locus |
14q21-q22 |
| Enzyme 13 SNPs |
SNPJam Report  |
| Enzyme 13 General References |
- Newgard CB, Nakano K, Hwang PK, Fletterick RJ: Sequence analysis of the cDNA encoding human liver glycogen phosphorylase reveals tissue-specific codon usage. Proc Natl Acad Sci U S A. 1986 Nov;83(21):8132-6. [PubMed
]
- Chang S, Rosenberg MJ, Morton H, Francomano CA, Biesecker LG: Identification of a mutation in liver glycogen phosphorylase in glycogen storage disease type VI. Hum Mol Genet. 1998 May;7(5):865-70. [PubMed
]
- Burwinkel B, Bakker HD, Herschkovitz E, Moses SW, Shin YS, Kilimann MW: Mutations in the liver glycogen phosphorylase gene (PYGL) underlying glycogenosis type VI. Am J Hum Genet. 1998 Apr;62(4):785-91. [PubMed
]
- Heilig R, Eckenberg R, Petit JL, Fonknechten N, Da Silva C, Cattolico L, Levy M, Barbe V, de Berardinis V, Ureta-Vidal A, Pelletier E, Vico V, Anthouard V, Rowen L, Madan A, Qin S, Sun H, Du H, Pepin K, Artiguenave F, Robert C, Cruaud C, Bruls T, Jaillon O, Friedlander L, Samson G, Brottier P, Cure S, Segurens B, Aniere F, Samain S, Crespeau H, Abbasi N, Aiach N, Boscus D, Dickhoff R, Dors M, Dubois I, Friedman C, Gouyvenoux M, James R, Madan A, Mairey-Estrada B, Mangenot S, Martins N, Menard M, Oztas S, Ratcliffe A, Shaffer T, Trask B, Vacherie B, Bellemere C, Belser C, Besnard-Gonnet M, Bartol-Mavel D, Boutard M, Briez-Silla S, Combette S, Dufosse-Laurent V, Ferron C, Lechaplais C, Louesse C, Muselet D, Magdelenat G, Pateau E, Petit E, Sirvain-Trukniewicz P, Trybou A, Vega-Czarny N, Bataille E, Bluet E, Bordelais I, Dubois M, Dumont C, Guerin T, Haffray S, Hammadi R, Muanga J, Pellouin V, Robert D, Wunderle E, Gauguet G, Roy A, Sainte-Marthe L, Verdier J, Verdier-Discala C, Hillier L, Fulton L, McPherson J, Matsuda F, Wilson R, Scarpelli C, Gyapay G, Wincker P, Saurin W, Quetier F, Waterston R, Hood L, Weissenbach J: The DNA sequence and analysis of human chromosome 14. Nature. 2003 Feb 6;421(6923):601-7. Epub 2003 Jan 1. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Gorin FA, Mullinax RL, Ignacio PC, Neve RL, Kurnit DM: McArdle's & Hers' diseases: glycogen phosphorylase transcriptional expression in human tissues. J Neurogenet. 1987 Dec;4(6):293-308. [PubMed
]
- Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed
]
- Rikova K, Guo A, Zeng Q, Possemato A, Yu J, Haack H, Nardone J, Lee K, Reeves C, Li Y, Hu Y, Tan Z, Stokes M, Sullivan L, Mitchell J, Wetzel R, Macneill J, Ren JM, Yuan J, Bakalarski CE, Villen J, Kornhauser JM, Smith B, Li D, Zhou X, Gygi SP, Gu TL, Polakiewicz RD, Rush J, Comb MJ: Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer. Cell. 2007 Dec 14;131(6):1190-203. [PubMed
]
- Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed
]
- Rath VL, Ammirati M, Danley DE, Ekstrom JL, Gibbs EM, Hynes TR, Mathiowetz AM, McPherson RK, Olson TV, Treadway JL, Hoover DJ: Human liver glycogen phosphorylase inhibitors bind at a new allosteric site. Chem Biol. 2000 Sep;7(9):677-82. [PubMed
]
- Rath VL, Ammirati M, LeMotte PK, Fennell KF, Mansour MN, Danley DE, Hynes TR, Schulte GK, Wasilko DJ, Pandit J: Activation of human liver glycogen phosphorylase by alteration of the secondary structure and packing of the catalytic core. Mol Cell. 2000 Jul;6(1):139-48. [PubMed
]
- Ekstrom JL, Pauly TA, Carty MD, Soeller WC, Culp J, Danley DE, Hoover DJ, Treadway JL, Gibbs EM, Fletterick RJ, Day YS, Myszka DG, Rath VL: Structure-activity analysis of the purine binding site of human liver glycogen phosphorylase. Chem Biol. 2002 Aug;9(8):915-24. [PubMed
]
|
| Enzyme 13 Metabolite References |
Not Available |
|
Enzyme 14
[top]
|
| Enzyme 14 ID |
5610 |
| Enzyme 14 Name |
Glycogen phosphorylase, muscle form |
| Enzyme 14 Synonyms |
- Myophosphorylase
|
| Enzyme 14 Gene Name |
PYGM |
| Enzyme 14 Protein Sequence |
>Glycogen phosphorylase, muscle form
MSRPLSDQEKRKQISVRGLAGVENVTELKKNFNRHLHFTLVKDRNVATPRDYYFALAHTV
RDHLVGRWIRTQQHYYEKDPKRIYYLSLEFYMGRTLQNTMVNLALENACDEATYQLGLDM
EELEEIEEDAGLGNGGLGRLAACFLDSMATLGLAAYGYGIRYEFGIFNQKISGGWQMEEA
DDWLRYGNPWEKARPEFTLPVHFYGHVEHTSQGAKWVDTQVVLAMPYDTPVPGYRNNVVN
TMRLWSAKAPNDFNLKDFNVGGYIQAVLDRNLAENISRVLYPNDNFFEGKELRLKQEYFV
VAATLQDIIRRFKSSKFGCRDPVRTNFDAFPDKVAIQLNDTHPSLAIPELMRILVDLERM
DWDKAWDVTVRTCAYTNHTVLPEALERWPVHLLETLLPRHLQIIYEINQRFLNRVAAAFP
GDVDRLRRMSLVEEGAVKRINMAHLCIAGSHAVNGVARIHSEILKKTIFKDFYELEPHKF
QNKTNGITPRRWLVLCNPGLAEVIAERIGEDFISDLDQLRKLLSFVDDEAFIRDVAKVKQ
ENKLKFAAYLEREYKVHINPNSLFDIQVKRIHEYKRQLLNCLHVITLYNRIKREPNKFFV
PRTVMIGGKAAPGYHMAKMIIRLVTAIGDVVNHDPAVGDRLRVIFLENYRVSLAEKVIPA
ADLSEQISTAGTEASGTGNMKFMLNGALTIGTMDGANVEMAEEAGEENFFIFGMRVEDVD
KLDQRGYNAQEYYDRIPELRQVIEQLSSGFFSPKQPDLFKDIVNMLMHHDRFKVFADYED
YIKCQEKVSALYKNPREWTRMVIRNIATSGKFSSDRTIAQYAREIWGVEPSRQRLPAPDE
AI
|
| Enzyme 14 Number of Residues |
842 |
| Enzyme 14 Molecular Weight |
97091.3 |
| Enzyme 14 Theoretical pI |
7.03 |
| Enzyme 14 GO Classification |
| Function |
- binding
- catalytic activity
- cofactor binding
- phosphorylase activity
- pyridoxal phosphate binding
- transferase activity
- transferase activity, transferring glycosyl groups
- transferase activity, transferring hexosyl groups
|
| Process |
- carbohydrate metabolic process
- metabolic process
- primary metabolic process
|
| Component |
| — |
|
| Enzyme 14 General Function |
Involved in phosphorylase activity |
| Enzyme 14 Specific Function |
Phosphorylase is an important allosteric enzyme in carbohydrate metabolism. Enzymes from different sources differ in their regulatory mechanisms and in their natural substrates. However, all known phosphorylases share catalytic and structural properties |
| Enzyme 14 Pathways |
- Starch and Sucrose Metabolism (map00500
)
|
| Enzyme 14 Reactions |
- [(1->4)-alpha-D-glucosyl]n + phosphate = [(1->4)-alpha-D-glucosyl]n-1 + alpha-D-glucose 1-phosphate [RN:R01821 R06050]
|
| Enzyme 14 Pfam Domain Function |
|
| Enzyme 14 Signals |
|
| Enzyme 14 Transmembrane Regions |
|
| Enzyme 14 Essentiality |
Not Available |
| Enzyme 14 GenBank ID Protein |
3153910  |
| Enzyme 14 UniProtKB/Swiss-Prot ID |
P11217  |
| Enzyme 14 UniProtKB/Swiss-Prot Entry Name |
PYGM_HUMAN  |
| Enzyme 14 PDB ID |
1XL1  |
| Enzyme 14 PDB File |
Show |
| Enzyme 14 3D Structure |
|
| Enzyme 14 Cellular Location |
Not Available |
| Enzyme 14 Gene Sequence |
>2529 bp
ATGTCCCGGCCCCTGTCAGACCAAGAGAAAAGAAAGCAAATCAGTGTGCGTGGCCTGGCC
GGCGTGGAGAACGTGACTGAGCTGAAAAAGAACTTCAACCGGCACCTGCATTTCACACTC
GTAAAGGACCGCAATGTGGCCACCCCACGAGACTACTACTTTGCTCTGGCCCATACCGTG
CGCGACCACCTCGTGGGGCGCTGGATCCGCACGCAGCAGCACTACTATGAGAAGGACCCC
AAGAGGATCTACTACCTGTCTTTAGAGTTCTATATGGGACGGACGCTACAGAACACCATG
GTGAACCTGGCCTTAGAGAATGCCTGTGACGAGGCCACCTACCAGCTGGGCCTGGACATG
GAGGAGCTGGAGGAAATTGAGGAGGATGCGGGGCTGGGCAACGGGGGCCTGGGCCGGCTG
GCAGCCTGCTTTCTTGACTCCATGGCAACACTGGGCCTGGCCGCCTATGGCTACGGGATT
CGCTATGAGTTTGGGATTTTTAACCAGAAGATCTCCGGGGGCTGGCAGATGGAGGAGGCC
GATGACTGGCTTCGCTACGGCAACCCCTGGGAGAAGGCCCGGCCCGAGTTCACGCTACCT
GTGCACTTCTACGGCCATGTGGAGCACACCAGCCAGGGTGCCAAGTGGGTGGACACACAG
GTGGTACTGGCCATGCCCTACGATACGCCCGTGCCTGGCTATCGCAACAATGTTGTCAAC
ACCATGCGCCTCTGGTCTGCCAAGGCTCCCAATGACTTCAACCTCAAGGACTTCAATGTC
GGTGGCTACATCCAGGCTGTGTTGGACCGAAACCTGGCGGAGAACATCTCTCGTGTCCTG
TACCCCAATGATAATTTCTTCGAAGGGAAGGAGCTGCGGCTGAAGCAGGAGTATTTCGTG
GTGGCTGCCACCCTCCAGGACATCATCCGTCGCTTCAAGTCTTCCAAGTTCGGCTGCCGT
GATCCCGTGCGCACGAACTTCGATGCCTTCCCAGATAAGGTGGCCATCCAGCTCAATGAC
ACCCACCCCTCCCTGGCCATCCCCGAGCTGATGAGGATCCTGGTGGACCTGGAACGGATG
GACTGGGACAAGGCGTGGGATGTGACAGTGAGGACCTGTGCCTACACCAACCACACGGTG
CTGCCCGAGGCCCTGGAGCGCTGGCCGGTGCACCTCTTGGAGACGCTGCTGCCGCGGCAC
CTCCAGATCATCTACGAGATCAACCAGCGCTTCCTCAACCGGGTGGCGGCCGCATTCCCA
GGGGACGTAGACCGGCTGCGGCGCATGTCGCTGGTGGAGGAGGGCGCAGTGAAGCGCATC
AACATGGCACACCTGTGCATCGCGGGGTCGCACGCCGTCAACGGCGTGGCGCGCATCCAC
TCCGAGATCCTCAAGAAGACCATCTTCAAAGACTTCTATGAGCTGGAGCCTCATAAGTTC
CAGAATAAGACCAACGGCATCACCCCTCGGCGCTGGCTGGTTCTGTGTAACCCCGGGCTG
GCAGAGGTCATTGCTGAGCGCATCGGGGAGGACTTCATCTCTGACCTGGACCAGCTGCGC
AAACTGCTCTCCTTTGTGGATGATGAAGCTTTCATTCGGGATGTGGCCAAAGTGAAGCAG
GAAAACAAGTTGAAGTTTGCTGCCTACCTAGAGAGGGAATACAAAGTCCACATCAACCCC
AACTCACTCTTCGACATCCAGGTGAAGCGGATTCACGAATATAAACGACAGCTCCTCAAC
TGCCTCCATGTCATCACCCTGTACAACCGCATCAAGAGGGAGCCCAATAAGTTTTTTGTG
CCTCGGACTGTGATGATTGGAGGGAAGGCTGCACCTGGGTACCACATGGCCAAGATGATC
ATCAGACTCGTCACAGCCATCGGGGATGTGGTCAACCATGACCCGGCAGTGGGTGACCGC
CTCCGTGTCATCTTCCTGGAGAACTACCGAGTCTCACTGGCCGAGAAAGTGATCCCAGCT
GCAGACCTCTCTGAGCAGATCTCCACTGCGGGCACTGAAGCCTCAGGCACCGGCAACATG
AAGTTCATGCTCAACGGGGCTCTGACCATTGGCACCATGGACGGGGCCAATGTGGAGATG
GCAGAAGAGGCGGGAGAGGAAAACTTCTTCATCTTTGGCATGCGGGTGGAGGATGTGGAT
AAGCTTGACCAAAGAGGGTACAATGCCCAGGAGTACTACGATCGCATTCCTGAGCTTCGG
CAGGTCATTGAGCAGCTGAGCAGTGGCTTCTTCTCCCCCAAACAGCCCGACCTGTTCAAG
GACATTGTCAATATGCTCATGCACCATGACCGGTTTAAAGTCTTCGCAGATTATGAAGAC
TACATTAAATGCCAGGAGAAAGTCAGCGCCTTGTACAAGAACCCAAGAGAGTGGACGCGG
ATGGTGATCCGGAACATAGCCACCTCTGGCAAGTTCTCCAGTGACCGCACCATTGCCCAG
TATGCCCGGGAGATCTGGGGTGTGGAGCCTTCCCGCCAGCGCCTGCCAGCCCCGGATGAG
GCCATCTGA
|
| Enzyme 14 GenBank Gene ID |
AF066859  |
| Enzyme 14 GeneCard ID |
PYGM  |
| Enzyme 14 GenAtlas ID |
PYGM  |
| Enzyme 14 HGNC ID |
HGNC:9726  |
| Enzyme 14 Chromosome Location |
1 |
| Enzyme 14 Locus |
11q12-q13.2 |
| Enzyme 14 SNPs |
SNPJam Report  |
| Enzyme 14 General References |
- Burke J, Hwang P, Anderson L, Lebo R, Gorin F, Fletterick R: Intron/exon structure of the human gene for the muscle isozyme of glycogen phosphorylase. Proteins. 1987;2(3):177-87. [PubMed
]
- Kubisch C, Wicklein EM, Jentsch TJ: Molecular diagnosis of McArdle disease: revised genomic structure of the myophosphorylase gene and identification of a novel mutation. Hum Mutat. 1998;12(1):27-32. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Hwang PK, See YP, Vincentini AM, Powers MA, Fletterick RJ, Crerar MM: Comparative sequence analysis of rat, rabbit, and human muscle glycogen phosphorylase cDNAs. Eur J Biochem. 1985 Oct 15;152(2):267-74. [PubMed
]
- Gautron S, Daegelen D, Mennecier F, Dubocq D, Kahn A, Dreyfus JC: Molecular mechanisms of McArdle's disease (muscle glycogen phosphorylase deficiency). RNA and DNA analysis. J Clin Invest. 1987 Jan;79(1):275-81. [PubMed
]
- Carty TJ, Tu J-I, Graves DJ: Regulation of glycogen phosphorylase. Role of the peptide region surrounding the phosphoserine residue in determining enzyme properties. J Biol Chem. 1975 Jul 10;250(13):4980-5. [PubMed
]
- Kim JE, Tannenbaum SR, White FM: Global phosphoproteome of HT-29 human colon adenocarcinoma cells. J Proteome Res. 2005 Jul-Aug;4(4):1339-46. [PubMed
]
- Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed
]
- Tsujino S, Shanske S, DiMauro S: Molecular genetic heterogeneity of myophosphorylase deficiency (McArdle's disease). N Engl J Med. 1993 Jul 22;329(4):241-5. [PubMed
]
- Tsujino S, Shanske S, Martinuzzi A, Heiman-Patterson T, DiMauro S: Two novel missense mutations (E654K, L396P) in Caucasian patients with myophosphorylase deficiency (McArdle's disease). Hum Mutat. 1995;6(3):276-7. [PubMed
]
- Tsujino S, Shanske S, Nonaka I, DiMauro S: The molecular genetic basis of myophosphorylase deficiency (McArdle's disease). Muscle Nerve. 1995;3:S23-7. [PubMed
]
- Vorgerd M, Kubisch C, Burwinkel B, Reichmann H, Mortier W, Tettenborn B, Pongratz D, Lindemuth R, Tegenthoff M, Malin JP, Kilimann MW: Mutation analysis in myophosphorylase deficiency (McArdle's disease). Ann Neurol. 1998 Mar;43(3):326-31. [PubMed
]
- Gamez J, Fernandez R, Bruno C, Andreu AL, Cervera C, Navarro C, Schwartz S, Dimauro S: A new mutation in the regulatory domain of the myophosphorylase gene affecting protein dimer contact. Muscle Nerve. 1999 Aug;22(8):1136-8. [PubMed
]
- Andreu AL, Bruno C, Tamburino L, Gamez J, Shanske S, Cervera C, Navarro C, DiMauro S: A new mutation in the myophosphorylase gene (Asn684Tyr) in a Spanish patient with McArdle's disease. Neuromuscul Disord. 1999 May;9(3):171-3. [PubMed
]
- Rubio JC, Martin MA, Garcia A, Campos Y, Cabello A, Culebras JM, Arenas J: McArdle's disease associated with homozygosity for the missense mutation Gly204Ser of the myophosphorylase gene in a Spanish patient. Neuromuscul Disord. 1999 May;9(3):174-5. [PubMed
]
- Fernandez R, Navarro C, Andreu AL, Bruno C, Shanske S, Gamez J, Teijeira S, Hernandez I, Teijeiro A, Fernandez JM, Musumeci O, DiMauro S: A novel missense mutation (W797R) in the myophosphorylase gene in Spanish patients with McArdle disease. Arch Neurol. 2000 Feb;57(2):217-9. [PubMed
]
- Rubio JC, Martin MA, Campos Y, Auciello R, Cabello A, Arenas J: A missense mutation W797R in the myophosphorylase gene in a Spanish patient with McArdle's disease. Muscle Nerve. 2000 Jan;23(1):129-31. [PubMed
]
- Rubio JC, Martin MA, Campos Y, Cabello A, Arenas J: A missense mutation T487N in the myophosphorylase gene in a Spanish patient with McArdle's disease. Neuromuscul Disord. 2000 Feb;10(2):138-40. [PubMed
]
- Martin MA, Rubio JC, Campos Y, Ricoy JR, Cabello A, Arenas J: A homozygous missense mutation (A659D) in the myophosphorylase gene in a Spanish patient with McArdle's disease. Neuromuscul Disord. 2000 Aug;10(6):447-9. [PubMed
]
- Martin MA, Rubio JC, Buchbinder J, Fernandez-Hojas R, del Hoyo P, Teijeira S, Gamez J, Navarro C, Fernandez JM, Cabello A, Campos Y, Cervera C, Culebras JM, Andreu AL, Fletterick R, Arenas J: Molecular heterogeneity of myophosphorylase deficiency (McArdle's disease): a genotype-phenotype correlation study. Ann Neurol. 2001 Nov;50(5):574-81. [PubMed
]
- Bruno C, Lanzillo R, Biedi C, Iadicicco L, Minetti C, Santoro L: Two new mutations in the myophosphorylase gene in Italian patients with McArdle's disease. Neuromuscul Disord. 2002 Jun;12(5):498-500. [PubMed
]
|
| Enzyme 14 Metabolite References |
Not Available |
|
Enzyme 15
[top]
|
| Enzyme 15 ID |
5612 |
| Enzyme 15 Name |
Glycogen phosphorylase, brain form |
| Enzyme 15 Synonyms |
Not Available |
| Enzyme 15 Gene Name |
PYGB |
| Enzyme 15 Protein Sequence |
>Glycogen phosphorylase, brain form
MAKPLTDSEKRKQISVRGLAGLGDVAEVRKSFNRHLHFTLVKDRNVATPRDYFFALAHTV
RDHLVGRWIRTQQHYYERDPKRIYYLSLEFYMGRTLQNTMVNLGLQNACDEAIYQLGLDL
EELEEIEEDAGLGNGGLGRLAACFLDSMATLGLAAYGYGIRYEFGIFNQKIVNGWQVEEA
DDWLRYGNPWEKARPEYMLPVHFYGRVEHTPDGVKWLDTQVVLAMPYDTPVPGYKNNTVN
TMRLWSAKAPNDFKLQDFNVGDYIEAVLDRNLAENISRVLYPNDNFFEGKELRLKQEYFV
VAATLQDIIRRFKSSKFGCRDPVRTCFETFPDKVAIQLNDTHPALSIPELMRILVDVEKV
DWDKAWEITKKTCAYTNHTVLPEALERWPVSMFEKLLPRHLEIIYAINQRHLDHVAALFP
GDVDRLRRMSVIEEGDCKRINMAHLCVIGSHAVNGVARIHSEIVKQSVFKDFYELEPEKF
QNKTNGITPRRWLLLCNPGLADTIVEKIGEEFLTDLSQLKKLLPLVSDEVFIRDVAKVKQ
ENKLKFSAFLEKEYKVKINPSSMFDVHVKRIHEYKRQLLNCLHVVTLYNRIKRDPAKAFV
PRTVMIGGKAAPGYHMAKLIIKLVTSIGDVVNHDPVVGDRLKVIFLENYRVSLAEKVIPA
ADLSQQISTAGTEASGTGNMKFMLNGALTIGTMDGANVEMAEEAGAENLFIFGLRVEDVE
ALDRKGYNAREYYDHLPELKQAVDQISSGFFSPKEPDCFKDIVNMLMHHDRFKVFADYEA
YMQCQAQVDQLYRNPKEWTKKVIRNIACSGKFSSDRTITEYAREIWGVEPSDLQIPPPNI
PRD
|
| Enzyme 15 Number of Residues |
843 |
| Enzyme 15 Molecular Weight |
96695.2 |
| Enzyme 15 Theoretical pI |
6.85 |
| Enzyme 15 GO Classification |
| Function |
- binding
- catalytic activity
- cofactor binding
- phosphorylase activity
- pyridoxal phosphate binding
- transferase activity
- transferase activity, transferring glycosyl groups
- transferase activity, transferring hexosyl groups
|
| Process |
- carbohydrate metabolic process
- metabolic process
- primary metabolic process
|
| Component |
| — |
|
| Enzyme 15 General Function |
Involved in phosphorylase activity |
| Enzyme 15 Specific Function |
Phosphorylase is an important allosteric enzyme in carbohydrate metabolism. Enzymes from different sources differ in their regulatory mechanisms and in their natural substrates. However, all known phosphorylases share catalytic and structural properties |
| Enzyme 15 Pathways |
- Starch and Sucrose Metabolism (map00500
)
|
| Enzyme 15 Reactions |
- [(1->4)-alpha-D-glucosyl]n + phosphate = [(1->4)-alpha-D-glucosyl]n-1 + alpha-D-glucose 1-phosphate [RN:R01821 R06050]
|
| Enzyme 15 Pfam Domain Function |
|
| Enzyme 15 Signals |
|
| Enzyme 15 Transmembrane Regions |
|
| Enzyme 15 Essentiality |
Not Available |
| Enzyme 15 GenBank ID Protein |
9650807  |
| Enzyme 15 UniProtKB/Swiss-Prot ID |
P11216  |
| Enzyme 15 UniProtKB/Swiss-Prot Entry Name |
PYGB_HUMAN  |
| Enzyme 15 PDB ID |
Not Available |
| Enzyme 15 Cellular Location |
Not Available |
| Enzyme 15 Gene Sequence |
>2532 bp
ATGGCGAAGCCGCTGACGGACAGCGAGAAGCGGAAGCAGATCAGCGTGCGCGGCCTGGCG
GGGCTAGGCGACGTGGCCGAGGTGCGGAAGAGCTTCAACCGGCACTTGCACTTCACGCTG
GTCAAGGACCGCAATGTGGCCACGCCCCGCGACTACTTCTTCGCGCTGGCGCACACGGTG
CGCGACCACCTCGTGGGCCGCTGGATCCGCACGCAGCAGCACTACTACGAGCGCGACCCC
AAGCGCATTTATTATCTTTCCCTGGAATTCTACATGGGTCGCACGCTGCAGAACACGATG
GTGAACCTGGGCCTTCAGAATGCCTGCGATGAAGCCATCTATCAGTTGGGGTTAGACTTG
GAGGAACTCGAGGAGATAGAAGAAGATGCTGGCCTTGGGAATGGAGGCCTGGGGAGGCTG
GCAGCGTGTTTCCTTGACTCAATGGCTACCTTGGGCCTGGCAGCATACGGCTATGGAATC
CGCTATGAATTTGGGATTTTTAACCAGAAGATTGTCAATGGCTGGCAGGTAGAGGAGGCC
GATGACTGGCTGCGCTACGGCAACCCCTGGGAGAAAGCGCGGCCTGAGTATATGCTTCCC
GTGCACTTCTACGGACGCGTGGAGCACACCCCCGACGGCGTGAAGTGGCTGGACACACAG
GTGGTGCTGGCCATGCCCTACGACACCCCAGTGCCCGGCTACAAGAACAACACCGTCAAC
ACCATGCGGCTGTGGTCCGCCAAGGCTCCCAACGACTTCAAGCTGCAGGACTTCAACGTG
GGAGACTACATCGAGGCGGTCCTGGACCGGAACTTGGCTGAGAACATCTCCAGGGTCCTG
TATCCAAATGATAACTTCTTTGAGGGGAAGGAGCTGCGGCTGAAGCAGGAGTACTTCGTG
GTGGCCGCCACGCTCCAGGACATCATCCGCCGCTTCAAGTCGTCCAAGTTCGGCTGCCGG
GACCCTGTGAGAACCTGTTTCGAGACGTTCCCAGACAAGGTGGCCATCCAGCTGAACGAC
ACCCACCCCGCCCTCTCCATCCCTGAGCTCATGCGGATCCTGGTGGACGTGGAGAAGGTG
GACTGGGACAAGGCCTGGGAAATCACGAAGAAGACCTGTGCATACACCAACCACACTGTG
CTGCCTGAGGCCTTGGAGCGCTGGCCCGTGTCCATGTTTGAGAAGCTGCTGCCGCGGCAC
CTGGAGATAATCTATGCCATCAACCAGCGGCACCTGGACCACGTGGCCGCGCTGTTTCCC
GGCGATGTGGACCGCCTGCGCAGGATGTCTGTGATCGAGGAGGGGGACTGCAAGCGGATC
AACATGGCCCACCTGTGTGTGATTGGGTCCCATGCTGTCAATGGTGTGGCGAGGATCCAC
TCGGAGATCGTGAAACAGTCGGTCTTTAAGGATTTTTATGAACTGGAGCCAGAGAAGTTC
CAGAATAAGACCAATGGCATCACCCCCCGCCGGTGGCTGCTGCTGTGCAACCCGGGGCTG
GCCGATACCATCGTGGAGAAAATTGGGGAGGAGTTCCTGACTGACCTGAGCCAGCTGAAG
AAGCTGCTGCCGCTGGTCAGTGACGAGGTGTTCATCAGGGACGTGGCCAAGGTCAAACAG
GAGAACAAGCTCAAGTTCTCGGCCTTCCTGGAGAAGGAGTACAAGGTGAAGATCAACCCC
TCCTCCATGTTCGATGTGCATGTGAAGAGGATCCACGAGTACAAGCGGCAGCTGCTCAAC
TGCCTGCACGTCGTCACCCTGTACAATCGAATCAAGAGAGACCCGGCCAAGGCTTTTGTG
CCCAGGACTGTTATGATTGGGGGCAAGGCAGCGCCCGGTTACCACATGGCCAAGCTGATC
ATCAAGTTGGTCACCTCCATCGGCGACGTCGTCAATCATGACCCAGTTGTGGGTGACAGG
TTGAAAGTGATCTTCCTGGAGAACTACCGTGTGTCCTTGGCTGAGAAAGTGATCCCGGCC
GCTGATCTGTCGCAGCAGATCTCCACTGCAGGCACCGAGGCCTCAGGCACAGGCAACATG
AAGTTCATGCTCAACGGGGCCCTCACCATCGGCACCATGGACGGCGCCAACGTGGAGATG
GCCGAGGAGGCCGGGGCCGAGAACCTCTTCATCTTCGGCCTGCGGGTGGAGGATGTCGAG
GCCTTGGACCGGAAAGGGTACAATGCCAGGGAGTACTACGACCACCTGCCCGAGCTGAAG
CAGGCCGTGGACCAGATCAGCAGTGGCTTTTTTTCTCCCAAGGAGCCAGACTGCTTCAAG
GACATCGTGAACATGCTGATGCACCATGACAGGTTCAAGGTGTTTGCAGACTATGAAGCC
TACATGCAGTGCCAGGCACAGGTGGACCAGCTGTACCGGAACCCCAAGGAGTGGACCAAG
AAGGTCATCAGGAACATCGCCTGCTCGGGCAAGTTCTCCAGTGACCGGACCATCACGGAG
TATGCACGGGAGATCTGGGGTGTGGAGCCCTCCGACCTGCAGATCCCGCCCCCCAACATC
CCCCGGGACTAG
|
| Enzyme 15 GenBank Gene ID |
AL121772  |
| Enzyme 15 GeneCard ID |
PYGB  |
| Enzyme 15 GenAtlas ID |
PYGB  |
| Enzyme 15 HGNC ID |
HGNC:9723  |
| Enzyme 15 Chromosome Location |
2 |
| Enzyme 15 Locus |
20p11.2-p11.1 |
| Enzyme 15 SNPs |
SNPJam Report  |
| Enzyme 15 General References |
- Newgard CB, Littman DR, van Genderen C, Smith M, Fletterick RJ: Human brain glycogen phosphorylase. Cloning, sequence analysis, chromosomal mapping, tissue expression, and comparison with the human liver and muscle isozymes. J Biol Chem. 1988 Mar 15;263(8):3850-7. [PubMed
]
- Gelinas RP, Froman BE, McElroy F, Tait RC, Gorin FA: Human brain glycogen phosphorylase: characterization of fetal cDNA and genomic sequences. Brain Res Mol Brain Res. 1989 Nov;6(2-3):177-85. [PubMed
]
- Deloukas P, Matthews LH, Ashurst J, Burton J, Gilbert JG, Jones M, Stavrides G, Almeida JP, Babbage AK, Bagguley CL, Bailey J, Barlow KF, Bates KN, Beard LM, Beare DM, Beasley OP, Bird CP, Blakey SE, Bridgeman AM, Brown AJ, Buck D, Burrill W, Butler AP, Carder C, Carter NP, Chapman JC, Clamp M, Clark G, Clark LN, Clark SY, Clee CM, Clegg S, Cobley VE, Collier RE, Connor R, Corby NR, Coulson A, Coville GJ, Deadman R, Dhami P, Dunn M, Ellington AG, Frankland JA, Fraser A, French L, Garner P, Grafham DV, Griffiths C, Griffiths MN, Gwilliam R, Hall RE, Hammond S, Harley JL, Heath PD, Ho S, Holden JL, Howden PJ, Huckle E, Hunt AR, Hunt SE, Jekosch K, Johnson CM, Johnson D, Kay MP, Kimberley AM, King A, Knights A, Laird GK, Lawlor S, Lehvaslaiho MH, Leversha M, Lloyd C, Lloyd DM, Lovell JD, Marsh VL, Martin SL, McConnachie LJ, McLay K, McMurray AA, Milne S, Mistry D, Moore MJ, Mullikin JC, Nickerson T, Oliver K, Parker A, Patel R, Pearce TA, Peck AI, Phillimore BJ, Prathalingam SR, Plumb RW, Ramsay H, Rice CM, Ross MT, Scott CE, Sehra HK, Shownkeen R, Sims S, Skuce CD, Smith ML, Soderlund C, Steward CA, Sulston JE, Swann M, Sycamore N, Taylor R, Tee L, Thomas DW, Thorpe A, Tracey A, Tromans AC, Vaudin M, Wall M, Wallis JM, Whitehead SL, Whittaker P, Willey DL, Williams L, Williams SA, Wilming L, Wray PW, Hubbard T, Durbin RM, Bentley DR, Beck S, Rogers J: The DNA sequence and comparative analysis of human chromosome 20. Nature. 2001 Dec 20-27;414(6866):865-71. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Gevaert K, Goethals M, Martens L, Van Damme J, Staes A, Thomas GR, Vandekerckhove J: Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides. Nat Biotechnol. 2003 May;21(5):566-9. Epub 2003 Mar 31. [PubMed
]
- Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed
]
- Rikova K, Guo A, Zeng Q, Possemato A, Yu J, Haack H, Nardone J, Lee K, Reeves C, Li Y, Hu Y, Tan Z, Stokes M, Sullivan L, Mitchell J, Wetzel R, Macneill J, Ren JM, Yuan J, Bakalarski CE, Villen J, Kornhauser JM, Smith B, Li D, Zhou X, Gygi SP, Gu TL, Polakiewicz RD, Rush J, Comb MJ: Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer. Cell. 2007 Dec 14;131(6):1190-203. [PubMed
]
- Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed
]
- Heibeck TH, Ding SJ, Opresko LK, Zhao R, Schepmoes AA, Yang F, Tolmachev AV, Monroe ME, Camp DG 2nd, Smith RD, Wiley HS, Qian WJ: An extensive survey of tyrosine phosphorylation revealing new sites in human mammary epithelial cells. J Proteome Res. 2009 Aug;8(8):3852-61. [PubMed
]
- Oppermann FS, Gnad F, Olsen JV, Hornberger R, Greff Z, Keri G, Mann M, Daub H: Large-scale proteomics analysis of the human kinome. Mol Cell Proteomics. 2009 Jul;8(7):1751-64. Epub 2009 Apr 15. [PubMed
]
|
| Enzyme 15 Metabolite References |
Not Available |
|
Enzyme 16
[top]
|
| Enzyme 16 ID |
5615 |
| Enzyme 16 Name |
Kynurenine/alpha-aminoadipate aminotransferase, mitochondrial |
| Enzyme 16 Synonyms |
- 2-aminoadipate aminotransferase
- 2-aminoadipate transaminase
- Alpha-aminoadipate aminotransferase
- AadAT
- KAT/AadAT
- Kynurenine aminotransferase II
- Kynurenine--oxoglutarate aminotransferase II
- Kynurenine--oxoglutarate transaminase II
|
| Enzyme 16 Gene Name |
AADAT |
| Enzyme 16 Protein Sequence |
>Kynurenine/alpha-aminoadipate aminotransferase, mitochondrial
MNYARFITAASAARNPSPIRTMTDILSRGPKSMISLAGGLPNPNMFPFKTAVITVENGKT
IQFGEEMMKRALQYSPSAGIPELLSWLKQLQIKLHNPPTIHYPPSQGQMDLCVTSGSQQG
LCKVFEMIINPGDNVLLDEPAYSGTLQSLHPLGCNIINVASDESGIVPDSLRDILSRWKP
EDAKNPQKNTPKFLYTVPNGNNPTGNSLTSERKKEIYELARKYDFLIIEDDPYYFLQFNK
FRVPTFLSMDVDGRVIRADSFSKIISSGLRIGFLTGPKPLIERVILHIQVSTLHPSTFNQ
LMISQLLHEWGEEGFMAHVDRVIDFYSNQKDAILAAADKWLTGLAEWHVPAAGMFLWIKV
KGINDVKELIEEKAVKMGVLMLPGNAFYVDSSAPSPYLRASFSSASPEQMDVAFQVLAQL
IKESL
|
| Enzyme 16 Number of Residues |
425 |
| Enzyme 16 Molecular Weight |
47351.2 |
| Enzyme 16 Theoretical pI |
6.96 |
| Enzyme 16 GO Classification |
| Function |
- binding
- catalytic activity
- cofactor binding
- pyridoxal phosphate binding
- transferase activity
- transferase activity, transferring nitrogenous groups
|
| Process |
- biosynthetic process
- metabolic process
|
| Component |
| — |
|
| Enzyme 16 General Function |
Involved in transferase activity, transferring nitrogenous groups |
| Enzyme 16 Specific Function |
Transaminase with broad substrate specificity. Has transaminase activity towards aminoadipate, kynurenine, methionine and glutamate. Shows activity also towards tryptophan, aspartate and hydroxykynurenine. Accepts a variety of oxo-acids as amino- group acceptors, with a preference for 2-oxoglutarate, 2- oxocaproic acid, phenylpyruvate and alpha-oxo-gamma-methiol butyric acid. Can also use glyoxylate as amino-group acceptor (in vitro) |
| Enzyme 16 Pathways |
|
| Enzyme 16 Reactions |
- L-2-aminoadipate + 2-oxoglutarate = 2-oxoadipate + L-glutamate [RN:R01939]
|
| Enzyme 16 Pfam Domain Function |
|
| Enzyme 16 Signals |
|
| Enzyme 16 Transmembrane Regions |
|
| Enzyme 16 Essentiality |
Not Available |
| Enzyme 16 GenBank ID Protein |
Not Available |
| Enzyme 16 UniProtKB/Swiss-Prot ID |
Q8N5Z0  |
| Enzyme 16 UniProtKB/Swiss-Prot Entry Name |
AADAT_HUMAN  |
| Enzyme 16 PDB ID |
Not Available |
| Enzyme 16 Cellular Location |
Not Available |
| Enzyme 16 Gene Sequence |
>1278 bp
ATGAATTACGCACGGTTCATCACGGCAGCGAGCGCAGCCAGAAACCCTTCTCCCATCCGG
ACCATGACTGACATATTGAGCAGAGGACCAAAATCGATGATCTCCTTGGCTGGTGGCTTA
CCAAATCCAAACATGTTTCCTTTTAAGACTGCCGTAATCACTGTAGAAAATGGAAAGACC
ATCCAATTTGGAGAAGAGATGATGAAGAGAGCACTTCAGTATTCTCCGAGTGCTGGAATT
CCAGAGCTTTTGTCCTGGCTAAAACAGTTACAAATAAAATTGCATAATCCTCCTACCATC
CATTACCCACCCAGTCAAGGACAAATGGATCTATGTGTCACATCTGGCAGCCAACAAGGT
CTTTGTAAGGTGTTTGAAATGATCATTAATCCTGGAGATAATGTCCTCCTAGATGAACCT
GCTTATTCAGGAACTCTTCAAAGTCTGCACCCACTGGGCTGCAACATTATTAATGTTGCC
AGTGATGAAAGTGGGATTGTTCCAGATTCCCTAAGAGACATACTTTCCAGATGGAAACCA
GAAGATGCAAAGAATCCCCAGAAAAACACCCCCAAATTTCTTTATACTGTTCCAAATGGC
AACAACCCTACTGGAAACTCATTAACCAGTGAACGCAAAAAGGAAATCTATGAGCTTGCA
AGAAAATATGATTTCCTCATAATAGAAGATGATCCTTACTATTTTCTCCAGTTTAACAAG
TTCAGGGTACCAACATTTCTTTCCATGGATGTTGATGGACGTGTCATCAGAGCTGACTCT
TTTTCAAAAATCATTTCCTCTGGGTTGAGAATAGGATTTTTAACTGGTCCAAAACCCTTA
ATAGAGAGAGTTATTTTACACATACAAGTTTCAACATTGCACCCCAGCACTTTTAACCAG
CTCATGATATCACAGCTTCTACACGAATGGGGAGAAGAAGGTTTCATGGCTCATGTAGAC
AGGGTTATTGATTTCTATAGTAACCAGAAGGATGCAATACTGGCAGCTGCAGACAAGTGG
TTAACTGGTTTGGCAGAATGGCATGTTCCTGCTGCTGGAATGTTTTTATGGATTAAAGTT
AAAGGCATTAATGATGTAAAAGAACTGATTGAAGAAAAGGCCGTTAAGATGGGGGTATTA
ATGCTCCCTGGAAATGCTTTCTACGTCGATAGCTCAGCTCCTAGCCCTTACTTGAGAGCA
TCCTTCTCTTCAGCTTCTCCAGAACAGATGGATGTGGCCTTCCAGGTATTAGCACAACTT
ATAAAAGAATCTTTATGA
|
| Enzyme 16 GenBank Gene ID |
AF097994  |
| Enzyme 16 GeneCard ID |
AADAT  |
| Enzyme 16 GenAtlas ID |
AADAT  |
| Enzyme 16 HGNC ID |
HGNC:17929  |
| Enzyme 16 Chromosome Location |
4 |
| Enzyme 16 Locus |
4q33 |
| Enzyme 16 SNPs |
SNPJam Report  |
| Enzyme 16 General References |
- Goh DL, Patel A, Thomas GH, Salomons GS, Schor DS, Jakobs C, Geraghty MT: Characterization of the human gene encoding alpha-aminoadipate aminotransferase (AADAT). Mol Genet Metab. 2002 Jul;76(3):172-80. [PubMed
]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Han Q, Cai T, Tagle DA, Robinson H, Li J: Substrate specificity and structure of human aminoadipate aminotransferase/kynurenine aminotransferase II. Biosci Rep. 2008 Aug;28(4):205-15. [PubMed
]
- Han Q, Robinson H, Li J: Crystal structure of human kynurenine aminotransferase II. J Biol Chem. 2008 Feb 8;283(6):3567-73. Epub 2007 Dec 5. [PubMed
]
- Rossi F, Garavaglia S, Montalbano V, Walsh MA, Rizzi M: Crystal structure of human kynurenine aminotransferase II, a drug target for the treatment of schizophrenia. J Biol Chem. 2008 Feb 8;283(6):3559-66. Epub 2007 Dec 5. [PubMed
]
|
| Enzyme 16 Metabolite References |
Not Available |
|
Enzyme 17
[top]
|
| Enzyme 17 ID |
5633 |
| Enzyme 17 Name |
Alanine--glyoxylate aminotransferase 2, mitochondrial |
| Enzyme 17 Synonyms |
- AGT 2
- (R)-3-amino-2-methylpropionate--pyruvate transaminase
- Beta-ALAAT II
- Beta-alanine-pyruvate aminotransferase
- D-AIBAT
|
| Enzyme 17 Gene Name |
AGXT2 |
| Enzyme 17 Protein Sequence |
>Alanine--glyoxylate aminotransferase 2, mitochondrial
MTLIWRHLLRPLCLVTSAPRILEMHPFLSLGTSRTSVTKLSLHTKPRMPPCDFMPERYQS
LGYNRVLEIHKEHLSPVVTAYFQKPLLLHQGHMEWLFDAEGSRYLDFFSGIVTVSVGHCH
PKVNAVAQKQLGRLWHTSTVFFHPPMHEYAEKLAALLPEPLKVIFLVNSGSEANELAMLM
ARAHSNNIDIISFRGAYHGCSPYTLGLTNVGTYKMELPGGTGCQPTMCPDVFRGPWGGSH
CRDSPVQTIRKCSCAPDCCQAKDQYIEQFKDTLSTSVAKSIAGFFAEPIQGVNGVVQYPK
GFLKEAFELVRARGGVCIADEVQTGFGRLGSHFWGFQTHDVLPDIVTMAKGIGNGFPMAA
VITTPEIAKSLAKCLQHFNTFGGNPMACAIGSAVLEVIKEENLQENSQEVGTYMLLKFAK
LRDEFEIVGDVRGKGLMIGIEMVQDKISCRPLPREEVNQIHEDCKHMGLLVGRGSIFSQT
FRIAPSMCITKPEVDFAVEVFRSALTQHMERRAK
|
| Enzyme 17 Number of Residues |
514 |
| Enzyme 17 Molecular Weight |
57155.9 |
| Enzyme 17 Theoretical pI |
7.91 |
| Enzyme 17 GO Classification |
| Function |
- binding
- catalytic activity
- cofactor binding
- pyridoxal phosphate binding
- transaminase activity
- transferase activity
- transferase activity, transferring nitrogenous groups
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 17 General Function |
Involved in transaminase activity |
| Enzyme 17 Specific Function |
L-alanine + glyoxylate = pyruvate + glycine |
| Enzyme 17 Pathways |
- Glycine, Serine and Threonine Metabolism (map00260
)
|
| Enzyme 17 Reactions |
- L-alanine + glyoxylate = pyruvate + glycine [RN:R00369]
|
| Enzyme 17 Pfam Domain Function |
|
| Enzyme 17 Signals |
|
| Enzyme 17 Transmembrane Regions |
|
| Enzyme 17 Essentiality |
Not Available |
| Enzyme 17 GenBank ID Protein |
12406973  |
| Enzyme 17 UniProtKB/Swiss-Prot ID |
Q9BYV1  |
| Enzyme 17 UniProtKB/Swiss-Prot Entry Name |
AGT2_HUMAN  |
| Enzyme 17 PDB ID |
Not Available |
| Enzyme 17 Cellular Location |
Not Available |
| Enzyme 17 Gene Sequence |
>1545 bp
ATGACTCTAATCTGGAGACATTTGCTGAGACCCTTGTGCCTGGTCACTTCCGCTCCCAGG
ATCCTTGAGATGCATCCTTTCCTGAGCCTAGGTACTTCCCGGACATCAGTAACCAAGCTC
AGTCTTCATACAAAGCCCAGAATGCCTCCATGTGACTTCATGCCTGAAAGATACCAGTCC
CTTGGCTACAACCGTGTCCTGGAAATCCACAAGGAACATCTTTCTCCTGTGGTGACGGCA
TATTTCCAGAAACCCCTGCTGCTCCACCAGGGGCACATGGAGTGGCTCTTTGATGCTGAA
GGAAGCAGATACCTGGATTTCTTTTCCGGGATTGTTACTGTCAGTGTTGGCCATTGCCAC
CCAAAGGTGAATGCAGTGGCACAAAAGCAGCTCGGCCGCCTGTGGCATACAAGCACCGTC
TTCTTCCACCCTCCAATGCATGAATATGCAGAGAAGCTTGCCGCACTTCTTCCTGAGCCT
CTTAAGGTCATTTTCTTGGTGAACAGTGGCTCAGAAGCCAATGAGCTGGCCATGCTGATG
GCCAGGGCGCACTCAAACAACATAGACATCATTTCTTTCAGAGGAGCCTACCATGGATGC
AGTCCTTACACACTTGGCTTGACAAACGTAGGGACCTACAAGATGGAACTCCCTGGTGGG
ACAGGTTGCCAACCAACAATGTGTCCAGATGTTTTTCGTGGCCCTTGGGGAGGAAGCCAC
TGTCGAGATTCTCCAGTGCAAACAATCAGGAAGTGCAGCTGTGCACCAGACTGCTGCCAA
GCTAAAGATCAGTATATTGAGCAATTCAAAGATACGCTGAGCACATCTGTGGCCAAGTCA
ATTGCTGGATTTTTCGCAGAACCTATTCAAGGTGTGAATGGAGTTGTCCAGTACCCAAAG
GGGTTTCTAAAGGAAGCCTTTGAGCTGGTGCGAGCAAGGGGAGGCGTGTGCATTGCAGAT
GAAGTGCAGACAGGATTTGGAAGGTTGGGCTCTCACTTCTGGGGCTTCCAAACCCACGAT
GTCCTGCCTGACATTGTCACCATGGCTAAAGGGATTGGGAATGGCTTTCCCATGGCAGCA
GTCATAACCACTCCAGAGATTGCCAAATCTTTGGCGAAATGCCTGCAGCACTTCAACACC
TTTGGAGGGAACCCCATGGCCTGTGCCATTGGATCTGCTGTGCTTGAGGTGATTAAAGAA
GAAAATCTACAGGAAAACAGTCAAGAAGTTGGGACCTACATGTTACTAAAGTTTGCTAAG
CTGCGGGATGAATTTGAAATTGTTGGAGACGTCCGAGGCAAAGGTCTCATGATAGGCATA
GAAATGGTGCAGGATAAGATAAGCTGTCGGCCTCTTCCCCGTGAAGAAGTAAATCAGATC
CATGAGGACTGCAAGCACATGGGACTCCTCGTTGGCAGAGGCAGCATTTTTTCTCAGACA
TTTCGCATTGCGCCCTCAATGTGCATCACTAAACCAGAAGTTGATTTTGCAGTAGAAGTA
TTTCGTTCTGCCTTAACCCAACACATGGAAAGAAGAGCTAAGTAA
|
| Enzyme 17 GenBank Gene ID |
AJ292204  |
| Enzyme 17 GeneCard ID |
AGXT2  |
| Enzyme 17 GenAtlas ID |
AGXT2  |
| Enzyme 17 HGNC ID |
HGNC:14412  |
| Enzyme 17 Chromosome Location |
5 |
| Enzyme 17 Locus |
5p13 |
| Enzyme 17 SNPs |
SNPJam Report  |
| Enzyme 17 General References |
- Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed
]
|
| Enzyme 17 Metabolite References |
Not Available |
|
Enzyme 18
[top]
|
| Enzyme 18 ID |
5637 |
| Enzyme 18 Name |
Ornithine aminotransferase, mitochondrial |
| Enzyme 18 Synonyms |
- Ornithine delta-aminotransferase
- Ornithine--oxo-acid aminotransferase
- Ornithine aminotransferase, hepatic form
- Ornithine aminotransferase, renal form
|
| Enzyme 18 Gene Name |
OAT |
| Enzyme 18 Protein Sequence |
>Ornithine aminotransferase, mitochondrial
MFSKLAHLQRFAVLSRGVHSSVASATSVATKKTVQGPPTSDDIFEREYKYGAHNYHPLPV
ALERGKGIYLWDVEGRKYFDFLSSYSAVNQGHCHPKIVNALKSQVDKLTLTSRAFYNNVL
GEYEEYITKLFNYHKVLPMNTGVEAGETACKLARKWGYTVKGIQKYKAKIVFAAGNFWGR
TLSAISSSTDPTSYDGFGPFMPGFDIIPYNDLPALERALQDPNVAAFMVEPIQGEAGVVV
PDPGYLMGVRELCTRHQVLFIADEIQTGLARTGRWLAVDYENVRPDIVLLGKALSGGLYP
VSAVLCDDDIMLTIKPGEHGSTYGGNPLGCRVAIAALEVLEEENLAENADKLGIILRNEL
MKLPSDVVTAVRGKGLLNAIVIKETKDWDAWKVCLRLRDNGLLAKPTHGDIIRFAPPLVI
KEDELRESIEIINKTILSF
|
| Enzyme 18 Number of Residues |
439 |
| Enzyme 18 Molecular Weight |
48534.4 |
| Enzyme 18 Theoretical pI |
7.05 |
| Enzyme 18 GO Classification |
| Function |
- binding
- catalytic activity
- cofactor binding
- pyridoxal phosphate binding
- transaminase activity
- transferase activity
- transferase activity, transferring nitrogenous groups
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 18 General Function |
Involved in transaminase activity |
| Enzyme 18 Specific Function |
L-ornithine + a 2-oxo acid = L-glutamate 5- semialdehyde + an L-amino acid |
| Enzyme 18 Pathways |
- Arginine and Proline Metabolism (map00330
)
|
| Enzyme 18 Reactions |
- L-ornithine + a 2-oxo acid = L-glutamate 5-semialdehyde + an L-amino acid [RN:R01343]
|
| Enzyme 18 Pfam Domain Function |
|
| Enzyme 18 Signals |
|
| Enzyme 18 Transmembrane Regions |
|
| Enzyme 18 Essentiality |
Not Available |
| Enzyme 18 GenBank ID Protein |
189069120  |
| Enzyme 18 UniProtKB/Swiss-Prot ID |
P04181  |
| Enzyme 18 UniProtKB/Swiss-Prot Entry Name |
OAT_HUMAN  |
| Enzyme 18 PDB ID |
1OAT  |
| Enzyme 18 PDB File |
Show |
| Enzyme 18 3D Structure |
|
| Enzyme 18 Cellular Location |
Not Available |
| Enzyme 18 Gene Sequence |
>1320 bp
ATGTTTTCCAAACTAGCACATTTGCAGAGGTTTGCTGTACTTAGTCGCGGAGTTCATTCT
TCAGTGGCTTCTGCTACATCTGTTGCAACTAAAAAAACAGTCCAAGGCCCTCCAACCTCT
GATGACATTTTTGAAAGGGAATATAAGTATGGTGCACACAACTACCATCCTTTACCTGTA
GCCCTGGAGAGAGGAAAAGGTATTTACTTATGGGATGTAGAAGGCAGAAAATATTTTGAC
TTCCTGAGTTCTTACAGTGCTGTCAACCAAGGGCATTGTCACCCCAAGATTGTGAATGCT
CTGAAGAGTCAAGTGGACAAATTGACCTTAACATCTAGAGCTTTCTATAATAACGTACTT
GGTGAATATGAGGAGTATATTACTAAACTTTTCAACTACCACAAAGTTCTTCCTATGAAT
ACAGGAGTGGAGGCTGGAGAGACTGCCTGTAAACTAGCTCGTAAGTGGGGCTATACCGTG
AAGGGCATTCAGAAATACAAAGCAAAGATTGTTTTTGCAGCTGGGAACTTCTGGGGTAGG
ACGTTGTCTGCTATCTCCAGTTCCACAGACCCAACCAGTTACGATGGTTTTGGACCATTT
ATGCCGGGATTCGACATCATTCCCTATAATGATCTGCCCGCACTGGAGCGTGCTCTTCAG
GATCCAAATGTGGCTGCGTTCATGGTAGAACCAATTCAGGGTGAAGCAGGCGTTGTTGTT
CCGGATCCAGGTTACCTAATGGGAGTGCGAGAGCTCTGCACCAGGCACCAGGTTCTCTTT
ATTGCTGATGAAATACAGACAGGATTGGCCAGAACTGGTAGATGGCTGGCTGTTGATTAT
GAAAATGTCAGACCTGATATAGTCCTCCTTGGAAAGGCCCTTTCTGGGGGCTTATACCCT
GTGTCTGCAGTGCTGTGTGATGATGACATCATGCTGACCATTAAGCCAGGGGAGCATGGG
TCCACATACGGTGGCAATCCACTAGGCTGCCGAGTGGCCATCGCAGCCCTTGAGGTTTTA
GAAGAAGAAAACCTTGCTGAAAATGCAGACAAATTGGGCATTATCTTGAGAAATGAACTC
ATGAAGCTACCTTCTGATGTTGTAACTGCCGTAAGAGGAAAAGGATTATTAAATGCTATT
GTCATTAAAGAAACCAAAGATTGGGATGCTTGGAAGGTGTGTCTACGACTTCGAGATAAT
GGACTTCTGGCCAAGCCAACCCATGGCGACATTATCAGGTTTGCGCCTCCGCTGGTGATC
AAGGAGGATGAGCTTCGAGAGTCCATTGAAATTATTAACAAGACCATCTTGTCTTTCTGA
|
| Enzyme 18 GenBank Gene ID |
AK312561  |
| Enzyme 18 GeneCard ID |
OAT  |
| Enzyme 18 GenAtlas ID |
OAT  |
| Enzyme 18 HGNC ID |
HGNC:8091  |
| Enzyme 18 Chromosome Location |
1 |
| Enzyme 18 Locus |
10q26 |
| Enzyme 18 SNPs |
SNPJam Report  |
| Enzyme 18 General References |
- Inana G, Totsuka S, Redmond M, Dougherty T, Nagle J, Shiono T, Ohura T, Kominami E, Katunuma N: Molecular cloning of human ornithine aminotransferase mRNA. Proc Natl Acad Sci U S A. 1986 Mar;83(5):1203-7. [PubMed
]
- Ramesh V, Shaffer MM, Allaire JM, Shih VE, Gusella JF: Investigation of gyrate atrophy using a cDNA clone for human ornithine aminotransferase. DNA. 1986 Dec;5(6):493-501. [PubMed
]
- Kobayashi T, Nishii M, Takagi Y, Titani K, Matsuzawa T: Molecular cloning and nucleotide sequence analysis of mRNA for human kidney ornithine aminotransferase. An examination of ornithine aminotransferase isozymes between liver and kidney. FEBS Lett. 1989 Sep 25;255(2):300-4. [PubMed
]
- Mitchell GA, Looney JE, Brody LC, Steel G, Suchanek M, Engelhardt JF, Willard HF, Valle D: Human ornithine-delta-aminotransferase. cDNA cloning and analysis of the structural gene. J Biol Chem. 1988 Oct 5;263(28):14288-95. [PubMed
]
- Zintz CB, Inana G: Analysis of the human ornithine aminotransferase gene family. Exp Eye Res. 1990 Jun;50(6):759-70. [PubMed
]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
- Deloukas P, Earthrowl ME, Grafham DV, Rubenfield M, French L, Steward CA, Sims SK, Jones MC, Searle S, Scott C, Howe K, Hunt SE, Andrews TD, Gilbert JG, Swarbreck D, Ashurst JL, Taylor A, Battles J, Bird CP, Ainscough R, Almeida JP, Ashwell RI, Ambrose KD, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Bates K, Beasley H, Bray-Allen S, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Cahill P, Camire D, Carter NP, Chapman JC, Clark SY, Clarke G, Clee CM, Clegg S, Corby N, Coulson A, Dhami P, Dutta I, Dunn M, Faulkner L, Frankish A, Frankland JA, Garner P, Garnett J, Gribble S, Griffiths C, Grocock R, Gustafson E, Hammond S, Harley JL, Hart E, Heath PD, Ho TP, Hopkins B, Horne J, Howden PJ, Huckle E, Hynds C, Johnson C, Johnson D, Kana A, Kay M, Kimberley AM, Kershaw JK, Kokkinaki M, Laird GK, Lawlor S, Lee HM, Leongamornlert DA, Laird G, Lloyd C, Lloyd DM, Loveland J, Lovell J, McLaren S, McLay KE, McMurray A, Mashreghi-Mohammadi M, Matthews L, Milne S, Nickerson T, Nguyen M, Overton-Larty E, Palmer SA, Pearce AV, Peck AI, Pelan S, Phillimore B, Porter K, Rice CM, Rogosin A, Ross MT, Sarafidou T, Sehra HK, Shownkeen R, Skuce CD, Smith M, Standring L, Sycamore N, Tester J, Thorpe A, Torcasso W, Tracey A, Tromans A, Tsolas J, Wall M, Walsh J, Wang H, Weinstock K, West AP, Willey DL, Whitehead SL, Wilming L, Wray PW, Young L, Chen Y, Lovering RC, Moschonas NK, Siebert R, Fechtel K, Bentley D, Durbin R, Hubbard T, Doucette-Stamm L, Beck S, Smith DR, Rogers J: The DNA sequence and comparative analysis of human chromosome 10. Nature. 2004 May 27;429(6990):375-81. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Ramesh V, Gusella JF, Shih VE: Molecular pathology of gyrate atrophy of the choroid and retina due to ornithine aminotransferase deficiency. Mol Biol Med. 1991 Feb;8(1):81-93. [PubMed
]
- Simmaco M, John RA, Barra D, Bossa F: The primary structure of ornithine aminotransferase. Identification of active-site sequence and site of post-translational proteolysis. FEBS Lett. 1986 Apr 7;199(1):39-42. [PubMed
]
- Shah SA, Shen BW, Brunger AT: Human ornithine aminotransferase complexed with L-canaline and gabaculine: structural basis for substrate recognition. Structure. 1997 Aug 15;5(8):1067-75. [PubMed
]
- Shen BW, Hennig M, Hohenester E, Jansonius JN, Schirmer T: Crystal structure of human recombinant ornithine aminotransferase. J Mol Biol. 1998 Mar 20;277(1):81-102. [PubMed
]
- Storici P, Capitani G, Muller R, Schirmer T, Jansonius JN: Crystal structure of human ornithine aminotransferase complexed with the highly specific and potent inhibitor 5-fluoromethylornithine. J Mol Biol. 1999 Jan 8;285(1):297-309. [PubMed
]
- Ramesh V, McClatchey AI, Ramesh N, Benoit LA, Berson EL, Shih VE, Gusella JF: Molecular basis of ornithine aminotransferase deficiency in B-6-responsive and -nonresponsive forms of gyrate atrophy. Proc Natl Acad Sci U S A. 1988 Jun;85(11):3777-80. [PubMed
]
- Inana G, Chambers C, Hotta Y, Inouye L, Filpula D, Pulford S, Shiono T: Point mutation affecting processing of the ornithine aminotransferase precursor protein in gyrate atrophy. J Biol Chem. 1989 Oct 15;264(29):17432-6. [PubMed
]
- Michaud J, Brody LC, Steel G, Fontaine G, Martin LS, Valle D, Mitchell G: Strand-separating conformational polymorphism analysis: efficacy of detection of point mutations in the human ornithine delta-aminotransferase gene. Genomics. 1992 Jun;13(2):389-94. [PubMed
]
- Brody LC, Mitchell GA, Obie C, Michaud J, Steel G, Fontaine G, Robert MF, Sipila I, Kaiser-Kupfer M, Valle D: Ornithine delta-aminotransferase mutations in gyrate atrophy. Allelic heterogeneity and functional consequences. J Biol Chem. 1992 Feb 15;267(5):3302-7. [PubMed
]
- Michaud J, Thompson GN, Brody LC, Steel G, Obie C, Fontaine G, Schappert K, Keith CG, Valle D, Mitchell GA: Pyridoxine-responsive gyrate atrophy of the choroid and retina: clinical and biochemical correlates of the mutation A226V. Am J Hum Genet. 1995 Mar;56(3):616-22. [PubMed
]
- Kobayashi T, Ogawa H, Kasahara M, Shiozawa Z, Matsuzawa T: A single amino acid substitution within the mature sequence of ornithine aminotransferase obstructs mitochondrial entry of the precursor. Am J Hum Genet. 1995 Aug;57(2):284-91. [PubMed
]
|
| Enzyme 18 Metabolite References |
Not Available |
|
Enzyme 19
[top]
|
| Enzyme 19 ID |
5703 |
| Enzyme 19 Name |
Kynurenine--oxoglutarate transaminase 1 |
| Enzyme 19 Synonyms |
- Cysteine-S-conjugate beta-lyase
- Glutamine transaminase K
- GTK
- Glutamine--phenylpyruvate transaminase
- Kynurenine aminotransferase I
- KATI
- Kynurenine--oxoglutarate transaminase I
|
| Enzyme 19 Gene Name |
CCBL1 |
| Enzyme 19 Protein Sequence |
>Kynurenine--oxoglutarate transaminase 1
MAKQLQARRLDGIDYNPWVEFVKLASEHDVVNLGQGFPDFPPPDFAVEAFQHAVSGDFML
NQYTKTFGYPPLTKILASFFGELLGQEIDPLRNVLVTVGGYGALFTAFQALVDEGDEVII
IEPFFDCYEPMTMMAGGRPVFVSLKPGPIQNGELGSSSNWQLDPMELAGKFTSRTKALVL
NTPNNPLGKVFSREELELVASLCQQHDVVCITDEVYQWMVYDGHQHISIASLPGMWERTL
TIGSAGKTFSATGWKVGWVLGPDHIMKHLRTVHQNSVFHCPTQSQAAVAESFEREQLLFR
QPSSYFVQFPQAMQRCRDHMIRSLQSVGLKPIIPQGSYFLITDISDFKRKMPDLPGAVDE
PYDRRFVKWMIKNKGLVAIPVSIFYSVPHQKHFDHYIRFCFVKDEATLQAMDEKLRKWKV
EL
|
| Enzyme 19 Number of Residues |
422 |
| Enzyme 19 Molecular Weight |
47874.8 |
| Enzyme 19 Theoretical pI |
6.45 |
| Enzyme 19 GO Classification |
| Function |
- 1-aminocyclopropane-1-carboxylate synthase activity
- binding
- carbon-sulfur lyase activity
- catalytic activity
- cofactor binding
- lyase activity
- pyridoxal phosphate binding
- transferase activity
- transferase activity, transferring nitrogenous groups
|
| Process |
- biosynthetic process
- metabolic process
|
| Component |
| — |
|
| Enzyme 19 General Function |
Involved in 1-aminocyclopropane-1-carboxylate synthase activity |
| Enzyme 19 Specific Function |
Catalyzes the irreversible transamination of the L- tryptophan metabolite L-kynurenine to form kynurenic acid (KA). Metabolizes the cysteine conjugates of certain halogenated alkenes and alkanes to form reactive metabolites. Catalyzes the beta- elimination of S-conjugates and Se-conjugates of L- (seleno)cysteine, resulting in the cleavage of the C-S or C-Se bond |
| Enzyme 19 Pathways |
|
| Enzyme 19 Reactions |
- RS-CH2-CH(NH3+)COO- = RSH + NH3 + pyruvate [RN:R03528]
|
| Enzyme 19 Pfam Domain Function |
|
| Enzyme 19 Signals |
|
| Enzyme 19 Transmembrane Regions |
|
| Enzyme 19 Essentiality |
Not Available |
| Enzyme 19 GenBank ID Protein |
758591  |
| Enzyme 19 UniProtKB/Swiss-Prot ID |
Q16773  |
| Enzyme 19 UniProtKB/Swiss-Prot Entry Name |
KAT1_HUMAN  |
| Enzyme 19 PDB ID |
1W7N  |
| Enzyme 19 PDB File |
Show |
| Enzyme 19 3D Structure |
|
| Enzyme 19 Cellular Location |
Not Available |
| Enzyme 19 Gene Sequence |
>1269 bp
ATGGCCAAACAGCTGCAGGCCCGAAGGCTAGACGGGATCGACTACAACCCCTGGGTGGAG
TTTGTGAAACTGGCCAGTGAGCATGACGTCGTGAACTTGGGCCAGGGCTTCCCGGATTTC
CCACCACCAGACTTTGCCGTGGAAGCCTTTCAGCACGCTGTCAGTGGAGACTTCATGCTT
AACCAGTACACCAAGACATTTGGTTACCCACCACTGACGAAGATCCTGGCAAGTTTCTTT
GGGGAGCTGCTGGGTCAGGAGATAGACCCGCTCAGGAATGTGCTGGTGACTGTTGGTGGC
TATGGGGCCCTGTTCACAGCCTTCCAGGCCCTGGTGGACGAAGGAGACGAGGTCATCATC
ATCGAACCCTTTTTTGACTGCTACGAGCCCATGACAATGATGGCAGGGGGTCGTCCTGTG
TTTGTGTCCCTGAAGCCGGGTCCCATCCAGAATGGAGAACTGGGTTCCAGCAGCAACTGG
CAGCTGGACCCCATGGAGCTGGCCGGCAAATTCACATCACGCACCAAAGCCCTGGTCCTC
AACACCCCCAACAACCCCCTGGGCAAGGTGTTCTCCAGGGAAGAGCTGGAGCTGGTGGCC
AGCCTTTGCCAGCAGCATGACGTGGTGTGTATCACTGATGAAGTCTACCAGTGGATGGTC
TACGACGGGCACCAGCACATCAGCATTGCCAGCCTCCCTGGCATGTGGGAACGGACCCTG
ACCATCGGCAGCGCCGGCAAGACCTTCAGCGCCACTGGCTGGAAGGTGGGCTGGGTCCTG
GGTCCAGATCACATCATGAAGCACCTGCGGACCGTGCACCAGAACTCCGTCTTCCACTGC
CCCACGCAGAGCCAGGCTGCAGTAGCCGAGAGCTTTGAACGGGAGCAGCTGCTCTTCCGC
CAACCCAGCAGCTACTTTGTGCAGTTCCCGCAGGCCATGCAGCGCTGCCGTGACCACATG
ATACGTAGCCTACAGTCAGTGGGCCTGAAGCCCATCATCCCTCAGGGCAGCTACTTCCTC
ATCACAGACATCTCAGACTTCAAGAGGAAGATGCCTGACTTGCCTGGAGCTGTGGATGAG
CCCTATGACAGACGCTTCGTCAAGTGGATGATCAAGAACAAGGGCTTGGTGGCCATCCCT
GTCTCCATCTTCTATAGTGTGCCACATCAGAAGCACTTTGACCACTATATCCGCTTCTGT
TTTGTGAAGGATGAAGCCACGCTCCAGGCCATGGACGAGAAGCTGCGGAAGTGGAAGGTG
GAACTCTAG
|
| Enzyme 19 GenBank Gene ID |
X82224  |
| Enzyme 19 GeneCard ID |
CCBL1  |
| Enzyme 19 GenAtlas ID |
CCBL1  |
| Enzyme 19 HGNC ID |
HGNC:1564  |
| Enzyme 19 Chromosome Location |
9 |
| Enzyme 19 Locus |
9q34.11 |
| Enzyme 19 SNPs |
SNPJam Report  |
| Enzyme 19 General References |
- Perry S, Harries H, Scholfield C, Lock T, King L, Gibson G, Goldfarb P: Molecular cloning and expression of a cDNA for human kidney cysteine conjugate beta-lyase. FEBS Lett. 1995 Mar 6;360(3):277-80. [PubMed
]
- Humphray SJ, Oliver K, Hunt AR, Plumb RW, Loveland JE, Howe KL, Andrews TD, Searle S, Hunt SE, Scott CE, Jones MC, Ainscough R, Almeida JP, Ambrose KD, Ashwell RI, Babbage AK, Babbage S, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beasley H, Beasley O, Bird CP, Bray-Allen S, Brown AJ, Brown JY, Burford D, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Chen Y, Clarke G, Clark SY, Clee CM, Clegg S, Collier RE, Corby N, Crosier M, Cummings AT, Davies J, Dhami P, Dunn M, Dutta I, Dyer LW, Earthrowl ME, Faulkner L, Fleming CJ, Frankish A, Frankland JA, French L, Fricker DG, Garner P, Garnett J, Ghori J, Gilbert JG, Glison C, Grafham DV, Gribble S, Griffiths C, Griffiths-Jones S, Grocock R, Guy J, Hall RE, Hammond S, Harley JL, Harrison ES, Hart EA, Heath PD, Henderson CD, Hopkins BL, Howard PJ, Howden PJ, Huckle E, Johnson C, Johnson D, Joy AA, Kay M, Keenan S, Kershaw JK, Kimberley AM, King A, Knights A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd C, Lloyd DM, Lovell J, Martin S, Mashreghi-Mohammadi M, Matthews L, McLaren S, McLay KE, McMurray A, Milne S, Nickerson T, Nisbett J, Nordsiek G, Pearce AV, Peck AI, Porter KM, Pandian R, Pelan S, Phillimore B, Povey S, Ramsey Y, Rand V, Scharfe M, Sehra HK, Shownkeen R, Sims SK, Skuce CD, Smith M, Steward CA, Swarbreck D, Sycamore N, Tester J, Thorpe A, Tracey A, Tromans A, Thomas DW, Wall M, Wallis JM, West AP, Whitehead SL, Willey DL, Williams SA, Wilming L, Wray PW, Young L, Ashurst JL, Coulson A, Blocker H, Durbin R, Sulston JE, Hubbard T, Jackson MJ, Bentley DR, Beck S, Rogers J, Dunham I: DNA sequence and analysis of human chromosome 9. Nature. 2004 May 27;429(6990):369-74. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Rossi F, Han Q, Li J, Li J, Rizzi M: Crystal structure of human kynurenine aminotransferase I. J Biol Chem. 2004 Nov 26;279(48):50214-20. Epub 2004 Sep 10. [PubMed
]
- Han Q, Robinson H, Cai T, Tagle DA, Li J: Structural insight into the inhibition of human kynurenine aminotransferase I/glutamine transaminase K. J Med Chem. 2009 May 14;52(9):2786-93. [PubMed
]
|
| Enzyme 19 Metabolite References |
Not Available |
|
Enzyme 20
[top]
|
| Enzyme 20 ID |
5763 |
| Enzyme 20 Name |
Branched-chain-amino-acid aminotransferase, mitochondrial |
| Enzyme 20 Synonyms |
- BCAT(m)
- Placental protein 18
- PP18
|
| Enzyme 20 Gene Name |
BCAT2 |
| Enzyme 20 Protein Sequence |
>Branched-chain-amino-acid aminotransferase, mitochondrial
MAAAALGQIWARKLLSVPWLLCGPRRYASSSFKAADLQLEMTQKPHKKPGPGEPLVFGKT
FTDHMLMVEWNDKGWGQPRIQPFQNLTLHPASSSLHYSLQLFEGMKAFKGKDQQVRLFRP
WLNMDRMLRSAMRLCLPSFDKLELLECIRRLIEVDKDWVPDAAGTSLYVRPVLIGNEPSL
GVSQPTRALLFVILCPVGAYFPGGSVTPVSLLADPAFIRAWVGGVGNYKLGGNYGPTVLV
QQEALKRGCEQVLWLYGPDHQLTEVGTMNIFVYWTHEDGVLELVTPPLNGVILPGVVRQS
LLDMAQTWGEFRVVERTITMKQLLRALEEGRVREVFGSGTACQVCPVHRILYKDRNLHIP
TMENGPELILRFQKELKEIQYGIRAHEWMFPV
|
| Enzyme 20 Number of Residues |
392 |
| Enzyme 20 Molecular Weight |
44287.4 |
| Enzyme 20 Theoretical pI |
8.82 |
| Enzyme 20 GO Classification |
| Function |
- branched-chain-amino-acid transaminase activity
- catalytic activity
- transaminase activity
- transferase activity
- transferase activity, transferring nitrogenous groups
|
| Process |
- branched chain family amino acid metabolic process
- cellular amino acid and derivative metabolic process
- cellular amino acid metabolic process
- cellular metabolic process
- metabolic process
|
| Component |
| — |
|
| Enzyme 20 General Function |
Involved in catalytic activity |
| Enzyme 20 Specific Function |
Catalyzes the first reaction in the catabolism of the essential branched chain amino acids leucine, isoleucine, and valine. May also function as a transporter of branched chain alpha-keto acids |
| Enzyme 20 Pathways |
- Pantothenate and CoA Biosynthesis (map00770
)
- Valine, Leucine and Isoleucine Degradation (map00280
)
|
| Enzyme 20 Reactions |
- L-leucine + 2-oxoglutarate = 4-methyl-2-oxopentanoate + L-glutamate [RN:R01090]
|
| Enzyme 20 Pfam Domain Function |
|
| Enzyme 20 Signals |
|
| Enzyme 20 Transmembrane Regions |
|
| Enzyme 20 Essentiality |
Not Available |
| Enzyme 20 GenBank ID Protein |
13699234  |
| Enzyme 20 UniProtKB/Swiss-Prot ID |
O15382  |
| Enzyme 20 UniProtKB/Swiss-Prot Entry Name |
BCAT2_HUMAN  |
| Enzyme 20 PDB ID |
1KTA  |
| Enzyme 20 PDB File |
Show |
| Enzyme 20 3D Structure |
|
| Enzyme 20 Cellular Location |
Not Available |
| Enzyme 20 Gene Sequence |
>1179 bp
ATGGCCGCAGCCGCTCTGGGGCAGATCTGGGCACGAAAGCTTCTCTCTGTCCCTTGGCTT
CTGTGTGGTCCCAGAAGATATGCCTCCTCCAGTTTCAAGGCTGCAGACCTGCAGCTGGAA
ATGACACAGAAGCCTCATAAGAAGCCTGGCCCCGGCGAGCCCCTGGTGTTTGGGAAGACA
TTTACCGACCACATGCTGATGGTGGAATGGAATGACAAGGGCTGGGGCCAGCCCCGAATC
CAGCCCTTCCAGAACCTCACGCTGCACCCAGCCTCCTCCAGCCTCCACTACTCCCTGCAG
CTGTTTGAGGGCATGAAGGCGTTCAAAGGCAAAGACCAGCAGGTGCGCCTCTTCCGCCCC
TGGCTCAACATGGACCGGATGCTGCGCTCAGCCATGCGCCTGTGCCTGCCGAGTTTCGAC
AAGCTGGAGTTGCTGGAGTGCATCCGCCGGCTCATCGAAGTGGACAAGGACTGGGTCCCC
GATGCCGCCGGCACCAGCCTCTATGTGCGGCCTGTGCTCATTGGGAACGAGCCCTCGCTG
GGTGTCAGCCAGCCCACGCGCGCGCTCCTGTTCGTCATTCTCTGCCCAGTGGGTGCCTAC
TTCCCTGGAGGCTCCGTGACCCCGGTCTCCCTCCTGGCCGACCCAGCCTTCATCCGGGCC
TGGGTGGGCGGGGTCGGCAACTACAAGTTAGGTGGGAATTATGGGCCCACCGTGTTAGTG
CAACAGGAGGCACTCAAGCGGGGCTGTGAACAGGTCCTCTGGCTGTATGGGCCCGACCAC
CAGCTCACCGAGGTGGGAACCATGAACATCTTTGTCTACTGGACCCACGAAGATGGGGTG
CTGGAGCTGGTGACGCCCCCGCTGAATGGTGTTATCCTGCCTGGAGTGGTCAGACAGAGT
CTACTGGACATGGCTCAGACCTGGGGTGAGTTCCGGGTGGTGGAGCGCACGATCACCATG
AAGCAGTTGCTGCGGGCCCTGGAGGAGGGCCGCGTGCGGGAAGTCTTTGGCTCGGGCACC
GCTTGCCAGGTCTGCCCAGTGCACCGAATCCTGTACAAAGACAGGAACCTCCACATTCCC
ACCATGGAAAATGGGCCTGAGCTGATCCTCCGCTTCCAGAAGGAGCTGAAGGAGATCCAG
TACGGAATCAGAGCCCACGAGTGGATGTTCCCGGTGTGA
|
| Enzyme 20 GenBank Gene ID |
AF268047  |
| Enzyme 20 GeneCard ID |
BCAT2  |
| Enzyme 20 GenAtlas ID |
BCAT2  |
| Enzyme 20 HGNC ID |
HGNC:977  |
| Enzyme 20 Chromosome Location |
1 |
| Enzyme 20 Locus |
19q13 |
| Enzyme 20 SNPs |
SNPJam Report  |
| Enzyme 20 General References |
- Bledsoe RK, Dawson PA, Hutson SM: Cloning of the rat and human mitochondrial branched chain aminotransferases (BCATm). Biochim Biophys Acta. 1997 Apr 25;1339(1):9-13. [PubMed
]
- Than NG, Sumegi B, Than GN, Bellyei S, Bohn H: Molecular cloning and characterization of placental tissue protein 18 (PP18a)/human mitochondrial branched-chain aminotransferase (BCATm) and its novel alternatively spliced PP18b variant. Placenta. 2001 Feb-Mar;22(2-3):235-43. [PubMed
]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Eden A, Simchen G, Benvenisty N: Two yeast homologs of ECA39, a target for c-Myc regulation, code for cytosolic and mitochondrial branched-chain amino acid aminotransferases. J Biol Chem. 1996 Aug 23;271(34):20242-5. [PubMed
]
- Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed
]
- Yennawar N, Dunbar J, Conway M, Hutson S, Farber G: The structure of human mitochondrial branched-chain aminotransferase. Acta Crystallogr D Biol Crystallogr. 2001 Apr;57(Pt 4):506-15. [PubMed
]
- Yennawar NH, Conway ME, Yennawar HP, Farber GK, Hutson SM: Crystal structures of human mitochondrial branched chain aminotransferase reaction intermediates: ketimine and pyridoxamine phosphate forms. Biochemistry. 2002 Oct 1;41(39):11592-601. [PubMed
]
- Goto M, Miyahara I, Hirotsu K, Conway M, Yennawar N, Islam MM, Hutson SM: Structural determinants for branched-chain aminotransferase isozyme-specific inhibition by the anticonvulsant drug gabapentin. J Biol Chem. 2005 Nov 4;280(44):37246-56. Epub 2005 Sep 1. [PubMed
]
- Yennawar NH, Islam MM, Conway M, Wallin R, Hutson SM: Human mitochondrial branched chain aminotransferase isozyme: structural role of the CXXC center in catalysis. J Biol Chem. 2006 Dec 22;281(51):39660-71. Epub 2006 Oct 18. [PubMed
]
|
| Enzyme 20 Metabolite References |
Not Available |
|
Enzyme 21
[top]
|
| Enzyme 21 ID |
5789 |
| Enzyme 21 Name |
Cystathionine gamma-lyase |
| Enzyme 21 Synonyms |
- Gamma-cystathionase
|
| Enzyme 21 Gene Name |
CTH |
| Enzyme 21 Protein Sequence |
>Cystathionine gamma-lyase
MQEKDASSQGFLPHFQHFATQAIHVGQDPEQWTSRAVVPPISLSTTFKQGAPGQHSGFEY
SRSGNPTRNCLEKAVAALDGAKYCLAFASGLAATVTITHLLKAGDQIICMDDVYGGTNRY
FRQVASEFGLKISFVDCSKIKLLEAAITPETKLVWIETPTNPTQKVIDIEGCAHIVHKHG
DIILVVDNTFMSPYFQRPLALGADISMYSATKYMNGHSDVVMGLVSVNCESLHNRLRFLQ
NSLGAVPSPIDCYLCNRGLKTLHVRMEKHFKNGMAVAQFLESNPWVEKVIYPGLPSHPQH
ELVKRQCTGCTGMVTFYIKGTLQHAEIFLKNLKLFTLAESLGGFESLAELPAIMTHASVL
KNDRDVLGISDTLIRLSVGLEDEEDLLEDLDQALKAAHPPSGSHS
|
| Enzyme 21 Number of Residues |
405 |
| Enzyme 21 Molecular Weight |
44507.6 |
| Enzyme 21 Theoretical pI |
6.69 |
| Enzyme 21 GO Classification |
| Function |
- binding
- catalytic activity
- cofactor binding
- pyridoxal phosphate binding
|
| Process |
- cellular amino acid and derivative metabolic process
- cellular amino acid metabolic process
- cellular metabolic process
- metabolic process
|
| Component |
| — |
|
| Enzyme 21 General Function |
Involved in pyridoxal phosphate binding |
| Enzyme 21 Specific Function |
Catalyzes the last step in the transsulfuration pathway from methionine to cysteine. Has broad substrate specificity. Converts cystathionine to cysteine, ammonia and 2-oxobutanoate. Converts two cysteine molecules to lanthionine and hydrogen sulfide. Can also accept homocysteine as substrate. Specificity depends on the levels of the endogenous substrates. Generates the endogenous signaling molecule hydrogen sulfide (H2S), and so contributes to the regulation of blood pressure |
| Enzyme 21 Pathways |
|
| Enzyme 21 Reactions |
- (1) L-cystathionine + H2O = L-cysteine + NH3 + 2-oxobutanoate (overall reaction) [RN:R01001]
- (2) (1a) L-cystathionine = L-cysteine + 2-ammoniobut-2-enoate [RN:R08632]
- (3) (1b) 2-ammoniobut-2-enoate + H2O = 2-oxobutanoate + NH3 (spontaneous) [RN:R08637]
|
| Enzyme 21 Pfam Domain Function |
|
| Enzyme 21 Signals |
|
| Enzyme 21 Transmembrane Regions |
|
| Enzyme 21 Essentiality |
Not Available |
| Enzyme 21 GenBank ID Protein |
62898313  |
| Enzyme 21 UniProtKB/Swiss-Prot ID |
P32929  |
| Enzyme 21 UniProtKB/Swiss-Prot Entry Name |
CGL_HUMAN  |
| Enzyme 21 PDB ID |
Not Available |
| Enzyme 21 Cellular Location |
Not Available |
| Enzyme 21 Gene Sequence |
>1218 bp
ATGCAGGAAAAAGACGCCTCCTCACAAGGTTTCCTGCCACACTTCCAACATTTCGCCACG
CAGGCGATCCATGTGGGCCAGGATCCAGAGCAATGGACCTCCAGGGCTGTAGTGCCCCCC
ATCTCACTGTCCACCACGTTCAAGCAAGGGGCGCCTGGCCAGCACTCGGGTTTTGAATAT
AGCCGTTCTGGAAATCCCACTAGGAATTGCCTTGAAAAAGCAGTGGCAGCACTGGATGGG
GCTAAGTACTGTTTGGCCTTTGCTTCAGGTTTAGCAGCCACTGTAACTATTACCCATCTT
TTAAAAGCAGGAGACCAAATTATTTGTATGGATGATGTGTATGGAGGTACAAACAGGTAC
TTCAGGCAAGTGGCATCTGAATTTGGATTAAAGATTTCTTTTGTTGATTGTTCCAAAATC
AAATTACTAGAGGCAGCAATTACACCAGAAACCAAGCTTGTTTGGATCGAAACCCCCACA
AACCCCACCCAGAAGGTGATTGACATTGAAGGCTGTGCACATATTGTCCATAAGCATGGA
GACATTATTTTGGTCGTGGATAACACTTTTATGTCACCATATTTCCAGCGCCCTTTGGCT
CTGGGAGCTGATATTTCTATGTATTCTGCAACAAAATACATGAATGGCCACAGTGATGTT
GTAATGGGCCTGGTGTCTGTTAATTGTGAAAGCCTTCATAATAGACTTCGTTTCTTGCAA
AACTCTCTTGGAGCAGTTCCATCTCCTATTGATTGTTACCTCTGCAATCGAGGTCTGAAG
ACTCTACATGTCCGAATGGAAAAGCATTTCAAAAACGGAATGGCAGTTGCCCAGTTCCTG
GAATCTAATCCTTGGGTAGAAAAGGTTATTTATCCTGGGCTGCCCTCTCATCCACAGCAT
GAGTTGGTGAAGCGTCAGTGTACAGGTTGTACAGGGATGGTCACCTTTTATATTAAGGGC
ACTCTTCAGCATGCTGAGATTTTCCTCAAGAACCTAAAGCTATTTACTCTGGCCGAGAGC
TTGGGAGGATTCGAAAGCCTTGCTGAGCTTCCGGCAATCATGACTCATGCATCAGTTCTT
AAGAATGACAGAGATGTCCTTGGAATTAGTGACACACTGATTCGACTTTCTGTGGGCTTA
GAGGATGAGGAAGACCTACTGGAAGATCTAGATCAAGCTTTGAAGGCAGCACACCCTCCA
AGTGGAATTCACAGCTAG
|
| Enzyme 21 GenBank Gene ID |
AK223376  |
| Enzyme 21 GeneCard ID |
CTH  |
| Enzyme 21 GenAtlas ID |
CTH  |
| Enzyme 21 HGNC ID |
HGNC:2501  |
| Enzyme 21 Chromosome Location |
1 |
| Enzyme 21 Locus |
1p31.1 |
| Enzyme 21 SNPs |
SNPJam Report  |
| Enzyme 21 General References |
- Lu Y, O'Dowd BF, Orrego H, Israel Y: Cloning and nucleotide sequence of human liver cDNA encoding for cystathionine gamma-lyase. Biochem Biophys Res Commun. 1992 Dec 15;189(2):749-58. [PubMed
]
- Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Steegborn C, Clausen T, Sondermann P, Jacob U, Worbs M, Marinkovic S, Huber R, Wahl MC: Kinetics and inhibition of recombinant human cystathionine gamma-lyase. Toward the rational control of transsulfuration. J Biol Chem. 1999 Apr 30;274(18):12675-84. [PubMed
]
- Matsuoka S, Ballif BA, Smogorzewska A, McDonald ER 3rd, Hurov KE, Luo J, Bakalarski CE, Zhao Z, Solimini N, Lerenthal Y, Shiloh Y, Gygi SP, Elledge SJ: ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage. Science. 2007 May 25;316(5828):1160-6. [PubMed
]
- Chiku T, Padovani D, Zhu W, Singh S, Vitvitsky V, Banerjee R: H2S biogenesis by human cystathionine gamma-lyase leads to the novel sulfur metabolites lanthionine and homolanthionine and is responsive to the grade of hyperhomocysteinemia. J Biol Chem. 2009 Apr 24;284(17):11601-12. Epub 2009 Mar 4. [PubMed
]
- Sun Q, Collins R, Huang S, Holmberg-Schiavone L, Anand GS, Tan CH, van-den-Berg S, Deng LW, Moore PK, Karlberg T, Sivaraman J: Structural basis for the inhibition mechanism of human cystathionine gamma-lyase, an enzyme responsible for the production of H(2)S. J Biol Chem. 2009 Jan 30;284(5):3076-85. Epub 2008 Nov 19. [PubMed
]
- Wang J, Hegele RA: Genomic basis of cystathioninuria (MIM 219500) revealed by multiple mutations in cystathionine gamma-lyase (CTH). Hum Genet. 2003 Apr;112(4):404-8. Epub 2003 Feb 6. [PubMed
]
- Zhu W, Lin A, Banerjee R: Kinetic properties of polymorphic variants and pathogenic mutants in human cystathionine gamma-lyase. Biochemistry. 2008 Jun 10;47(23):6226-32. Epub 2008 May 14. [PubMed
]
|
| Enzyme 21 Metabolite References |
Not Available |
|
Enzyme 22
[top]
|
| Enzyme 22 ID |
5944 |
| Enzyme 22 Name |
L-serine dehydratase/L-threonine deaminase |
| Enzyme 22 Synonyms |
- SDH
- L-serine deaminase
- L-threonine dehydratase
- TDH
|
| Enzyme 22 Gene Name |
SDS |
| Enzyme 22 Protein Sequence |
>L-serine dehydratase/L-threonine deaminase
MMSGEPLHVKTPIRDSMALSKMAGTSVYLKMDSAQPSGSFKIRGIGHFCKRWAKQGCAHF
VCSSAGNAGMAAAYAARQLGVPATIVVPSTTPALTIERLKNEGATVKVVGELLDEAFELA
KALAKNNPGWVYIPPFDDPLIWEGHASIVKELKETLWEKPGAIALSVGGGGLLCGVVQGL
QEVGWGDVPVIAMETFGAHSFHAATTAGKLVSLPKITSVAKALGVKTVGAQALKLFQEHP
IFSEVISDQEAVAAIEKFVDDEKILVEPACGAALAAVYSHVIQKLQLEGNLRTPLPSLVV
IVCGGSNISLAQLRALKEQLGMTNRLPK
|
| Enzyme 22 Number of Residues |
328 |
| Enzyme 22 Molecular Weight |
34625.1 |
| Enzyme 22 Theoretical pI |
8.14 |
| Enzyme 22 GO Classification |
| Function |
- binding
- catalytic activity
- cofactor binding
- pyridoxal phosphate binding
|
| Process |
- cellular amino acid and derivative metabolic process
- cellular amino acid metabolic process
- cellular metabolic process
- metabolic process
|
| Component |
| — |
|
| Enzyme 22 General Function |
Involved in catalytic activity |
| Enzyme 22 Specific Function |
L-serine = pyruvate + NH(3) |
| Enzyme 22 Pathways |
- Cysteine Metabolism (map00272
)
- Glycine, Serine and Threonine Metabolism (map00260
)
|
| Enzyme 22 Reactions |
- L-threonine = 2-oxobutanoate + NH3 [RN:R00996]
|
| Enzyme 22 Pfam Domain Function |
|
| Enzyme 22 Signals |
|
| Enzyme 22 Transmembrane Regions |
|
| Enzyme 22 Essentiality |
Not Available |
| Enzyme 22 GenBank ID Protein |
158258957  |
| Enzyme 22 UniProtKB/Swiss-Prot ID |
P20132  |
| Enzyme 22 UniProtKB/Swiss-Prot Entry Name |
SDHL_HUMAN  |
| Enzyme 22 PDB ID |
1P5J  |
| Enzyme 22 PDB File |
Show |
| Enzyme 22 3D Structure |
|
| Enzyme 22 Cellular Location |
Not Available |
| Enzyme 22 Gene Sequence |
>987 bp
ATGATGTCTGGAGAACCCCTGCACGTGAAGACCCCCATCCGTGACAGCATGGCCCTGTCC
AAAATGGCCGGCACCAGCGTCTACCTCAAGATGGACAGTGCCCAGCCCTCCGGCTCCTTC
AAGATCCGGGGCATTGGGCACTTCTGCAAGAGGTGGGCCAAGCAAGGCTGTGCACATTTT
GTCTGCTCCTCGGCGGGCAACGCAGGCATGGCGGCTGCATATGCGGCCAGGCAACTCGGC
GTCCCCGCCACCATCGTGGTGCCCAGCACCACACCTGCTCTCACCATTGAGCGCCTCAAG
AATGAAGGTGCCACAGTCAAGGTGGTGGGTGAGTTATTGGATGAAGCCTTCGAGCTGGCC
AAGGCCCTAGCGAAGAACAACCCGGGTTGGGTCTACATTCCCCCCTTTGATGACCCCCTC
ATCTGGGAAGGCCACGCTTCCATCGTGAAAGAGCTGAAGGAGACACTGTGGGAAAAGCCG
GGGGCCATCGCGCTGTCAGTGGGCGGCGGGGGCCTGCTGTGTGGAGTGGTCCAGGGGCTG
CAGGAGGTGGGCTGGGGGGACGTGCCTGTCATCGCCATGGAGACTTTTGGTGCCCACAGC
TTCCACGCTGCCACCACCGCAGGCAAACTTGTCTCCCTGCCCAAGATCACCAGTGTTGCC
AAGGCCCTGGGCGTGAAGACTGTGGGGGCTCAGGCCCTGAAGCTGTTTCAGGAACACCCC
ATTTTCTCTGAAGTTATCTCGGACCAGGAGGCTGTGGCCGCCATTGAGAAGTTCGTGGAT
GATGAGAAGATCCTGGTGGAGCCCGCCTGCGGGGCAGCCCTGGCCGCTGTCTATAGCCAC
GTGATCCAGAAGCTCCAACTGGAGGGGAATCTCCGAACCCCGCTGCCATCCCTCGTGGTC
ATCGTCTGCGGGGGCAGCAACATCAGCCTGGCCCAGCTGCGGGCGCTCAAGGAACAGCTG
GGCATGACAAATAGGTTGCCCAAGTGA
|
| Enzyme 22 GenBank Gene ID |
AK292760  |
| Enzyme 22 GeneCard ID |
SDS  |
| Enzyme 22 GenAtlas ID |
SDS  |
| Enzyme 22 HGNC ID |
HGNC:10691  |
| Enzyme 22 Chromosome Location |
1 |
| Enzyme 22 Locus |
12q24.13 |
| Enzyme 22 SNPs |
SNPJam Report  |
| Enzyme 22 General References |
- Ogawa H, Gomi T, Konishi K, Date T, Nakashima H, Nose K, Matsuda Y, Peraino C, Pitot HC, Fujioka M: Human liver serine dehydratase. cDNA cloning and sequence homology with hydroxyamino acid dehydratases from other sources. J Biol Chem. 1989 Sep 25;264(27):15818-23. [PubMed
]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
- Yamada T, Komoto J, Kasuya T, Takata Y, Ogawa H, Mori H, Takusagawa F: A catalytic mechanism that explains a low catalytic activity of serine dehydratase like-1 from human cancer cells: crystal structure and site-directed mutagenesis studies. Biochim Biophys Acta. 2008 May;1780(5):809-18. Epub 2008 Feb 19. [PubMed
]
- Sun L, Li X, Dong Y, Yang M, Liu Y, Han X, Zhang X, Pang H, Rao Z: Crystallization and preliminary crystallographic analysis of human serine dehydratase. Acta Crystallogr D Biol Crystallogr. 2003 Dec;59(Pt 12):2297-9. Epub 2003 Nov 27. [PubMed
]
|
| Enzyme 22 Metabolite References |
Not Available |
|
Enzyme 23
[top]
|
| Enzyme 23 ID |
5947 |
| Enzyme 23 Name |
Pyridoxine-5'-phosphate oxidase |
| Enzyme 23 Synonyms |
- Pyridoxamine-phosphate oxidase
|
| Enzyme 23 Gene Name |
PNPO |
| Enzyme 23 Protein Sequence |
>Pyridoxine-5'-phosphate oxidase
MTCWLRGVTATFGRPAEWPGYLSHLCGRSAAMDLGPMRKSYRGDREAFEETHLTSLDPVK
QFAAWFEEAVQCPDIGEANAMCLATCTRDGKPSARMLLLKGFGKDGFRFFTNFESRKGKE
LDSNPFASLVFYWEPLNRQVRVEGPVKKLPEEEAECYFHSRPKSSQIGAVVSHQSSVIPD
REYLRKKNEELEQLYQDQEVPKPKSWGGYVLYPQVMEFWQGQTNRLHDRIVFRRGLPTGD
SPLGPMTHRGEEDWLYERLAP
|
| Enzyme 23 Number of Residues |
261 |
| Enzyme 23 Molecular Weight |
29987.8 |
| Enzyme 23 Theoretical pI |
7.09 |
| Enzyme 23 GO Classification |
| Function |
- FMN binding
- binding
- catalytic activity
- nucleotide binding
- oxidoreductase activity
- oxidoreductase activity, acting on the CH-NH2 group of donors
- oxidoreductase activity, acting on the CH-NH2 group of donors, oxygen as acceptor
- pyridoxamine-phosphate oxidase activity
|
| Process |
- metabolic process
- oxidation reduction
- pyridoxine biosynthetic process
- pyridoxine metabolic process
- small molecule metabolic process
- vitamin B6 metabolic process
- vitamin metabolic process
- water-soluble vitamin metabolic process
|
| Component |
| — |
|
| Enzyme 23 General Function |
Involved in pyridoxamine-phosphate oxidase activity |
| Enzyme 23 Specific Function |
Catalyzes the oxidation of either pyridoxine 5'- phosphate (PNP) or pyridoxamine 5'-phosphate (PMP) into pyridoxal 5'-phosphate (PLP) |
| Enzyme 23 Pathways |
|
| Enzyme 23 Reactions |
- (1) pyridoxamine 5'-phosphate + H2O + O2 = pyridoxal 5'-phosphate + NH3 + H2O2 [RN:R00277]
- (2) pyridoxine 5'-phosphate + O2 = pyridoxal 5'-phosphate + H2O2 [RN:R00278]
|
| Enzyme 23 Pfam Domain Function |
|
| Enzyme 23 Signals |
|
| Enzyme 23 Transmembrane Regions |
|
| Enzyme 23 Essentiality |
Not Available |
| Enzyme 23 GenBank ID Protein |
Not Available |
| Enzyme 23 UniProtKB/Swiss-Prot ID |
Q9NVS9  |
| Enzyme 23 UniProtKB/Swiss-Prot Entry Name |
PNPO_HUMAN  |
| Enzyme 23 PDB ID |
1NRG  |
| Enzyme 23 PDB File |
Show |
| Enzyme 23 3D Structure |
|
| Enzyme 23 Cellular Location |
Not Available |
| Enzyme 23 Gene Sequence |
>786 bp
ATGACGTGCTGGCTGCGGGGCGTCACGGCGACGTTCGGGCGACCTGCCGAGTGGCCAGGC
TACCTCAGTCACCTGTGTGGTCGCAGTGCTGCCATGGACCTGGGACCCATGCGCAAGAGT
TACCGCGGGGACCGAGAGGCATTTGAGGAGACTCATCTGACCTCCCTTGACCCAGTGAAA
CAGTTTGCTGCCTGGTTTGAGGAGGCTGTTCAGTGTCCTGACATAGGGGAAGCCAATGCC
ATGTGTCTGGCTACCTGCACCAGAGATGGAAAACCCTCTGCTCGCATGTTGCTGCTGAAG
GGCTTCGGGAAAGATGGCTTCCGCTTCTTCACTAACTTCGAGAGTCGAAAAGGAAAAGAG
CTGGACTCTAATCCCTTTGCTTCCCTTGTCTTCTACTGGGAGCCACTTAACCGTCAGGTG
CGTGTGGAAGGCCCTGTGAAGAAACTGCCTGAGGAGGAGGCTGAGTGCTACTTCCACTCC
CGCCCCAAGAGCAGCCAGATTGGGGCTGTGGTCAGCCACCAGAGTTCTGTGATCCCTGAT
CGGGAGTATCTGAGAAAGAAAAATGAGGAACTGGAACAGCTCTACCAGGATCAAGAGGTG
CCCAAGCCAAAATCCTGGGGTGGCTATGTCCTGTACCCTCAGGTGATGGAGTTCTGGCAA
GGTCAAACCAACCGCCTGCATGACCGGATAGTCTTTCGGCGGGGCCTACCCACAGGAGAT
TCCCCTTTGGGGCCCATGACCCACCGCGGGGAGGAAGACTGGCTCTATGAGAGACTTGCA
CCTTAA
|
| Enzyme 23 GenBank Gene ID |
AF468030  |
| Enzyme 23 GeneCard ID |
PNPO  |
| Enzyme 23 GenAtlas ID |
PNPO  |
| Enzyme 23 HGNC ID |
HGNC:30260  |
| Enzyme 23 Chromosome Location |
1 |
| Enzyme 23 Locus |
17q21.32 |
| Enzyme 23 SNPs |
SNPJam Report  |
| Enzyme 23 General References |
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Molina H, Horn DM, Tang N, Mathivanan S, Pandey A: Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry. Proc Natl Acad Sci U S A. 2007 Feb 13;104(7):2199-204. Epub 2007 Feb 7. [PubMed
]
- Musayev FN, Di Salvo ML, Ko TP, Schirch V, Safo MK: Structure and properties of recombinant human pyridoxine 5'-phosphate oxidase. Protein Sci. 2003 Jul;12(7):1455-63. [PubMed
]
- Mills PB, Surtees RA, Champion MP, Beesley CE, Dalton N, Scambler PJ, Heales SJ, Briddon A, Scheimberg I, Hoffmann GF, Zschocke J, Clayton PT: Neonatal epileptic encephalopathy caused by mutations in the PNPO gene encoding pyridox(am)ine 5'-phosphate oxidase. Hum Mol Genet. 2005 Apr 15;14(8):1077-86. Epub 2005 Mar 16. [PubMed
]
|
| Enzyme 23 Metabolite References |
Not Available |
|
Enzyme 24
[top]
|
| Enzyme 24 ID |
5959 |
| Enzyme 24 Name |
Formimidoyltransferase-cyclodeaminase |
| Enzyme 24 Synonyms |
- Formiminotransferase-cyclodeaminase
- FTCD
- LCHC1
- Glutamate formimidoyltransferase
- Glutamate formiminotransferase
- Glutamate formyltransferase
- Formimidoyltetrahydrofolate cyclodeaminase
- Formiminotetrahydrofolate cyclodeaminase
|
| Enzyme 24 Gene Name |
FTCD |
| Enzyme 24 Protein Sequence |
>Formimidoyltransferase-cyclodeaminase
MSQLVECVPNFSEGKNQEVIDAISGAITQTPGCVLLDVDAGPSTNRTVYTFVGPPECVVE
GALNAARVASRLIDMSRHQGEHPRMGALDVCPFIPVRGVSVDECVLCAQAFGQRLAEELD
VPVYLYGEAARMDSRRTLPAIRAGEYEALPKKLQQADWAPDFGPSSFVPSWGATATGARK
FLIAFNINLLGTKEQAHRIALNLREQGRGKDQPGRLKKVQGIGWYLDEKNLAQVSTNLLD
FEVTALHTVYEETCREAQELSLPVVGSQLVGLVPLKALLDAAAFYCEKENLFILEEEQRI
RLVVSRLGLDSLCPFSPKERIIEYLVPERGPERGLGSKSLRAFVGEVGARSAAPGGGSVA
AAAAAMGAALGSMVGLMTYGRRQFQSLDTTMRRLIPPFREASAKLTTLVDADAEAFTAYL
EAMRLPKNTPEEKDRRTAALQEGLRRAVSVPLTLAETVASLWPALQELARCGNLACRSDL
QVAAKALEMGVFGAYFNVLINLRDITDEAFKDQIHHRVSSLLQEAKTQAALVLDCLETRQ
E
|
| Enzyme 24 Number of Residues |
541 |
| Enzyme 24 Molecular Weight |
58925.9 |
| Enzyme 24 Theoretical pI |
5.45 |
| Enzyme 24 GO Classification |
| Function |
- amino acid binding
- binding
- carboxylic acid binding
- catalytic activity
- folic acid binding
- transferase activity
|
| Process |
- cellular metabolic process
- metabolic process
|
| Component |
| — |
|
| Enzyme 24 General Function |
Involved in catalytic activity |
| Enzyme 24 Specific Function |
Binds and promotes bundling of vimentin filaments originating from the Golgi |
| Enzyme 24 Pathways |
|
| Enzyme 24 Reactions |
- 5-formimidoyltetrahydrofolate = 5,10-methenyltetrahydrofolate + NH3 [RN:R02302]
|
| Enzyme 24 Pfam Domain Function |
|
| Enzyme 24 Signals |
|
| Enzyme 24 Transmembrane Regions |
|
| Enzyme 24 Essentiality |
Not Available |
| Enzyme 24 GenBank ID Protein |
6537208  |
| Enzyme 24 UniProtKB/Swiss-Prot ID |
O95954  |
| Enzyme 24 UniProtKB/Swiss-Prot Entry Name |
FTCD_HUMAN  |
| Enzyme 24 PDB ID |
Not Available |
| Enzyme 24 Cellular Location |
Not Available |
| Enzyme 24 Gene Sequence |
>1626 bp
ATGTCCCAGCTGGTGGAATGCGTCCCCAACTTTTCGGAGGGGAAGAACCAGGAGGTGATC
GACGCCATCTCTGGAGCCATCACACAGACCCCGGGCTGCGTGCTGCTGGATGTGGACGCA
GGCCCTTCCACCAACCGCACCGTGTACACCTTCGTGGGGCCGCCGGAGTGCGTGGTGGAG
GGGGCCCTCAACGCTGCCCGGGTAGCTTCCCGACTTATCGACATGAGCAGGCACCAAGGA
GAGCACCCCCGCATGGGGGCCCTAGACGTCTGCCCCTTCATCCCCGTGAGGGGCGTCAGC
GTGGATGAGTGTGTGCTCTGCGCCCAGGCCTTTGGCCAGAGGCTGGCAGAGGAGCTGGAC
GTGCCAGTTTACCTGTACGGCGAGGCAGCCAGGATGGACAGTCGCCGGACCCTGCCGGCC
ATCCGGGCCGGGGAGTACGAGGCCCTCCCTAAGAAGCTCCAGCAGGCCGACTGGGCGCCC
GACTTTGGTCCCAGCTCCTTTGTCCCCAGTTGGGGGGCCACGGCCACGGGGGCGAGGAAG
TTCCTCATTGCTTTTAACATCAACCTGCTCGGCACAAAGGAGCAAGCCCACCGCATCGCG
CTCAACCTGCGGGAGCAGGGCCGCGGGAAGGACCAGCCAGGACGTCTGAAGAAAGTTCAG
GGCATTGGCTGGTACCTGGATGAGAAGAACCTGGCTCAGGTGTCCACCAATCTTCTGGAC
TTTGAGGTCACGGCACTGCACACGGTCTACGAGGAGACCTGCCGAGAAGCACAGGAGCTG
AGCCTCCCAGTGGTGGGCTCACAGCTGGTGGGCCTGGTGCCCCTGAAGGCTCTGCTGGAT
GCGGCCGCCTTCTACTGCGAGAAGGAGAACCTCTTCATCCTGGAGGAGGAGCAGCGGATC
AGGCTGGTGGTGAGCCGGCTGGGCCTGGACTCCCTGTGCCCCTTCAGCCCTAAGGAGCGG
ATCATCGAGTACCTGGTCCCTGAGCGCGGGCCTGAGCGAGGCCTGGGCAGCAAGTCCCTG
CGCGCCTTCGTGGGGGAGGTGGGTGCCCGCTCTGCGGCCCCCGGGGGCGGCTCGGTGGCG
GCGGCCGCTGCGGCCATGGGTGCGGCGCTGGGCTCCATGGTGGGCCTCATGACCTACGGG
CGGCGCCAATTCCAGTCCCTGGACACGACGATGCGGCGCCTGATCCCGCCCTTCCGCGAG
GCTTCGGCCAAGCTAACCACGCTGGTGGATGCCGACGCCGAGGCCTTCACCGCCTACCTG
GAAGCAATGAGGCTCCCCAAGAACACACCTGAGGAAAAGGACAGGCGCACGGCGGCCCTA
CAGGAGGGTCTGAGGCGGGCAGTCTCTGTGCCGCTGACGCTGGCGGAGACGGTGGCCTCG
CTGTGGCCGGCGCTGCAGGAACTGGCCCGGTGTGGGAACCTGGCCTGCCGGTCAGACCTC
CAGGTGGCGGCCAAAGCCCTGGAGATGGGCGTGTTTGGCGCATATTTCAACGTGCTCATC
AACCTGAGGGACATCACAGACGAGGCATTTAAGGACCAGATCCACCATCGTGTTTCCAGC
CTCCTGCAGGAAGCCAAGACCCAGGCTGCACTGGTGCTGGACTGCTTGGAGACCCGGCAG
GAGTGA
|
| Enzyme 24 GenBank Gene ID |
AF169017  |
| Enzyme 24 GeneCard ID |
FTCD  |
| Enzyme 24 GenAtlas ID |
FTCD  |
| Enzyme 24 HGNC ID |
HGNC:3974  |
| Enzyme 24 Chromosome Location |
2 |
| Enzyme 24 Locus |
21q22.3 |
| Enzyme 24 SNPs |
SNPJam Report  |
| Enzyme 24 General References |
- Solans A, Estivill X, de la Luna S: Cloning and characterization of human FTCD on 21q22.3, a candidate gene for glutamate formiminotransferase deficiency. Cytogenet Cell Genet. 2000;88(1-2):43-9. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Lapierre P, Hajoui O, Homberg JC, Alvarez F: Formiminotransferase cyclodeaminase is an organ-specific autoantigen recognized by sera of patients with autoimmune hepatitis. Gastroenterology. 1999 Mar;116(3):643-9. [PubMed
]
- Hillman RT, Green RE, Brenner SE: An unappreciated role for RNA surveillance. Genome Biol. 2004;5(2):R8. Epub 2004 Feb 2. [PubMed
]
- Hagiwara H, Tajika Y, Matsuzaki T, Suzuki T, Aoki T, Takata K: Localization of Golgi 58K protein (formiminotransferase cyclodeaminase) to the centrosome. Histochem Cell Biol. 2006 Aug;126(2):251-9. Epub 2006 Mar 14. [PubMed
]
- Hilton JF, Christensen KE, Watkins D, Raby BA, Renaud Y, de la Luna S, Estivill X, MacKenzie RE, Hudson TJ, Rosenblatt DS: The molecular basis of glutamate formiminotransferase deficiency. Hum Mutat. 2003 Jul;22(1):67-73. [PubMed
]
|
| Enzyme 24 Metabolite References |
Not Available |
|
Enzyme 25
[top]
|
| Enzyme 25 ID |
5975 |
| Enzyme 25 Name |
Glutamate decarboxylase 2 |
| Enzyme 25 Synonyms |
- 65 kDa glutamic acid decarboxylase
- GAD-65
- Glutamate decarboxylase 65 kDa isoform
|
| Enzyme 25 Gene Name |
GAD2 |
| Enzyme 25 Protein Sequence |
>Glutamate decarboxylase 2
MASPGSGFWSFGSEDGSGDSENPGTARAWCQVAQKFTGGIGNKLCALLYGDAEKPAESGG
SQPPRAAARKAACACDQKPCSCSKVDVNYAFLHATDLLPACDGERPTLAFLQDVMNILLQ
YVVKSFDRSTKVIDFHYPNELLQEYNWELADQPQNLEEILMHCQTTLKYAIKTGHPRYFN
QLSTGLDMVGLAADWLTSTANTNMFTYEIAPVFVLLEYVTLKKMREIIGWPGGSGDGIFS
PGGAISNMYAMMIARFKMFPEVKEKGMAALPRLIAFTSEHSHFSLKKGAAALGIGTDSVI
LIKCDERGKMIPSDLERRILEAKQKGFVPFLVSATAGTTVYGAFDPLLAVADICKKYKIW
MHVDAAWGGGLLMSRKHKWKLSGVERANSVTWNPHKMMGVPLQCSALLVREEGLMQNCNQ
MHASYLFQQDKHYDLSYDTGDKALQCGRHVDVFKLWLMWRAKGTTGFEAHVDKCLELAEY
LYNIIKNREGYEMVFDGKPQHTNVCFWYIPPSLRTLEDNEERMSRLSKVAPVIKARMMEY
GTTMVSYQPLGDKVNFFRMVISNPAATHQDIDFLIEEIERLGQDL
|
| Enzyme 25 Number of Residues |
585 |
| Enzyme 25 Molecular Weight |
65410.8 |
| Enzyme 25 Theoretical pI |
6.89 |
| Enzyme 25 GO Classification |
| Function |
- binding
- carbon-carbon lyase activity
- carboxy-lyase activity
- catalytic activity
- cofactor binding
- lyase activity
- pyridoxal phosphate binding
|
| Process |
- carboxylic acid metabolic process
- cellular metabolic process
- metabolic process
- organic acid metabolic process
- oxoacid metabolic process
|
| Component |
| — |
|
| Enzyme 25 General Function |
Involved in carboxy-lyase activity |
| Enzyme 25 Specific Function |
Catalyzes the production of GABA |
| Enzyme 25 Pathways |
|
| Enzyme 25 Reactions |
- L-glutamate = 4-aminobutanoate + CO2 [RN:R00261]
|
| Enzyme 25 Pfam Domain Function |
|
| Enzyme 25 Signals |
|
| Enzyme 25 Transmembrane Regions |
|
| Enzyme 25 Essentiality |
Not Available |
| Enzyme 25 GenBank ID Protein |
Not Available |
| Enzyme 25 UniProtKB/Swiss-Prot ID |
Q05329  |
| Enzyme 25 UniProtKB/Swiss-Prot Entry Name |
DCE2_HUMAN  |
| Enzyme 25 PDB ID |
Not Available |
| Enzyme 25 Cellular Location |
Not Available |
| Enzyme 25 Gene Sequence |
>1758 bp
ATGGCATCTCCGGGCTCTGGCTTTTGGTCTTTCGGGTCGGAAGATGGCTCTGGGGATTCC
GAGAATCCCGGCACAGCGCGAGCCTGGTGCCAAGTGGCTCAGAAGTTCACGGGCGGCATC
GGAAACAAACTGTGCGCCCTGCTCTACGGAGACGCCGAGAAGCCGGCGGAGAGCGGCGGG
AGCCAACCCCCGCGGGCCGCCGCCCGGAAGGCCGCCTGCGCCTGCGACCAGAAGCCCTGC
AGCTGCTCCAAAGTGGATGTCAACTACGCGTTTCTCCATGCAACAGACCTGCTGCCGGCG
TGTGATGGAGAAAGGCCCACTTTGGCGTTTCTGCAAGATGTTATGAACATTTTACTTCAG
TATGTGGTGAAAAGTTTCGATAGATCAACCAAAGTGATTGATTTCCATTATCCTAATGAG
CTTCTCCAAGAATATAATTGGGAATTGGCAGACCAACCACAAAATTTGGAGGAAATTTTG
ATGCATTGCCAAACAACTCTAAAATATGCAATTAAAACAGGGCATCCTAGATACTTCAAT
CAACTTTCTACTGGTTTGGATATGGTTGGATTAGCAGCAGACTGGCTGACATCAACAGCA
AATACTAACATGTTCACCTATGAAATTGCTCCAGTATTTGTGCTTTTGGAATATGTCACA
CTAAAGAAAATGAGAGAAATCATTGGCTGGCCAGGGGGCTCTGGCGATGGGATATTTTCT
CCCGGTGGCGCCATATCTAACATGTATGCCATGATGATCGCACGCTTTAAGATGTTCCCA
GAAGTCAAGGAGAAAGGAATGGCTGCTCTTCCCAGGCTCATTGCCTTCACGTCTGAACAT
AGTCATTTTTCTCTCAAGAAGGGAGCTGCAGCCTTAGGGATTGGAACAGACAGCGTGATT
CTGATTAAATGTGATGAGAGAGGGAAAATGATTCCATCTGATCTTGAAAGAAGGATTCTT
GAAGCCAAACAGAAAGGGTTTGTTCCTTTCCTCGTGAGTGCCACAGCTGGAACCACCGTG
TACGGAGCATTTGACCCCCTCTTAGCTGTCGCTGACATTTGCAAAAAGTATAAGATCTGG
ATGCATGTGGATGCAGCTTGGGGTGGGGGATTACTGATGTCCCGAAAACACAAGTGGAAA
CTGAGTGGCGTGGAGAGGGCCAACTCTGTGACGTGGAATCCACACAAGATGATGGGAGTC
CCTTTGCAGTGCTCTGCTCTCCTGGTTAGAGAAGAGGGATTGATGCAGAATTGCAACCAA
ATGCATGCCTCCTACCTCTTTCAGCAAGATAAACATTATGACCTGTCCTATGACACTGGA
GACAAGGCCTTACAGTGCGGACGCCACGTTGATGTTTTTAAACTATGGCTGATGTGGAGG
GCAAAGGGGACTACCGGGTTTGAAGCGCATGTTGATAAATGTTTGGAGTTGGCAGAGTAT
TTATACAACATCATAAAAAACCGAGAAGGATATGAGATGGTGTTTGATGGGAAGCCTCAG
CACACAAATGTCTGCTTCTGGTACATTCCTCCAAGCTTGCGTACTCTGGAAGACAATGAA
GAGAGAATGAGTCGCCTCTCGAAGGTGGCTCCAGTGATTAAAGCCAGAATGATGGAGTAT
GGAACCACAATGGTCAGCTACCAACCCTTGGGAGACAAGGTCAATTTCTTCCGCATGGTC
ATCTCAAACCCAGCGGCAACTCACCAAGACATTGACTTCCTGATTGAAGAAATAGAACGC
CTTGGACAAGATTTATAA
|
| Enzyme 25 GenBank Gene ID |
M81882  |
| Enzyme 25 GeneCard ID |
GAD2  |
| Enzyme 25 GenAtlas ID |
GAD2  |
| Enzyme 25 HGNC ID |
HGNC:4093  |
| Enzyme 25 Chromosome Location |
1 |
| Enzyme 25 Locus |
10p11.23 |
| Enzyme 25 SNPs |
SNPJam Report  |
| Enzyme 25 General References |
- Karlsen AE, Hagopian WA, Grubin CE, Dube S, Disteche CM, Adler DA, Barmeier H, Mathewes S, Grant FJ, Foster D, et al.: Cloning and primary structure of a human islet isoform of glutamic acid decarboxylase from chromosome 10. Proc Natl Acad Sci U S A. 1991 Oct 1;88(19):8337-41. [PubMed
]
- Bu DF, Erlander MG, Hitz BC, Tillakaratne NJ, Kaufman DL, Wagner-McPherson CB, Evans GA, Tobin AJ: Two human glutamate decarboxylases, 65-kDa GAD and 67-kDa GAD, are each encoded by a single gene. Proc Natl Acad Sci U S A. 1992 Mar 15;89(6):2115-9. [PubMed
]
- Bu DF, Tobin AJ: The exon-intron organization of the genes (GAD1 and GAD2) encoding two human glutamate decarboxylases (GAD67 and GAD65) suggests that they derive from a common ancestral GAD. Genomics. 1994 May 1;21(1):222-8. [PubMed
]
- Mauch L, Abney CC, Berg H, Scherbaum WA, Liedvogel B, Northemann W: Characterization of a linear epitope within the human pancreatic 64-kDa glutamic acid decarboxylase and its autoimmune recognition by sera from insulin-dependent diabetes mellitus patients. Eur J Biochem. 1993 Mar 1;212(2):597-603. [PubMed
]
- Kim J, Richter W, Aanstoot HJ, Shi Y, Fu Q, Rajotte R, Warnock G, Baekkeskov S: Differential expression of GAD65 and GAD67 in human, rat, and mouse pancreatic islets. Diabetes. 1993 Dec;42(12):1799-808. [PubMed
]
- Namchuk M, Lindsay L, Turck CW, Kanaani J, Baekkeskov S: Phosphorylation of serine residues 3, 6, 10, and 13 distinguishes membrane anchored from soluble glutamic acid decarboxylase 65 and is restricted to glutamic acid decarboxylase 65alpha. J Biol Chem. 1997 Jan 17;272(3):1548-57. [PubMed
]
- Kanaani J, el-Husseini Ael-D, Aguilera-Moreno A, Diacovo JM, Bredt DS, Baekkeskov S: A combination of three distinct trafficking signals mediates axonal targeting and presynaptic clustering of GAD65. J Cell Biol. 2002 Sep 30;158(7):1229-38. [PubMed
]
- Corper AL, Stratmann T, Apostolopoulos V, Scott CA, Garcia KC, Kang AS, Wilson IA, Teyton L: A structural framework for deciphering the link between I-Ag7 and autoimmune diabetes. Science. 2000 Apr 21;288(5465):505-11. [PubMed
]
- Fenalti G, Law RH, Buckle AM, Langendorf C, Tuck K, Rosado CJ, Faux NG, Mahmood K, Hampe CS, Banga JP, Wilce M, Schmidberger J, Rossjohn J, El-Kabbani O, Pike RN, Smith AI, Mackay IR, Rowley MJ, Whisstock JC: GABA production by glutamic acid decarboxylase is regulated by a dynamic catalytic loop. Nat Struct Mol Biol. 2007 Apr;14(4):280-6. Epub 2007 Mar 25. [PubMed
]
|
| Enzyme 25 Metabolite References |
Not Available |
|
Enzyme 26
[top]
|
| Enzyme 26 ID |
5976 |
| Enzyme 26 Name |
Glutamate decarboxylase 1 |
| Enzyme 26 Synonyms |
- 67 kDa glutamic acid decarboxylase
- GAD-67
- Glutamate decarboxylase 67 kDa isoform
|
| Enzyme 26 Gene Name |
GAD1 |
| Enzyme 26 Protein Sequence |
>Glutamate decarboxylase 1
MASSTPSSSATSSNAGADPNTTNLRPTTYDTWCGVAHGCTRKLGLKICGFLQRTNSLEEK
SRLVSAFKERQSSKNLLSCENSDRDARFRRTETDFSNLFARDLLPAKNGEEQTVQFLLEV
VDILLNYVRKTFDRSTKVLDFHHPHQLLEGMEGFNLELSDHPESLEQILVDCRDTLKYGV
RTGHPRFFNQLSTGLDIIGLAGEWLTSTANTNMFTYEIAPVFVLMEQITLKKMREIVGWS
SKDGDGIFSPGGAISNMYSIMAARYKYFPEVKTKGMAAVPKLVLFTSEQSHYSIKKAGAA
LGFGTDNVILIKCNERGKIIPADFEAKILEAKQKGYVPFYVNATAGTTVYGAFDPIQEIA
DICEKYNLWLHVDAAWGGGLLMSRKHRHKLNGIERANSVTWNPHKMMGVLLQCSAILVKE
KGILQGCNQMCAGYLFQPDKQYDVSYDTGDKAIQCGRHVDIFKFWLMWKAKGTVGFENQI
NKCLELAEYLYAKIKNREEFEMVFNGEPEHTNVCFWYIPQSLRGVPDSPQRREKLHKVAP
KIKALMMESGTTMVGYQPQGDKANFFRMVISNPAATQSDIDFLIEEIERLGQDL
|
| Enzyme 26 Number of Residues |
594 |
| Enzyme 26 Molecular Weight |
66896.1 |
| Enzyme 26 Theoretical pI |
7.67 |
| Enzyme 26 GO Classification |
| Function |
- binding
- carbon-carbon lyase activity
- carboxy-lyase activity
- catalytic activity
- cofactor binding
- lyase activity
- pyridoxal phosphate binding
|
| Process |
- carboxylic acid metabolic process
- cellular metabolic process
- metabolic process
- organic acid metabolic process
- oxoacid metabolic process
|
| Component |
| — |
|
| Enzyme 26 General Function |
Involved in carboxy-lyase activity |
| Enzyme 26 Specific Function |
Catalyzes the production of GABA |
| Enzyme 26 Pathways |
|
| Enzyme 26 Reactions |
- L-glutamate = 4-aminobutanoate + CO2 [RN:R00261]
|
| Enzyme 26 Pfam Domain Function |
|
| Enzyme 26 Signals |
|
| Enzyme 26 Transmembrane Regions |
|
| Enzyme 26 Essentiality |
Not Available |
| Enzyme 26 GenBank ID Protein |
62988850  |
| Enzyme 26 UniProtKB/Swiss-Prot ID |
Q99259  |
| Enzyme 26 UniProtKB/Swiss-Prot Entry Name |
DCE1_HUMAN  |
| Enzyme 26 PDB ID |
Not Available |
| Enzyme 26 Cellular Location |
Not Available |
| Enzyme 26 Gene Sequence |
>1785 bp
ATGGCGTCTTCGACCCCATCTTCGTCCGCAACCTCCTCGAACGCGGGAGCGGACCCCAAT
ACCACTAACCTGCGCCCCACAACGTACGATACCTGGTGCGGCGTGGCCCATGGATGCACC
AGAAAACTGGGGCTCAAGATCTGCGGCTTCTTGCAAAGGACCAACAGCCTGGAAGAGAAG
AGTCGCCTTGTGAGTGCCTTCAAGGAGAGGCAATCCTCCAAGAACCTGCTTTCCTGTGAA
AACAGCGACCGGGATGCCCGCTTCCGGCGCACAGAGACTGACTTCTCTAATCTGTTTGCT
AGAGATCTGCTTCCGGCTAAGAACGGTGAGGAGCAAACCGTGCAATTCCTCCTGGAAGTG
GTGGACATACTCCTCAACTATGTCCGCAAGACATTTGATCGCTCCACCAAGGTGCTGGAC
TTTCATCACCCACACCAGTTGCTGGAAGGCATGGAGGGCTTCAACTTGGAGCTCTCTGAC
CACCCCGAGTCCCTGGAGCAGATCCTGGTTGACTGCAGAGACACCTTGAAGTATGGGGTT
CGCACAGGTCATCCTCGATTTTTCAACCAGCTCTCCACTGGATTGGATATTATTGGCCTA
GCTGGAGAATGGCTGACATCAACGGCCAATACCAACATGTTTACATATGAAATTGCACCA
GTGTTTGTCCTCATGGAACAAATAACACTTAAGAAGATGAGAGAGATAGTTGGATGGTCA
AGTAAAGATGGTGATGGGATATTTTCTCCTGGGGGCGCCATATCCAACATGTACAGCATC
ATGGCTGCTCGCTACAAGTACTTCCCGGAAGTTAAGACAAAGGGCATGGCGGCTGTGCCT
AAACTGGTCCTCTTCACCTCAGAACAGAGTCACTATTCCATAAAGAAAGCTGGGGCTGCA
CTTGGCTTTGGAACTGACAATGTGATTTTGATAAAGTGCAATGAAAGGGGGAAAATAATT
CCAGCTGATTTTGAGGCAAAAATTCTTGAAGCCAAACAGAAGGGATATGTTCCCTTTTAT
GTCAATGCAACTGCTGGCACGACTGTTTATGGAGCTTTTGATCCGATACAAGAGATTGCA
GATATATGTGAGAAATATAACCTTTGGTTGCATGTCGATGCTGCCTGGGGAGGTGGGCTG
CTCATGTCCAGGAAGCACCGCCATAAACTCAACGGCATAGAAAGGGCCAACTCAGTCACC
TGGAACCCTCACAAGATGATGGGCGTGCTGTTGCAGTGCTCTGCCATTCTCGTCAAGGAA
AAGGGTATACTCCAAGGATGCAACCAGATGTGTGCAGGATACCTCTTCCAGCCAGACAAG
CAGTATGATGTCTCCTACGACACCGGGGACAAGGCAATTCAGTGTGGCCGCCACGTGGAT
ATCTTCAAGTTCTGGCTGATGTGGAAAGCAAAGGGCACAGTGGGATTTGAAAACCAGATC
AACAAATGCCTGGAACTGGCTGAATACCTCTATGCCAAGATTAAAAACAGAGAAGAATTT
GAGATGGTTTTCAATGGCGAGCCTGAGCACACAAACGTCTGTTTTTGGTATATTCCACAA
AGCCTCAGGGGTGTGCCAGACAGCCCTCAACGACGGGAAAAGCTACACAAGGTGGCTCCA
AAAATCAAAGCCCTGATGATGGAGTCAGGTACGACCATGGTTGGCTACCAGCCCCAAGGG
GACAAGGCCAACTTCTTCCGGATGGTCATCTCCAACCCAGCCGCTACCCAGTCTGACATT
GACTTCCTCATTGAGGAGATAGAAAGACTGGGCCAGGATCTGTAA
|
| Enzyme 26 GenBank Gene ID |
AC007405  |
| Enzyme 26 GeneCard ID |
GAD1  |
| Enzyme 26 GenAtlas ID |
GAD1  |
| Enzyme 26 HGNC ID |
HGNC:4092  |
| Enzyme 26 Chromosome Location |
2 |
| Enzyme 26 Locus |
2q31 |
| Enzyme 26 SNPs |
SNPJam Report  |
| Enzyme 26 General References |
- Bu DF, Erlander MG, Hitz BC, Tillakaratne NJ, Kaufman DL, Wagner-McPherson CB, Evans GA, Tobin AJ: Two human glutamate decarboxylases, 65-kDa GAD and 67-kDa GAD, are each encoded by a single gene. Proc Natl Acad Sci U S A. 1992 Mar 15;89(6):2115-9. [PubMed
]
- Bu DF, Tobin AJ: The exon-intron organization of the genes (GAD1 and GAD2) encoding two human glutamate decarboxylases (GAD67 and GAD65) suggests that they derive from a common ancestral GAD. Genomics. 1994 May 1;21(1):222-8. [PubMed
]
- Kelly C, Carter ND, Johnstone AP, Nussey SS: Cloning of large isoform of human brain glutamic acid decarboxylase. Lancet. 1991 Dec 7;338(8780):1468-9. [PubMed
]
- Kelly CD, Edwards Y, Johnstone AP, Harfst E, Nogradi A, Nussey SS, Povey S, Carter ND: Nucleotide sequence and chromosomal assignment of a cDNA encoding the large isoform of human glutamate decarboxylase. Ann Hum Genet. 1992 Jul;56(Pt 3):255-65. [PubMed
]
- Yamashita K, Cram DS, Harrison LC: Molecular cloning of full-length glutamic acid decarboxylase 67 from human pancreas and islets. Biochem Biophys Res Commun. 1993 May 14;192(3):1347-52. [PubMed
]
- Kawasaki E, Moriuchi R, Watanabe M, Saitoh K, Brunicardi FC, Watt PC, Yamaguchi T, Mullen Y, Akazawa S, Miyamoto T, et al.: Cloning and expression of large isoform of glutamic acid decarboxylase from human pancreatic islet. Biochem Biophys Res Commun. 1993 May 14;192(3):1353-9. [PubMed
]
- Chessler SD, Lernmark A: Alternative splicing of GAD67 results in the synthesis of a third form of glutamic-acid decarboxylase in human islets and other non-neural tissues. J Biol Chem. 2000 Feb 18;275(7):5188-92. [PubMed
]
- Hillier LW, Graves TA, Fulton RS, Fulton LA, Pepin KH, Minx P, Wagner-McPherson C, Layman D, Wylie K, Sekhon M, Becker MC, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Kremitzki C, Oddy L, Du H, Sun H, Bradshaw-Cordum H, Ali J, Carter J, Cordes M, Harris A, Isak A, van Brunt A, Nguyen C, Du F, Courtney L, Kalicki J, Ozersky P, Abbott S, Armstrong J, Belter EA, Caruso L, Cedroni M, Cotton M, Davidson T, Desai A, Elliott G, Erb T, Fronick C, Gaige T, Haakenson W, Haglund K, Holmes A, Harkins R, Kim K, Kruchowski SS, Strong CM, Grewal N, Goyea E, Hou S, Levy A, Martinka S, Mead K, McLellan MD, Meyer R, Randall-Maher J, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Shah N, Swearengen-Shahid S, Snider J, Strong JT, Thompson J, Yoakum M, Leonard S, Pearman C, Trani L, Radionenko M, Waligorski JE, Wang C, Rock SM, Tin-Wollam AM, Maupin R, Latreille P, Wendl MC, Yang SP, Pohl C, Wallis JW, Spieth J, Bieri TA, Berkowicz N, Nelson JO, Osborne J, Ding L, Meyer R, Sabo A, Shotland Y, Sinha P, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Jones TA, She X, Ciccarelli FD, Izaurralde E, Taylor J, Schmutz J, Myers RM, Cox DR, Huang X, McPherson JD, Mardis ER, Clifton SW, Warren WC, Chinwalla AT, Eddy SR, Marra MA, Ovcharenko I, Furey TS, Miller W, Eichler EE, Bork P, Suyama M, Torrents D, Waterston RH, Wilson RK: Generation and annotation of the DNA sequences of human chromosomes 2 and 4. Nature. 2005 Apr 7;434(7034):724-31. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Cram DS, Barnett LD, Joseph JL, Harrison LC: Cloning and partial nucleotide sequence of human glutamic acid decarboxylase cDNA from brain and pancreatic islets. Biochem Biophys Res Commun. 1991 May 15;176(3):1239-44. [PubMed
]
- Persson H, Pelto-Huikko M, Metsis M, Soder O, Brene S, Skog S, Hokfelt T, Ritzen EM: Expression of the neurotransmitter-synthesizing enzyme glutamic acid decarboxylase in male germ cells. Mol Cell Biol. 1990 Sep;10(9):4701-11. [PubMed
]
- Fenalti G, Law RH, Buckle AM, Langendorf C, Tuck K, Rosado CJ, Faux NG, Mahmood K, Hampe CS, Banga JP, Wilce M, Schmidberger J, Rossjohn J, El-Kabbani O, Pike RN, Smith AI, Mackay IR, Rowley MJ, Whisstock JC: GABA production by glutamic acid decarboxylase is regulated by a dynamic catalytic loop. Nat Struct Mol Biol. 2007 Apr;14(4):280-6. Epub 2007 Mar 25. [PubMed
]
- Lynex CN, Carr IM, Leek JP, Achuthan R, Mitchell S, Maher ER, Woods CG, Bonthon DT, Markham AF: Homozygosity for a missense mutation in the 67 kDa isoform of glutamate decarboxylase in a family with autosomal recessive spastic cerebral palsy: parallels with Stiff-Person Syndrome and other movement disorders. BMC Neurol. 2004 Nov 30;4(1):20. [PubMed
]
|
| Enzyme 26 Metabolite References |
Not Available |
|
Enzyme 27
[top]
|
| Enzyme 27 ID |
6059 |
| Enzyme 27 Name |
Cystathionine beta-synthase |
| Enzyme 27 Synonyms |
- Beta-thionase
- Serine sulfhydrase
|
| Enzyme 27 Gene Name |
CBS |
| Enzyme 27 Protein Sequence |
>Cystathionine beta-synthase
MPSETPQAEVGPTGCPHRSGPHSAKGSLEKGSPEDKEAKEPLWIRPDAPSRCTWQLGRPA
SESPHHHTAPAKSPKILPDILKKIGDTPMVRINKIGKKFGLKCELLAKCEFFNAGGSVKD
RISLRMIEDAERDGTLKPGDTIIEPTSGNTGIGLALAAAVRGYRCIIVMPEKMSSEKVDV
LRALGAEIVRTPTNARFDSPESHVGVAWRLKNEIPNSHILDQYRNASNPLAHYDTTADEI
LQQCDGKLDMLVASVGTGGTITGIARKLKEKCPGCRIIGVDPEGSILAEPEELNQTEQTT
YEVEGIGYDFIPTVLDRTVVDKWFKSNDEEAFTFARMLIAQEGLLCGGSAGSTVAVAVKA
AQELQEGQRCVVILPDSVRNYMTKFLSDRWMLQKGFLKEEDLTEKKPWWWHLRVQELGLS
APLTVLPTITCGHTIEILREKGFDQAPVVDEAGVILGMVTLGNMLSSLLAGKVQPSDQVG
KVIYKQFKQIRLTDTLGRLSHILEMDHFALVVHEQIQYHSTGKSSQRQMVFGVVTAIDLL
NFVAAQERDQK
|
| Enzyme 27 Number of Residues |
551 |
| Enzyme 27 Molecular Weight |
60586.0 |
| Enzyme 27 Theoretical pI |
6.63 |
| Enzyme 27 GO Classification |
| Function |
- binding
- carbon-oxygen lyase activity
- catalytic activity
- cofactor binding
- cystathionine beta-synthase activity
- hydro-lyase activity
- lyase activity
- pyridoxal phosphate binding
|
| Process |
- L-serine metabolic process
- cellular amino acid and derivative metabolic process
- cellular amino acid metabolic process
- cellular metabolic process
- cysteine biosynthetic process
- cysteine biosynthetic process from serine
- cysteine biosynthetic process via cystathionine
- metabolic process
- serine family amino acid metabolic process
- sulfur amino acid biosynthetic process
- sulfur amino acid metabolic process
|
| Component |
- cell part
- cytoplasm
- intracellular part
|
|
| Enzyme 27 General Function |
Involved in cysteine biosynthetic process from serine |
| Enzyme 27 Specific Function |
Only known pyridoxal phosphate-dependent enzyme that contains heme. Important regulator of hydrogen sulfide, especially in the brain, utilizing cysteine instead of serine to catalyze the formation of hydrogen sulfide. Hydrogen sulfide is a gastratransmitter with signaling and cytoprotective effects such as acting as a neuromodulator in the brain to protect neurons against hypoxic injury |
| Enzyme 27 Pathways |
- Glycine, Serine and Threonine Metabolism (map00260
)
- Methionine Metabolism (map00271
)
- Selenoamino Acid Metabolism (map00450
)
|
| Enzyme 27 Reactions |
- L-serine + L-homocysteine = L-cystathionine + H2O [RN:R01290]
|
| Enzyme 27 Pfam Domain Function |
|
| Enzyme 27 Signals |
|
| Enzyme 27 Transmembrane Regions |
|
| Enzyme 27 Essentiality |
Not Available |
| Enzyme 27 GenBank ID Protein |
388716  |
| Enzyme 27 UniProtKB/Swiss-Prot ID |
P35520  |
| Enzyme 27 UniProtKB/Swiss-Prot Entry Name |
CBS_HUMAN  |
| Enzyme 27 PDB ID |
1JBQ  |
| Enzyme 27 PDB File |
Show |
| Enzyme 27 3D Structure |
|
| Enzyme 27 Cellular Location |
Not Available |
| Enzyme 27 Gene Sequence |
>1656 bp
ATGCCTTCTGAGACCCCCCAGGCAGAAGTGGGGCCCACAGGCTGCCCCCACCGCTCAGGG
CCACACTCGGCGAAGGGGAGCCTGGAGAAGGGGTCCCCAGAGGATAAGGAAGCCAAGGAG
CCCCTGTGGATCCGGCCCGATGCTCCGAGCAGGTGCACCTGGCAGCTGGGCCGGCCTGCC
TCCGAGTCCCCACATCACCACACTGCCCCGGCAAAATCTCCAAAAATCTTGCCAGATATT
CTGAAGAAAATCGGGGACACCCCTATGGTCAGAATCAACAAGATTGGGAAGAAGTTCGGC
CTGAAGTGTGAGCTCTTGGCCAAGTGTGAGTTCTTCAACGCGGGCGGGAGCGTGAAGGAC
CGCATCAGCCTGCGGATGATTGAGGATGCTGAGCGCGACGGGACGCTGAAGCCCGGGGAC
ACGATTATCGAGCCGACATCCGGGAACACCGGGATCGGGCTGGCCCTGGCTGCGGCAGTG
AGGGGCTATCGCTGCATCATCGTGATGCCAGAGAAGATGAGCTCCGAGAAGGTGGACGTG
CTGCGGGCACTGGGGGCTGAGATTGTGAGGACGCCCACCAATGCCAGGTTCGACTCCCCG
GAGTCACACGTGGGGGTGGCCTGGCGGCTGAAGAACGAAATCCCCAATTCTCACATCCTA
GACCAGTACCGCAACGCCAGCAACCCCCTGGCTCACTACGACACCACCGCTGATGAGATC
CTGCAGCAGTGTGATGGGAAGCTGGACATGCTGGTGGCTTCAGTGGGCACGGGCGGCACC
ATCACGGGCATTGCCAGGAAGCTGAAGGAGAAGTGTCCTGGATGCAGGATCATTGGGGTG
GATCCCGAAGGGTCCATCCTCGCAGAGCCGGAGGAGCTGAACCAGACGGAGCAGACAACC
TACGAGGTGGAAGGGATCGGCTACGACTTCATCCCCACGGTGCTGGACAGGACGGTGGTG
GACAAGTGGTTCAAGAGCAACGATGAGGAGGCGTTCACCTTTGCCCGCATGCTGATCGCG
CAAGAGGGGCTGCTGTGCGGTGGCAGTGCTGGCAGCACGGTGGCGGTGGCCGTGAAGGCT
GCGCAGGAGCTGCAGGAGGGCCAGCGCTGCGTGGTCATTCTGCCCGACTCAGTGCGGAAC
TACATGACCAAGTTCCTGAGCGACAGGTGGATGCTGCAGAAGGGCTTTCTGAAGGAGGAG
GACCTCACGGAGAAGAAGCCCTGGTGGTGGCACCTCCGTGTTCAGGAGCTGGGCCTGTCA
GCCCCGCTGACCGTGCTCCCGACCATCACCTGTGGGCACACCATCGAGATCCTCCGGGAG
AAGGGCTTCGACCAGGCGCCCGTGGTGGATGAGGCGGGGGTAATCCTGGGAATGGTGACG
CTTGGGAACATGCTCTCGTCCCTGCTTGCCGGGAAGGTGCAGCCGTCAGACCAAGTTGGC
AAAGTCATCTACAAGCAGTTCAAACAGATCCGCCTCACGGACACGCTGGGCAGGCTCTCG
CACATCCTGGAGATGGACCACTTCGCCCTGGTGGTGCACGAGCAGATCCAGTACCACAGC
ACCGGGAAGTCCAGTCAGCGGCAGATGGTGTTCGGGGTGGTCACCGCCATTGACTTGCTG
AACTTCGTGGCCGCCCAGGAGCGGGACCAGAAGTGA
|
| Enzyme 27 GenBank Gene ID |
L19501  |
| Enzyme 27 GeneCard ID |
CBS  |
| Enzyme 27 GenAtlas ID |
CBS  |
| Enzyme 27 HGNC ID |
HGNC:1550  |
| Enzyme 27 Chromosome Location |
2 |
| Enzyme 27 Locus |
21q22.3 |
| Enzyme 27 SNPs |
SNPJam Report  |
| Enzyme 27 General References |
- Kraus JP, Le K, Swaroop M, Ohura T, Tahara T, Rosenberg LE, Roper MD, Kozich V: Human cystathionine beta-synthase cDNA: sequence, alternative splicing and expression in cultured cells. Hum Mol Genet. 1993 Oct;2(10):1633-8. [PubMed
]
- Chasse JF, Paly E, Paris D, Paul V, Sinet PM, Kamoun P, London J: Genomic organization of the human cystathionine beta-synthase gene: evidence for various cDNAs. Biochem Biophys Res Commun. 1995 Jun 26;211(3):826-32. [PubMed
]
- Kruger WD, Cox DR: A yeast system for expression of human cystathionine beta-synthase: structural and functional conservation of the human and yeast genes. Proc Natl Acad Sci U S A. 1994 Jul 5;91(14):6614-8. [PubMed
]
- Chasse JF, Paul V, Escanez R, Kamoun P, London J: Human cystathionine beta-synthase: gene organization and expression of different 5' alternative splicing. Mamm Genome. 1997 Dec;8(12):917-21. [PubMed
]
- Kraus JP, Oliveriusova J, Sokolova J, Kraus E, Vlcek C, de Franchis R, Maclean KN, Bao L, Bukovsk, Patterson D, Paces V, Ansorge W, Kozich V: The human cystathionine beta-synthase (CBS) gene: complete sequence, alternative splicing, and polymorphisms. Genomics. 1998 Sep 15;52(3):312-24. [PubMed
]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
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- Kabil O, Zhou Y, Banerjee R: Human cystathionine beta-synthase is a target for sumoylation. Biochemistry. 2006 Nov 14;45(45):13528-36. [PubMed
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- Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed
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- Meier M, Janosik M, Kery V, Kraus JP, Burkhard P: Structure of human cystathionine beta-synthase: a unique pyridoxal 5'-phosphate-dependent heme protein. EMBO J. 2001 Aug 1;20(15):3910-6. [PubMed
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- Taoka S, Lepore BW, Kabil O, Ojha S, Ringe D, Banerjee R: Human cystathionine beta-synthase is a heme sensor protein. Evidence that the redox sensor is heme and not the vicinal cysteines in the CXXC motif seen in the crystal structure of the truncated enzyme. Biochemistry. 2002 Aug 20;41(33):10454-61. [PubMed
]
- Kraus JP, Janosik M, Kozich V, Mandell R, Shih V, Sperandeo MP, Sebastio G, de Franchis R, Andria G, Kluijtmans LA, Blom H, Boers GH, Gordon RB, Kamoun P, Tsai MY, Kruger WD, Koch HG, Ohura T, Gaustadnes M: Cystathionine beta-synthase mutations in homocystinuria. Hum Mutat. 1999;13(5):362-75. [PubMed
]
- Kozich V, Kraus JP: Screening for mutations by expressing patient cDNA segments in E. coli: homocystinuria due to cystathionine beta-synthase deficiency. Hum Mutat. 1992;1(2):113-23. [PubMed
]
- Kozich V, de Franchis R, Kraus JP: Molecular defect in a patient with pyridoxine-responsive homocystinuria. Hum Mol Genet. 1993 Jun;2(6):815-6. [PubMed
]
- Hu FL, Gu Z, Kozich V, Kraus JP, Ramesh V, Shih VE: Molecular basis of cystathionine beta-synthase deficiency in pyridoxine responsive and nonresponsive homocystinuria. Hum Mol Genet. 1993 Nov;2(11):1857-60. [PubMed
]
- de Franchis R, Kozich V, McInnes RR, Kraus JP: Identical genotypes in siblings with different homocystinuric phenotypes: identification of three mutations in cystathionine beta-synthase using an improved bacterial expression system. Hum Mol Genet. 1994 Jul;3(7):1103-8. [PubMed
]
- Marble M, Geraghty MT, de Franchis R, Kraus JP, Valle D: Characterization of a cystathionine beta-synthase allele with three mutations in cis in a patient with B6 nonresponsive homocystinuria. Hum Mol Genet. 1994 Oct;3(10):1883-6. [PubMed
]
- Kraus JP: Komrower Lecture. Molecular basis of phenotype expression in homocystinuria. J Inherit Metab Dis. 1994;17(4):383-90. [PubMed
]
- Shih VE, Fringer JM, Mandell R, Kraus JP, Berry GT, Heidenreich RA, Korson MS, Levy HL, Ramesh V: A missense mutation (I278T) in the cystathionine beta-synthase gene prevalent in pyridoxine-responsive homocystinuria and associated with mild clinical phenotype. Am J Hum Genet. 1995 Jul;57(1):34-9. [PubMed
]
- Sebastio G, Sperandeo MP, Panico M, de Franchis R, Kraus JP, Andria G: The molecular basis of homocystinuria due to cystathionine beta-synthase deficiency in Italian families, and report of four novel mutations. Am J Hum Genet. 1995 Jun;56(6):1324-33. [PubMed
]
- Kluijtmans LA, Blom HJ, Boers GH, van Oost BA, Trijbels FJ, van den Heuvel LP: Two novel missense mutations in the cystathionine beta-synthase gene in homocystinuric patients. Hum Genet. 1995 Aug;96(2):249-50. [PubMed
]
- Kruger WD, Cox DR: A yeast assay for functional detection of mutations in the human cystathionine beta-synthase gene. Hum Mol Genet. 1995 Jul;4(7):1155-61. [PubMed
]
- Sperandeo MP, Panico M, Pepe A, Candito M, de Franchis R, Kraus JP, Andria G, Sebastio G: Molecular analysis of patients affected by homocystinuria due to cystathionine beta-synthase deficiency: report of a new mutation in exon 8 and a deletion in intron 11. J Inherit Metab Dis. 1995;18(2):211-4. [PubMed
]
- Kluijtmans LA, Boers GH, Stevens EM, Renier WO, Kraus JP, Trijbels FJ, van den Heuvel LP, Blom HJ: Defective cystathionine beta-synthase regulation by S-adenosylmethionine in a partially pyridoxine responsive homocystinuria patient. J Clin Invest. 1996 Jul 15;98(2):285-9. [PubMed
]
- Sperandeo MP, Candito M, Sebastio G, Rolland MO, Turc-Carel C, Giudicelli H, Dellamonica P, Andria G: Homocysteine response to methionine challenge in four obligate heterozygotes for homocystinuria and relationship with cystathionine beta-synthase mutations. J Inherit Metab Dis. 1996;19(3):351-6. [PubMed
]
- Dawson PA, Cox AJ, Emmerson BT, Dudman NP, Kraus JP, Gordon RB: Characterisation of five missense mutations in the cystathionine beta-synthase gene from three patients with B6-nonresponsive homocystinuria. Eur J Hum Genet. 1997 Jan-Feb;5(1):15-21. [PubMed
]
- Kim CE, Gallagher PM, Guttormsen AB, Refsum H, Ueland PM, Ose L, Folling I, Whitehead AS, Tsai MY, Kruger WD: Functional modeling of vitamin responsiveness in yeast: a common pyridoxine-responsive cystathionine beta-synthase mutation in homocystinuria. Hum Mol Genet. 1997 Dec;6(13):2213-21. [PubMed
]
- Aral B, Coude M, London J, Aupetit J, Chasse JF, Zabot MT, Chadefaux-Vekemans B, Kamoun P: Two novel mutations (K384E and L539S) in the C-terminal moiety of the cystathionine beta-synthase protein in two French pyridoxine-responsive homocystinuria patients. Hum Mutat. 1997;9(1):81-2. [PubMed
]
- Kozich V, Janosik M, Sokolova J, Oliveriusova J, Orendac M, Kraus JP, Elleder D: Analysis of CBS alleles in Czech and Slovak patients with homocystinuria: report on three novel mutations E176K, W409X and 1223 + 37 del99. J Inherit Metab Dis. 1997 Jul;20(3):363-6. [PubMed
]
- Tsai MY, Wong PW, Garg U, Hanson NQ, Schwichtenberg K: Two Novel Mutations in the Cystathionine beta-synthase Gene of Homocystinuric Patients. Mol Diagn. 1997 Jun;2(2):129-133. [PubMed
]
- Gordon RB, Cox AJ, Dawson PA, Emmerson BT, Kraus JP, Dudman NP: Mutational analysis of the cystathionine beta-synthase gene: a splicing mutation, two missense mutations and an insertion in patients with homocystinuria. Mutations in brief no. 120. Online. Hum Mutat. 1998;11(4):332. [PubMed
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- Gallagher PM, Naughten E, Hanson NQ, Schwichtenberg K, Bignell M, Yuan M, Ward P, Yap S, Whitehead AS, Tsai MY: Characterization of mutations in the cystathionine beta-synthase gene in Irish patients with homocystinuria. Mol Genet Metab. 1998 Dec;65(4):298-302. [PubMed
]
- de Franchis R, Kraus E, Kozich V, Sebastio G, Kraus JP: Four novel mutations in the cystathionine beta-synthase gene: effect of a second linked mutation on the severity of the homocystinuric phenotype. Hum Mutat. 1999;13(6):453-7. [PubMed
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- Gat-Yablonski G, Mandel H, Fowler B, Taleb O, Sela BA: Homocystinuria in the Arab population of Israel: identification of two novel mutations using DGGE analysis. Hum Mutat. 2000 Oct;16(4):372. [PubMed
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- Janosik M, Oliveriusova J, Janosikova B, Sokolova J, Kraus E, Kraus JP, Kozich V: Impaired heme binding and aggregation of mutant cystathionine beta-synthase subunits in homocystinuria. Am J Hum Genet. 2001 Jun;68(6):1506-13. Epub 2001 May 15. [PubMed
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- Castro R, Heil SG, Rivera I, Jakobs C, de Almeida IT, Blom HJ: Molecular genetic analysis of the cystathionine beta-synthase gene in Portuguese homocystinuria patients: three novel mutations. Clin Genet. 2001 Aug;60(2):161-3. [PubMed
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- Maclean KN, Gaustadnes M, Oliveriusova J, Janosik M, Kraus E, Kozich V, Kery V, Skovby F, Rudiger N, Ingerslev J, Stabler SP, Allen RH, Kraus JP: High homocysteine and thrombosis without connective tissue disorders are associated with a novel class of cystathionine beta-synthase (CBS) mutations. Hum Mutat. 2002 Jun;19(6):641-55. [PubMed
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- Gaustadnes M, Wilcken B, Oliveriusova J, McGill J, Fletcher J, Kraus JP, Wilcken DE: The molecular basis of cystathionine beta-synthase deficiency in Australian patients: genotype-phenotype correlations and response to treatment. Hum Mutat. 2002 Aug;20(2):117-26. [PubMed
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- Urreizti R, Balcells S, Rodes M, Vilarinho L, Baldellou A, Couce ML, Munoz C, Campistol J, Pinto X, Vilaseca MA, Grinberg D: Spectrum of CBS mutations in 16 homocystinuric patients from the Iberian Peninsula: high prevalence of T191M and absence of I278T or G307S. Hum Mutat. 2003 Jul;22(1):103. [PubMed
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- Kruger WD, Wang L, Jhee KH, Singh RH, Elsas LJ 2nd: Cystathionine beta-synthase deficiency in Georgia (USA): correlation of clinical and biochemical phenotype with genotype. Hum Mutat. 2003 Dec;22(6):434-41. [PubMed
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|
| Enzyme 27 Metabolite References |
Not Available |
|
Enzyme 28
[top]
|
| Enzyme 28 ID |
6069 |
| Enzyme 28 Name |
Serine--pyruvate aminotransferase |
| Enzyme 28 Synonyms |
- SPT
- Alanine--glyoxylate aminotransferase
- AGT
|
| Enzyme 28 Gene Name |
AGXT |
| Enzyme 28 Protein Sequence |
>Serine--pyruvate aminotransferase
MASHKLLVTPPKALLKPLSIPNQLLLGPGPSNLPPRIMAAGGLQMIGSMSKDMYQIMDEI
KEGIQYVFQTRNPLTLVISGSGHCALEAALVNVLEPGDSFLVGANGIWGQRAVDIGERIG
ARVHPMTKDPGGHYTLQEVEEGLAQHKPVLLFLTHGESSTGVLQPLDGFGELCHRYKCLL
LVDSVASLGGTPLYMDRQGIDILYSGSQKALNAPPGTSLISFSDKAKKKMYSRKTKPFSF
YLDIKWLANFWGCDDQPRMYHHTIPVISLYSLRESLALIAEQGLENSWRQHREAAAYLHG
RLQALGLQLFVKDPALRLPTVTTVAVPAGYDWRDIVSYVIDHFDIEIMGGLGPSTGKVLR
IGLLGCNATRENVDRVTEALRAALQHCPKKKL
|
| Enzyme 28 Number of Residues |
392 |
| Enzyme 28 Molecular Weight |
43009.5 |
| Enzyme 28 Theoretical pI |
8.55 |
| Enzyme 28 GO Classification |
| Function |
| — |
| Process |
|
| Component |
| — |
|
| Enzyme 28 General Function |
Involved in metabolic process |
| Enzyme 28 Specific Function |
L-serine + pyruvate = 3-hydroxypyruvate + L- alanine |
| Enzyme 28 Pathways |
- Glycine, Serine and Threonine Metabolism (map00260
)
|
| Enzyme 28 Reactions |
- L-serine + pyruvate = 3-hydroxypyruvate + L-alanine [RN:R00585]
|
| Enzyme 28 Pfam Domain Function |
|
| Enzyme 28 Signals |
|
| Enzyme 28 Transmembrane Regions |
|
| Enzyme 28 Essentiality |
Not Available |
| Enzyme 28 GenBank ID Protein |
36582  |
| Enzyme 28 UniProtKB/Swiss-Prot ID |
P21549  |
| Enzyme 28 UniProtKB/Swiss-Prot Entry Name |
SPYA_HUMAN  |
| Enzyme 28 PDB ID |
1H0C  |
| Enzyme 28 PDB File |
Show |
| Enzyme 28 3D Structure |
|
| Enzyme 28 Cellular Location |
Not Available |
| Enzyme 28 Gene Sequence |
>1179 bp
ATGGCCTCTCACAAGCTGCTGGTGACCCCCCCCAAGGCCCTGCTCAAGCCCCTCTCCATC
CCCAACCAGCTCCTGCTGGGGCCTGGTCCTTCCAACCTGCCTCCTCGCATCATGGCAGCC
GGGGGGCTGCAGATGATCGGGTCCATGAGCAAGGATATGTACCAGATCATGGACGAGATC
AAGGAAGGCATCCAGTACGTGTTCCAGACCAGGAACCCACTCACACTGGTCATCTCTGGC
TCGGGACACTGTGCCCTGGAGGCCGCCCTGGTCAATGTGCTGGAGCCTGGGGACTCCTTC
CTGGTTGGGGCCAATGGCATTTGGGGGCAGCGAGCCGTGGACATCGGGGAGCGCATAGGA
GCCCGAGTGCACCCGATGACCAAGGACCCTGGAGGCCACTACACACTGCAGGAGGTGGAG
GAGGGCCTGGCCCAGCACAAGCCAGTGCTGCTGTTCTTAACCCACGGGGAGTCGTCCACC
GGCGTGCTGCAGCCCCTTGATGGCTTCGGGGAACTCTGCCACAGGTACAAGTGCCTGCTC
CTGGTGGATTCGGTGGCATCCCTGGGCGGGACCCCCCTTTACATGGACCGGCAAGGCATC
GACATCCTGTACTCGGGCTCCCAGAAGGCCCTGAACGCCCCTCCAGGGACCTCGCTCATC
TCCTTCAGTGACAAGGCCAAAAAGAAGATGTACTCCCGCAAGACGAAGCCCTTCTCCTTC
TACCTGGACATCAAGTGGCTGGCCAACTTCTGGGGCTGTGACGACCAGCCCAGGATGTAC
CATCACACAATCCCCGTCATCAGCCTGTACAGCCTGAGAGAGAGCCTGGCCCTCATTGCG
GAACAGGGCCTGGAGAACAGCTGGCGCCAGCACCGCGAGGCCGCGGCGTATCTGCATGGG
CGCCTGCAGGCACTGGGGCTGCAGCTCTTCGTGAAGGACCCGGCGCTCCGGCTTCCCACA
GTCACCACTGTGGCTGTACCCGCTGGCTATGACTGGAGAGACATCGTCAGCTACGTCATA
GACCACTTCGACATTGAGATCATGGGTGGCCTTGGGCCCTCCACGGGGAAGGTGCTGCGG
ATCGGCCTGCTGGGCTGCAATGCCACCCGCGAGAATGTGGACCGCGTGACGGAGGCCCTG
AGGGCGGCCCTGCAGCACTGCCCCAAGAAGAAGCTGTGA
|
| Enzyme 28 GenBank Gene ID |
X56092  |
| Enzyme 28 GeneCard ID |
AGXT  |
| Enzyme 28 GenAtlas ID |
AGXT  |
| Enzyme 28 HGNC ID |
HGNC:341  |
| Enzyme 28 Chromosome Location |
2 |
| Enzyme 28 Locus |
2q37.3 |
| Enzyme 28 SNPs |
SNPJam Report  |
| Enzyme 28 General References |
- Nishiyama K, Berstein G, Oda T, Ichiyama A: Cloning and nucleotide sequence of cDNA encoding human liver serine-pyruvate aminotransferase. Eur J Biochem. 1990 Nov 26;194(1):9-18. [PubMed
]
- Purdue PE, Takada Y, Danpure CJ: Identification of mutations associated with peroxisome-to-mitochondrion mistargeting of alanine/glyoxylate aminotransferase in primary hyperoxaluria type 1. J Cell Biol. 1990 Dec;111(6 Pt 1):2341-51. [PubMed
]
- Takada Y, Kaneko N, Esumi H, Purdue PE, Danpure CJ: Human peroxisomal L-alanine: glyoxylate aminotransferase. Evolutionary loss of a mitochondrial targeting signal by point mutation of the initiation codon. Biochem J. 1990 Jun 1;268(2):517-20. [PubMed
]
- Purdue PE, Lumb MJ, Fox M, Griffo G, Hamon-Benais C, Povey S, Danpure CJ: Characterization and chromosomal mapping of a genomic clone encoding human alanine:glyoxylate aminotransferase. Genomics. 1991 May;10(1):34-42. [PubMed
]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
- Hillier LW, Graves TA, Fulton RS, Fulton LA, Pepin KH, Minx P, Wagner-McPherson C, Layman D, Wylie K, Sekhon M, Becker MC, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Kremitzki C, Oddy L, Du H, Sun H, Bradshaw-Cordum H, Ali J, Carter J, Cordes M, Harris A, Isak A, van Brunt A, Nguyen C, Du F, Courtney L, Kalicki J, Ozersky P, Abbott S, Armstrong J, Belter EA, Caruso L, Cedroni M, Cotton M, Davidson T, Desai A, Elliott G, Erb T, Fronick C, Gaige T, Haakenson W, Haglund K, Holmes A, Harkins R, Kim K, Kruchowski SS, Strong CM, Grewal N, Goyea E, Hou S, Levy A, Martinka S, Mead K, McLellan MD, Meyer R, Randall-Maher J, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Shah N, Swearengen-Shahid S, Snider J, Strong JT, Thompson J, Yoakum M, Leonard S, Pearman C, Trani L, Radionenko M, Waligorski JE, Wang C, Rock SM, Tin-Wollam AM, Maupin R, Latreille P, Wendl MC, Yang SP, Pohl C, Wallis JW, Spieth J, Bieri TA, Berkowicz N, Nelson JO, Osborne J, Ding L, Meyer R, Sabo A, Shotland Y, Sinha P, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Jones TA, She X, Ciccarelli FD, Izaurralde E, Taylor J, Schmutz J, Myers RM, Cox DR, Huang X, McPherson JD, Mardis ER, Clifton SW, Warren WC, Chinwalla AT, Eddy SR, Marra MA, Ovcharenko I, Furey TS, Miller W, Eichler EE, Bork P, Suyama M, Torrents D, Waterston RH, Wilson RK: Generation and annotation of the DNA sequences of human chromosomes 2 and 4. Nature. 2005 Apr 7;434(7034):724-31. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Zhang X, Roe SM, Hou Y, Bartlam M, Rao Z, Pearl LH, Danpure CJ: Crystal structure of alanine:glyoxylate aminotransferase and the relationship between genotype and enzymatic phenotype in primary hyperoxaluria type 1. J Mol Biol. 2003 Aug 15;331(3):643-52. [PubMed
]
- Nishiyama K, Funai T, Katafuchi R, Hattori F, Onoyama K, Ichiyama A: Primary hyperoxaluria type I due to a point mutation of T to C in the coding region of the serine:pyruvate aminotransferase gene. Biochem Biophys Res Commun. 1991 May 15;176(3):1093-9. [PubMed
]
- Purdue PE, Lumb MJ, Allsop J, Minatogawa Y, Danpure CJ: A glycine-to-glutamate substitution abolishes alanine:glyoxylate aminotransferase catalytic activity in a subset of patients with primary hyperoxaluria type 1. Genomics. 1992 May;13(1):215-8. [PubMed
]
- Minatogawa Y, Tone S, Allsop J, Purdue PE, Takada Y, Danpur CJ, Kido R: A serine-to-phenylalanine substitution leads to loss of alanine:glyoxylate aminotransferase catalytic activity and immunoreactivity in a patient with primary hyperoxaluria type 1. Hum Mol Genet. 1992 Nov;1(8):643-4. [PubMed
]
- Danpure CJ, Purdue PE, Fryer P, Griffiths S, Allsop J, Lumb MJ, Guttridge KM, Jennings PR, Scheinman JI, Mauer SM, et al.: Enzymological and mutational analysis of a complex primary hyperoxaluria type 1 phenotype involving alanine:glyoxylate aminotransferase peroxisome-to-mitochondrion mistargeting and intraperoxisomal aggregation. Am J Hum Genet. 1993 Aug;53(2):417-32. [PubMed
]
- Danpure CJ: Primary hyperoxaluria type 1 and peroxisome-to-mitochondrion mistargeting of alanine:glyoxylate aminotransferase. Biochimie. 1993;75(3-4):309-15. [PubMed
]
- von Schnakenburg C, Rumsby G: Primary hyperoxaluria type 1: a cluster of new mutations in exon 7 of the AGXT gene. J Med Genet. 1997 Jun;34(6):489-92. [PubMed
]
- von Schnakenburg C, Rumsby G: Identification of new mutations in primary hyperoxaluria type 1 (PH1). J Nephrol. 1998 Mar-Apr;11 Suppl 1:15-7. [PubMed
]
- Amoroso A, Pirulli D, Puzzer D, Ferri L, Crovella S, Ferrettini C, Marangella M, Mazzola G, Florian F: Gene symbol: AGXT. Disease: primary hyperoxaluria type I. Hum Genet. 1999 May;104(5):441. [PubMed
]
- Pirulli D, Puzzer D, Ferri L, Crovella S, Amoroso A, Ferrettini C, Marangella M, Mazzola G, Florian F: Molecular analysis of hyperoxaluria type 1 in Italian patients reveals eight new mutations in the alanine: glyoxylate aminotransferase gene. Hum Genet. 1999 Jun;104(6):523-5. [PubMed
]
- Rinat C, Wanders RJ, Drukker A, Halle D, Frishberg Y: Primary hyperoxaluria type I: a model for multiple mutations in a monogenic disease within a distinct ethnic group. J Am Soc Nephrol. 1999 Nov;10(11):2352-8. [PubMed
]
- Basmaison O, Rolland MO, Cochat P, Bozon D: Identification of 5 novel mutations in the AGXT gene. Hum Mutat. 2000 Jun;15(6):577. [PubMed
]
- Lumb MJ, Danpure CJ: Functional synergism between the most common polymorphism in human alanine:glyoxylate aminotransferase and four of the most common disease-causing mutations. J Biol Chem. 2000 Nov 17;275(46):36415-22. [PubMed
]
- Coulter-Mackie MB, Tung A, Henderson HE, Toone JR, Applegarth DA: The AGT gene in Africa: a distinctive minor allele haplotype, a polymorphism (V326I), and a novel PH1 mutation (A112D) in Black Africans. Mol Genet Metab. 2003 Jan;78(1):44-50. [PubMed
]
- Santana A, Salido E, Torres A, Shapiro LJ: Primary hyperoxaluria type 1 in the Canary Islands: a conformational disease due to I244T mutation in the P11L-containing alanine:glyoxylate aminotransferase. Proc Natl Acad Sci U S A. 2003 Jun 10;100(12):7277-82. Epub 2003 May 30. [PubMed
]
- van Woerden CS, Groothoff JW, Wijburg FA, Annink C, Wanders RJ, Waterham HR: Clinical implications of mutation analysis in primary hyperoxaluria type 1. Kidney Int. 2004 Aug;66(2):746-52. [PubMed
]
- Monico CG, Olson JB, Milliner DS: Implications of genotype and enzyme phenotype in pyridoxine response of patients with type I primary hyperoxaluria. Am J Nephrol. 2005 Mar-Apr;25(2):183-8. Epub 2005 Apr 21. [PubMed
]
- Frishberg Y, Rinat C, Shalata A, Khatib I, Feinstein S, Becker-Cohen R, Weismann I, Wanders RJ, Rumsby G, Roels F, Mandel H: Intra-familial clinical heterogeneity: absence of genotype-phenotype correlation in primary hyperoxaluria type 1 in Israel. Am J Nephrol. 2005 May-Jun;25(3):269-75. Epub 2005 Jun 15. [PubMed
]
- Coulter-Mackie MB, Lian Q, Applegarth D, Toone J: The major allele of the alanine:glyoxylate aminotransferase gene: nine novel mutations and polymorphisms associated with primary hyperoxaluria type 1. Mol Genet Metab. 2005 Sep-Oct;86(1-2):172-8. Epub 2005 Jun 15. [PubMed
]
|
| Enzyme 28 Metabolite References |
Not Available |
|
Enzyme 29
[top]
|
| Enzyme 29 ID |
6072 |
| Enzyme 29 Name |
Serine hydroxymethyltransferase, mitochondrial |
| Enzyme 29 Synonyms |
- SHMT
- Glycine hydroxymethyltransferase
- Serine methylase
|
| Enzyme 29 Gene Name |
SHMT2 |
| Enzyme 29 Protein Sequence |
>Serine hydroxymethyltransferase, mitochondrial
MLYFSLFWAARPLQRCGQLVRMAIRAQHSNAAQTQTGEANRGWTGQESLSDSDPEMWELL
QREKDRQCRGLELIASENFCSRAALEALGSCLNNKYSEGYPGKRYYGGAEVVDEIELLCQ
RRALEAFDLDPAQWGVNVQPYSGSPANLAVYTALLQPHDRIMGLDLPDGGHLTHGYMSDV
KRISATSIFFESMPYKLNPKTGLIDYNQLALTARLFRPRLIIAGTSAYARLIDYARMREV
CDEVKAHLLADMAHISGLVAAKVIPSPFKHADIVTTTTHKTLRGARSGLIFYRKGVKAVD
PKTGREIPYTFEDRINFAVFPSLQGGPHNHAIAAVAVALKQACTPMFREYSLQVLKNARA
MADALLERGYSLVSGGTDNHLVLVDLRPKGLDGARAERVLELVSITANKNTCPGDRSAIT
PGGLRLGAPALTSRQFREDDFRRVVDFIDEGVNIGLEVKSKTAKLQDFKSFLLKDSETSQ
RLANLRQRVEQFARAFPMPGFDEH
|
| Enzyme 29 Number of Residues |
504 |
| Enzyme 29 Molecular Weight |
55992.4 |
| Enzyme 29 Theoretical pI |
8.67 |
| Enzyme 29 GO Classification |
| Function |
- binding
- catalytic activity
- cofactor binding
- glycine hydroxymethyltransferase activity
- methyltransferase activity
- pyridoxal phosphate binding
- transferase activity
- transferase activity, transferring one-carbon groups
|
| Process |
- L-serine metabolic process
- cellular amino acid and derivative metabolic process
- cellular amino acid metabolic process
- cellular metabolic process
- glycine metabolic process
- metabolic process
- serine family amino acid metabolic process
|
| Component |
| — |
|
| Enzyme 29 General Function |
Involved in catalytic activity |
| Enzyme 29 Specific Function |
Interconversion of serine and glycine |
| Enzyme 29 Pathways |
|
| Enzyme 29 Reactions |
- 5,10-methylenetetrahydrofolate + glycine + H2O = tetrahydrofolate + L-serine [RN:R00945]
|
| Enzyme 29 Pfam Domain Function |
|
| Enzyme 29 Signals |
|
| Enzyme 29 Transmembrane Regions |
|
| Enzyme 29 Essentiality |
Not Available |
| Enzyme 29 GenBank ID Protein |
15080303  |
| Enzyme 29 UniProtKB/Swiss-Prot ID |
P34897  |
| Enzyme 29 UniProtKB/Swiss-Prot Entry Name |
GLYM_HUMAN  |
| Enzyme 29 PDB ID |
Not Available |
| Enzyme 29 Cellular Location |
Not Available |
| Enzyme 29 Gene Sequence |
>1515 bp
ATGCTGTACTTCTCTTTGTTTTGGGCGGCTCGGCCTCTGCAGAGATGTGGGCAGCTGGTC
AGGATGGCCATTCGGGCTCAGCACAGCAACGCAGCCCAGACTCAGACTGGGGAAGCAAAC
AGGGGCTGGACAGGCCAGGAGAGCCTGTCGGACAGTGATCCTGAGATGTGGGAGTTGCTG
CAGAGGGAGAAGGACAGGCAGTGTCGTGGCCTGGAGCTCATTGCCTCAGAGAACTTCTGC
AGCCGAGCTGCGCTGGAGGCCCTGGGGTCCTGTCTGAACAACAAGTACTCGGAGGGTTAT
CCTGGCAAGAGATACTATGGGGGAGCAGAGGTGGTGGATGAAATTGAGCTGCTGTGCCAG
CGCCGGGCCTTGGAAGCCTTTGACCTGGATCCTGCACAGTGGGGAGTCAATGTCCAGCCC
TACTCCGGGTCCCCAGCCAACCTGGCCGTCTACACAGCCCTTCTGCAACCTCACGACCGG
ATCATGGGGCTGGACCTGCCCGATGGGGGCCATCTCACCCACGGCTACATGTCTGACGTC
AAGCGGATATCAGCCACGTCCATCTTCTTCGAGTCTATGCCCTATAAGCTCAACCCCAAA
ACTGGCCTCATTGACTACAACCAGCTGGCACTGACTGCTCGACTTTTCCGGCCACGGCTC
ATCATAGCTGGCACCAGCGCCTATGCTCGCCTCATTGACTACGCCCGCATGAGAGAGGTG
TGTGATGAAGTCAAAGCACACCTGCTGGCAGACATGGCCCACATCAGTGGCCTGGTGGCT
GCCAAGGTGATTCCCTCGCCTTTCAAGCACGCGGACATCGTCACCACCACTACTCACAAG
ACTCTTCGAGGGGCCAGGTCAGGGCTCATCTTCTACCGGAAAGGGGTGAAGGCTGTGGAC
CCCAAGACTGGCCGGGAGATCCCTTACACATTTGAGGACCGAATCAACTTTGCCGTGTTC
CCATCCCTGCAGGGGGGCCCCCACAATCATGCCATTGCTGCAGTAGCTGTGGCCCTAAAG
CAGGCCTGCACCCCCATGTTCCGGGAGTACTCCCTGCAGGTTCTGAAGAATGCTCGGGCC
ATGGCAGATGCCCTGCTAGAGCGAGGCTACTCACTGGTATCAGGTGGTACTGACAACCAC
CTGGTGCTGGTGGACCTGCGGCCCAAGGGCCTGGATGGAGCTCGGGCTGAGCGGGTGCTA
GAGCTTGTATCCATCACTGCCAACAAGAACACCTGTCCTGGAGACCGAAGTGCCATCACA
CCGGGCGGCCTGCGGCTTGGGGCCCCAGCCTTAACTTCTCGACAGTTCCGTGAGGATGAC
TTCCGGAGAGTTGTGGACTTTATAGATGAAGGGGTCAACATTGGCTTAGAGGTGAAGAGC
AAGACTGCCAAGCTCCAGGATTTCAAATCCTTCCTGCTTAAGGACTCAGAAACAAGTCAG
CGTCTGGCCAACCTCAGGCAACGGGTGGAGCAGTTTGCCAGGGCCTTCCCCATGCCTGGT
TTTGATGAGCATTGA
|
| Enzyme 29 GenBank Gene ID |
BC011911  |
| Enzyme 29 GeneCard ID |
SHMT2  |
| Enzyme 29 GenAtlas ID |
SHMT2  |
| Enzyme 29 HGNC ID |
HGNC:10852  |
| Enzyme 29 Chromosome Location |
1 |
| Enzyme 29 Locus |
12q12-q14 |
| Enzyme 29 SNPs |
SNPJam Report  |
| Enzyme 29 General References |
- Stover PJ, Chen LH, Suh JR, Stover DM, Keyomarsi K, Shane B: Molecular cloning, characterization, and regulation of the human mitochondrial serine hydroxymethyltransferase gene. J Biol Chem. 1997 Jan 17;272(3):1842-8. [PubMed
]
- Garrow TA, Brenner AA, Whitehead VM, Chen XN, Duncan RG, Korenberg JR, Shane B: Cloning of human cDNAs encoding mitochondrial and cytosolic serine hydroxymethyltransferases and chromosomal localization. J Biol Chem. 1993 Jun 5;268(16):11910-6. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Snell K, Baumann U, Byrne PC, Chave KJ, Renwick SB, Sanders PG, Whitehouse SK: The genetic organization and protein crystallographic structure of human serine hydroxymethyltransferase. Adv Enzyme Regul. 2000;40:353-403. [PubMed
]
- Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed
]
|
| Enzyme 29 Metabolite References |
Not Available |
|
Enzyme 30
[top]
|
| Enzyme 30 ID |
6074 |
| Enzyme 30 Name |
Serine hydroxymethyltransferase, cytosolic |
| Enzyme 30 Synonyms |
- SHMT
- Glycine hydroxymethyltransferase
- Serine methylase
|
| Enzyme 30 Gene Name |
SHMT1 |
| Enzyme 30 Protein Sequence |
>Serine hydroxymethyltransferase, cytosolic
MTMPVNGAHKDADLWSSHDKMLAQPLKDSDVEVYNIIKKESNRQRVGLELIASENFASRA
VLEALGSCLNNKYSEGYPGQRYYGGTEFIDELETLCQKRALQAYKLDPQCWGVNVQPYSG
SPANFAVYTALVEPHGRIMGLDLPDGGHLTHGFMTDKKKISATSIFFESMPYKVNPDTGY
INYDQLEENARLFHPKLIIAGTSCYSRNLEYARLRKIADENGAYLMADMAHISGLVAAGV
VPSPFEHCHVVTTTTHKTLRGCRAGMIFYRKGVKSVDPKTGKEILYNLESLINSAVFPGL
QGGPHNHAIAGVAVALKQAMTLEFKVYQHQVVANCRALSEALTELGYKIVTGGSDNHLIL
VDLRSKGTDGGRAEKVLEACSIACNKNTCPGDRSALRPSGLRLGTPALTSRGLLEKDFQK
VAHFIHRGIELTLQIQSDTGVRATLKEFKERLAGDKYQAAVQALREEVESFASLFPLPGL
PDF
|
| Enzyme 30 Number of Residues |
483 |
| Enzyme 30 Molecular Weight |
53082.2 |
| Enzyme 30 Theoretical pI |
7.77 |
| Enzyme 30 GO Classification |
| Function |
- binding
- catalytic activity
- cofactor binding
- glycine hydroxymethyltransferase activity
- methyltransferase activity
- pyridoxal phosphate binding
- transferase activity
- transferase activity, transferring one-carbon groups
|
| Process |
- L-serine metabolic process
- cellular amino acid and derivative metabolic process
- cellular amino acid metabolic process
- cellular metabolic process
- glycine metabolic process
- metabolic process
- serine family amino acid metabolic process
|
| Component |
| — |
|
| Enzyme 30 General Function |
Involved in catalytic activity |
| Enzyme 30 Specific Function |
Interconversion of serine and glycine |
| Enzyme 30 Pathways |
|
| Enzyme 30 Reactions |
- 5,10-methylenetetrahydrofolate + glycine + H2O = tetrahydrofolate + L-serine [RN:R00945]
|
| Enzyme 30 Pfam Domain Function |
|
| Enzyme 30 Signals |
|
| Enzyme 30 Transmembrane Regions |
|
| Enzyme 30 Essentiality |
Not Available |
| Enzyme 30 GenBank ID Protein |
14124914  |
| Enzyme 30 UniProtKB/Swiss-Prot ID |
P34896  |
| Enzyme 30 UniProtKB/Swiss-Prot Entry Name |
GLYC_HUMAN  |
| Enzyme 30 PDB ID |
1BJ4  |
| Enzyme 30 PDB File |
Show |
| Enzyme 30 3D Structure |
|
| Enzyme 30 Cellular Location |
Not Available |
| Enzyme 30 Gene Sequence |
>1452 bp
ATGACGATGCCAGTCAACGGGGCCCACAAGGATGCTGACCTGTGGTCCTCACATGACAAG
ATGCTGGCACAACCCCTCAAAGACAGTGATGTTGAGGTTTACAACATCATTAAGAAGGAG
AGTAACCGGCAGAGGGTTGGATTGGAGCTGATTGCCTCGGAGAATTTCGCCAGCCGAGCA
GTTTTGGAGGCCCTAGGCTCTTGCTTAAATAACAAATACTCTGAGGGGTACCCGGGCCAG
AGATACTATGGCGGGACTGAGTTTATTGATGAACTGGAGACCCTCTGTCAGAAGCGAGCC
CTGCAGGCCTATAAGCTGGACCCACAGTGCTGGGGGGTCAACGTCCAGCCCTACTCAGGC
TCCCCTGCAAACTTTGCTGTGTACACTGCCCTGGTGGAACCCCATGGGCGCATCATGGGC
CTGGACCTTCCGGATGGGGGCCACCTGACCCATGGGTTCATGACAGACAAGAAGAAAATC
TCTGCCACGTCCATCTTCTTTGAATCTATGCCCTACAAGGTGAACCCAGATACTGGCTAC
ATCAACTATGACCAGCTGGAGGAGAACGCACGCCTCTTCCACCCGAAGCTGATCATCGCA
GGAACCAGCTGCTACTCCCGAAACCTGGAATATGCCCGGCTACGGAAGATTGCAGATGAG
AACGGGGCGTATCTCATGGCGGACATGGCTCACATCAGCGGGCTGGTGGCGGCTGGCGTG
GTGCCCTCCCCATTTGAACACTGCCATGTGGTGACCACCACCACTCACAAGACCCTGCGA
GGCTGCCGAGCTGGCATGATCTTCTACAGGAAAGGAGTGAAAAGTGTGGATCCCAAGACT
GGCAAAGAGATTCTGTACAACCTGGAGTCTCTTATCAATTCTGCTGTGTTCCCTGGCCTG
CAGGGAGGTCCCCACAACCACGCCATTGCTGGGGTTGCTGTGGCACTGAAGCAAGCTATG
ACTCTGGAATTTAAAGTTTATCAACACCAGGTGGTGGCCAACTGCAGGGCTCTGTCTGAG
GCCCTGACGGAGCTGGGCTACAAAATAGTCACAGGTGGTTCTGACAACCATTTGATCCTT
GTGGATCTCCGTTCCAAAGGCACAGATGGTGGAAGGGCTGAGAAGGTGCTAGAAGCCTGT
TCTATTGCCTGCAACAAGAACACCTGTCCAGGTGACAGAAGCGCTCTGCGGCCCAGTGGA
CTGCGGCTGGGGACCCCAGCACTGACGTCCCGTGGACTTTTGGAAAAAGACTTCCAAAAA
GTAGCCCACTTTATTCACAGAGGGATAGAGCTGACCCTGCAGATCCAGAGCGACACTGGT
GTCAGAGCCACCCTGAAAGAGTTCAAGGAGAGACTGGCAGGGGATAAGTACCAGGCGGCC
GTGCAGGCTCTCCGGGAGGAGGTTGAGAGCTTCGCCTCTTTCTTCCCTCTGCCTGGCCTG
CCTGACTTCTAA
|
| Enzyme 30 GenBank Gene ID |
BC007979  |
| Enzyme 30 GeneCard ID |
SHMT1  |
| Enzyme 30 GenAtlas ID |
SHMT1  |
| Enzyme 30 HGNC ID |
HGNC:10850  |
| Enzyme 30 Chromosome Location |
1 |
| Enzyme 30 Locus |
17p11.2 |
| Enzyme 30 SNPs |
SNPJam Report  |
| Enzyme 30 General References |
- Garrow TA, Brenner AA, Whitehead VM, Chen XN, Duncan RG, Korenberg JR, Shane B: Cloning of human cDNAs encoding mitochondrial and cytosolic serine hydroxymethyltransferases and chromosomal localization. J Biol Chem. 1993 Jun 5;268(16):11910-6. [PubMed
]
- Chave KJ, Snell K, Sanders PG: Isolation and characterisation of human genomic sequences encoding cytosolic serine hydroxymethyltransferase. Biochem Soc Trans. 1997 Feb;25(1):53S. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed
]
- Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed
]
- Renwick SB, Snell K, Baumann U: The crystal structure of human cytosolic serine hydroxymethyltransferase: a target for cancer chemotherapy. Structure. 1998 Sep 15;6(9):1105-16. [PubMed
]
|
| Enzyme 30 Metabolite References |
Not Available |
|
Enzyme 31
[top]
|
| Enzyme 31 ID |
6075 |
| Enzyme 31 Name |
Glycine dehydrogenase [decarboxylating], mitochondrial |
| Enzyme 31 Synonyms |
- Glycine cleavage system P protein
- Glycine decarboxylase
|
| Enzyme 31 Gene Name |
GLDC |
| Enzyme 31 Protein Sequence |
>Glycine dehydrogenase [decarboxylating], mitochondrial
MQSCARAWGLRLGRGVGGGRRLAGGSGPCWAPRSRDSSSGGGDSAAAGASRLLERLLPRH
DDFARRHIGPGDKDQREMLQTLGLASIDELIEKTVPANIRLKRPLKMEDPVCENEILATL
HAISSKNQIWRSYIGMGYYNCSVPQTILRNLLENSGWITQYTPYQPEVSQGRLESLLNYQ
TMVCDITGLDMANASLLDEGTAAAEALQLCYRHNKRRKFLVDPRCHPQTIAVVQTRAKYT
GVLTELKLPCEMDFSGKDVSGVLFQYPDTEGKVEDFTELVERAHQSGSLACCATDLLALC
ILRPPGEFGVDIALGSSQRFGVPLGYGGPHAAFFAVRESLVRMMPGRMVGVTRDATGKEV
YRLALQTREQHIRRDKATSNICTAQALLANMAAMFAIYHGSHGLEHIARRVHNATLILSE
GLKRAGHQLQHDLFFDTLKIQCGCSVKEVLGRAAQRQINFRLFEDGTLGISLDETVNEKD
LDDLLWIFGCESSAELVAESMGEECRGIPGSVFKRTSPFLTHQVFNSYHSETNIVRYMKK
LENKDISLVHSMIPLGSCTMKLNSSSELAPITWKEFANIHPFVPLDQAQGYQQLFRELEK
DLCELTGYDQVCFQPNSGAQGEYAGLATIRAYLNQKGEGHRTVCLIPKSAHGTNPASAHM
AGMKIQPVEVDKYGNIDAVHLKAMVDKHKENLAAIMITYPSTNGVFEENISDVCDLIHQH
GGQVYLDGANMNAQVGICRPGDFGSDVSHLNLHKTFCIPHGGGGPGMGPIGVKKHLAPFL
PNHPVISLKRNEDACPVGTVSAAPWGSSSILPISWAYIKMMGGKGLKQATETAILNANYM
AKRLETHYRILFRGARGYVGHEFILDTRPFKKSANIEAVDVAKRLQDYGFHAPTMSWPVA
GTLMVEPTESEDKAELDRFCDAMISIRQEIADIEEGRIDPRVNPLKMSPHSLTCVTSSHW
DRPYSREVAAFPLPFVKPENKFWPTIARIDDIYGDQHLVCTCPPMEVYESPFSEQKRASS
|
| Enzyme 31 Number of Residues |
1020 |
| Enzyme 31 Molecular Weight |
112728.8 |
| Enzyme 31 Theoretical pI |
7.11 |
| Enzyme 31 GO Classification |
| Function |
- binding
- catalytic activity
- cofactor binding
- glycine dehydrogenase (decarboxylating) activity
- lyase activity
- oxidoreductase activity
- oxidoreductase activity, acting on the CH-NH2 group of donors
- oxidoreductase activity, acting on the CH-NH2 group of donors, disulfide as acceptor
- pyridoxal phosphate binding
|
| Process |
- cellular amino acid and derivative metabolic process
- cellular amino acid metabolic process
- cellular metabolic process
- glycine metabolic process
- metabolic process
- oxidation reduction
- serine family amino acid metabolic process
|
| Component |
| — |
|
| Enzyme 31 General Function |
Involved in lyase activity |
| Enzyme 31 Specific Function |
The glycine cleavage system catalyzes the degradation of glycine. The P protein binds the alpha-amino group of glycine through its pyridoxal phosphate cofactor; CO(2) is released and the remaining methylamine moiety is then transferred to the lipoamide cofactor of the H protein |
| Enzyme 31 Pathways |
- Glycine, Serine and Threonine Metabolism (map00260
)
|
| Enzyme 31 Reactions |
- glycine + H-protein-lipoyllysine = H-protein-S-aminomethyldihydrolipoyllysine + CO2 [RN:R03425]
|
| Enzyme 31 Pfam Domain Function |
|
| Enzyme 31 Signals |
|
| Enzyme 31 Transmembrane Regions |
|
| Enzyme 31 Essentiality |
Not Available |
| Enzyme 31 GenBank ID Protein |
189054321  |
| Enzyme 31 UniProtKB/Swiss-Prot ID |
P23378  |
| Enzyme 31 UniProtKB/Swiss-Prot Entry Name |
GCSP_HUMAN  |
| Enzyme 31 PDB ID |
Not Available |
| Enzyme 31 Cellular Location |
Not Available |
| Enzyme 31 Gene Sequence |
>3063 bp
ATGCAGTCCTGTGCCAGGGCGTGGGGGCTGCGCCTGGGCCGCGGGGTCGGGGGCGGCCGC
CGCCTGGCTGGGGGATCGGGGCCGTGCTGGGCGCCGCGGAGCCGGGACAGCAGCAGTGGC
GGCGGGGACAGCGCCGCGGCTGGGGCCTCGCGCCTCCTGGAGCGCCTTCTGCCCAGACAC
GACGACTTCGCTCGGAGGCACATCGGCCCTGGGGACAAAGACCAGAGAGAGATGCTGCAG
ACCTTGGGGCTGGCGAGCATTGATGAATTGATCGAGAAGACGGTCCCTGCCAACATCCGT
TTGAAAAGACCCTTGAAAATGGAAGACCCTGTTTGTGAAAATGAAATCCTTGCAACTCTG
CATGCCATTTCAAGCAAAAACCAGATCTGGAGATCGTATATTGGCATGGGCTATTATAAC
TGCTCAGTGCCACAGACGATTTTGCGGAACTTACTGGAGAACTCAGGATGGATCACCCAG
TATACTCCATACCAGCCTGAGGTGTCTCAGGGGAGGCTGGAGAGTTTACTCAACTACCAG
ACCATGGTGTGTGACATCACAGGCCTGGACATGGCCAATGCATCCCTGCTGGATGAGGGG
ACTGCAGCCGCAGAGGCACTGCAGCTGTGCTACAGACACAACAAGAGGAGGAAATTTCTC
GTTGATCCCCGTTGCCACCCACAGACAATAGCTGTTGTCCAGACTCGAGCCAAATATACT
GGAGTCCTCACTGAGCTGAAGCTACCCTGTGAAATGGACTTCAGTGGAAAAGATGTCAGT
GGAGTGTTGTTCCAGTACCCAGACACGGAGGGGAAGGTGGAAGACTTTACGGAACTCGTG
GAGAGAGCTCATCAGAGTGGGAGCCTGGCCTGCTGTGCTACTGACCTTTTAGCTTTGTGC
ATCTTGAGGCCACCTGGAGAATTTGGGGTAGACATCGCCCTGGGCAGCTCCCAGAGATTT
GGAGTGCCACTGGGCTATGGGGGACCCCATGCAGCATTTTTTGCTGTCCGAGAAAGCTTG
GTGAGAATGATGCCTGGAAGAATGGTGGGGGTAACAAGAGATGCCACTGGGAAAGAAGTG
TATCGTCTTGCTCTTCAAACCAGGGAGCAACACATTCGGAGAGACAAGGCTACCAGCAAC
ATCTGTACAGCTCAGGCCCTCTTGGCGAATATGGCTGCCATGTTTGCAATCTACCATGGT
TCCCATGGGCTGGAGCATATTGCTAGGAGGGTACATAATGCCACTTTGATTTTGTCAGAA
GGTCTCAAGCGAGCAGGGCATCAACTCCAGCATGACCTGTTCTTTGATACCTTGAAGATT
CAGTGTGGCTGCTCAGTGAAGGAGGTCTTGGGCAGGGCCGCTCAGCGGCAGATCAATTTT
CGGCTTTTTGAGGATGGCACACTTGGTATTTCTCTTGATGAAACAGTCAATGAAAAAGAT
CTGGACGATTTGTTGTGGATCTTTGGTTGTGAGTCATCTGCAGAACTGGTTGCTGAAAGC
ATGGGAGAGGAGTGCAGAGGTATTCCAGGGTCTGTGTTCAAGAGGACCAGCCCGTTCCTC
ACCCATCAAGTGTTCAACAGCTACCACTCTGAAACAAACATTGTCCGGTACATGAAGAAA
CTGGAAAATAAAGACATTTCCCTTGTTCACAGCATGATTCCACTGGGATCCTGCACCATG
AAACTGAACAGTTCGTCTGAACTCGCACCTATCACATGGAAAGAATTTGCAAACATCCAC
CCCTTTGTGCCTCTGGATCAAGCTCAAGGATATCAGCAGCTTTTCCGAGAGCTTGAGAAG
GATTTGTGTGAACTCACAGGTTATGACCAGGTCTGTTTCCAGCCAAACAGCGGAGCCCAG
GGAGAATATGCTGGACTGGCCACTATCCGAGCCTACTTAAACCAGAAAGGAGAGGGGCAC
AGAACGGTTTGCCTCATTCCGAAATCAGCACATGGGACCAACCCAGCAAGTGCCCACATG
GCAGGCATGAAGATTCAGCCTGTGGAGGTGGATAAATATGGGAATATCGATGCAGTTCAC
CTCAAGGCCATGGTGGATAAGCACAAGGAGAACCTAGCAGCTATCATGATTACATACCCA
TCCACCAATGGGGTGTTTGAAGAGAACATCAGTGACGTGTGTGACCTCATCCATCAACAT
GGAGGACAGGTCTACCTAGACGGGGCAAATATGAATGCTCAGGTGGGAATCTGTCGCCCT
GGAGACTTCGGGTCTGATGTCTCGCACCTAAATCTTCACAAGACCTTCTGCATTCCCCAC
GGAGGAGGTGGTCCTGGCATGGGGCCCATCGGAGTGAAGAAACATCTCGCCCCGTTTTTG
CCCAATCATCCCGTCATTTCACTAAAGCGGAATGAGGATGCCTGTCCTGTGGGAACCGTC
AGTGCGGCCCCATGGGGCTCCAGTTCCATCTTGCCCATTTCCTGGGCTTATATCAAGATG
ATGGGAGGCAAGGGTCTTAAACAAGCCACGGAAACTGCGATATTAAATGCCAACTACATG
GCCAAGCGATTAGAAACACACTACAGAATTCTTTTCAGGGGTGCAAGAGGTTATGTGGGT
CATGAATTTATTTTGGACACGAGACCCTTCAAAAAGTCTGCAAATATTGAGGCTGTGGAT
GTGGCCAAGAGACTCCAGGATTATGGATTTCACGCCCCTACCATGTCCTGGCCTGTGGCA
GGGACCCTCATGGTGGAGCCCACTGAGTCGGAGGACAAGGCAGAGCTGGACAGATTCTGT
GATGCCATGATCAGCATTCGGCAGGAAATTGCTGACATTGAGGAGGGCCGCATCGACCCC
AGGGTCAATCCGCTGAAGATGTCTCCACACTCCCTGACCTGCGTTACATCTTCCCACTGG
GACCGGCCTTATTCCAGAGAGGTGGCAGCATTCCCACTCCCCTTCGTGAAACCAGAGAAC
AAATTCTGGCCAACGATTGCCCGGATTGATGACATATATGGAGATCAGCACCTGGTTTGT
ACCTGCCCACCCATGGAAGTTTATGAGTCTCCATTTTCTGAACAAAAGAGGGCGTCTTCT
TAG
|
| Enzyme 31 GenBank Gene ID |
AK314156  |
| Enzyme 31 GeneCard ID |
GLDC  |
| Enzyme 31 GenAtlas ID |
GLDC  |
| Enzyme 31 HGNC ID |
HGNC:4313  |
| Enzyme 31 Chromosome Location |
9 |
| Enzyme 31 Locus |
9p22 |
| Enzyme 31 SNPs |
SNPJam Report  |
| Enzyme 31 General References |
- Kure S, Narisawa K, Tada K: Structural and expression analyses of normal and mutant mRNA encoding glycine decarboxylase: three-base deletion in mRNA causes nonketotic hyperglycinemia. Biochem Biophys Res Commun. 1991 Feb 14;174(3):1176-82. [PubMed
]
- Kume A, Koyata H, Sakakibara T, Ishiguro Y, Kure S, Hiraga K: The glycine cleavage system. Molecular cloning of the chicken and human glycine decarboxylase cDNAs and some characteristics involved in the deduced protein structures. J Biol Chem. 1991 Feb 15;266(5):3323-9. [PubMed
]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
- Humphray SJ, Oliver K, Hunt AR, Plumb RW, Loveland JE, Howe KL, Andrews TD, Searle S, Hunt SE, Scott CE, Jones MC, Ainscough R, Almeida JP, Ambrose KD, Ashwell RI, Babbage AK, Babbage S, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beasley H, Beasley O, Bird CP, Bray-Allen S, Brown AJ, Brown JY, Burford D, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Chen Y, Clarke G, Clark SY, Clee CM, Clegg S, Collier RE, Corby N, Crosier M, Cummings AT, Davies J, Dhami P, Dunn M, Dutta I, Dyer LW, Earthrowl ME, Faulkner L, Fleming CJ, Frankish A, Frankland JA, French L, Fricker DG, Garner P, Garnett J, Ghori J, Gilbert JG, Glison C, Grafham DV, Gribble S, Griffiths C, Griffiths-Jones S, Grocock R, Guy J, Hall RE, Hammond S, Harley JL, Harrison ES, Hart EA, Heath PD, Henderson CD, Hopkins BL, Howard PJ, Howden PJ, Huckle E, Johnson C, Johnson D, Joy AA, Kay M, Keenan S, Kershaw JK, Kimberley AM, King A, Knights A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd C, Lloyd DM, Lovell J, Martin S, Mashreghi-Mohammadi M, Matthews L, McLaren S, McLay KE, McMurray A, Milne S, Nickerson T, Nisbett J, Nordsiek G, Pearce AV, Peck AI, Porter KM, Pandian R, Pelan S, Phillimore B, Povey S, Ramsey Y, Rand V, Scharfe M, Sehra HK, Shownkeen R, Sims SK, Skuce CD, Smith M, Steward CA, Swarbreck D, Sycamore N, Tester J, Thorpe A, Tracey A, Tromans A, Thomas DW, Wall M, Wallis JM, West AP, Whitehead SL, Willey DL, Williams SA, Wilming L, Wray PW, Young L, Ashurst JL, Coulson A, Blocker H, Durbin R, Sulston JE, Hubbard T, Jackson MJ, Bentley DR, Beck S, Rogers J, Dunham I: DNA sequence and analysis of human chromosome 9. Nature. 2004 May 27;429(6990):369-74. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Zahedi RP, Lewandrowski U, Wiesner J, Wortelkamp S, Moebius J, Schutz C, Walter U, Gambaryan S, Sickmann A: Phosphoproteome of resting human platelets. J Proteome Res. 2008 Feb;7(2):526-34. Epub 2007 Dec 19. [PubMed
]
- Kure S, Takayanagi M, Narisawa K, Tada K, Leisti J: Identification of a common mutation in Finnish patients with nonketotic hyperglycinemia. J Clin Invest. 1992 Jul;90(1):160-4. [PubMed
]
- Toone JR, Applegarth DA, Coulter-Mackie MB, James ER: Recurrent mutations in P- and T-proteins of the glycine cleavage complex and a novel T-protein mutation (N145I): a strategy for the molecular investigation of patients with nonketotic hyperglycinemia (NKH). Mol Genet Metab. 2001 Apr;72(4):322-5. [PubMed
]
- Applegarth DA, Toone JR: Nonketotic hyperglycinemia (glycine encephalopathy): laboratory diagnosis. Mol Genet Metab. 2001 Sep-Oct;74(1-2):139-46. [PubMed
]
|
| Enzyme 31 Metabolite References |
Not Available |
|
Enzyme 32
[top]
|
| Enzyme 32 ID |
6131 |
| Enzyme 32 Name |
Alanine aminotransferase 1 |
| Enzyme 32 Synonyms |
- ALT1
- Glutamate pyruvate transaminase 1
- GPT 1
- Glutamic--alanine transaminase 1
- Glutamic--pyruvic transaminase 1
|
| Enzyme 32 Gene Name |
GPT |
| Enzyme 32 Protein Sequence |
>Alanine aminotransferase 1
MASSTGDRSQAVRHGLRAKVLTLDGMNPRVRRVEYAVRGPIVQRALELEQELRQGVKKPF
TEVIRANIGDAQAMGQRPITFLRQVLALCVNPDLLSSPNFPDDAKKRAERILQACGGHSL
GAYSVSSGIQLIREDVARYIERRDGGIPADPNNVFLSTGASDAIVTVLKLLVAGEGHTRT
GVLIPIPQYPLYSATLAELGAVQVDYYLDEERAWALDVAELHRALGQARDHCRPRALCVI
NPGNPTGQVQTRECIEAVIRFAFEERLFLLADEVYQDNVYAAGSQFHSFKKVLMEMGPPY
AGQQELASFHSTSKGYMGECGFRGGYVEVVNMDAAVQQQMLKLMSVRLCPPVPGQALLDL
VVSPPAPTDPSFAQFQAEKQAVLAELAAKAKLTEQVFNEAPGISCNPVQGAMYSFPRVQL
PPRAVERAQELGLAPDMFFCLRLLEETGICVVPGSGFGQREGTYHFRMTILPPLEKLRLL
LEKLSRFHAKFTLEYS
|
| Enzyme 32 Number of Residues |
496 |
| Enzyme 32 Molecular Weight |
54636.4 |
| Enzyme 32 Theoretical pI |
7.20 |
| Enzyme 32 GO Classification |
| Function |
- 1-aminocyclopropane-1-carboxylate synthase activity
- binding
- carbon-sulfur lyase activity
- catalytic activity
- cofactor binding
- lyase activity
- pyridoxal phosphate binding
- transferase activity
- transferase activity, transferring nitrogenous groups
|
| Process |
- biosynthetic process
- metabolic process
|
| Component |
| — |
|
| Enzyme 32 General Function |
Involved in 1-aminocyclopropane-1-carboxylate synthase activity |
| Enzyme 32 Specific Function |
Catalyzes the reversible transamination between alanine and 2-oxoglutarate to form pyruvate and glutamate. Participates in cellular nitrogen metabolism and also in liver gluconeogenesis starting with precursors transported from skeletal muscles |
| Enzyme 32 Pathways |
|
| Enzyme 32 Reactions |
- L-alanine + 2-oxoglutarate = pyruvate + L-glutamate [RN:R00258]
|
| Enzyme 32 Pfam Domain Function |
|
| Enzyme 32 Signals |
|
| Enzyme 32 Transmembrane Regions |
|
| Enzyme 32 Essentiality |
Not Available |
| Enzyme 32 GenBank ID Protein |
Not Available |
| Enzyme 32 UniProtKB/Swiss-Prot ID |
P24298  |
| Enzyme 32 UniProtKB/Swiss-Prot Entry Name |
ALAT1_HUMAN  |
| Enzyme 32 PDB ID |
Not Available |
| Enzyme 32 Cellular Location |
Not Available |
| Enzyme 32 Gene Sequence |
>1491 bp
ATGGCCTCGAGCACAGGTGACCGGAGCCAGGCGGTGAGGCATGGACTGAGGGCGAAGGTG
CTGACGCTGGACGGCATGAACCCGCGTGTGCGGAGAGTGGAGTACGCAGTGCGTGGCCCC
ATAGTGCAGCGAGCCTTGGAGCTGGAGCAGGAGCTGCGCCAGGGTGTGAAGAAGCCTTTC
ACCGAGGTCATCCGTGCCAACATCGGGGACGCACAGGCTATGGGGCAGAGGCCCATCACC
TTCCTGCGCCAGGTCTTGGCCCTCTGTGTTAACCCTGATCTTCTGAGCAGCCCCAACTTC
CCTGACGATGCCAAGAAAAGGGCGGAGCGCATCTTGCAGGCGTGTGGGGGCCACAGTCTG
GGGGCCTACAGCGTCAGCTCCGGCATCCAGCTGATCCGGGAGGACGTGGCGCGGTACATT
GAGAGGCGTGACGGAGGCATCCCTGCGGACCCCAACAACGTCTTCCTGTCCACAGGGGCC
AGCGATGCCATCGTGACGGTGCTGAAGCTGCTGGTGGCCGGCGAGGGCCACACACGCACG
GGTGTGCTCATCCCCATCCCCCAGTACCCACTCTACTCGGCCACGCTGGCAGAGCTGGGC
GCAGTGCAGGTGGATTACTACCTGGACGAGGAGCGTGCCTGGGCGCTGGACGTGGCCGAG
CTTCACCGTGCACTGGGCCAGGCGCGTGACCACTGCCGCCCTCGTGCGCTCTGTGTCATC
AACCCTGGCAACCCCACCGGGCAGGTGCAGACCCGCGAGTGCATCGAGGCCGTGATCCGC
TTCGCCTTCGAAGAGCGGCTCTTTCTGCTGGCGGACGAGGTGTACCAGGACAACGTGTAC
GCCGCGGGTTCGCAGTTCCACTCATTCAAGAAGGTGCTCATGGAGATGGGGCCGCCCTAC
GCCGGGCAGCAGGAGCTTGCCTCCTTCCACTCCACCTCCAAGGGCTACATGGGCGAGTGC
GGGTTCCGCGGCGGCTATGTGGAGGTGGTGAACATGGACGCTGCAGTGCAGCAGCAGATG
CTGAAGCTGATGAGTGTGCGGCTGTGCCCGCCGGTGCCAGGACAGGCCCTGCTGGACCTG
GTGGTCAGCCCGCCCGCGCCCACCGACCCCTCCTTTGCGCAGTTCCAGGCTGAGAAGCAG
GCAGTGCTGGCAGAGCTGGCGGCCAAGGCCAAGCTCACCGAGCAGGTCTTCAATGAGGCT
CCTGGCATCAGCTGCAACCCAGTGCAGGGCGCCATGTACTCCTTCCCGCGCGTGCAGCTG
CCCCCGCGGGCGGTGGAGCGCGCTCAGGAGCTGGGCCTGGCCCCCGATATGTTCTTCTGC
CTGCGCCTCCTGGAGGAGACCGGCATCTGCGTGGTGCCAGGGAGCGGCTTTGGGCAGCGG
GAAGGCACCTACCACTTCCGGATGACCATTCTGCCCCCCTTGGAGAAACTGCGGCTGCTG
CTGGAGAAGCTGAGCAGGTTCCATGCCAAGTTCACCCTCGAGTACTCCTAG
|
| Enzyme 32 GenBank Gene ID |
BT006992  |
| Enzyme 32 GeneCard ID |
GPT  |
| Enzyme 32 GenAtlas ID |
GPT  |
| Enzyme 32 HGNC ID |
HGNC:4552  |
| Enzyme 32 Chromosome Location |
8 |
| Enzyme 32 Locus |
8q24.3 |
| Enzyme 32 SNPs |
SNPJam Report  |
| Enzyme 32 General References |
- Sohocki MM, Sullivan LS, Harrison WR, Sodergren EJ, Elder FF, Weinstock G, Tanase S, Daiger SP: Human glutamate pyruvate transaminase (GPT): localization to 8q24.3, cDNA and genomic sequences, and polymorphic sites. Genomics. 1997 Mar 1;40(2):247-52. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Ishiguro M, Takio K, Suzuki M, Oyama R, Matsuzawa T, Titani K: Complete amino acid sequence of human liver cytosolic alanine aminotransferase (GPT) determined by a combination of conventional and mass spectral methods. Biochemistry. 1991 Oct 29;30(43):10451-7. [PubMed
]
- Yang RZ, Blaileanu G, Hansen BC, Shuldiner AR, Gong DW: cDNA cloning, genomic structure, chromosomal mapping, and functional expression of a novel human alanine aminotransferase. Genomics. 2002 Mar;79(3):445-50. [PubMed
]
|
| Enzyme 32 Metabolite References |
Not Available |
|
Enzyme 33
[top]
|
| Enzyme 33 ID |
6132 |
| Enzyme 33 Name |
Phosphoserine aminotransferase |
| Enzyme 33 Synonyms |
- Phosphohydroxythreonine aminotransferase
- PSAT
|
| Enzyme 33 Gene Name |
PSAT1 |
| Enzyme 33 Protein Sequence |
>Phosphoserine aminotransferase
MDAPRQVVNFGPGPAKLPHSVLLEIQKELLDYKGVGISVLEMSHRSSDFAKIINNTENLV
RELLAVPDNYKVIFLQGGGCGQFSAVPLNLIGLKAGRCADYVVTGAWSAKAAEEAKKFGT
INIVHPKLGSYTKIPDPSTWNLNPDASYVYYCANETVHGVEFDFIPDVKGAVLVCDMSSN
FLSKPVDVSKFGVIFAGAQKNVGSAGVTVVIVRDDLLGFALRECPSVLEYKVQAGNSSLY
NTPPCFSIYVMGLVLEWIKNNGGAAAMEKLSSIKSQTIYEIIDNSQGFYVCPVEPQNRSK
MNIPFRIGNAKGDDALEKRFLDKALELNMLSLKGHRSVGGIRASLYNAVTIEDVQKLAAF
MKKFLEMHQL
|
| Enzyme 33 Number of Residues |
370 |
| Enzyme 33 Molecular Weight |
40422.4 |
| Enzyme 33 Theoretical pI |
7.77 |
| Enzyme 33 GO Classification |
| Function |
- binding
- catalytic activity
- cofactor binding
- pyridoxal phosphate binding
|
| Process |
- L-serine biosynthetic process
- L-serine metabolic process
- cellular amino acid and derivative metabolic process
- cellular amino acid metabolic process
- cellular metabolic process
- metabolic process
- serine family amino acid metabolic process
|
| Component |
| — |
|
| Enzyme 33 General Function |
Involved in metabolic process |
| Enzyme 33 Specific Function |
Catalyzes the reversible conversion of 3- phosphohydroxypyruvate to phosphoserine and of 3-hydroxy-2-oxo-4- phosphonooxybutanoate to phosphohydroxythreonine |
| Enzyme 33 Pathways |
- Glycine, Serine and Threonine Metabolism (map00260
)
- Vitamin B6 Metabolism (map00750
)
|
| Enzyme 33 Reactions |
- (1) O-phospho-L-serine + 2-oxoglutarate = 3-phosphonooxypyruvate + L-glutamate [RN:R04173]
- (2) 4-phosphonooxy-L-threonine + 2-oxoglutarate = (3R)-3-hydroxy-2-oxo-4-phosphonooxybutanoate + L-glutamate
|
| Enzyme 33 Pfam Domain Function |
|
| Enzyme 33 Signals |
|
| Enzyme 33 Transmembrane Regions |
|
| Enzyme 33 Essentiality |
Not Available |
| Enzyme 33 GenBank ID Protein |
17402893  |
| Enzyme 33 UniProtKB/Swiss-Prot ID |
Q9Y617  |
| Enzyme 33 UniProtKB/Swiss-Prot Entry Name |
SERC_HUMAN  |
| Enzyme 33 PDB ID |
Not Available |
| Enzyme 33 Cellular Location |
Not Available |
| Enzyme 33 Gene Sequence |
>1113 bp
ATGGACGCCCCCAGGCAGGTGGTCAACTTTGGGCCTGGTCCCGCCAAGCTGCCGCACTCA
GTGTTGTTAGAGATACAAAAGGAATTATTAGACTACAAAGGAGTTGGCATTAGTGTTCTT
GAAATGAGTCACAGGTCATCAGATTTTGCCAAGATTATTAACAATACAGAGAATCTTGTG
CGGGAATTGCTAGCTGTTCCAGACAACTATAAGGTGATTTTTCTGCAAGGAGGTGGGTGC
GGCCAGTTCAGTGCTGTCCCCTTAAACCTCATTGGCTTGAAAGCAGGAAGGTGTGCTGAC
TATGTGGTGACAGGAGCTTGGTCAGCTAAGGCCGCAGAAGAAGCCAAGAAGTTTGGGACT
ATAAATATCGTTCACCCTAAACTTGGGAGTTATACAAAAATTCCAGATCCAAGCACCTGG
AACCTCAACCCAGATGCCTCCTACGTGTATTATTGCGCAAATGAGACGGTGCATGGTGTG
GAGTTTGACTTTATACCCGATGTCAAGGGAGCAGTACTGGTTTGTGACATGTCCTCAAAC
TTCCTGTCCAAGCCAGTGGATGTTTCCAAGTTTGGTGTGATTTTTGCTGGTGCCCAGAAG
AATGTTGGCTCTGCTGGGGTCACCGTGGTGATTGTCCGTGATGACCTGCTGGGGTTTGCC
CTCCGAGAGTGCCCCTCGGTCCTGGAATACAAGGTGCAGGCTGGAAACAGCTCCTTGTAC
AACACGCCTCCATGTTTCAGCATCTACGTCATGGGCTTGGTTCTGGAGTGGATTAAAAAC
AATGGAGGTGCCGCGGCCATGGAGAAGCTTAGCTCCATCAAATCTCAAACAATTTATGAG
ATTATTGATAATTCTCAAGGATTCTACGTTTGTCCAGTGGAGCCCCAAAATAGAAGCAAG
ATGAATATTCCATTCCGCATTGGCAATGCCAAAGGAGATGATGCTTTAGAAAAAAGATTT
CTTGATAAAGCTCTTGAACTCAATATGTTGTCCTTGAAAGGGCATAGGTCTGTGGGAGGC
ATCCGGGCCTCTCTGTATAATGCTGTCACAATTGAAGACGTTCAGAAGCTGGCCGCCTTC
ATGAAAAAATTTTTGGAGATGCATCAGCTATGA
|
| Enzyme 33 GenBank Gene ID |
NM_058179.2  |
| Enzyme 33 GeneCard ID |
PSAT1  |
| Enzyme 33 GenAtlas ID |
PSAT1  |
| Enzyme 33 HGNC ID |
HGNC:19129  |
| Enzyme 33 Chromosome Location |
9 |
| Enzyme 33 Locus |
9q21.2 |
| Enzyme 33 SNPs |
SNPJam Report  |
| Enzyme 33 General References |
- Baek JY, Jun DY, Taub D, Kim YH: Characterization of human phosphoserine aminotransferase involved in the phosphorylated pathway of L-serine biosynthesis. Biochem J. 2003 Jul 1;373(Pt 1):191-200. [PubMed
]
- Humphray SJ, Oliver K, Hunt AR, Plumb RW, Loveland JE, Howe KL, Andrews TD, Searle S, Hunt SE, Scott CE, Jones MC, Ainscough R, Almeida JP, Ambrose KD, Ashwell RI, Babbage AK, Babbage S, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beasley H, Beasley O, Bird CP, Bray-Allen S, Brown AJ, Brown JY, Burford D, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Chen Y, Clarke G, Clark SY, Clee CM, Clegg S, Collier RE, Corby N, Crosier M, Cummings AT, Davies J, Dhami P, Dunn M, Dutta I, Dyer LW, Earthrowl ME, Faulkner L, Fleming CJ, Frankish A, Frankland JA, French L, Fricker DG, Garner P, Garnett J, Ghori J, Gilbert JG, Glison C, Grafham DV, Gribble S, Griffiths C, Griffiths-Jones S, Grocock R, Guy J, Hall RE, Hammond S, Harley JL, Harrison ES, Hart EA, Heath PD, Henderson CD, Hopkins BL, Howard PJ, Howden PJ, Huckle E, Johnson C, Johnson D, Joy AA, Kay M, Keenan S, Kershaw JK, Kimberley AM, King A, Knights A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd C, Lloyd DM, Lovell J, Martin S, Mashreghi-Mohammadi M, Matthews L, McLaren S, McLay KE, McMurray A, Milne S, Nickerson T, Nisbett J, Nordsiek G, Pearce AV, Peck AI, Porter KM, Pandian R, Pelan S, Phillimore B, Povey S, Ramsey Y, Rand V, Scharfe M, Sehra HK, Shownkeen R, Sims SK, Skuce CD, Smith M, Steward CA, Swarbreck D, Sycamore N, Tester J, Thorpe A, Tracey A, Tromans A, Thomas DW, Wall M, Wallis JM, West AP, Whitehead SL, Willey DL, Williams SA, Wilming L, Wray PW, Young L, Ashurst JL, Coulson A, Blocker H, Durbin R, Sulston JE, Hubbard T, Jackson MJ, Bentley DR, Beck S, Rogers J, Dunham I: DNA sequence and analysis of human chromosome 9. Nature. 2004 May 27;429(6990):369-74. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed
]
- Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed
]
- Hart CE, Race V, Achouri Y, Wiame E, Sharrard M, Olpin SE, Watkinson J, Bonham JR, Jaeken J, Matthijs G, Van Schaftingen E: Phosphoserine aminotransferase deficiency: a novel disorder of the serine biosynthesis pathway. Am J Hum Genet. 2007 May;80(5):931-7. Epub 2007 Mar 30. [PubMed
]
|
| Enzyme 33 Metabolite References |
Not Available |
|
Enzyme 34
[top]
|
| Enzyme 34 ID |
6167 |
| Enzyme 34 Name |
Histidine decarboxylase |
| Enzyme 34 Synonyms |
- HDC
|
| Enzyme 34 Gene Name |
HDC |
| Enzyme 34 Protein Sequence |
>Histidine decarboxylase
MMEPEEYRERGREMVDYICQYLSTVRERRVTPDVQPGYLRAQLPESAPEDPDSWDSIFGD
IERIIMPGVVHWQSPHMHAYYPALTSWPSLLGDMLADAINCLGFTWASSPACTELEMNVM
DWLAKMLGLPEHFLHHHPSSQGGGVLQSTVSESTLIALLAARKNKILEMKTSEPDADESC
LNARLVAYASDQAHSSVEKAGLISLVKMKFLPVDDNFSLRGEALQKAIEEDKQRGLVPVF
VCATLGTTGVCAFDCLSELGPICAREGLWLHIDAAYAGTAFLCPEFRGFLKGIEYADSFT
FNPSKWMMVHFDCTGFWVKDKYKLQQTFSVNPIYLRHANSGVATDFMHWQIPLSRRFRSV
KLWFVIRSFGVKNLQAHVRHGTEMAKYFESLVRNDPSFEIPAKRHLGLVVFRLKGPNCLT
ENVLKEIAKAGRLFLIPATIQDKLIIRFTVTSQFTTRDDILRDWNLIRDAATLILSQHCT
SQPSPRVGNLISQIRGARAWACGTSLQSVSGAGDDPVQARKIIKQPQRVGAGPMKRENGL
HLETLLDPVDDCFSEEAPDATKHKLSSFLFSYLSVQTKKKTVRSLSCNSVPVSAQKPLPT
EASVKNGGSSRVRIFSRFPEDMMMLKKSAFKKLIKFYSVPSFPECSSQCGLQLPCCPLQA
MV
|
| Enzyme 34 Number of Residues |
662 |
| Enzyme 34 Molecular Weight |
74139.8 |
| Enzyme 34 Theoretical pI |
8.06 |
| Enzyme 34 GO Classification |
| Function |
- binding
- carbon-carbon lyase activity
- carboxy-lyase activity
- catalytic activity
- cofactor binding
- lyase activity
- pyridoxal phosphate binding
|
| Process |
- carboxylic acid metabolic process
- cellular amino acid and derivative metabolic process
- cellular metabolic process
- metabolic process
- organic acid metabolic process
- oxoacid metabolic process
|
| Component |
| — |
|
| Enzyme 34 General Function |
Involved in carboxy-lyase activity |
| Enzyme 34 Specific Function |
L-histidine = histamine + CO(2) |
| Enzyme 34 Pathways |
|
| Enzyme 34 Reactions |
- L-histidine = histamine + CO2 [RN:R01167]
|
| Enzyme 34 Pfam Domain Function |
|
| Enzyme 34 Signals |
|
| Enzyme 34 Transmembrane Regions |
|
| Enzyme 34 Essentiality |
Not Available |
| Enzyme 34 GenBank ID Protein |
32109  |
| Enzyme 34 UniProtKB/Swiss-Prot ID |
P19113  |
| Enzyme 34 UniProtKB/Swiss-Prot Entry Name |
DCHS_HUMAN  |
| Enzyme 34 PDB ID |
Not Available |
| Enzyme 34 Cellular Location |
Not Available |
| Enzyme 34 Gene Sequence |
>1989 bp
ATGATGGAGCCTGAGGAGTACAGAGAGAGAGGGAGAGAGATGGTGGATTACATCTGCCAG
TACCTGAGCACTGTGCGGGAGAGACGTGTGACGCCAGACGTGCAGCCTGGCTACCTGCGA
GCCCAGCTGCCTGAGAGTGCTCCTGAGGACCCCGACAGCTGGGACAGCATCTTTGGGGAC
ATTGAACGAATCATCATGCCTGGGGTGGTACATTGGCAGAGCCCCCATATGCACGCCTAC
TACCCAGCCCTCACCTCTTGGCCCTCCCTGCTAGGAGACATGCTGGCTGATGCCATCAAC
TGCTTGGGATTCACCTGGGCATCCAGCCCTGCGTGTACAGAGCTGGAGATGAACGTCATG
GACTGGTTGGCAAAAATGCTGGGACTTCCAGAGCACTTCTTGCACCACCACCCCAGCAGC
CAGGGCGGAGGCGTCCTGCAGCAGACGGTCAGTGAATCCACTTTGATTGCCCTGCTGGCA
GCAAGGAAGAACAAAATCCTGGAAATGAAAACGTCTGAGCCCGATGCTGATGAGTCCTGC
CTAAATGCCCGACTCGTGGCCTATGCCTCTGACCAGGCTCACTCCTCTGTGGAAAAGGCT
GGTTTGATTTCCCTTGTGAAGATGAAATTTCTGCCTGTGGATGACAACTTCTCACTCCGA
GGGGAAGCTCTTCAGAAGGCCATCGAGGAAGACAAGCAGCGGGGCTTGGTGCCCGTCTTT
GTCTGTGCAACACTAGGGACCACTGGGGTCTGTGCATTTGACTGCCTGTCAGAGCTGGGC
CCCATCTGTGCCCGTGAGGGGCTGTGGCTCCACATCGATGCTGCTTATGCAGGCACTGCC
TTCCTGTGCCCCGAGTTCCGGGGGTTTCTGAAGGGGATTGAGTATGCCGACTCCTTCACC
TTTAATCCTTCCAAGTGGATGATGGTGCATTTTGACTGTACTGGGTTCTGGGTCAAGGAC
AAGTACAAGCTGCAGCAGACCTTCAGTGTGAATCCCATCTACCTCAGGCATGCCAACTCA
GGCGTGGCCACCGACTTCATGCACTGGCAGATCCCCCTGAGCCGACGGTTTCGCTCTGTT
AAACTCTGGTTCGTGATTCGGTCCTTCGGGGTGAAGAATCTTCAAGCACATGTCAGACAT
GGTACTGAAATGGCTAAATATTTTGAATCTCTGGTCAGAAACGACCCTTCCTTTGAAATT
CCTGCCAAGAGGCACCTTGGCCTGGTGGTTTTTCGTCTAAAGGGTCCTAATTGTCTCACA
GAAAATGTGTTAAAGGAAATAGCTAAAGCTGGCCGTCTCTTCCTCATCCCGGCCACTATC
CAGGACAAGTTAATCATCCGTTTCACTGTGACATCCCAGTTTACCACTAGGGATGACATC
CTGAGAGACTGGAATCTCATTCGAGATGCTGCCACTCTCATCCTGAGTCAGCACTGTACT
TCCCAACCCAGCCCTCGGGTTGGGAACCTCATCTCCCAAATCAGGGGTGCCAGAGCCTGG
GCCTGTGGAACGTCCCTTCAGTCTGTCAGTGGGGCAGGAGATGATCCAGTCCAGGCCAGG
AAGATCATCAAGCAGCCTCAGCGTGTGGGAGCCGGTCCCATGAAAAGGGAAAATGGCCTC
CATCTTGAAACCCTGCTGGACCCAGTTGATGACTGCTTTTCAGAAGAGGCCCCAGATGCC
ACCAAGCACAAGCTGTCCTCCTTCCTGTTCAGTTACTTGTCTGTGCAGACTAAGAAGAAG
ACGGTGCGCTCCCTCAGTTGCAACAGTGTGCCAGTGAGTGCTCAGAAGCCACTGCCCACA
GAGGCCTCTGTGAAGAATGGGGGCTCCTCCAGGGTCAGAATCTTTTCCAGGTTTCCAGAA
GACATGATGATGCTGAAGAAAAGTGCCTTCAAAAAACTCATCAAATTCTACAGCGTCCCC
AGCTTTCCTGAATGCAGCTCTCAATGTGGACTCCAGCTGCCCTGTTGCCCTCTGCAGGCC
ATGGTTTAG
|
| Enzyme 34 GenBank Gene ID |
X54297  |
| Enzyme 34 GeneCard ID |
HDC  |
| Enzyme 34 GenAtlas ID |
HDC  |
| Enzyme 34 HGNC ID |
HGNC:4855  |
| Enzyme 34 Chromosome Location |
1 |
| Enzyme 34 Locus |
15q21-q22 |
| Enzyme 34 SNPs |
SNPJam Report  |
| Enzyme 34 General References |
- Yamauchi K, Sato R, Tanno Y, Ohkawara Y, Maeyama K, Watanabe T, Satoh K, Yoshizawa M, Shibahara S, Takishima T: Nucleotide sequence of the cDNA encoding L-histidine decarboxylase derived from human basophilic leukemia cell line, KU-812-F. Nucleic Acids Res. 1990 Oct 11;18(19):5891. [PubMed
]
- Zahnow CA, Yi HF, McBride OW, Joseph DR: Cloning of the cDNA encoding human histidine decarboxylase from an erythroleukemia cell line and mapping of the gene locus to chromosome 15. DNA Seq. 1991;1(6):395-400. [PubMed
]
- Mamune-Sato R, Yamauchi K, Tanno Y, Ohkawara Y, Ohtsu H, Katayose D, Maeyama K, Watanabe T, Shibahara S, Takishima T: Functional analysis of alternatively spliced transcripts of the human histidine decarboxylase gene and its expression in human tissues and basophilic leukemia cells. Eur J Biochem. 1992 Oct 15;209(2):533-9. [PubMed
]
- Yatsunami K, Ohtsu H, Tsuchikawa M, Higuchi T, Ishibashi K, Shida A, Shima Y, Nakagawa S, Yamauchi K, Yamamoto M, et al.: Structure of the L-histidine decarboxylase gene. J Biol Chem. 1994 Jan 14;269(2):1554-9. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Sjoblom T, Jones S, Wood LD, Parsons DW, Lin J, Barber TD, Mandelker D, Leary RJ, Ptak J, Silliman N, Szabo S, Buckhaults P, Farrell C, Meeh P, Markowitz SD, Willis J, Dawson D, Willson JK, Gazdar AF, Hartigan J, Wu L, Liu C, Parmigiani G, Park BH, Bachman KE, Papadopoulos N, Vogelstein B, Kinzler KW, Velculescu VE: The consensus coding sequences of human breast and colorectal cancers. Science. 2006 Oct 13;314(5797):268-74. Epub 2006 Sep 7. [PubMed
]
|
| Enzyme 34 Metabolite References |
Not Available |
|
Enzyme 35
[top]
|
| Enzyme 35 ID |
6168 |
| Enzyme 35 Name |
Serine palmitoyltransferase 1 |
| Enzyme 35 Synonyms |
- Long chain base biosynthesis protein 1
- LCB 1
- Serine-palmitoyl-CoA transferase 1
- SPT 1
- SPT1
|
| Enzyme 35 Gene Name |
SPTLC1 |
| Enzyme 35 Protein Sequence |
>Serine palmitoyltransferase 1
MATATEQWVLVEMVQALYEAPAYHLILEGILILWIIRLLFSKTYKLQERSDLTVKEKEEL
IEEWQPEPLVPPVPKDHPALNYNIVSGPPSHKTVVNGKECINFASFNFLGLLDNPRVKAA
ALASLKKYGVGTCGPRGFYGTFDVHLDLEDRLAKFMKTEEAIIYSYGFATIASAIPAYSK
RGDIVFVDRAACFAIQKGLQASRSDIKLFKHNDMADLERLLKEQEIEDQKNPRKARVTRR
FIVVEGLYMNTGTICPLPELVKLKYKYKARIFLEESLSFGVLGEHGRGVTEHYGINIDDI
DLISANMENALASIGGFCCGRSFVIDHQRLSGQGYCFSASLPPLLAAAAIEALNIMEENP
GIFAVLKEKCGQIHKALQGISGLKVVGESLSPAFHLQLEESTGSREQDVRLLQEIVDQCM
NRSIALTQARYLEKEEKCLPPPSIRVVVTVEQTEEELERAASTIKEVAQAVLL
|
| Enzyme 35 Number of Residues |
473 |
| Enzyme 35 Molecular Weight |
52743.4 |
| Enzyme 35 Theoretical pI |
5.87 |
| Enzyme 35 GO Classification |
| Function |
- binding
- catalytic activity
- cofactor binding
- pyridoxal phosphate binding
- transferase activity
- transferase activity, transferring nitrogenous groups
|
| Process |
- biosynthetic process
- metabolic process
|
| Component |
| — |
|
| Enzyme 35 General Function |
Involved in transferase activity, transferring nitrogenous groups |
| Enzyme 35 Specific Function |
Serine palmitoyltransferase (SPT). The heterodimer formed with LCB2 (SPTLC2 or SPTLC3) constitutes the catalytic core. The composition of the serine palmitoyltransferase (SPT) complex determines the substrate preference. The SPTLC1-SPTLC2- SSSPTA complex shows a strong preference for C16-CoA substrate, while the SPTLC1-SPTLC3-SSSPTA isozyme uses both C14-CoA and C16- CoA as substrates, with a slight preference for C14-CoA. The SPTLC1-SPTLC2-SSSPTB complex shows a strong preference for C18-CoA substrate, while the SPTLC1-SPTLC3-SSSPTB isozyme displays an ability to use a broader range of acyl-CoAs, without apparent preference |
| Enzyme 35 Pathways |
|
| Enzyme 35 Reactions |
- palmitoyl-CoA + L-serine = CoA + 3-dehydro-D-sphinganine + CO2 [RN:R01281]
|
| Enzyme 35 Pfam Domain Function |
|
| Enzyme 35 Signals |
|
| Enzyme 35 Transmembrane Regions |
|
| Enzyme 35 Essentiality |
Not Available |
| Enzyme 35 GenBank ID Protein |
2564247  |
| Enzyme 35 UniProtKB/Swiss-Prot ID |
O15269  |
| Enzyme 35 UniProtKB/Swiss-Prot Entry Name |
SPTC1_HUMAN  |
| Enzyme 35 PDB ID |
Not Available |
| Enzyme 35 Cellular Location |
Not Available |
| Enzyme 35 Gene Sequence |
>1422 bp
ATGGCGACCGCCACGGAGCAGTGGGTTCTGGTGGAGATGGTACAGGCGCTTTACGAGGCT
CCTGCTTACCATCTTATTTTGGAAGGGATTCTGATCCTCTGGATAATCAGACTTCTTTTC
TCTAAGACTTACAAATTACAAGAACGATCTGATCTTACAGTCAAGGAAAAAGAAGAACTG
ATTGAAGAGTGGCAACCAGAACCTCTTGTTCCTCCTGTCCCAAAAGACCATCCTGCTCTC
AACTACAACATCGTTTCAGGCCCTCCAAGCCACAAAACTGTGGTGAATGGAAAAGAATGT
ATAAACTTCGCCTCATTTAATTTTCTTGGATTGTTGGATAACCCTAGGGTTAAGGCAGCA
GCTTTAGCATCTCTAAAGAAGTATGGCGTGGGGACTTGTGGACCCAGAGGATTTTATGGC
ACATTTGATGTTCATTTGGATTTGGAAGACCGCCTGGCAAAATTTATGAAGACAGAAGAA
GCCATTATATACTCATATGGATTTGCCACCATAGCCAGTGCTATTCCTGCTTACTCTAAA
AGAGGGGACATTGTTTTTGTAGATAGAGCTGCCTGCTTTGCTATTCAGAAAGGATTACAG
GCATCCCGTAGTGACATTAAGTTATTTAAGCATAATGACATGGCTGACCTCGAGCGACTA
CTAAAAGAACAAGAGATCGAAGATCAAAAGAATCCTCGCAAGGCTCGTGTAACTCGGCGT
TTCATTGTAGTAGAAGGATTGTATATGAATACTGGAACTATTTGTCCTCTTCCAGAATTG
GTTAAGTTAAAATACAAATACAAAGCAAGAATCTTCCTGGAGGAAAGCCTTTCATTTGGA
GTCCTAGGAGAGCATGGCCGAGGAGTCACTGAACACTATGGAATCAATATTGATGATATT
GATCTTATCAGTGCCAACATGGAGAATGCACTTGCTTCTATTGGAGGTTTCTGCTGTGGC
AGGTCTTTTGTAATTGACCATCAGCGACTTTCCGGCCAGGGATACTGCTTTTCAGCTTCG
TTACCTCCCCTGTTAGCTGCTGCAGCAATTGAGGCCCTCAACATCATGGAAGAGAATCCA
GGTATTTTTGCAGTGTTGAAGGAAAAGTGCGGACAAATTCATAAAGCTTTACAAGGCATT
TCTGGATTAAAAGTGGTGGGGGAGTCCCTTTCTCCAGCCTTTCACCTACAACTGGAAGAG
AGCACTGGGTCTCGCGAGCAAGATGTCAGACTGCTTCAGGAAATTGTAGATCAATGCATG
AACAGAAGTATTGCATTAACTCAGGCGCGCTACTTGGAGAAAGAAGAGAAGTGTCTCCCT
CCTCCCAGCATTCGGGTTGTGGTCACGGTGGAACAAACAGAGGAAGAACTGGAGAGAGCT
GCGTCCACCATCAAGGAGGTAGCCCAGGCCGTCCTGCTCTAG
|
| Enzyme 35 GenBank Gene ID |
Y08685  |
| Enzyme 35 GeneCard ID |
SPTLC1  |
| Enzyme 35 GenAtlas ID |
SPTLC1  |
| Enzyme 35 HGNC ID |
HGNC:11277  |
| Enzyme 35 Chromosome Location |
9 |
| Enzyme 35 Locus |
9q22.2 |
| Enzyme 35 SNPs |
SNPJam Report  |
| Enzyme 35 General References |
- Weiss B, Stoffel W: Human and murine serine-palmitoyl-CoA transferase--cloning, expression and characterization of the key enzyme in sphingolipid synthesis. Eur J Biochem. 1997 Oct 1;249(1):239-47. [PubMed
]
- Dawkins JL, Hulme DJ, Brahmbhatt SB, Auer-Grumbach M, Nicholson GA: Mutations in SPTLC1, encoding serine palmitoyltransferase, long chain base subunit-1, cause hereditary sensory neuropathy type I. Nat Genet. 2001 Mar;27(3):309-12. [PubMed
]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
- Humphray SJ, Oliver K, Hunt AR, Plumb RW, Loveland JE, Howe KL, Andrews TD, Searle S, Hunt SE, Scott CE, Jones MC, Ainscough R, Almeida JP, Ambrose KD, Ashwell RI, Babbage AK, Babbage S, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beasley H, Beasley O, Bird CP, Bray-Allen S, Brown AJ, Brown JY, Burford D, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Chen Y, Clarke G, Clark SY, Clee CM, Clegg S, Collier RE, Corby N, Crosier M, Cummings AT, Davies J, Dhami P, Dunn M, Dutta I, Dyer LW, Earthrowl ME, Faulkner L, Fleming CJ, Frankish A, Frankland JA, French L, Fricker DG, Garner P, Garnett J, Ghori J, Gilbert JG, Glison C, Grafham DV, Gribble S, Griffiths C, Griffiths-Jones S, Grocock R, Guy J, Hall RE, Hammond S, Harley JL, Harrison ES, Hart EA, Heath PD, Henderson CD, Hopkins BL, Howard PJ, Howden PJ, Huckle E, Johnson C, Johnson D, Joy AA, Kay M, Keenan S, Kershaw JK, Kimberley AM, King A, Knights A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd C, Lloyd DM, Lovell J, Martin S, Mashreghi-Mohammadi M, Matthews L, McLaren S, McLay KE, McMurray A, Milne S, Nickerson T, Nisbett J, Nordsiek G, Pearce AV, Peck AI, Porter KM, Pandian R, Pelan S, Phillimore B, Povey S, Ramsey Y, Rand V, Scharfe M, Sehra HK, Shownkeen R, Sims SK, Skuce CD, Smith M, Steward CA, Swarbreck D, Sycamore N, Tester J, Thorpe A, Tracey A, Tromans A, Thomas DW, Wall M, Wallis JM, West AP, Whitehead SL, Willey DL, Williams SA, Wilming L, Wray PW, Young L, Ashurst JL, Coulson A, Blocker H, Durbin R, Sulston JE, Hubbard T, Jackson MJ, Bentley DR, Beck S, Rogers J, Dunham I: DNA sequence and analysis of human chromosome 9. Nature. 2004 May 27;429(6990):369-74. [PubMed
]
- Hornemann T, Richard S, Rutti MF, Wei Y, von Eckardstein A: Cloning and initial characterization of a new subunit for mammalian serine-palmitoyltransferase. J Biol Chem. 2006 Dec 8;281(49):37275-81. Epub 2006 Oct 4. [PubMed
]
- Han G, Gupta SD, Gable K, Niranjanakumari S, Moitra P, Eichler F, Brown RH Jr, Harmon JM, Dunn TM: Identification of small subunits of mammalian serine palmitoyltransferase that confer distinct acyl-CoA substrate specificities. Proc Natl Acad Sci U S A. 2009 May 19;106(20):8186-91. Epub 2009 May 5. [PubMed
]
- Breslow DK, Collins SR, Bodenmiller B, Aebersold R, Simons K, Shevchenko A, Ejsing CS, Weissman JS: Orm family proteins mediate sphingolipid homeostasis. Nature. 2010 Feb 25;463(7284):1048-53. [PubMed
]
- Verhoeven K, Coen K, De Vriendt E, Jacobs A, Van Gerwen V, Smouts I, Pou-Serradell A, Martin JJ, Timmerman V, De Jonghe P: SPTLC1 mutation in twin sisters with hereditary sensory neuropathy type I. Neurology. 2004 Mar 23;62(6):1001-2. [PubMed
]
- Meggouh F, Bienfait HM, Weterman MA, de Visser M, Baas F: Charcot-Marie-Tooth disease due to a de novo mutation of the RAB7 gene. Neurology. 2006 Oct 24;67(8):1476-8. [PubMed
]
- Sjoblom T, Jones S, Wood LD, Parsons DW, Lin J, Barber TD, Mandelker D, Leary RJ, Ptak J, Silliman N, Szabo S, Buckhaults P, Farrell C, Meeh P, Markowitz SD, Willis J, Dawson D, Willson JK, Gazdar AF, Hartigan J, Wu L, Liu C, Parmigiani G, Park BH, Bachman KE, Papadopoulos N, Vogelstein B, Kinzler KW, Velculescu VE: The consensus coding sequences of human breast and colorectal cancers. Science. 2006 Oct 13;314(5797):268-74. Epub 2006 Sep 7. [PubMed
]
|
| Enzyme 35 Metabolite References |
Not Available |
|
Enzyme 36
[top]
|
| Enzyme 36 ID |
6170 |
| Enzyme 36 Name |
Serine palmitoyltransferase 2 |
| Enzyme 36 Synonyms |
- Long chain base biosynthesis protein 2
- LCB 2
- Long chain base biosynthesis protein 2a
- LCB2a
- Serine-palmitoyl-CoA transferase 2
- SPT 2
|
| Enzyme 36 Gene Name |
SPTLC2 |
| Enzyme 36 Protein Sequence |
>Serine palmitoyltransferase 2
MRPEPGGCCCRRTVRANGCVANGEVRNGYVRSSAAAAAAAAAGQIHHVTQNGGLYKRPFN
EAFEETPMLVAVLTYVGYGVLTLFGYLRDFLRYWRIEKCHHATEREEQKDFVSLYQDFEN
FYTRNLYMRIRDNWNRPICSVPGARVDIMERQSHDYNWSFKYTGNIIKGVINMGSYNYLG
FARNTGSCQEAAAKVLEEYGAGVCSTRQEIGNLDKHEELEELVARFLGVEAAMAYGMGFA
TNSMNIPALVGKGCLILSDELNHASLVLGARLSGATIRIFKHNNMQSLEKLLKDAIVYGQ
PRTRRPWKKILILVEGIYSMEGSIVRLPEVIALKKKYKAYLYLDEAHSIGALGPTGRGVV
EYFGLDPEDVDVMMGTFTKSFGASGGYIGGKKELIDYLRTHSHSAVYATSLSPPVVEQII
TSMKCIMGQDGTSLGKECVQQLAENTRYFRRRLKEMGFIIYGNEDSPVVPLMLYMPAKIG
AFGREMLKRNIGVVVVGFPATPIIESRARFCLSAAHTKEILDTALKEIDEVGDLLQLKYS
RHRLVPLLDRPFDETTYEETED
|
| Enzyme 36 Number of Residues |
562 |
| Enzyme 36 Molecular Weight |
62923.8 |
| Enzyme 36 Theoretical pI |
7.85 |
| Enzyme 36 GO Classification |
| Function |
- binding
- catalytic activity
- cofactor binding
- pyridoxal phosphate binding
- transferase activity
- transferase activity, transferring nitrogenous groups
|
| Process |
- biosynthetic process
- metabolic process
|
| Component |
| — |
|
| Enzyme 36 General Function |
Involved in transferase activity |
| Enzyme 36 Specific Function |
Serine palmitoyltransferase (SPT). The heterodimer formed with LCB1/SPTLC1 constitutes the catalytic core. The composition of the serine palmitoyltransferase (SPT) complex determines the substrate preference. The SPTLC1-SPTLC2-SSSPTA complex shows a strong preference for C16-CoA substrate, while the SPTLC1-SPTLC2-SSSPTB complex displays a preference for C18-CoA substrate |
| Enzyme 36 Pathways |
|
| Enzyme 36 Reactions |
- palmitoyl-CoA + L-serine = CoA + 3-dehydro-D-sphinganine + CO2 [RN:R01281]
|
| Enzyme 36 Pfam Domain Function |
|
| Enzyme 36 Signals |
|
| Enzyme 36 Transmembrane Regions |
|
| Enzyme 36 Essentiality |
Not Available |
| Enzyme 36 GenBank ID Protein |
2564249  |
| Enzyme 36 UniProtKB/Swiss-Prot ID |
O15270  |
| Enzyme 36 UniProtKB/Swiss-Prot Entry Name |
SPTC2_HUMAN  |
| Enzyme 36 PDB ID |
Not Available |
| Enzyme 36 Cellular Location |
Not Available |
| Enzyme 36 Gene Sequence |
>1689 bp
ATGCGGCCGGAGCCCGGAGGCTGCTGCTGCCGCCGCACGGTGCGGGCGAATGGCTGCGTG
GCGAACGGGGAAGTACGGAACGGGTACGTGAGGAGCAGCGCTGCAGCCGCAGCCGCAGCC
GCCGCCGGCCAGATCCATCATGTTACACAAAATGGAGGACTATATAAAAGACCGTTTAAT
GAAGCTTTTGAAGAAACACCAATGCTGGTTGCTGTGCTCACGTATGTGGGGTATGGCGTA
CTCACCCTCTTTGGATATCTTCGAGATTTCTTGAGGTATTGGAGAATTGAAAAGTGTCAC
CATGCAACAGAAAGAGAAGAACAAAAGGACTTTGTGTCATTGTATCAAGATTTTGAAAAC
TTTTATACAAGGAATCTGTACATGAGGATAAGAGACAACTGGAATCGGCCAATCTGTAGT
GTGCCTGGAGCCAGGGTGGACATCATGGAGAGACAGTCTCATGATTATAACTGGTCCTTC
AAGTATACAGGGAATATAATAAAGGGTGTTATAAACATGGGTTCCTACAACTATCTTGGA
TTTGCACGGAATACTGGATCATGTCAAGAAGCAGCCGCCAAAGTCCTTGAGGAGTATGGA
GCTGGAGTGTGCAGTACTCGGCAGGAAATTGGAAACCTGGACAAGCATGAAGAACTAGAG
GAGCTTGTAGCAAGGTTCTTAGGAGTAGAAGCTGCTATGGCGTATGGCATGGGATTTGCA
ACGAATTCAATGAACATTCCTGCTCTTGTTGGCAAAGGTTGCCTGATTCTGAGTGATGAA
CTGAACCATGCATCACTGGTTCTGGGAGCCAGACTGTCAGGAGCAACCATTAGAATCTTC
AAACACAACAATATGCAAAGCCTAGAGAAGCTATTGAAAGATGCCATTGTTTATGGTCAG
CCTCGGACACGAAGGCCCTGGAAGAAAATTCTCATCCTTGTGGAAGGAATATATAGCATG
GAGGGATCTATTGTTCGTCTTCCTGAAGTGATTGCCCTCAAGAAGAAATACAAGGCATAC
TTGTATCTGGATGAGGCTCACAGCATTGGCGCCCTGGGCCCCACAGGCCGGGGTGTGGTG
GAGTACTTTGGCCTGGATCCCGAGGATGTGGATGTTATGATGGGAACGTTCACAAAGAGT
TTTGGTGCTTCTGGAGGATATATTGGAGGCAAGAAGGAGCTGATAGACTACCTGCGAACA
CATTCTCATAGTGCAGTGTATGCCACGTCATTGTCACCTCCTGTAGTGGAGCAGATCATC
ACCTCCATGAAGTGCATCATGGGGCAGGATGGCACCAGCCTTGGTAAAGAGTGTGTACAA
CAGTTAGCTGAAAACACCAGGTATTTCAGGAGACGCCTGAAAGAGATGGGCTTCATCATC
TATGGAAATGAAGACTCTCCAGTAGTGCCTTTGATGCTCTACATGCCTGCCAAAATTGGC
GCCTTTGGACGGGAGATGCTGAAGCGGAACATCGGTGTCGTTGTGGTTGGATTTCCTGCC
ACCCCAATTATTGAGTCCAGAGCCAGGTTTTGCCTGTCAGCAGCTCATACCAAAGAAATA
CTTGATACTGCTTTAAAGGAGATAGATGAAGTTGGGGACCTATTGCAGCTGAAGTATTCC
CGTCATCGGTTGGTACCTCTACTGGACAGGCCCTTTGACGAGACGACGTATGAAGAAACA
GAAGACTGA
|
| Enzyme 36 GenBank Gene ID |
Y08686  |
| Enzyme 36 GeneCard ID |
SPTLC2  |
| Enzyme 36 GenAtlas ID |
SPTLC2  |
| Enzyme 36 HGNC ID |
HGNC:11278  |
| Enzyme 36 Chromosome Location |
1 |
| Enzyme 36 Locus |
14q24.3 |
| Enzyme 36 SNPs |
SNPJam Report  |
| Enzyme 36 General References |
- Weiss B, Stoffel W: Human and murine serine-palmitoyl-CoA transferase--cloning, expression and characterization of the key enzyme in sphingolipid synthesis. Eur J Biochem. 1997 Oct 1;249(1):239-47. [PubMed
]
- Nagase T, Ishikawa K, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O: Prediction of the coding sequences of unidentified human genes. IX. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro. DNA Res. 1998 Feb 28;5(1):31-9. [PubMed
]
- Heilig R, Eckenberg R, Petit JL, Fonknechten N, Da Silva C, Cattolico L, Levy M, Barbe V, de Berardinis V, Ureta-Vidal A, Pelletier E, Vico V, Anthouard V, Rowen L, Madan A, Qin S, Sun H, Du H, Pepin K, Artiguenave F, Robert C, Cruaud C, Bruls T, Jaillon O, Friedlander L, Samson G, Brottier P, Cure S, Segurens B, Aniere F, Samain S, Crespeau H, Abbasi N, Aiach N, Boscus D, Dickhoff R, Dors M, Dubois I, Friedman C, Gouyvenoux M, James R, Madan A, Mairey-Estrada B, Mangenot S, Martins N, Menard M, Oztas S, Ratcliffe A, Shaffer T, Trask B, Vacherie B, Bellemere C, Belser C, Besnard-Gonnet M, Bartol-Mavel D, Boutard M, Briez-Silla S, Combette S, Dufosse-Laurent V, Ferron C, Lechaplais C, Louesse C, Muselet D, Magdelenat G, Pateau E, Petit E, Sirvain-Trukniewicz P, Trybou A, Vega-Czarny N, Bataille E, Bluet E, Bordelais I, Dubois M, Dumont C, Guerin T, Haffray S, Hammadi R, Muanga J, Pellouin V, Robert D, Wunderle E, Gauguet G, Roy A, Sainte-Marthe L, Verdier J, Verdier-Discala C, Hillier L, Fulton L, McPherson J, Matsuda F, Wilson R, Scarpelli C, Gyapay G, Wincker P, Saurin W, Quetier F, Waterston R, Hood L, Weissenbach J: The DNA sequence and analysis of human chromosome 14. Nature. 2003 Feb 6;421(6923):601-7. Epub 2003 Jan 1. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Nagiec MM, Lester RL, Dickson RC: Sphingolipid synthesis: identification and characterization of mammalian cDNAs encoding the Lcb2 subunit of serine palmitoyltransferase. Gene. 1996 Oct 24;177(1-2):237-41. [PubMed
]
- Takeda J, Yano H, Eng S, Zeng Y, Bell GI: A molecular inventory of human pancreatic islets: sequence analysis of 1000 cDNA clones. Hum Mol Genet. 1993 Nov;2(11):1793-8. [PubMed
]
- Hornemann T, Richard S, Rutti MF, Wei Y, von Eckardstein A: Cloning and initial characterization of a new subunit for mammalian serine-palmitoyltransferase. J Biol Chem. 2006 Dec 8;281(49):37275-81. Epub 2006 Oct 4. [PubMed
]
- Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed
]
- Han G, Gupta SD, Gable K, Niranjanakumari S, Moitra P, Eichler F, Brown RH Jr, Harmon JM, Dunn TM: Identification of small subunits of mammalian serine palmitoyltransferase that confer distinct acyl-CoA substrate specificities. Proc Natl Acad Sci U S A. 2009 May 19;106(20):8186-91. Epub 2009 May 5. [PubMed
]
|
| Enzyme 36 Metabolite References |
Not Available |
|
Enzyme 37
[top]
|
| Enzyme 37 ID |
6224 |
| Enzyme 37 Name |
Cysteine sulfinic acid decarboxylase |
| Enzyme 37 Synonyms |
- Cysteine-sulfinate decarboxylase
- Sulfinoalanine decarboxylase
|
| Enzyme 37 Gene Name |
CSAD |
| Enzyme 37 Protein Sequence |
>Cysteine sulfinic acid decarboxylase
MADSEALPSLAGDPVAVEALLRAVFGVVVDEAIQKGTSVSQKVCEWKEPEELKQLLDLEL
RSQGESQKQILERCRAVIRYSVKTGHPRFFNQLFSGLDPHALAGRIITESLNTSQYTYEI
APVFVLMEEEVLRKLRALVGWSSGDGIFCPGGSISNMYAVNLARYQRYPDCKQRGLRTLP
PLALFTSKECHYSIQKGAAFLGLGTDSVRVVKADERGKMVPEDLERQIGMAEAEGAVPFL
VSATSGTTVLGAFDPLEAIADVCQRHGLWLHVDAAWGGSVLLSQTHRHLLDGIQRADSVA
WNPHKLLAAGLQCSALLLQDTSNLLKRCHGSQASYLFQQDKFYDVALDTGDKVVQCGRRV
DCLKLWLMWKAQGDQGLERRIDQAFVLARYLVEEMKKREGFELVMEPEFVNVCFWFVPPS
LRGKQESPDYHERLSKVAPVLKERMVKEGSMMIGYQPHGTRGNFFRVVVANSALTCADMD
FLLNELERLGQDL
|
| Enzyme 37 Number of Residues |
493 |
| Enzyme 37 Molecular Weight |
55022.8 |
| Enzyme 37 Theoretical pI |
6.44 |
| Enzyme 37 GO Classification |
| Function |
- binding
- carbon-carbon lyase activity
- carboxy-lyase activity
- catalytic activity
- cofactor binding
- lyase activity
- pyridoxal phosphate binding
|
| Process |
- carboxylic acid metabolic process
- cellular metabolic process
- metabolic process
- organic acid metabolic process
- oxoacid metabolic process
|
| Component |
| — |
|
| Enzyme 37 General Function |
Involved in carboxy-lyase activity |
| Enzyme 37 Specific Function |
3-sulfino-L-alanine = hypotaurine + CO(2) |
| Enzyme 37 Pathways |
- Taurine and Hypotaurine Metabolism (map00430
)
|
| Enzyme 37 Reactions |
- 3-sulfino-L-alanine = hypotaurine + CO2 [RN:R02466]
|
| Enzyme 37 Pfam Domain Function |
|
| Enzyme 37 Signals |
|
| Enzyme 37 Transmembrane Regions |
|
| Enzyme 37 Essentiality |
Not Available |
| Enzyme 37 GenBank ID Protein |
4894560  |
| Enzyme 37 UniProtKB/Swiss-Prot ID |
Q9Y600  |
| Enzyme 37 UniProtKB/Swiss-Prot Entry Name |
CSAD_HUMAN  |
| Enzyme 37 PDB ID |
Not Available |
| Enzyme 37 Cellular Location |
Not Available |
| Enzyme 37 Gene Sequence |
>1482 bp
ATGGCTGACTCAGAAGCACTCCCCTCCCTTGCTGGGGACCCAGTGGCTGTGGAAGCCTTG
CTCCGGGCCGTGTTTGGGGTTGTTGTGGATGAGGCCATTCAGAAAGGAACCAGTGTCTCC
CAGAAGGTCTGTGAGTGGAAGGAGCCTGAGGAGCTGAAGCAGCTGCTGGATTTGGAGCTG
CGGAGCCAGGGCGAGTCACAGAAGCAGATCCTGGAGCGGTGTCGGGCTGTGATTCGCTAC
AGTGTCAAGACTGGTCACCCTCGGTTCTTCAACCAGCTCTTCTCTGGGTTGGATCCCCAT
GCTCTGGCCGGGCGCATTATCACTGAGAGCCTCAACACCAGCCAGTACACATATGAAATC
GCCCCCGTGTTTGTGCTCATGGAAGAGGAGGTGCTGAGGAAACTGCGGGCCCTGGTGGGC
TGGAGCTCTGGGGACGGAATCTTCTGCCCTGGTGGCTCCATCTCCAACATGTATGCTGTA
AATCTGGCCCGCTATCAGCGCTACCCGGATTGCAAGCAGAGGGGCCTCCGCACACTGCCG
CCCCTGGCCCTATTCACATCGAAGGAGTGTCACTACTCCATCCAGAAGGGAGCTGCGTTT
CTGGGACTTGGCACCGACAGTGTCCGAGTGGTCAAGGCTGATGAGAGAGGGAAAATGGTC
CCCGAGGATCTGGAGAGGCAGATTGGTATGGCCGAGGCTGAGGGTGCTGTGCCGTTCCTG
GTCAGTGCCACCTCTGGCACCACTGTGCTAGGGGCCTTTGACCCCCTGGGGGCAATTGCT
GATGTGTGCCAGCGTCATGGGCTATGGCTGCATGTGGATGCTGCCTGGGGTGGGAGCGTC
CTGCTGTCACAGACACACAGGCATCTCCTGGATGGGATCCAGAGGGCTGACTCTGTGGCC
TGGAATCCCCACAAGCTCCTCGCAGCAGGCCTGCAATGCTCTGCACTTCTTCTCCAGGAT
ACCTCGAACCTGCTCAAGCGCTGCCATGGGTCCCAGGCCAGCTACCTTTTCCAGCAGGAC
AAGTTCTACGATGTGGCTCTGGACACGGGAGACAAGGTGGTGCAGTGTGGCCGCCGTGTG
GACTGTCTGAAGCTGTGGCTCATGTGGAAGGCACAGGGCGATCAAGGGCTGGAGCGGCGC
ATCGACCAGGCCTTTGTCCTTGCCCGGTACCTGGTGGAGGAAATGAAGAAGCGGGAAGGG
TTTGAGCTAGTCATGGAGCCTGAGTTTGTCAATGTGTGTTTCTGGTTCGTACCCCCCAGC
CTGCGAGGGAAGCAGGAGAGTCCAGATTACCACGAAAGGCTGTCAAAGGTGGCCCCCGTG
CTCAAGGAGCGCATGGTGAAGGAGGGCTCCATGATGATTGGCTACCAGCCCCACGGGACC
CGGGGCAACTTCTTCCGTGTGGTTGTGGCCAACTCTGCACTGACCTGTGCTGATATGGAC
TTCCTCCTCAACGAGCTGGAGCGGCTAGGCCAGGACCTGTGA
|
| Enzyme 37 GenBank Gene ID |
AF116547  |
| Enzyme 37 GeneCard ID |
CSAD  |
| Enzyme 37 GenAtlas ID |
CSAD  |
| Enzyme 37 HGNC ID |
HGNC:18966  |
| Enzyme 37 Chromosome Location |
1 |
| Enzyme 37 Locus |
12q13.11-q14.3 |
| Enzyme 37 SNPs |
SNPJam Report  |
| Enzyme 37 General References |
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
|
| Enzyme 37 Metabolite References |
Not Available |
|
Enzyme 38
[top]
|
| Enzyme 38 ID |
6322 |
| Enzyme 38 Name |
Ornithine decarboxylase |
| Enzyme 38 Synonyms |
- ODC
|
| Enzyme 38 Gene Name |
ODC1 |
| Enzyme 38 Protein Sequence |
>Ornithine decarboxylase
MNNFGNEEFDCHFLDEGFTAKDILDQKINEVSSSDDKDAFYVADLGDILKKHLRWLKALP
RVTPFYAVKCNDSKAIVKTLAATGTGFDCASKTEIQLVQSLGVPPERIIYANPCKQVSQI
KYAANNGVQMMTFDSEVELMKVARAHPKAKLVLRIATDDSKAVCRLSVKFGATLRTSRLL
LERAKELNIDVVGVSFHVGSGCTDPETFVQAISDARCVFDMGAEVGFSMYLLDIGGGFPG
SEDVKLKFEEITGVINPALDKYFPSDSGVRIIAEPGRYYVASAFTLAVNIIAKKIVLKEQ
TGSDDEDESSEQTFMYYVNDGVYGSFNCILYDHAHVKPLLQKRPKPDEKYYSSSIWGPTC
DGLDRIVERCDLPEMHVGDWMLFENMGAYTVAAASTFNGFQRPTIYYVMSGPAWQLMQQF
QNPDFPPEVEEQDASTLPVSCAWESGMKRHRAACASASINV
|
| Enzyme 38 Number of Residues |
461 |
| Enzyme 38 Molecular Weight |
51147.7 |
| Enzyme 38 Theoretical pI |
4.88 |
| Enzyme 38 GO Classification |
| Function |
|
| Process |
- cellular amino acid and derivative metabolic process
- cellular amino acid derivative metabolic process
- cellular biogenic amine metabolic process
- cellular metabolic process
- metabolic process
- polyamine biosynthetic process
- polyamine metabolic process
|
| Component |
| — |
|
| Enzyme 38 General Function |
Involved in catalytic activity |
| Enzyme 38 Specific Function |
L-ornithine = putrescine + CO(2) |
| Enzyme 38 Pathways |
- Arginine and Proline Metabolism (map00330
)
|
| Enzyme 38 Reactions |
- L-ornithine = putrescine + CO2 [RN:R00670]
|
| Enzyme 38 Pfam Domain Function |
|
| Enzyme 38 Signals |
|
| Enzyme 38 Transmembrane Regions |
|
| Enzyme 38 Essentiality |
Not Available |
| Enzyme 38 GenBank ID Protein |
29893806  |
| Enzyme 38 UniProtKB/Swiss-Prot ID |
P11926  |
| Enzyme 38 UniProtKB/Swiss-Prot Entry Name |
DCOR_HUMAN  |
| Enzyme 38 PDB ID |
1D7K  |
| Enzyme 38 PDB File |
Show |
| Enzyme 38 3D Structure |
|
| Enzyme 38 Cellular Location |
Not Available |
| Enzyme 38 Gene Sequence |
>1386 bp
ATGAACAACTTTGGTAATGAAGAGTTTGACTGCCACTTCCTCGATGAAGGTTTTACTGCC
AAGGACATTCTGGACCAGAAAATTAATGAAGTTTCTTCTTCTGATGATAAGGATGCCTTC
TATGTGGCAGACCTGGGAGACATTCTAAAGAAACATCTGAGGTGGTTAAAAGCTCTCCCT
CGTGTCACCCCCTTTTATGCAGTCAAATGTAATGATAGCAAAGCCATCGTGAAGACCCTT
GCTGCTACCGGGACAGGATTTGACTGTGCTAGCAAGACTGAAATACAGTTGGTGCAGAGT
CTGGGGGTGCCTCCAGAGAGGATTATCTATGCAAATCCTTGTAAACAAGTATCTCAAATT
AAGTATGCTGCTAATAATGGAGTCCAGATGATGACTTTTGATAGTGAAGTTGAGTTGATG
AAAGTTGCCAGAGCACATCCCAAAGCAAAGTTGGTTTTGCGGATTGCCACTGATGATTCC
AAAGCAGTCTGTCGTCTCAGTGTGAAATTCGGTGCCACGCTCAGAACCAGCAGGCTCCTT
TTGGAACGGGCGAAAGAGCTAAATATCGATGTTGTTGGTGTCAGCTTCCATGTAGGAAGC
GGCTGTACCGATCCTGAGACCTTCGTGCAGGCAATCTCTGATGCCCGCTGTGTTTTTGAC
ATGGGGGCTGAGGTTGGTTTCAGCATGTATCTGCTTGATATTGGCGGTGGCTTTCCTGGA
TCTGAGGATGTGAAACTTAAATTTGAAGAGATCACCGGCGTAATCAACCCAGCGTTGGAC
AAATACTTTCCGTCAGACTCTGGAGTGAGAATCATAGCTGAGCCCGGCAGATACTATGTT
GCATCAGCTTTCACGCTTGCAGTTAATATCATTGCCAAGAAAATTGTATTAAAGGAACAG
ACGGGCTCTGATGACGAAGATGAGTCGAGTGAGCAGACCTTTATGTATTATGTGAATGAT
GGCGTCTATGGATCATTTAATTGCATACTCTATGACCACGCACATGTAAAGCCCCTTCTG
CAAAAGAGACCTAAACCAGATGAGAAGTATTATTCATCCAGCATATGGGGACCAACATGT
GATGGCCTCGATCGGATTGTTGAGCGCTGTGACCTGCCTGAAATGCATGTGGGTGATTGG
ATGCTCTTTGAAAACATGGGCGCTTACACTGTTGCTGCTGCCTCTACGTTCAATGGCTTC
CAGAGGCCGACGATCTACTATGTGATGTCAGGGCCTGCGTGGCAACTCATGCAGCAATTC
CAGAACCCCGACTTCCCACCCGAAGTAGAGGAACAGGATGCCAGCACCCTGCCTGTGTCT
TGTGCCTGGGAGAGTGGGATGAAACGCCACAGAGCAGCCTGTGCTTCGGCTAGTATTAAT
GTGTAG
|
| Enzyme 38 GenBank Gene ID |
M16650  |
| Enzyme 38 GeneCard ID |
ODC1  |
| Enzyme 38 GenAtlas ID |
ODC1  |
| Enzyme 38 HGNC ID |
HGNC:8109  |
| Enzyme 38 Chromosome Location |
2 |
| Enzyme 38 Locus |
2p25 |
| Enzyme 38 SNPs |
SNPJam Report  |
| Enzyme 38 General References |
- Hickok NJ, Seppanen PJ, Gunsalus GL, Janne OA: Complete amino acid sequence of human ornithine decarboxylase deduced from complementary DNA. DNA. 1987 Jun;6(3):179-87. [PubMed
]
- Fitzgerald MC, Flanagan MA: Characterization and sequence analysis of the human ornithine decarboxylase gene. DNA. 1989 Nov;8(9):623-34. [PubMed
]
- van Steeg H, van Oostrom CT, Martens JW, van Kreyl C, Schepens J, Wieringa B: Nucleotide sequence of the human ornithine decarboxylase gene. Nucleic Acids Res. 1989 Nov 11;17(21):8855-6. [PubMed
]
- Hickok NJ, Wahlfors J, Crozat A, Halmekyto M, Alhonen L, Janne J, Janne OA: Human ornithine decarboxylase-encoding loci: nucleotide sequence of the expressed gene and characterization of a pseudogene. Gene. 1990 Sep 14;93(2):257-63. [PubMed
]
- Moshier JA, Gilbert JD, Skunca M, Dosescu J, Almodovar KM, Luk GD: Isolation and expression of a human ornithine decarboxylase gene. J Biol Chem. 1990 Mar 25;265(9):4884-92. [PubMed
]
- Moshier JA, Osborne DL, Skunca M, Dosescu J, Gilbert JD, Fitzgerald MC, Polidori G, Wagner RL, Friezner Degen SJ, Luk GD, et al.: Multiple promoter elements govern expression of the human ornithine decarboxylase gene in colon carcinoma cells. Nucleic Acids Res. 1992 May 25;20(10):2581-90. [PubMed
]
- Wright PS, Cooper JR, Cross-Doersen DE, Miller JA, Chmielewski PA, Wagner RL, Streng KA, Flanagan MA: Regulation of ornithine decarboxylase mRNA levels in human breast cancer cells: pattern of expression and involvement of core enhancer promoter element. Cell Growth Differ. 1995 Sep;6(9):1097-102. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Hsieh JT, Denning MF, Heidel SM, Verma AK: Expression of human chromosome 2 ornithine decarboxylase gene in ornithine decarboxylase-deficient Chinese hamster ovary cells. Cancer Res. 1990 Apr 15;50(8):2239-44. [PubMed
]
- Kaczmarek L, Calabretta B, Ferrari S, de Riel JK: Cell-cycle-dependent expression of human ornithine decarboxylase. J Cell Physiol. 1987 Sep;132(3):545-51. [PubMed
]
- Bauer PM, Fukuto JM, Buga GM, Pegg AE, Ignarro LJ: Nitric oxide inhibits ornithine decarboxylase by S-nitrosylation. Biochem Biophys Res Commun. 1999 Aug 27;262(2):355-8. [PubMed
]
- Bauer PM, Buga GM, Fukuto JM, Pegg AE, Ignarro LJ: Nitric oxide inhibits ornithine decarboxylase via S-nitrosylation of cysteine 360 in the active site of the enzyme. J Biol Chem. 2001 Sep 14;276(37):34458-64. Epub 2001 Jul 18. [PubMed
]
- Leong WF, Chow VT: Transcriptomic and proteomic analyses of rhabdomyosarcoma cells reveal differential cellular gene expression in response to enterovirus 71 infection. Cell Microbiol. 2006 Apr;8(4):565-80. [PubMed
]
- Almrud JJ, Oliveira MA, Kern AD, Grishin NV, Phillips MA, Hackert ML: Crystal structure of human ornithine decarboxylase at 2.1 A resolution: structural insights to antizyme binding. J Mol Biol. 2000 Jan 7;295(1):7-16. [PubMed
]
|
| Enzyme 38 Metabolite References |
Not Available |
|
Enzyme 39
[top]
|
| Enzyme 39 ID |
6341 |
| Enzyme 39 Name |
Sphingosine-1-phosphate lyase 1 |
| Enzyme 39 Synonyms |
- SP-lyase 1
- SPL 1
- hSPL
- Sphingosine-1-phosphate aldolase
|
| Enzyme 39 Gene Name |
SGPL1 |
| Enzyme 39 Protein Sequence |
>Sphingosine-1-phosphate lyase 1
MPSTDLLMLKAFEPYLEILEVYSTKAKNYVNGHCTKYEPWQLIAWSVVWTLLIVWGYEFV
FQPESLWSRFKKKCFKLTRKMPIIGRKIQDKLNKTKDDISKNMSFLKVDKEYVKALPSQG
LSSSAVLEKLKEYSSMDAFWQEGRASGTVYSGEEKLTELLVKAYGDFAWSNPLHPDIFPG
LRKIEAEIVRIACSLFNGGPDSCGCVTSGGTESILMACKAYRDLAFEKGIKTPEIVAPQS
AHAAFNKAASYFGMKIVRVPLTKMMEVDVRAMRRAISRNTAMLVCSTPQFPHGVIDPVPE
VAKLAVKYKIPLHVDACLGGFLIVFMEKAGYPLEHPFDFRVKGVTSISADTHKYGYAPKG
SSLVLYSDKKYRNYQFFVDTDWQGGIYASPTIAGSRPGGISAACWAALMHFGENGYVEAT
KQIIKTARFLKSELENIKGIFVFGNPQLSVIALGSRDFDIYRLSNLMTAKGWNLNQLQFP
PSIHFCITLLHARKRVAIQFLKDIRESVTQIMKNPKAKTTGMGAIYGMAQTTVDRNMVAE
LSSVFLDSLYSTDTVTQGSQMNGSPKPH
|
| Enzyme 39 Number of Residues |
568 |
| Enzyme 39 Molecular Weight |
63523.3 |
| Enzyme 39 Theoretical pI |
9.57 |
| Enzyme 39 GO Classification |
| Function |
- binding
- carbon-carbon lyase activity
- carboxy-lyase activity
- catalytic activity
- cofactor binding
- lyase activity
- pyridoxal phosphate binding
|
| Process |
- carboxylic acid metabolic process
- cellular metabolic process
- metabolic process
- organic acid metabolic process
- oxoacid metabolic process
|
| Component |
| — |
|
| Enzyme 39 General Function |
Involved in carboxy-lyase activity |
| Enzyme 39 Specific Function |
Cleaves phosphorylated sphingoid bases (PSBs), such as sphingosine-1-phosphate, into fatty aldehydes and phosphoethanolamine. Elevates stress-induced ceramide production and apoptosis |
| Enzyme 39 Pathways |
|
| Enzyme 39 Reactions |
- sphinganine 1-phosphate = phosphoethanolamine + palmitaldehyde [RN:R02464]
|
| Enzyme 39 Pfam Domain Function |
|
| Enzyme 39 Signals |
|
| Enzyme 39 Transmembrane Regions |
|
| Enzyme 39 Essentiality |
Not Available |
| Enzyme 39 GenBank ID Protein |
10129683  |
| Enzyme 39 UniProtKB/Swiss-Prot ID |
O95470  |
| Enzyme 39 UniProtKB/Swiss-Prot Entry Name |
SGPL1_HUMAN  |
| Enzyme 39 PDB ID |
Not Available |
| Enzyme 39 Cellular Location |
Not Available |
| Enzyme 39 Gene Sequence |
>1707 bp
ATGCCTAGCACAGACCTTCTGATGTTGAAGGCCTTTGAGCCCTACTTAGAGATTTTGGAA
GTATACTCCACAAAAGCCAAGAATTATGTAAATGGACATTGCACCAAGTATGAGCCCTGG
CAGCTAATTGCATGGAGTGTCGTGTGGACCCTGCTGATAGTCTGGGGATATGAGTTTGTC
TTCCAGCCAGAGAGTTTATGGTCAAGGTTTAAAAAGAAATGTTTTAAGCTCACCAGGAAG
ATGCCCATTATTGGTCGTAAGATTCAAGACAAGTTGAACAAGACCAAGGATGATATTAGC
AAGAACATGTCATTCCTGAAAGTGGACAAAGAGTATGTGAAAGCTTTACCCTCCCAGGGT
CTGAGCTCATCTGCTGTTTTGGAGAAACTTAAGGAGTACAGCTCTATGGACGCCTTCTGG
CAAGAGGGGAGAGCCTCTGGAACAGTGTACAGTGGGGAGGAGAAGCTCACTGAGCTCCTT
GTGAAGGCTTATGGAGATTTTGCATGGAGTAACCCCCTGCATCCAGATATCTTCCCAGGA
CTACGCAAGATAGAGGCAGAAATTGTGAGGATAGCTTGTTCCCTGTTCAATGGGGGACCA
GATTCGTGTGGATGTGTGACTTCTGGGGGAACAGAAAGCATACTGATGGCCTGCAAAGCA
TATCGGGATCTGGCCTTTGAGAAGGGGATCAAAACTCCAGAAATTGTGGCTCCCCAAAGT
GCCCATGCTGCATTTAACAAAGCAGCCAGTTACTTTGGGATGAAGATTGTGCGGGTCCCA
TTGACGAAGATGATGGAGGTGGATGTGCGGGCAATGAGAAGAGCTATCTCCAGGAACACT
GCCATGCTCGTCTGTTCTACCCCACAGTTTCCTCATGGTGTAATAGATCCTGTCCCTGAA
GTGGCCAAGCTGGCTGTCAAATACAAAATACCCCTTCATGTCGACGCTTGTCTGGGAGGC
TTCCTCATCGTCTTTATGGAGAAAGCAGGATACCCACTGGAGCACCCATTTGATTTCCGG
GTGAAAGGTGTAACCAGCATTTCAGCTGACACCCATAAGTATGGCTATGCCCCAAAAGGC
TCATCATTGGTGTTGTATAGTGACAAGAAGTACAGGAACTATCAGTTCTTCGTCGATACA
GATTGGCAGGGTGGCATCTATGCTTCCCCAACCATCGCAGGCTCACGGCCTGGTGGCATT
AGCGCAGCTGCTTGGGCTGCCTTGATGCACTTCGGTGAGAACGGCTATGTTGAAGCTACC
AAACAGATCATCAAAACTGCTCGCTTCCTCAAGTCAGAACTGGAAAATATCAAAGGCATC
TTTGTTTTTGGGAATCCCCAATTGTCAGTCATTGCTCTGGGATCCCGTGATTTTGACATC
TACCGACTATCAAACCTGATGACTGCTAAGGGGTGGAACTTGAACCAGTTGCAGTTCCCA
CCCAGTATTCATTTCTGCATCACATTACTACACGCCCGGAAACGAGTAGCTATACAATTC
CTAAAGGACATTCGAGAATCTGTCACTCAAATCATGAAGAATCCTAAAGCGAAGACCACA
GGAATGGGTGCCATCTATGGCATGGCCCAGACAACTGTTGACAGGAATATGGTTGCAGAA
TTGTCCTCAGTCTTCTTGGACAGCTTGTACAGCACCGACACTGTCACCCAGGGCAGCCAG
ATGAATGGTTCTCCAAAACCCCACTGA
|
| Enzyme 39 GenBank Gene ID |
AJ011304  |
| Enzyme 39 GeneCard ID |
SGPL1  |
| Enzyme 39 GenAtlas ID |
SGPL1  |
| Enzyme 39 HGNC ID |
HGNC:10817  |
| Enzyme 39 Chromosome Location |
1 |
| Enzyme 39 Locus |
10q21 |
| Enzyme 39 SNPs |
SNPJam Report  |
| Enzyme 39 General References |
- Van Veldhoven PP, Gijsbers S, Mannaerts GP, Vermeesch JR, Brys V: Human sphingosine-1-phosphate lyase: cDNA cloning, functional expression studies and mapping to chromosome 10q22(1). Biochim Biophys Acta. 2000 Sep 27;1487(2-3):128-34. [PubMed
]
- Reiss U, Oskouian B, Zhou J, Gupta V, Sooriyakumaran P, Kelly S, Wang E, Merrill AH Jr, Saba JD: Sphingosine-phosphate lyase enhances stress-induced ceramide generation and apoptosis. J Biol Chem. 2004 Jan 9;279(2):1281-90. Epub 2003 Oct 21. [PubMed
]
- Nagase T, Ishikawa K, Kikuno R, Hirosawa M, Nomura N, Ohara O: Prediction of the coding sequences of unidentified human genes. XV. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro. DNA Res. 1999 Oct 29;6(5):337-45. [PubMed
]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Zhan X, Desiderio DM: Nitroproteins from a human pituitary adenoma tissue discovered with a nitrotyrosine affinity column and tandem mass spectrometry. Anal Biochem. 2006 Jul 15;354(2):279-89. Epub 2006 Jun 5. [PubMed
]
- Daub H, Olsen JV, Bairlein M, Gnad F, Oppermann FS, Korner R, Greff Z, Keri G, Stemmann O, Mann M: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. Mol Cell. 2008 Aug 8;31(3):438-48. [PubMed
]
- Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed
]
- Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed
]
|
| Enzyme 39 Metabolite References |
Not Available |
|
Enzyme 40
[top]
|
| Enzyme 40 ID |
6344 |
| Enzyme 40 Name |
Pyridoxal kinase |
| Enzyme 40 Synonyms |
- Pyridoxine kinase
|
| Enzyme 40 Gene Name |
PDXK |
| Enzyme 40 Protein Sequence |
>Pyridoxal kinase
MEEECRVLSIQSHVIRGYVGNRAATFPLQVLGFEIDAVNSVQFSNHTGYAHWKGQVLNSD
ELQELYEGLRLNNMNKYDYVLTGYTRDKSFLAMVVDIVQELKQQNPRLVYVCDPVLGDKW
DGEGSMYVPEDLLPVYKEKVVPLADIITPNQFEAELLSGRKIHSQEEALRVMDMLHSMGP
DTVVITSSDLPSPQGSNYLIVLGSQRRRNPAGSVVMERIRMDIRKVDAVFVGTGDLFAAM
LLAWTHKHPNNLKVACEKTVSTLHHVLQRTIQCAKAQAGEGVRPSPMQLELRMVQSKRDI
EDPEIVVQATVL
|
| Enzyme 40 Number of Residues |
312 |
| Enzyme 40 Molecular Weight |
35102.1 |
| Enzyme 40 Theoretical pI |
6.05 |
| Enzyme 40 GO Classification |
| Function |
- catalytic activity
- kinase activity
- pyridoxal kinase activity
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- metabolic process
- pyridoxine biosynthetic process
- pyridoxine metabolic process
- small molecule metabolic process
- vitamin B6 metabolic process
- vitamin metabolic process
- water-soluble vitamin metabolic process
|
| Component |
| — |
|
| Enzyme 40 General Function |
Involved in pyridoxal kinase activity |
| Enzyme 40 Specific Function |
Required for synthesis of pyridoxal-5-phosphate from vitamin B6 |
| Enzyme 40 Pathways |
|
| Enzyme 40 Reactions |
- ATP + pyridoxal = ADP + pyridoxal 5'-phosphate [RN:R00174]
|
| Enzyme 40 Pfam Domain Function |
|
| Enzyme 40 Signals |
|
| Enzyme 40 Transmembrane Regions |
|
| Enzyme 40 Essentiality |
Not Available |
| Enzyme 40 GenBank ID Protein |
Not Available |
| Enzyme 40 UniProtKB/Swiss-Prot ID |
O00764  |
| Enzyme 40 UniProtKB/Swiss-Prot Entry Name |
PDXK_HUMAN  |
| Enzyme 40 PDB ID |
1RFV  |
| Enzyme 40 PDB File |
Show |
| Enzyme 40 3D Structure |
|
| Enzyme 40 Cellular Location |
Not Available |
| Enzyme 40 Gene Sequence |
>939 bp
ATGGAGGAGGAGTGCCGGGTGCTCTCCATACAGAGCCACGTCATCCGCGGCTACGTGGGC
AACCGGGCGGCCACGTTCCCGCTGCAGGTTTTGGGATTTGAGATTGACGCGGTGAACTCT
GTCCAGTTTTCAAACCACACAGGCTATGCCCACTGGAAGGGCCAAGTGCTGAATTCAGAT
GAGCTCCAGGAGTTGTACGAAGGCCTGAGGCTGAACAACATGAATAAATATGACTACGTG
CTCACAGGTTATACGAGGGACAAGTCGTTCCTGGCCATGGTGGTGGACATTGTGCAGGAG
CTGAAGCAGCAGAACCCCAGGCTGGTGTACGTGTGTGATCCAGTCTTGGGTGACAAGTGG
GACGGCGAAGGCTCGATGTACGTCCCGGAGGACCTCCTTCCCGTCTACAAAGAAAAAGTG
GTGCCGCTTGCAGACATTATCACGCCCAACCAGTTTGAGGCCGAGTTACTGAGTGGCCGG
AAGATCCACAGCCAGGAGGAAGCCTTGCGGGTGATGGACATGCTGCACTCTATGGGCCCC
GACACCGTGGTCATCACCAGCTCCGACCTGCCCTCCCCGCAGGGCAGCAACTACCTGATT
GTGCTGGGGAGTCAGAGGAGGAGGAATCCCGCTGGCTCCGTGGTGATGGAACGCATCCGG
ATGGACATTCGCAAAGTGGACGCCGTCTTTGTGGGCACTGGGGACCTGTTTGCTGCCATG
CTCCTGGCGTGGACACACAAGCACCCCAATAACCTCAAGGTGGCCTGTGAGAAGACCGTG
TCTACCTTGCACCACGTTCTGCAGAGGACCATCCAGTGTGCAAAAGCCCAGGCCGGGGAA
GGAGTGAGGCCCAGCCCCATGCAGCTGGAGCTGCGGATGGTGCAGAGCAAAAGGGACATC
GAGGACCCAGAGATCGTCGTCCAGGCCACGGTGCTGTGA
|
| Enzyme 40 GenBank Gene ID |
U89606  |
| Enzyme 40 GeneCard ID |
PDXK  |
| Enzyme 40 GenAtlas ID |
PDXK  |
| Enzyme 40 HGNC ID |
HGNC:8819  |
| Enzyme 40 Chromosome Location |
2 |
| Enzyme 40 Locus |
21q22.3 |
| Enzyme 40 SNPs |
SNPJam Report  |
| Enzyme 40 General References |
- Hanna MC, Turner AJ, Kirkness EF: Human pyridoxal kinase. cDNA cloning, expression, and modulation by ligands of the benzodiazepine receptor. J Biol Chem. 1997 Apr 18;272(16):10756-60. [PubMed
]
- Fang X, Zhou ZM, Lu L, Yin LL, Li JM, Zhen Y, Wang H, Sha JH: Expression of a novel pyridoxal kinase mRNA splice variant, PKH-T, in human testis. Asian J Androl. 2004 Jun;6(2):83-91. [PubMed
]
- Hattori M, Fujiyama A, Taylor TD, Watanabe H, Yada T, Park HS, Toyoda A, Ishii K, Totoki Y, Choi DK, Groner Y, Soeda E, Ohki M, Takagi T, Sakaki Y, Taudien S, Blechschmidt K, Polley A, Menzel U, Delabar J, Kumpf K, Lehmann R, Patterson D, Reichwald K, Rump A, Schillhabel M, Schudy A, Zimmermann W, Rosenthal A, Kudoh J, Schibuya K, Kawasaki K, Asakawa S, Shintani A, Sasaki T, Nagamine K, Mitsuyama S, Antonarakis SE, Minoshima S, Shimizu N, Nordsiek G, Hornischer K, Brant P, Scharfe M, Schon O, Desario A, Reichelt J, Kauer G, Blocker H, Ramser J, Beck A, Klages S, Hennig S, Riesselmann L, Dagand E, Haaf T, Wehrmeyer S, Borzym K, Gardiner K, Nizetic D, Francis F, Lehrach H, Reinhardt R, Yaspo ML: The DNA sequence of human chromosome 21. Nature. 2000 May 18;405(6784):311-9. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Lee HS, Moon BJ, Choi SY, Kwon OS: Human pyridoxal kinase: overexpression and properties of the recombinant enzyme. Mol Cells. 2000 Aug 31;10(4):452-9. [PubMed
]
- Daub H, Olsen JV, Bairlein M, Gnad F, Oppermann FS, Korner R, Greff Z, Keri G, Stemmann O, Mann M: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. Mol Cell. 2008 Aug 8;31(3):438-48. [PubMed
]
- Oppermann FS, Gnad F, Olsen JV, Hornberger R, Greff Z, Keri G, Mann M, Daub H: Large-scale proteomics analysis of the human kinome. Mol Cell Proteomics. 2009 Jul;8(7):1751-64. Epub 2009 Apr 15. [PubMed
]
|
| Enzyme 40 Metabolite References |
Not Available |
|
Enzyme 41
[top]
|
| Enzyme 41 ID |
7724 |
| Enzyme 41 Name |
Arginine decarboxylase |
| Enzyme 41 Synonyms |
- ADC
- ARGDC
- ODC-paralogue
- ODC-p
- Ornithine decarboxylase-like protein
|
| Enzyme 41 Gene Name |
ADC |
| Enzyme 41 Protein Sequence |
>Arginine decarboxylase
MAGYLSESDFVMVEEGFSTRDLLKELTLGASQATTDEVAAFFVADLGAIVRKHFCFLKCL
PRVRPFYAVKCNSSPGVLKVLAQLGLGFSCANKAEMELVQHIGIPASKIICANPCKQIAQ
IKYAAKHGIQLLSFDNEMELAKVVKSHPSAKMVLCIATDDSHSLSCLSLKFGVSLKSCRH
LLENAKKHHVEVVGVSFHIGSGCPDPQAYAQSIADARLVFEMGTELGHKMHVLDLGGGFP
GTEGAKVRFEEIASVINSALDLYFPEGCGVDIFAELGRYYVTSAFTVAVSIIAKKEVLLD
QPGREEENGSTSKTIVYHLDEGVYGIFNSVLFDNICPTPILQKKPSTEQPLYSSSLWGPA
VDGCDCVAEGLWLPQLHVGDWLVFDNMGAYTVGMGSPFWGTQACHITYAMSRVAWEALRR
QLMAAEQEDDVEGVCKPLSCGWEITDTLCVGPVFTPASIM
|
| Enzyme 41 Number of Residues |
460 |
| Enzyme 41 Molecular Weight |
49979.2 |
| Enzyme 41 Theoretical pI |
5.41 |
| Enzyme 41 GO Classification |
| Function |
|
| Process |
- cellular amino acid and derivative metabolic process
- cellular amino acid derivative metabolic process
- cellular biogenic amine metabolic process
- cellular metabolic process
- metabolic process
- polyamine biosynthetic process
- polyamine metabolic process
|
| Component |
| — |
|
| Enzyme 41 General Function |
Involved in catalytic activity |
| Enzyme 41 Specific Function |
Decarboxylates L-arginine to agmatine. Truncated splice isoforms probably lack activity |
| Enzyme 41 Pathways |
|
| Enzyme 41 Reactions |
- L-arginine = agmatine + CO2 [RN:R00566]
|
| Enzyme 41 Pfam Domain Function |
|
| Enzyme 41 Signals |
|
| Enzyme 41 Transmembrane Regions |
|
| Enzyme 41 Essentiality |
Not Available |
| Enzyme 41 GenBank ID Protein |
Not Available |
| Enzyme 41 UniProtKB/Swiss-Prot ID |
Q96A70  |
| Enzyme 41 UniProtKB/Swiss-Prot Entry Name |
ADC_HUMAN  |
| Enzyme 41 PDB ID |
Not Available |
| Enzyme 41 Cellular Location |
Not Available |
| Enzyme 41 Gene Sequence |
>1383 bp
ATGGCTGGCTACCTGAGTGAATCGGACTTTGTGATGGTGGAGGAGGGCTTCAGTACCCGA
GACCTGCTGAAGGAACTCACTCTGGGGGCCTCACAGGCCACCACGGACGAGGTAGCTGCC
TTCTTCGTGGCTGACCTGGGTGCCATAGTGAGGAAGCACTTTTGCTTTCTGAAGTGCCTG
CCACGAGTCCGGCCCTTTTATGCTGTCAAGTGCAACAGCAGCCCAGGTGTGCTGAAGGTT
CTGGCCCAGCTGGGGCTGGGCTTTAGCTGTGCCAACAAGGCAGAGATGGAGTTGGTCCAG
CATATTGGAATCCCTGCCAGTAAGATCATCTGCGCCAACCCCTGTAAGCAAATTGCACAG
ATCAAATATGCTGCCAAGCATGGGATCCAGCTGCTGAGCTTTGACAATGAGATGGAGCTG
GCAAAGGTGGTAAAGAGCCACCCCAGTGCCAAGATGGTTCTGTGCATTGCTACCGATGAC
TCCCACTCCCTGAGCTGCCTGAGCCTAAAGTTTGGAGTGTCACTGAAATCCTGCAGACAC
CTGCTTGAAAATGCGAAGAAGCACCATGTGGAGGTGGTGGGTGTGAGTTTTCACATTGGC
AGTGGCTGTCCTGACCCTCAGGCCTATGCTCAGTCCATCGCAGACGCCCGGCTCGTGTTT
GAAATGGGCACCGAGCTGGGTCACAAGATGCACGTTCTGGACCTTGGTGGTGGCTTCCCT
GGCACAGAAGGGGCCAAAGTGAGATTTGAAGAGATTGCTTCCGTGATCAACTCAGCCTTG
GACCTGTACTTCCCAGAGGGCTGTGGCGTGGACATCTTTGCTGAGCTGGGGCGCTACTAC
GTGACCTCGGCCTTCACTGTGGCAGTCAGCATCATTGCCAAGAAGGAGGTTCTGCTAGAC
CAGCCTGGCAGGGAGGAGGAAAATGGTTCCACCTCCAAGACCATCGTGTACCACCTTGAT
GAGGGCGTGTATGGGATCTTCAACTCAGTCCTGTTTGACAACATCTGCCCTACCCCCATC
CTGCAGAAGAAACCATCCACGGAGCAGCCCCTGTACAGCAGCAGCCTGTGGGGCCCGGCG
GTTGATGGCTGTGATTGCGTGGCTGAGGGCCTGTGGCTGCCGCAACTACACGTAGGGGAC
TGGCTGGTCTTTGACAACATGGGCGCCTACACTGTGGGCATGGGTTCCCCCTTTTGGGGG
ACCCAGGCCTGCCACATCACCTATGCCATGTCCCGGGTGGCCTGGGAAGCGCTGCGAAGG
CAGCTGATGGCTGCAGAACAGGAGGATGACGTGGAGGGTGTGTGCAAGCCTCTGTCCTGC
GGCTGGGAGATCACAGACACCCTGTGCGTGGGCCCTGTCTTCACCCCAGCGAGCATCATG
TGA
|
| Enzyme 41 GenBank Gene ID |
AY050634  |
| Enzyme 41 GeneCard ID |
ADC  |
| Enzyme 41 GenAtlas ID |
ADC  |
| Enzyme 41 HGNC ID |
HGNC:29957  |
| Enzyme 41 Chromosome Location |
1 |
| Enzyme 41 Locus |
1p35.1 |
| Enzyme 41 SNPs |
SNPJam Report  |
| Enzyme 41 General References |
- Pitkanen LT, Heiskala M, Andersson LC: Expression of a novel human ornithine decarboxylase-like protein in the central nervous system and testes. Biochem Biophys Res Commun. 2001 Oct 12;287(5):1051-7. [PubMed
]
- Zhu MY, Iyo A, Piletz JE, Regunathan S: Expression of human arginine decarboxylase, the biosynthetic enzyme for agmatine. Biochim Biophys Acta. 2004 Jan 22;1670(2):156-64. [PubMed
]
- Nagase T, Kikuno R, Ohara O: Prediction of the coding sequences of unidentified human genes. XXII. The complete sequences of 50 new cDNA clones which code for large proteins. DNA Res. 2001 Dec 31;8(6):319-27. [PubMed
]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
- Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
|
| Enzyme 41 Metabolite References |
Not Available |
|
Enzyme 42
[top]
|
| Enzyme 42 ID |
7966 |
| Enzyme 42 Name |
Hypothetical protein GAD1 |
| Enzyme 42 Synonyms |
Not Available |
| Enzyme 42 Gene Name |
GAD1 |
| Enzyme 42 Protein Sequence |
>Hypothetical protein GAD1
MASSTPSSSATSSNAGADPNTTNLRPTTYDTWCGVAHGCTRKLGLKICGFLQRTNSLEEK
SRLVSAFKERQSSKNLLSCENSDRDARFRRTETDFSNLFARDLLPAKNGEEQTVQFLLEV
VDILLNYVRKTFDRSTKVLDFHHPHQLLEGMEGFNLELSDHPESLEQILVDCRDTLKYGV
RTGHPRFFNQLSTGLDIIGLAGEWLTSTANTNMFTYEIAPVFVLMEQITLKKMREIVGWS
SKDGDGIFSPGGAISNMYSIMAARYKYFPEVKTKGMAAVPKLVLFTSEQSHYSIKKAGAA
LGFGTDNVILIKCNERGKIIPADFEAKILEAKQKGYVPFYVNATAGTTVYGAFDPIQEIA
DICEKYNLWLHVDAAWGGGLLMSRKHRHKLNGIERANSVTWNPHKMMGVLLQCSAILVKE
KGILQGCNQMCAGYLFQPDKQYDVSYDTGDKAIQCGRHVDIFKFWLMWKAKGTVGFENQI
NKCLELAEYLYAKIKNREEFEMVFNGEPEHTNVCFWYIPQSLRGVPDSPQRREKLHKVAP
KIKALMMESGTTMVGYQPQGDKANFFRMVISNPAATQSDIDFLIEEIERLGQDL
|
| Enzyme 42 Number of Residues |
594 |
| Enzyme 42 Molecular Weight |
66897 |
| Enzyme 42 Theoretical pI |
7.67 |
| Enzyme 42 GO Classification |
| Function |
- carbon-carbon lyase activity
- carboxy-lyase activity
- catalytic activity
- lyase activity
|
| Process |
- amino acid and derivative metabolism
- amino acid metabolism
- cellular metabolism
- metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 42 General Function |
Amino acid transport and metabolism |
| Enzyme 42 Specific Function |
Not Available |
| Enzyme 42 Pathways |
Not Available |
| Enzyme 42 Reactions |
Not Available |
| Enzyme 42 Pfam Domain Function |
|
| Enzyme 42 Signals |
|
| Enzyme 42 Transmembrane Regions |
|
| Enzyme 42 Essentiality |
Not Available |
| Enzyme 42 GenBank ID Protein |
62988850  |
| Enzyme 42 UniProtKB/Swiss-Prot ID |
Q53TQ7  |
| Enzyme 42 UniProtKB/Swiss-Prot Entry Name |
Q53TQ7_HUMAN  |
| Enzyme 42 PDB ID |
Not Available |
| Enzyme 42 Cellular Location |
Not Available |
| Enzyme 42 Gene Sequence |
>1785 bp
ATGGCGTCTTCGACCCCATCTTCGTCCGCAACCTCCTCGAACGCGGGAGCGGACCCCAAT
ACCACTAACCTGCGCCCCACAACGTACGATACCTGGTGCGGCGTGGCCCATGGATGCACC
AGAAAACTGGGGCTCAAGATCTGCGGCTTCTTGCAAAGGACCAACAGCCTGGAAGAGAAG
AGTCGCCTTGTGAGTGCCTTCAAGGAGAGGCAATCCTCCAAGAACCTGCTTTCCTGTGAA
AACAGCGACCGGGATGCCCGCTTCCGGCGCACAGAGACTGACTTCTCTAATCTGTTTGCT
AGAGATCTGCTTCCGGCTAAGAACGGTGAGGAGCAAACCGTGCAATTCCTCCTGGAAGTG
GTGGACATACTCCTCAACTATGTCCGCAAGACATTTGATCGCTCCACCAAGGTGCTGGAC
TTTCATCACCCACACCAGTTGCTGGAAGGCATGGAGGGCTTCAACTTGGAGCTCTCTGAC
CACCCCGAGTCCCTGGAGCAGATCCTGGTTGACTGCAGAGACACCTTGAAGTATGGGGTT
CGCACAGGTCATCCTCGATTTTTCAACCAGCTCTCCACTGGATTGGATATTATTGGCCTA
GCTGGAGAATGGCTGACATCAACGGCCAATACCAACATGTTTACATATGAAATTGCACCA
GTGTTTGTCCTCATGGAACAAATAACACTTAAGAAGATGAGAGAGATAGTTGGATGGTCA
AGTAAAGATGGTGATGGGATATTTTCTCCTGGGGGCGCCATATCCAACATGTACAGCATC
ATGGCTGCTCGCTACAAGTACTTCCCGGAAGTTAAGACAAAGGGCATGGCGGCTGTGCCT
AAACTGGTCCTCTTCACCTCAGAACAGAGTCACTATTCCATAAAGAAAGCTGGGGCTGCA
CTTGGCTTTGGAACTGACAATGTGATTTTGATAAAGTGCAATGAAAGGGGGAAAATAATT
CCAGCTGATTTTGAGGCAAAAATTCTTGAAGCCAAACAGAAGGGATATGTTCCCTTTTAT
GTCAATGCAACTGCTGGCACGACTGTTTATGGAGCTTTTGATCCGATACAAGAGATTGCA
GATATATGTGAGAAATATAACCTTTGGTTGCATGTCGATGCTGCCTGGGGAGGTGGGCTG
CTCATGTCCAGGAAGCACCGCCATAAACTCAACGGCATAGAAAGGGCCAACTCAGTCACC
TGGAACCCTCACAAGATGATGGGCGTGCTGTTGCAGTGCTCTGCCATTCTCGTCAAGGAA
AAGGGTATACTCCAAGGATGCAACCAGATGTGTGCAGGATACCTCTTCCAGCCAGACAAG
CAGTATGATGTCTCCTACGACACCGGGGACAAGGCAATTCAGTGTGGCCGCCACGTGGAT
ATCTTCAAGTTCTGGCTGATGTGGAAAGCAAAGGGCACAGTGGGATTTGAAAACCAGATC
AACAAATGCCTGGAACTGGCTGAATACCTCTATGCCAAGATTAAAAACAGAGAAGAATTT
GAGATGGTTTTCAATGGCGAGCCTGAGCACACAAACGTCTGTTTTTGGTATATTCCACAA
AGCCTCAGGGGTGTGCCAGACAGCCCTCAACGACGGGAAAAGCTACACAAGGTGGCTCCA
AAAATCAAAGCCCTGATGATGGAGTCAGGTACGACCATGGTTGGCTACCAGCCCCAAGGG
GACAAGGCCAACTTCTTCCGGATGGTCATCTCCAACCCAGCCGCTACCCAGTCTGACATT
GACTTCCTCATTGAGGAGATAGAAAGACTGGGCCAGGATCTGTAA
|
| Enzyme 42 GenBank Gene ID |
AC007405  |
| Enzyme 42 GeneCard ID |
GAD1  |
| Enzyme 42 GenAtlas ID |
GAD1  |
| Enzyme 42 HGNC ID |
HGNC:4092  |
| Enzyme 42 Chromosome Location |
2 |
| Enzyme 42 Locus |
2q31 |
| Enzyme 42 SNPs |
SNPJam Report  |
| Enzyme 42 General References |
Not Available |
| Enzyme 42 Metabolite References |
Not Available |
|
Enzyme 43
[top]
|
| Enzyme 43 ID |
8009 |
| Enzyme 43 Name |
Cysteine desulfurase, mitochondrial |
| Enzyme 43 Synonyms |
Not Available |
| Enzyme 43 Gene Name |
NFS1 |
| Enzyme 43 Protein Sequence |
>Cysteine desulfurase, mitochondrial
MLLRAAWRRAAVAVTAAPGPKPAAPTRGLRLRVGDRAPQSAVPADTAAAPEVGPVLRPLY
MDVQATTPLDPRVLDAMLPYLINYYGNPHSRTHAYGWESEAAMERARQQVASLIGADPRE
IIFTSGATESNNIAIKGVARFYRSRKKHLITTQTEHKCVLDSCRSLEAEGFQVTYLPVQK
SGIIDLKELEAAIQPDTSLVSVMTVNNEIGVKQPIAEIGRICSSRKVYFHTDAAQAVGKI
PLDVNDMKIDLMSISGHKIYGPKGVGAIYIRRRPRVRVEALQSGGGQERGMRSGTVPTPL
VVGLGAACEVAQQEMEYDHKRISKLSERLIQNIMKSLPDVVMNGDPKHHYPGCINLSFAY
VEGESLLMALKDVALSSGSACTSASLEPSYVLRAIGTDEDLAHSSIRFGIGRFTTEEEVD
YTVEKCIQHVKRLREMSPLWEMVQDGIDLKSIKWTQH
|
| Enzyme 43 Number of Residues |
457 |
| Enzyme 43 Molecular Weight |
50195.2 |
| Enzyme 43 Theoretical pI |
8.45 |
| Enzyme 43 GO Classification |
| Function |
- binding
- catalytic activity
- cofactor binding
- cysteine desulfurase activity
- pyridoxal phosphate binding
- sulfurtransferase activity
- transferase activity
- transferase activity, transferring sulfur-containing groups
|
| Process |
- cellular amino acid and derivative metabolic process
- cellular amino acid metabolic process
- cellular metabolic process
- cysteine metabolic process
- metabolic process
- sulfur amino acid metabolic process
|
| Component |
| — |
|
| Enzyme 43 General Function |
Involved in metabolic process |
| Enzyme 43 Specific Function |
Catalyzes the removal of elemental sulfur from cysteine to produce alanine. It supplies the inorganic sulfur for iron- sulfur (Fe-S) clusters. May be involved in the biosynthesis of molybdenum cofactor |
| Enzyme 43 Pathways |
Not Available |
| Enzyme 43 Reactions |
- L-cysteine + [enzyme]-cysteine = L-alanine + [enzyme]-S-sulfanylcysteine [RN:R07460]
|
| Enzyme 43 Pfam Domain Function |
|
| Enzyme 43 Signals |
|
| Enzyme 43 Transmembrane Regions |
|
| Enzyme 43 Essentiality |
Not Available |
| Enzyme 43 GenBank ID Protein |
24042327  |
| Enzyme 43 UniProtKB/Swiss-Prot ID |
Q9Y697  |
| Enzyme 43 UniProtKB/Swiss-Prot Entry Name |
NFS1_HUMAN  |
| Enzyme 43 PDB ID |
Not Available |
| Enzyme 43 Cellular Location |
Not Available |
| Enzyme 43 Gene Sequence |
>1374 bp
ATGCTGCTCCGAGTCGCTTGGAGGCGGGCGGCAGTGGCGGTGACAGCGGCTCCAGGGCCG
AAGCCCGCGGCGCCCACTCGGGGGCTGCGCCTGCGCGTTGGAGACCGTGCTCCTCAGTCT
GCGGTTCCCGCAGATACAACCGCTGCCCCGGAGGTGGGGCCAGTGCTGCGACCTCTCTAT
ATGGATGTGCAAGCTACAACTCCTCTGGACCCCCGGGTGCTTGATGCCATGCTCCCTTAC
CTAATCAACTACTATGGGAACCCACACTCCCGGACACATGCTTATGGCTGGGAGAGTGAG
GCAGCCATGGAACGTGCTCGTCAGCAAGTAGCATCTCTGATTGGAGCTGATCCTCGTGAG
ATCATTTTTACTAGTGGTGCTACTGAATCCAACAACATAGCAATTAAGGGGGTGGCCCGA
TTCTACAGGTCACGGAAAAAGCACTTGATCACCACCCAGACAGAACACAAATGTGTCTTG
GACTCCTGCCGTTCACTGGAAGCTGAGGGCTTTCAGGTCACCTACCTCCCAGTGCAGAAG
AGTGGGATCATTGACCTAAAGGAACTAGAGGCTGCTATCCAGCCAGATACTAGCCTGGTG
TCAGTCATGACTGTGAACAATGAGATTGGAGTGAAGCAGCCTATTGCAGAAATAGGGCGG
ATTTGCAGTTCCAGAAAGGTATATTTCCATACTGATGCAGCCCAGGCTGTTGGAAAAATC
CCACTTGATGTCAATGACATGAAAATTGATCTCATGAGCATTAGTGGTCACAAAATCTAC
GGTCCCAAAGGGGTTGGTGCCATCTACATCCGTCGCCGGCCCCGTGTGCGTGTGGAGGCC
CTGCAGAGTGGAGGGGGGCAGGAGCGGGGTATGCGGTCTGGGACAGTGCCCACACCCTTA
GTGGTGGGGTTGGGGGCTGCGTGTGAGGTGGCACAGCAAGAGATGGAGTATGACCACAAG
CGAATCTCAAAGTTGTCAGAGCGGCTGATACAGAATATAATGAAGAGCCTTCCAGATGTG
GTGATGAATGGGGACCCTAAGCACCATTATCCCGGCTGTATCAACCTCTCCTTTGCATAT
GTGGAAGGGGAAAGTCTGCTGATGGCACTGAAGGACGTTGCCTTATCCTCAGGGAGTGCC
TGCACCTCTGCATCCCTGGAGCCCTCTTATGTGCTTAGAGCAATTGGCACTGATGAGGAT
TTAGCGCACTCTTCTATCAGGTTTGGAATTGGCGCTTTCACTACAGAGGAGGAAGTGGAC
TACACAGTGGAGAAATGCATTCAGCATGTGAATCGTCTTCGAGAAATGAGCCCTCTCTGG
GAGATGGTTCAGGATGGCATTGACCTCAAGAGCATCAAGTGGACCCAACACTAG
|
| Enzyme 43 GenBank Gene ID |
AF097025  |
| Enzyme 43 GeneCard ID |
NFS1  |
| Enzyme 43 GenAtlas ID |
NFS1  |
| Enzyme 43 HGNC ID |
HGNC:15910  |
| Enzyme 43 Chromosome Location |
2 |
| Enzyme 43 Locus |
20q11.22 |
| Enzyme 43 SNPs |
SNPJam Report  |
| Enzyme 43 General References |
- Land T, Rouault TA: Targeting of a human iron-sulfur cluster assembly enzyme, nifs, to different subcellular compartments is regulated through alternative AUG utilization. Mol Cell. 1998 Dec;2(6):807-15. [PubMed
]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
- Deloukas P, Matthews LH, Ashurst J, Burton J, Gilbert JG, Jones M, Stavrides G, Almeida JP, Babbage AK, Bagguley CL, Bailey J, Barlow KF, Bates KN, Beard LM, Beare DM, Beasley OP, Bird CP, Blakey SE, Bridgeman AM, Brown AJ, Buck D, Burrill W, Butler AP, Carder C, Carter NP, Chapman JC, Clamp M, Clark G, Clark LN, Clark SY, Clee CM, Clegg S, Cobley VE, Collier RE, Connor R, Corby NR, Coulson A, Coville GJ, Deadman R, Dhami P, Dunn M, Ellington AG, Frankland JA, Fraser A, French L, Garner P, Grafham DV, Griffiths C, Griffiths MN, Gwilliam R, Hall RE, Hammond S, Harley JL, Heath PD, Ho S, Holden JL, Howden PJ, Huckle E, Hunt AR, Hunt SE, Jekosch K, Johnson CM, Johnson D, Kay MP, Kimberley AM, King A, Knights A, Laird GK, Lawlor S, Lehvaslaiho MH, Leversha M, Lloyd C, Lloyd DM, Lovell JD, Marsh VL, Martin SL, McConnachie LJ, McLay K, McMurray AA, Milne S, Mistry D, Moore MJ, Mullikin JC, Nickerson T, Oliver K, Parker A, Patel R, Pearce TA, Peck AI, Phillimore BJ, Prathalingam SR, Plumb RW, Ramsay H, Rice CM, Ross MT, Scott CE, Sehra HK, Shownkeen R, Sims S, Skuce CD, Smith ML, Soderlund C, Steward CA, Sulston JE, Swann M, Sycamore N, Taylor R, Tee L, Thomas DW, Thorpe A, Tracey A, Tromans AC, Vaudin M, Wall M, Wallis JM, Whitehead SL, Whittaker P, Willey DL, Williams L, Williams SA, Wilming L, Wray PW, Hubbard T, Durbin RM, Bentley DR, Beck S, Rogers J: The DNA sequence and comparative analysis of human chromosome 20. Nature. 2001 Dec 20-27;414(6866):865-71. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Stanchi F, Bertocco E, Toppo S, Dioguardi R, Simionati B, Cannata N, Zimbello R, Lanfranchi G, Valle G: Characterization of 16 novel human genes showing high similarity to yeast sequences. Yeast. 2001 Jan 15;18(1):69-80. [PubMed
]
- Tong WH, Rouault T: Distinct iron-sulfur cluster assembly complexes exist in the cytosol and mitochondria of human cells. EMBO J. 2000 Nov 1;19(21):5692-700. [PubMed
]
- Marelja Z, Stocklein W, Nimtz M, Leimkuhler S: A novel role for human Nfs1 in the cytoplasm: Nfs1 acts as a sulfur donor for MOCS3, a protein involved in molybdenum cofactor biosynthesis. J Biol Chem. 2008 Sep 12;283(37):25178-85. Epub 2008 Jul 23. [PubMed
]
- Shi Y, Ghosh MC, Tong WH, Rouault TA: Human ISD11 is essential for both iron-sulfur cluster assembly and maintenance of normal cellular iron homeostasis. Hum Mol Genet. 2009 Aug 15;18(16):3014-25. Epub 2009 May 18. [PubMed
]
|
| Enzyme 43 Metabolite References |
Not Available |
|
Enzyme 44
[top]
|
| Enzyme 44 ID |
8563 |
| Enzyme 44 Name |
Proline synthase co-transcribed bacterial homolog protein |
| Enzyme 44 Synonyms |
Not Available |
| Enzyme 44 Gene Name |
PROSC |
| Enzyme 44 Protein Sequence |
>Proline synthase co-transcribed bacterial homolog protein
MWRAGSMSAELGVGCALRAVNERVQQAVARRPRDLPAIQPRLVAVSKTKPADMVIEAYGH
GQRTFGENYVQELLEKASNPKILSLCPEIKWHFIGHLQKQNVNKLMAVPNLFMLETVDSV
KLADKVNSSWQRKGSPERLKVMVQINTSGEESKHGLPPSETIAIVEHINAKCPNLEFVGL
MTIGSFGHDLSQGPNPDFQLLLSLREELCKKLNIPADQVELSMGMSADFQHAVEVGSTNV
RIGSTIFGERDYSKKPTPDKCAADVKAPLEVAQEH
|
| Enzyme 44 Number of Residues |
275 |
| Enzyme 44 Molecular Weight |
30343.7 |
| Enzyme 44 Theoretical pI |
7.57 |
| Enzyme 44 GO Classification |
Not Available |
| Enzyme 44 General Function |
Not Available |
| Enzyme 44 Specific Function |
Not Available |
| Enzyme 44 Pathways |
Not Available |
| Enzyme 44 Reactions |
Not Available |
| Enzyme 44 Pfam Domain Function |
|
| Enzyme 44 Signals |
|
| Enzyme 44 Transmembrane Regions |
|
| Enzyme 44 Essentiality |
Not Available |
| Enzyme 44 GenBank ID Protein |
4126978  |
| Enzyme 44 UniProtKB/Swiss-Prot ID |
O94903  |
| Enzyme 44 UniProtKB/Swiss-Prot Entry Name |
PROSC_HUMAN  |
| Enzyme 44 PDB ID |
Not Available |
| Enzyme 44 Cellular Location |
Not Available |
| Enzyme 44 Gene Sequence |
>828 bp
ATGTGGAGAGCTGGCAGCATGTCGGCCGAGCTGGGAGTCGGGTGCGCATTGCGGGCGGTG
AACGAGCGCGTGCAGCAGGCTGTGGCGCGGCGGCCGCGGGATCTCCCAGCCATCCAGCCC
CGGCTAGTGGCGGTCAGCAAAACCAAACCTGCAGACATGGTGATCGAGGCCTATGGACAT
GGGCAGCGCACTTTTGGCGAGAACTACGTTCAGGAACTGCTAGAAAAAGCATCAAATCCC
AAAATTCTGTCTTTGTGTCCTGAGATCAAATGGCACTTCATTGGCCACCTACAGAAACAA
AATGTCAACAAATTGATGGCTGTCCCCAATCTCTTCATGCTGGAAACAGTGGATTCTGTG
AAGTTGGCAGACAAAGTGAACAGTTCCTGGCAGAGAAAAGGTTCTCCTGAAAGGTTAAAG
GTTATGGTCCAGATTAACACCAGCGGAGAAGAGAGTAAACATGGCCTTCCACCTTCAGAG
ACCATAGCCATCGTGGAGCACATAAACGCCAAGTGTCCTAACCTGGAGTTTGTGGGGCTG
ATGACCATAGGAAGCTTTGGGCATGATCTTAGTCAAGGACCAAATCCAGACTTCCAGCTG
TTATTGTCCCTCCGGGAGGAGCTGTGTAAAAAGCTGAACATCCCTGCTGACCAGGTTGAG
CTGAGCATGGGCATGTCCGCGGATTTCCAGCATGCGGTTGAAGTAGGATCTACAAATGTC
CGAATAGGAAGCACGATTTTTGGAGAGCGGGATTACTCAAAGAAACCCACCCCGGACAAG
TGCGCAGCAGACGTGAAGGCCCCGCTGGAGGTGGCACAGGAGCACTGA
|
| Enzyme 44 GenBank Gene ID |
AB018566  |
| Enzyme 44 GeneCard ID |
PROSC  |
| Enzyme 44 GenAtlas ID |
PROSC  |
| Enzyme 44 HGNC ID |
HGNC:9457  |
| Enzyme 44 Chromosome Location |
8 |
| Enzyme 44 Locus |
8p11.2 |
| Enzyme 44 SNPs |
SNPJam Report  |
| Enzyme 44 General References |
- Ikegawa S, Isomura M, Koshizuka Y, Nakamura Y: Cloning and characterization of human and mouse PROSC (proline synthetase co-transcribed) genes. J Hum Genet. 1999;44(5):337-42. [PubMed
]
- Wiemann S, Weil B, Wellenreuther R, Gassenhuber J, Glassl S, Ansorge W, Bocher M, Blocker H, Bauersachs S, Blum H, Lauber J, Dusterhoft A, Beyer A, Kohrer K, Strack N, Mewes HW, Ottenwalder B, Obermaier B, Tampe J, Heubner D, Wambutt R, Korn B, Klein M, Poustka A: Toward a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs. Genome Res. 2001 Mar;11(3):422-35. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed
]
|
| Enzyme 44 Metabolite References |
Not Available |
|
Enzyme 45
[top]
|
| Enzyme 45 ID |
8585 |
| Enzyme 45 Name |
Aminoadipate aminotransferase, isoform CRA_b |
| Enzyme 45 Synonyms |
- SubName: Putative uncharacterized protein AADAT
- SubName: cDNA, FLJ95590, Homo sapiens L-kynurenine/alpha-aminoadipate aminotransferase (KATII), mRNA
|
| Enzyme 45 Gene Name |
AADAT |
| Enzyme 45 Protein Sequence |
>Aminoadipate aminotransferase, isoform CRA_b
MNYARFITAASAARNPSPIRTMTDILSRGPKSMISLAGGLPNPNMFPFKTAVITVENGKT
IQFGEEMMKRALQYSPSAGIPELLSWLKQLQIKLHNPPTIHYPPSQGQMDLCVTSGSQQG
LCKVFEMIINPGDNVLLDEPAYSGTLQSLHPLGCNIINVASDESGIVPDSLRDILSRWKP
EDAKNPQKNTPKFLYTVPNGNNPTGNSLTSERKKEIYELARKYDFLIIEDDPYYFLQFNK
FRVPTFLSMDVDGRVIRADSFSKIISSGLRIGFLTGPKPLIERVILHIQVSTLHPSTFNQ
LMISQLLHEWGEEGFMAHVDRVIDFYSNQKDAILAAADKWLTGLAEWHVPAAGMFLWIKV
KGINDVKELIEEKAVKMGVLMLPGNAFYVDSSAPSPYLRASFSSASPEQMDVAFQVLAQL
IKESL
|
| Enzyme 45 Number of Residues |
425 |
| Enzyme 45 Molecular Weight |
47351.2 |
| Enzyme 45 Theoretical pI |
6.96 |
| Enzyme 45 GO Classification |
| Function |
- binding
- catalytic activity
- cofactor binding
- pyridoxal phosphate binding
- transferase activity
- transferase activity, transferring nitrogenous groups
|
| Process |
- biosynthetic process
- metabolic process
|
| Component |
| — |
|
| Enzyme 45 General Function |
Transcription |
| Enzyme 45 Specific Function |
Not Available |
| Enzyme 45 Pathways |
Not Available |
| Enzyme 45 Reactions |
Not Available |
| Enzyme 45 Pfam Domain Function |
|
| Enzyme 45 Signals |
|
| Enzyme 45 Transmembrane Regions |
|
| Enzyme 45 Essentiality |
Not Available |
| Enzyme 45 GenBank ID Protein |
63995206  |
| Enzyme 45 UniProtKB/Swiss-Prot ID |
Q4W5N8  |
| Enzyme 45 UniProtKB/Swiss-Prot Entry Name |
Q4W5N8_HUMAN  |
| Enzyme 45 PDB ID |
Not Available |
| Enzyme 45 Cellular Location |
Not Available |
| Enzyme 45 Gene Sequence |
>1278 bp
ATGAATTACGCACGGTTCATCACGGCAGCGAGCGCAGCCAGAAACCCTTCTCCCATCCGG
ACCATGACTGACATATTGAGCAGAGGACCAAAATCGATGATCTCCTTGGCTGGTGGCTTA
CCAAATCCAAACATGTTTCCTTTTAAGACTGCCGTAATCACTGTAGAAAATGGAAAGACC
ATCCAATTTGGAGAAGAGATGATGAAGAGAGCACTTCAGTATTCTCCGAGTGCTGGAATT
CCAGAGCTTTTGTCCTGGCTAAAACAGTTACAAATAAAATTGCATAATCCTCCTACCATC
CATTACCCACCCAGTCAAGGACAAATGGATCTATGTGTCACATCTGGCAGCCAACAAGGT
CTTTGTAAGGTGTTTGAAATGATCATTAATCCTGGAGATAATGTCCTCCTAGATGAACCT
GCTTATTCAGGAACTCTTCAAAGTCTGCACCCACTGGGCTGCAACATTATTAATGTTGCC
AGTGATGAAAGTGGGATTGTTCCAGATTCCCTAAGAGACATACTTTCCAGATGGAAACCA
GAAGATGCAAAGAATCCCCAGAAAAACACCCCCAAATTTCTTTATACTGTTCCAAATGGC
AACAACCCTACTGGAAACTCATTAACCAGTGAACGCAAAAAGGAAATCTATGAGCTTGCA
AGAAAATATGATTTCCTCATAATAGAAGATGATCCTTACTATTTTCTCCAGTTTAACAAG
TTCAGGGTACCAACATTTCTTTCCATGGATGTTGATGGACGTGTCATCAGAGCTGACTCT
TTTTCAAAAATCATTTCCTCTGGGTTGAGAATAGGATTTTTAACTGGTCCAAAACCCTTA
ATAGAGAGAGTTATTTTACACATACAAGTTTCAACATTGCACCCCAGCACTTTTAACCAG
CTCATGATATCACAGCTTCTACACGAATGGGGAGAAGAAGGTTTCATGGCTCATGTAGAC
AGGGTTATTGATTTCTATAGTAACCAGAAGGATGCAATACTGGCAGCTGCAGACAAGTGG
TTAACTGGTTTGGCAGAATGGCATGTTCCTGCTGCTGGAATGTTTTTATGGATTAAAGTT
AAAGGCATTAATGATGTAAAAGAACTGATTGAAGAAAAGGCCGTTAAGATGGGGGTATTA
ATGCTCCCTGGAAATGCTTTCTACGTCGATAGCTCAGCTCCTAGCCCTTACTTGAGAGCA
TCCTTCTCTTCAGCTTCTCCAGAACAGATGGATGTGGCCTTCCAGGTATTAGCACAACTT
ATAAAAGAATCTTTATGA
|
| Enzyme 45 GenBank Gene ID |
AC084866  |
| Enzyme 45 GeneCard ID |
AADAT  |
| Enzyme 45 GenAtlas ID |
Not Available |
| Enzyme 45 HGNC ID |
Not Available |
| Enzyme 45 Chromosome Location |
4 |
| Enzyme 45 Locus |
4q33 |
| Enzyme 45 SNPs |
SNPJam Report  |
| Enzyme 45 General References |
- Venter JC, Adams MD, Myers EW, Li PW, Mural RJ, Sutton GG, Smith HO, Yandell M, Evans CA, Holt RA, Gocayne JD, Amanatides P, Ballew RM, Huson DH, Wortman JR, Zhang Q, Kodira CD, Zheng XH, Chen L, Skupski M, Subramanian G, Thomas PD, Zhang J, Gabor Miklos GL, Nelson C, Broder S, Clark AG, Nadeau J, McKusick VA, Zinder N, Levine AJ, Roberts RJ, Simon M, Slayman C, Hunkapiller M, Bolanos R, Delcher A, Dew I, Fasulo D, Flanigan M, Florea L, Halpern A, Hannenhalli S, Kravitz S, Levy S, Mobarry C, Reinert K, Remington K, Abu-Threideh J, Beasley E, Biddick K, Bonazzi V, Brandon R, Cargill M, Chandramouliswaran I, Charlab R, Chaturvedi K, Deng Z, Di Francesco V, Dunn P, Eilbeck K, Evangelista C, Gabrielian AE, Gan W, Ge W, Gong F, Gu Z, Guan P, Heiman TJ, Higgins ME, Ji RR, Ke Z, Ketchum KA, Lai Z, Lei Y, Li Z, Li J, Liang Y, Lin X, Lu F, Merkulov GV, Milshina N, Moore HM, Naik AK, Narayan VA, Neelam B, Nusskern D, Rusch DB, Salzberg S, Shao W, Shue B, Sun J, Wang Z, Wang A, Wang X, Wang J, Wei M, Wides R, Xiao C, Yan C, Yao A, Ye J, Zhan M, Zhang W, Zhang H, Zhao Q, Zheng L, Zhong F, Zhong W, Zhu S, Zhao S, Gilbert D, Baumhueter S, Spier G, Carter C, Cravchik A, Woodage T, Ali F, An H, Awe A, Baldwin D, Baden H, Barnstead M, Barrow I, Beeson K, Busam D, Carver A, Center A, Cheng ML, Curry L, Danaher S, Davenport L, Desilets R, Dietz S, Dodson K, Doup L, Ferriera S, Garg N, Gluecksmann A, Hart B, Haynes J, Haynes C, Heiner C, Hladun S, Hostin D, Houck J, Howland T, Ibegwam C, Johnson J, Kalush F, Kline L, Koduru S, Love A, Mann F, May D, McCawley S, McIntosh T, McMullen I, Moy M, Moy L, Murphy B, Nelson K, Pfannkoch C, Pratts E, Puri V, Qureshi H, Reardon M, Rodriguez R, Rogers YH, Romblad D, Ruhfel B, Scott R, Sitter C, Smallwood M, Stewart E, Strong R, Suh E, Thomas R, Tint NN, Tse S, Vech C, Wang G, Wetter J, Williams S, Williams M, Windsor S, Winn-Deen E, Wolfe K, Zaveri J, Zaveri K, Abril JF, Guigo R, Campbell MJ, Sjolander KV, Karlak B, Kejariwal A, Mi H, Lazareva B, Hatton T, Narechania A, Diemer K, Muruganujan A, Guo N, Sato S, Bafna V, Istrail S, Lippert R, Schwartz R, Walenz B, Yooseph S, Allen D, Basu A, Baxendale J, Blick L, Caminha M, Carnes-Stine J, Caulk P, Chiang YH, Coyne M, Dahlke C, Mays A, Dombroski M, Donnelly M, Ely D, Esparham S, Fosler C, Gire H, Glanowski S, Glasser K, Glodek A, Gorokhov M, Graham K, Gropman B, Harris M, Heil J, Henderson S, Hoover J, Jennings D, Jordan C, Jordan J, Kasha J, Kagan L, Kraft C, Levitsky A, Lewis M, Liu X, Lopez J, Ma D, Majoros W, McDaniel J, Murphy S, Newman M, Nguyen T, Nguyen N, Nodell M, Pan S, Peck J, Peterson M, Rowe W, Sanders R, Scott J, Simpson M, Smith T, Sprague A, Stockwell T, Turner R, Venter E, Wang M, Wen M, Wu D, Wu M, Xia A, Zandieh A, Zhu X: The sequence of the human genome. Science. 2001 Feb 16;291(5507):1304-51. [PubMed
]
|
| Enzyme 45 Metabolite References |
Not Available |
|
Enzyme 46
[top]
|
| Enzyme 46 ID |
8882 |
| Enzyme 46 Name |
Threonine synthase-like 1 |
| Enzyme 46 Synonyms |
- TSH1
|
| Enzyme 46 Gene Name |
THNSL1 |
| Enzyme 46 Protein Sequence |
>Threonine synthase-like 1
MLHFNRCHHLKKITQKCFSSIHVKTDKHAQRFLSRTFALAELRKSWYSTHSLVGDKNIIL
MGPPGAGKTTVGRIIGQKLGCCVIDVDDDILEKTWNMSVSEKLQDVGNEQFLEEEGKAVL
NFSASGSVISLTGSNPMHDASMWHLKKNGIIVYLDVPLLDLICRLKLMKTDRIVGQNSGT
SMKDLLKFRRQYYKKWYDARVFCESGASPEEVADKVLNAIKRYQDVDSETFISTRHVWPE
DCEQKVSAKFFSEAVIEGLASDGGLFVPAKEFPKLSCGEWKSLVGATYVERAQILLERCI
HPADIPAARLGEMIETAYGENFACSKIAPVRHLSGNQFILELFHGPTGSFKDLSLQLMPH
IFAHCIPPSCNYMILVATSGDTGSAVLNGFSRLNKNDKQRIAVVAFFPENGVSDFQKAQI
IGSQRENGWAVGVESDFDFCQTAIKRIFNDSDFTGFLTVEYGTILSSANSINWGRLLPQV
VYHASAYLDLVSQGFISFGSPVDVCIPTGNFGNILAAVYAKMMGIPIRKFICASNQNHVL
TDFIKTGHYDLRERKLAQTFSPSIDILKSSNLERHLHLMANKDGQLMTELFNRLESQHHF
QIEKALVEKLQQDFVADWCSEGECLAAINSTYNTSGYILDPHTAVAKVVADRVQDKTCPV
IISSTAHYSKFAPAIMQALKIKEINETSSSQLYLLGSYNALPPLHEALLERTKQQEKMEY
QVCAADMNVLKSHVEQLVQNQFI
|
| Enzyme 46 Number of Residues |
743 |
| Enzyme 46 Molecular Weight |
83069.5 |
| Enzyme 46 Theoretical pI |
7.13 |
| Enzyme 46 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- adenyl ribonucleotide binding
- binding
- carbon-oxygen lyase activity
- carbon-oxygen lyase activity, acting on phosphates
- catalytic activity
- cofactor binding
- kinase activity
- lyase activity
- nucleoside binding
- purine nucleoside binding
- pyridoxal phosphate binding
- shikimate kinase activity
- threonine synthase activity
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- aspartate family amino acid metabolic process
- cellular amino acid and derivative metabolic process
- cellular amino acid metabolic process
- cellular metabolic process
- metabolic process
- threonine biosynthetic process
- threonine metabolic process
|
| Component |
| — |
|
| Enzyme 46 General Function |
Involved in catalytic activity |
| Enzyme 46 Specific Function |
Not Available |
| Enzyme 46 Pathways |
Not Available |
| Enzyme 46 Reactions |
Not Available |
| Enzyme 46 Pfam Domain Function |
|
| Enzyme 46 Signals |
|
| Enzyme 46 Transmembrane Regions |
|
| Enzyme 46 Essentiality |
Not Available |
| Enzyme 46 GenBank ID Protein |
Not Available |
| Enzyme 46 UniProtKB/Swiss-Prot ID |
Q8IYQ7  |
| Enzyme 46 UniProtKB/Swiss-Prot Entry Name |
THNS1_HUMAN  |
| Enzyme 46 PDB ID |
Not Available |
| Enzyme 46 Cellular Location |
Not Available |
| Enzyme 46 Gene Sequence |
>2232 bp
ATGCTCCACTTTAACCGATGTCATCATCTGAAAAAGATAACACAGAAATGTTTTTCTAGT
ATACATGTTAAAACGGATAAACATGCACAGCGATTTCTTTCAAGAACCTTTGCACTTGCG
GAATTGAGGAAGTCATGGTATTCAACCCACTCTCTTGTTGGAGACAAAAATATTATCCTG
ATGGGACCTCCTGGTGCTGGGAAAACAACAGTAGGCAGAATAATAGGTCAGAAACTAGGT
TGTTGTGTCATAGATGTGGATGATGATATCCTTGAAAAAACCTGGAATATGAGTGTGTCT
GAAAAATTACAGGATGTTGGTAATGAGCAATTTTTAGAAGAGGAAGGAAAAGCTGTGTTA
AACTTCTCTGCATCTGGAAGTGTGATTTCCCTTACTGGGTCCAATCCAATGCATGATGCT
AGCATGTGGCATCTGAAGAAAAATGGAATAATTGTATACCTGGATGTACCTCTACTAGAT
CTAATTTGTCGTCTAAAATTAATGAAGACAGATAGGATTGTAGGTCAGAATTCTGGAACA
TCTATGAAAGACTTACTTAAATTTAGAAGACAGTATTATAAGAAGTGGTATGATGCTCGT
GTTTTCTGTGAAAGTGGGGCTTCCCCAGAGGAGGTAGCTGACAAAGTGCTGAATGCAATT
AAAAGATACCAAGATGTGGACTCGGAAACATTCATTTCAACAAGACACGTTTGGCCTGAA
GACTGTGAACAGAAGGTTTCAGCAAAATTCTTTAGTGAAGCTGTAATTGAGGGGTTGGCT
TCTGATGGTGGCCTCTTTGTTCCTGCAAAGGAGTTTCCAAAATTAAGCTGCGGGGAGTGG
AAAAGCCTAGTAGGAGCAACCTACGTAGAAAGAGCACAGATACTGTTGGAAAGATGTATC
CATCCTGCAGACATACCTGCTGCCAGGTTGGGAGAAATGATTGAAACTGCTTATGGGGAA
AACTTTGCCTGCTCAAAAATTGCTCCTGTCAGGCACCTTTCAGGCAACCAGTTCATCCTG
GAGTTGTTTCATGGACCAACAGGATCATTTAAAGATTTGTCTTTACAGCTTATGCCTCAT
ATTTTTGCACACTGTATCCCACCAAGTTGCAATTATATGATACTTGTAGCTACTTCAGGA
GACACAGGGAGTGCAGTCTTAAATGGTTTTAGTCGTCTAAATAAGAATGATAAGCAAAGG
ATAGCTGTGGTTGCATTTTTTCCTGAGAATGGAGTAAGTGATTTTCAAAAAGCACAAATA
ATTGGCAGTCAGAGAGAAAATGGATGGGCAGTGGGTGTTGAGTCAGATTTTGATTTTTGC
CAGACAGCTATAAAAAGAATTTTTAATGATTCTGATTTTACTGGCTTTCTTACTGTGGAA
TATGGAACAATCTTAAGTTCGGCTAACTCCATAAACTGGGGCCGACTACTTCCGCAGGTA
GTTTATCATGCTTCCGCATATCTTGATCTTGTTAGTCAAGGATTTATTTCTTTTGGAAGC
CCAGTCGATGTCTGTATTCCCACAGGAAACTTTGGTAACATTTTAGCAGCAGTGTATGCC
AAAATGATGGGAATCCCGATTCGAAAATTTATCTGTGCCTCTAATCAGAACCATGTTTTG
ACTGATTTTATAAAAACAGGACATTATGATCTAAGGGAAAGAAAACTAGCACAAACCTTT
TCACCGTCAATAGATATTCTCAAATCTTCAAACCTAGAACGACATTTACACTTGATGGCT
AATAAAGATGGACAGCTAATGACAGAATTATTTAATCGATTAGAAAGTCAGCATCATTTC
CAGATAGAAAAGGCTCTAGTTGAGAAACTTCAGCAGGATTTTGTAGCTGACTGGTGCTCT
GAGGGAGAGTGCCTAGCAGCTATTAACTCCACCTATAATACTTCAGGGTATATTTTGGAT
CCACACACTGCTGTTGCAAAAGTGGTTGCAGATAGGGTGCAAGACAAAACTTGCCCTGTG
ATTATCTCATCTACAGCCCATTACTCAAAGTTTGCACCTGCTATCATGCAGGCTTTAAAG
ATTAAAGAAATCAATGAGACTTCATCAAGTCAGCTCTATTTGCTGGGTTCATACAATGCA
TTACCTCCACTGCATGAGGCTTTATTAGAGAGAACAAAACAGCAAGAGAAGATGGAGTAC
CAGGTCTGTGCAGCTGATATGAATGTCTTGAAGAGTCATGTGGAACAACTTGTCCAAAAT
CAATTCATATGA
|
| Enzyme 46 GenBank Gene ID |
AK125249  |
| Enzyme 46 GeneCard ID |
THNSL1  |
| Enzyme 46 GenAtlas ID |
THNSL1  |
| Enzyme 46 HGNC ID |
HGNC:26160  |
| Enzyme 46 Chromosome Location |
1 |
| Enzyme 46 Locus |
10p12.1 |
| Enzyme 46 SNPs |
SNPJam Report  |
| Enzyme 46 General References |
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
- Deloukas P, Earthrowl ME, Grafham DV, Rubenfield M, French L, Steward CA, Sims SK, Jones MC, Searle S, Scott C, Howe K, Hunt SE, Andrews TD, Gilbert JG, Swarbreck D, Ashurst JL, Taylor A, Battles J, Bird CP, Ainscough R, Almeida JP, Ashwell RI, Ambrose KD, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Bates K, Beasley H, Bray-Allen S, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Cahill P, Camire D, Carter NP, Chapman JC, Clark SY, Clarke G, Clee CM, Clegg S, Corby N, Coulson A, Dhami P, Dutta I, Dunn M, Faulkner L, Frankish A, Frankland JA, Garner P, Garnett J, Gribble S, Griffiths C, Grocock R, Gustafson E, Hammond S, Harley JL, Hart E, Heath PD, Ho TP, Hopkins B, Horne J, Howden PJ, Huckle E, Hynds C, Johnson C, Johnson D, Kana A, Kay M, Kimberley AM, Kershaw JK, Kokkinaki M, Laird GK, Lawlor S, Lee HM, Leongamornlert DA, Laird G, Lloyd C, Lloyd DM, Loveland J, Lovell J, McLaren S, McLay KE, McMurray A, Mashreghi-Mohammadi M, Matthews L, Milne S, Nickerson T, Nguyen M, Overton-Larty E, Palmer SA, Pearce AV, Peck AI, Pelan S, Phillimore B, Porter K, Rice CM, Rogosin A, Ross MT, Sarafidou T, Sehra HK, Shownkeen R, Skuce CD, Smith M, Standring L, Sycamore N, Tester J, Thorpe A, Torcasso W, Tracey A, Tromans A, Tsolas J, Wall M, Walsh J, Wang H, Weinstock K, West AP, Willey DL, Whitehead SL, Wilming L, Wray PW, Young L, Chen Y, Lovering RC, Moschonas NK, Siebert R, Fechtel K, Bentley D, Durbin R, Hubbard T, Doucette-Stamm L, Beck S, Smith DR, Rogers J: The DNA sequence and comparative analysis of human chromosome 10. Nature. 2004 May 27;429(6990):375-81. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed
]
|
| Enzyme 46 Metabolite References |
Not Available |
|
Enzyme 47
[top]
|
| Enzyme 47 ID |
9163 |
| Enzyme 47 Name |
Alanine--glyoxylate aminotransferase 2-like 1 |
| Enzyme 47 Synonyms |
Not Available |
| Enzyme 47 Gene Name |
AGXT2L1 |
| Enzyme 47 Protein Sequence |
>Alanine--glyoxylate aminotransferase 2-like 1
MCELYSKRDTLGLRKKHIGPSCKVFFASDPIKIVRAQRQYMFDENGEQYLDCINNVAHVG
HCHPGVVKAALKQMELLNTNSRFLHDNIVEYAKRLSATLPEKLSVCYFTNSGSEANDLAL
RLARQFRGHQDVITLDHAYHGHLSSLIEISPYKFQKGKDVKKEFVHVAPTPDTYRGKYRE
DHADSASAYADEVKKIIEDAHNSGRKIAAFIAESMQSCGGQIIPPAGYFQKVAEYVHGAG
GVFIADEVQVGFGRVGKHFWSFQMYGEDFVPDIVTMGKPMGNGHPVACVVTTKEIAEAFS
SSGMEYFNTYGGNPVSCAVGLAVLDIIENEDLQGNAKRVGNYLTELLKKQKAKHTLIGDI
RGIGLFIGIDLVKDHLKRTPATAEAQHIIYKMKEKRVLLSADGPHRNVLKIKPPMCFTEE
DAKFMVDQLDRILTVLEEAMGTKTESVTSENTPCKTKMLKEAHIELLRDSTTDSKENPSR
KRNGMCTDTHSLLSKRLKT
|
| Enzyme 47 Number of Residues |
499 |
| Enzyme 47 Molecular Weight |
55670.4 |
| Enzyme 47 Theoretical pI |
8.22 |
| Enzyme 47 GO Classification |
| Function |
- binding
- catalytic activity
- cofactor binding
- pyridoxal phosphate binding
- transaminase activity
- transferase activity
- transferase activity, transferring nitrogenous groups
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 47 General Function |
Involved in transaminase activity |
| Enzyme 47 Specific Function |
Not Available |
| Enzyme 47 Pathways |
Not Available |
| Enzyme 47 Reactions |
Not Available |
| Enzyme 47 Pfam Domain Function |
|
| Enzyme 47 Signals |
|
| Enzyme 47 Transmembrane Regions |
|
| Enzyme 47 Essentiality |
Not Available |
| Enzyme 47 GenBank ID Protein |
63992119  |
| Enzyme 47 UniProtKB/Swiss-Prot ID |
Q8TBG4  |
| Enzyme 47 UniProtKB/Swiss-Prot Entry Name |
AT2L1_HUMAN  |
| Enzyme 47 PDB ID |
Not Available |
| Enzyme 47 Cellular Location |
Not Available |
| Enzyme 47 Gene Sequence |
>1500 bp
ATGTGCGAGCTGTACAGTAAGCGGGACACTCTGGGGCTGAGGAAGAAGCACATCGGGCCC
TCATGCAAAGTTTTCTTTGCATCGGATCCCATCAAAATAGTGAGAGCCCAGAGGCAGTAC
ATGTTTGATGAGAACGGTGAACAGTACTTGGACTGCATCAACAATGTTGCCCATGTGGGA
CACTGTCACCCAGGAGTGGTCAAAGCTGCCCTGAAACAGATGGAACTGCTAAATACAAAT
TCTCGATTCCTCCACGACAACATTGTTGAGTATGCCAAACGCCTTTCAGCAACTCTGCCG
GAGAAACTCTCTGTTTGTTATTTTACAAATTCAGGATCCGAAGCCAACGACTTAGCCTTA
CGCCTGGCTCGGCAGTTCAGAGGCCACCAGGATGTGATCACTCTTGACCATGCTTACCAT
GGTCACCTATCATCCTTAATTGAGATTAGCCCATATAAGTTTCAGAAAGGAAAAGATGTC
AAAAAAGAATTTGTACATGTGGCACCAACTCCAGATACTTACAGAGGAAAATATAGAGAA
GACCATGCAGACTCAGCCAGTGCTTATGCAGATGAAGTGAAGAAAATCATTGAAGATGCT
CATAACAGTGGAAGGAAGATTGCTGCCTTTATTGCTGAATCCATGCAGAGTTGTGGCGGA
CAAATAATTCCTCCAGCAGGCTACTTCCAGAAAGTGGCAGAATATGTACACGGTGCAGGG
GGTGTGTTTATAGCTGATGAAGTTCAAGTGGGCTTTGGCAGAGTTGGGAAACATTTCTGG
AGCTTCCAGATGTATGGTGAAGACTTTGTTCCAGACATCGTCACAATGGGAAAACCGATG
GGCAACGGCCACCCGGTGGCATGTGTGGTAACAACCAAAGAAATTGCAGAAGCCTTCAGC
AGCTCTGGGATGGAATATTTTAATACGTATGGAGGAAATCCAGTATCTTGTGCTGTTGGT
TTGGCTGTCCTGGATATAATTGAAAATGAAGACCTTCAAGGAAATGCCAAGAGAGTAGGG
AATTATCTCACTGAGTTACTGAAAAAACAGAAGGCTAAACACACTTTGATAGGAGATATT
AGGGGCATTGGCCTTTTTATTGGAATTGATTTAGTGAAGGACCATCTGAAAAGGACCCCT
GCCACAGCTGAAGCTCAGCACATCATCTACAAGATGAAAGAAAAACGAGTGCTTCTCAGT
GCCGATGGACCTCATAGAAATGTACTTAAAATAAAACCACCTATGTGCTTCACTGAAGAA
GATGCAAAGTTCATGGTGGACCAACTTGATAGGATTCTAACAGTTTTAGAAGAAGCTATG
GGAACCAAAACCGAAAGTGTGACCTCTGAGAATACTCCATGCAAAACAAAGATGCTGAAA
GAAGCCCACATAGAACTGCTTAGGGACAGCACCACTGACTCCAAAGAAAATCCCAGCAGA
AAGAGAAATGGAATGTGCACGGATACACATTCACTGCTCAGTAAGAGGCTCAAGACATGA
|
| Enzyme 47 GenBank Gene ID |
AC097473  |
| Enzyme 47 GeneCard ID |
AGXT2L1  |
| Enzyme 47 GenAtlas ID |
AGXT2L1  |
| Enzyme 47 HGNC ID |
HGNC:14404  |
| Enzyme 47 Chromosome Location |
4 |
| Enzyme 47 Locus |
4q25 |
| Enzyme 47 SNPs |
SNPJam Report  |
| Enzyme 47 General References |
- Lee IS, Muragaki Y, Ideguchi T, Hase T, Tsuji M, Ooshima A, Okuno E, Kido R: Molecular cloning and sequencing of a cDNA encoding alanine-glyoxylate aminotransferase 2 from rat kidney. J Biochem. 1995 Apr;117(4):856-62. [PubMed
]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
- Hillier LW, Graves TA, Fulton RS, Fulton LA, Pepin KH, Minx P, Wagner-McPherson C, Layman D, Wylie K, Sekhon M, Becker MC, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Kremitzki C, Oddy L, Du H, Sun H, Bradshaw-Cordum H, Ali J, Carter J, Cordes M, Harris A, Isak A, van Brunt A, Nguyen C, Du F, Courtney L, Kalicki J, Ozersky P, Abbott S, Armstrong J, Belter EA, Caruso L, Cedroni M, Cotton M, Davidson T, Desai A, Elliott G, Erb T, Fronick C, Gaige T, Haakenson W, Haglund K, Holmes A, Harkins R, Kim K, Kruchowski SS, Strong CM, Grewal N, Goyea E, Hou S, Levy A, Martinka S, Mead K, McLellan MD, Meyer R, Randall-Maher J, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Shah N, Swearengen-Shahid S, Snider J, Strong JT, Thompson J, Yoakum M, Leonard S, Pearman C, Trani L, Radionenko M, Waligorski JE, Wang C, Rock SM, Tin-Wollam AM, Maupin R, Latreille P, Wendl MC, Yang SP, Pohl C, Wallis JW, Spieth J, Bieri TA, Berkowicz N, Nelson JO, Osborne J, Ding L, Meyer R, Sabo A, Shotland Y, Sinha P, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Jones TA, She X, Ciccarelli FD, Izaurralde E, Taylor J, Schmutz J, Myers RM, Cox DR, Huang X, McPherson JD, Mardis ER, Clifton SW, Warren WC, Chinwalla AT, Eddy SR, Marra MA, Ovcharenko I, Furey TS, Miller W, Eichler EE, Bork P, Suyama M, Torrents D, Waterston RH, Wilson RK: Generation and annotation of the DNA sequences of human chromosomes 2 and 4. Nature. 2005 Apr 7;434(7034):724-31. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
|
| Enzyme 47 Metabolite References |
Not Available |
|
Enzyme 48
[top]
|
| Enzyme 48 ID |
9258 |
| Enzyme 48 Name |
Alanine aminotransferase 2 |
| Enzyme 48 Synonyms |
- ALT2
- Glutamate pyruvate transaminase 2
- GPT 2
- Glutamic--alanine transaminase 2
- Glutamic--pyruvic transaminase 2
|
| Enzyme 48 Gene Name |
GPT2 |
| Enzyme 48 Protein Sequence |
>Alanine aminotransferase 2
MQRAAALVRRGCGPRTPSSWGRSQSSAAAEASAVLKVRPERSRRERILTLESMNPQVKAV
EYAVRGPIVLKAGEIELELQRGIKKPFTEVIRANIGDAQAMGQQPITFLRQVMALCTYPN
LLDSPSFPEDAKKRARRILQACGGNSLGSYSASQGVNCIREDVAAYITRRDGGVPADPDN
IYLTTGASDGISTILKILVSGGGKSRTGVMIPIPQYPLYSAVISELDAIQVNYYLDEENC
WALNVNELRRAVQEAKDHCDPKVLCIINPGNPTGQVQSRKCIEDVIHFAWEEKLFLLADE
VYQDNVYSPDCRFHSFKKVLYEMGPEYSSNVELASFHSTSKGYMGECGYRGGYMEVINLH
PEIKGQLVKLLSVRLCPPVSGQAAMDIVVNPPVAGEESFEQFSREKESVLGNLAKKAKLT
EDLFNQVPGIHCNPLQGAMYAFPRIFIPAKAVEAAQAHQMAPDMFYCMKLLEETGICVVP
GSGFGQREGTYHFRMTILPPVEKLKTVLQKVKDFHINFLEKYA
|
| Enzyme 48 Number of Residues |
523 |
| Enzyme 48 Molecular Weight |
57903.1 |
| Enzyme 48 Theoretical pI |
7.77 |
| Enzyme 48 GO Classification |
| Function |
- binding
- catalytic activity
- cofactor binding
- pyridoxal phosphate binding
- transferase activity
- transferase activity, transferring nitrogenous groups
|
| Process |
- biosynthetic process
- metabolic process
|
| Component |
| — |
|
| Enzyme 48 General Function |
Involved in transferase activity, transferring nitrogenous groups |
| Enzyme 48 Specific Function |
Catalyzes the reversible transamination between alanine and 2-oxoglutarate to form pyruvate and glutamate |
| Enzyme 48 Pathways |
|
| Enzyme 48 Reactions |
- L-alanine + 2-oxoglutarate = pyruvate + L-glutamate [RN:R00258]
|
| Enzyme 48 Pfam Domain Function |
|
| Enzyme 48 Signals |
|
| Enzyme 48 Transmembrane Regions |
|
| Enzyme 48 Essentiality |
Not Available |
| Enzyme 48 GenBank ID Protein |
19046894  |
| Enzyme 48 UniProtKB/Swiss-Prot ID |
Q8TD30  |
| Enzyme 48 UniProtKB/Swiss-Prot Entry Name |
ALAT2_HUMAN  |
| Enzyme 48 PDB ID |
Not Available |
| Enzyme 48 Cellular Location |
Not Available |
| Enzyme 48 Gene Sequence |
>1572 bp
ATGCAGCGGGCGGCGGCGCTGGTCCGGCGGGGCTGTGGTCCCCGGACCCCCAGCTCCTGG
GGCCGCAGCCAGAGCAGCGCGGCCGCCGAGGCCTCGGCGGTGCTCAAGGTGCGGCCCGAG
CGCAGCCGGCGCGAGCGCATCCTCACGCTGGAGTCCATGAACCCGCAGGTGAAGGCGGTG
GAGTACGCCGTGCGGGGACCCATCGTGCTCAAGGCCGGCGAGATCGAGCTCGAGCTGCAG
CGGGGTATCAAAAAGCCATTCACAGAGGTCATCCGAGCCAACATCGGGGACGCCCAGGCT
ATGGGGCAGCAGCCAATCACCTTCCTCCGGCAGGTGATGGCACTATGCACCTACCCAAAC
CTGCTGGACAGCCCCAGCTTCCCAGAAGATGCTAAGAAACGTGCCCGGCGGATCCTGCAG
GCTTGTGGCGGGAACAGCCTGGGGTCCTACAGTGCTAGCCAGGGTGTCAACTGCATCCGT
GAAGATGTGGCTGCCTACATCACCAGGAGGGATGGCGGTGTGCCTGCGGACCCCGACAAC
ATCTACCTGACCACGGGAGCTAGTGACGGCATTTCTACGATCCTGAAGATCCTCGTCTCC
GGGGGCGGCAAGTCACGGACAGGTGTGATGATCCCCATCCCACAATATCCCCTCTATTCA
GCTGTCATCTCTGAGCTCGACGCCATCCAGGTGAATTACTACCTGGACGAGGAGAACTGC
TGGGCGCTGAATGTGAATGAGCTCCGGCGGGCGGTGCAGGAGGCCAAAGACCACTGTGAT
CCTAAGGTGCTCTGCATAATCAACCCTGGGAACCCCACAGGCCAGGTACAAAGCAGAAAG
TGCATAGAAGATGTGATCCACTTTGCCTGGGAAGAGAAGCTCTTTCTCCTGGCTGATGAG
GTGTACCAGGACAACGTGTACTCTCCAGATTGCAGATTCCACTCCTTCAAGAAGGTGCTG
TACGAGATGGGGCCCGAGTACTCCAGCAACGTGGAGCTCGCCTCCTTCCACTCCACCTCC
AAGGGCTACATGGGCGAGTGTGGTTACAGAGGAGGCTACATGGAGGTGATCAACCTGCAC
CCTGAGATCAAGGGCCAGCTGGTGAAGCTGCTGTCGGTGCGCCTGTGCCCCCCAGTGTCT
GGGCAGGCCGCCATGGACATTGTCGTGAACCCCCCGGTGGCAGGAGAGGAGTCCTTTGAG
CAATTCAGCCGAGAGAAGGAGTCGGTCCTGGGTAATCTGGCCAAAAAAGCAAAGCTGACG
GAAGACCTGTTTAACCAAGTCCCAGGAATTCACTGCAACCCCTTGCAGGGGGCCATGTAC
GCCTTCCCTCGGATCTTCATTCCTGCCAAAGCTGTGGAGGCTGCTCAGGCCCATCAAATG
GCTCCAGACATGTTCTACTGCATGAAGCTCCTGGAGGAGACTGGCATCTGTGTCGTGCCC
GGCAGTGGCTTTGGGCAGAGGGAAGGCACTTACCACTTCAGGATGACTATCCTCCCTCCA
GTGGAGAAGCTGAAAACGGTGCTGCAGAAGGTGAAAGACTTCCACATCAACTTCCTGGAG
AAGTACGCGTGA
|
| Enzyme 48 GenBank Gene ID |
AY029173  |
| Enzyme 48 GeneCard ID |
GPT2  |
| Enzyme 48 GenAtlas ID |
GPT2  |
| Enzyme 48 HGNC ID |
HGNC:18062  |
| Enzyme 48 Chromosome Location |
1 |
| Enzyme 48 Locus |
16q12.1 |
| Enzyme 48 SNPs |
SNPJam Report  |
| Enzyme 48 General References |
- Yang RZ, Blaileanu G, Hansen BC, Shuldiner AR, Gong DW: cDNA cloning, genomic structure, chromosomal mapping, and functional expression of a novel human alanine aminotransferase. Genomics. 2002 Mar;79(3):445-50. [PubMed
]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
- Martin J, Han C, Gordon LA, Terry A, Prabhakar S, She X, Xie G, Hellsten U, Chan YM, Altherr M, Couronne O, Aerts A, Bajorek E, Black S, Blumer H, Branscomb E, Brown NC, Bruno WJ, Buckingham JM, Callen DF, Campbell CS, Campbell ML, Campbell EW, Caoile C, Challacombe JF, Chasteen LA, Chertkov O, Chi HC, Christensen M, Clark LM, Cohn JD, Denys M, Detter JC, Dickson M, Dimitrijevic-Bussod M, Escobar J, Fawcett JJ, Flowers D, Fotopulos D, Glavina T, Gomez M, Gonzales E, Goodstein D, Goodwin LA, Grady DL, Grigoriev I, Groza M, Hammon N, Hawkins T, Haydu L, Hildebrand CE, Huang W, Israni S, Jett J, Jewett PB, Kadner K, Kimball H, Kobayashi A, Krawczyk MC, Leyba T, Longmire JL, Lopez F, Lou Y, Lowry S, Ludeman T, Manohar CF, Mark GA, McMurray KL, Meincke LJ, Morgan J, Moyzis RK, Mundt MO, Munk AC, Nandkeshwar RD, Pitluck S, Pollard M, Predki P, Parson-Quintana B, Ramirez L, Rash S, Retterer J, Ricke DO, Robinson DL, Rodriguez A, Salamov A, Saunders EH, Scott D, Shough T, Stallings RL, Stalvey M, Sutherland RD, Tapia R, Tesmer JG, Thayer N, Thompson LS, Tice H, Torney DC, Tran-Gyamfi M, Tsai M, Ulanovsky LE, Ustaszewska A, Vo N, White PS, Williams AL, Wills PL, Wu JR, Wu K, Yang J, Dejong P, Bruce D, Doggett NA, Deaven L, Schmutz J, Grimwood J, Richardson P, Rokhsar DS, Eichler EE, Gilna P, Lucas SM, Myers RM, Rubin EM, Pennacchio LA: The sequence and analysis of duplication-rich human chromosome 16. Nature. 2004 Dec 23;432(7020):988-94. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
|
| Enzyme 48 Metabolite References |
Not Available |
|
Enzyme 49
[top]
|
| Enzyme 49 ID |
9426 |
| Enzyme 49 Name |
Pyridoxal phosphate phosphatase |
| Enzyme 49 Synonyms |
- PLP phosphatase
|
| Enzyme 49 Gene Name |
PDXP |
| Enzyme 49 Protein Sequence |
>Pyridoxal phosphate phosphatase
MARCERLRGAALRDVLGRAQGVLFDCDGVLWNGERAVPGAPELLERLARAGKAALFVSNN
SRRARPELALRFARLGFGGLRAEQLFSSALCAARLLRQRLPGPPDAPGAVFVLGGEGLRA
ELRAAGLRLAGDPSAGDGAAPRVRAVLVGYDEHFSFAKLREACAHLRDPECLLVATDRDP
WHPLSDGSRTPGTGSLAAAVETASGRQALVVGKPSPYMFECITENFSIDPARTLMVGDRL
ETDILFGHRCGMTTVLTLTGVSRLEEAQAYLAAGQHDLVPHYYVESIADLTEGLED
|
| Enzyme 49 Number of Residues |
296 |
| Enzyme 49 Molecular Weight |
31697.7 |
| Enzyme 49 Theoretical pI |
6.51 |
| Enzyme 49 GO Classification |
| Function |
- catalytic activity
- hydrolase activity
- hydrolase activity, acting on ester bonds
- phosphatase activity
- phosphoric ester hydrolase activity
|
| Process |
|
| Component |
| — |
|
| Enzyme 49 General Function |
Involved in catalytic activity |
| Enzyme 49 Specific Function |
Pyridoxal phosphate phosphatase. Has some activity towards pyridoxal 5'-phosphate (PLP), pyridoxine 5'-phosphate (PMP) and Pyridoxine 5'-phosphate (PNP), with a highest activity with PLP followed by PNP |
| Enzyme 49 Pathways |
|
| Enzyme 49 Reactions |
- pyridoxal 5'-phosphate + H2O = pyridoxal + phosphate [RN:R00173]
|
| Enzyme 49 Pfam Domain Function |
|
| Enzyme 49 Signals |
|
| Enzyme 49 Transmembrane Regions |
|
| Enzyme 49 Essentiality |
Not Available |
| Enzyme 49 GenBank ID Protein |
Not Available |
| Enzyme 49 UniProtKB/Swiss-Prot ID |
Q96GD0  |
| Enzyme 49 UniProtKB/Swiss-Prot Entry Name |
PLPP_HUMAN  |
| Enzyme 49 PDB ID |
Not Available |
| Enzyme 49 Cellular Location |
Not Available |
| Enzyme 49 Gene Sequence |
>891 bp
ATGGCGCGCTGCGAGAGGCTGCGCGGAGCGGCCCTGCGCGACGTGCTGGGCCGGGCGCAG
GGGGTCCTGTTCGACTGTGACGGGGTGCTGTGGAACGGCGAGCGCGCCGTGCCGGGCGCC
CCGGAGCTGCTGGAGCGGCTGGCGCGGGCCGGCAAGGCGGCTCTGTTTGTGAGCAACAAC
AGCCGGCGCGCGCGGCCCGAGCTGGCCCTGCGCTTCGCGCGCCTCGGCTTCGGGGGGCTG
CGCGCCGAGCAGCTCTTCAGCTCCGCGCTGTGCGCCGCGCGCCTGCTGCGCCAGCGCCTG
CCCGGGCCTCCGGACGCGCCGGGCGCCGTGTTCGTGCTGGGCGGCGAGGGGCTGCGCGCC
GAGCTGCGCGCCGCGGGGCTGCGCCTGGCCGGGGACCCGAGCGCGGGGGACGGCGCGGCC
CCGCGCGTGCGCGCCGTGCTTGTGGGCTACGACGAGCACTTCTCCTTCGCCAAGCTGAGG
GAGGCGTGCGCGCACCTGCGCGACCCCGAGTGCCTACTCGTGGCCACCGACCGTGACCCA
TGGCACCCGCTGAGCGACGGCAGCCGGACCCCTGGCACCGGGAGCCTGGCCGCTGCAGTG
GAGACAGCCTCGGGACGCCAGGCCCTGGTGGTGGGCAAGCCCAGCCCCTACATGTTCGAG
TGCATCACGGAGAACTTCAGCATCGACCCCGCACGCACGCTTATGGTGGGTGACCGCCTG
GAGACCGACATCCTCTTTGGCCACCGCTGCGGCATGACCACTGTGCTCACGCTCACAGGA
GTCTCCCGCCTAGAAGAGGCCCAGGCCTACCTAGCGGCCGGCCAGCACGACCTCGTGCCC
CATTACTATGTGGAGAGCATCGCAGACTTGACAGAGGGGTTGGAGGACTGA
|
| Enzyme 49 GenBank Gene ID |
AY125047  |
| Enzyme 49 GeneCard ID |
PDXP  |
| Enzyme 49 GenAtlas ID |
PDXP  |
| Enzyme 49 HGNC ID |
HGNC:30259  |
| Enzyme 49 Chromosome Location |
2 |
| Enzyme 49 Locus |
22cen-q12.3 |
| Enzyme 49 SNPs |
SNPJam Report  |
| Enzyme 49 General References |
- Jang YM, Kim DW, Kang TC, Won MH, Baek NI, Moon BJ, Choi SY, Kwon OS: Human pyridoxal phosphatase. Molecular cloning, functional expression, and tissue distribution. J Biol Chem. 2003 Dec 12;278(50):50040-6. Epub 2003 Sep 30. [PubMed
]
- Dunham I, Shimizu N, Roe BA, Chissoe S, Hunt AR, Collins JE, Bruskiewich R, Beare DM, Clamp M, Smink LJ, Ainscough R, Almeida JP, Babbage A, Bagguley C, Bailey J, Barlow K, Bates KN, Beasley O, Bird CP, Blakey S, Bridgeman AM, Buck D, Burgess J, Burrill WD, O'Brien KP, et al.: The DNA sequence of human chromosome 22. Nature. 1999 Dec 2;402(6761):489-95. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Gao G, Fonda ML: Identification of an essential cysteine residue in pyridoxal phosphatase from human erythrocytes. J Biol Chem. 1994 Mar 18;269(11):8234-9. [PubMed
]
|
| Enzyme 49 Metabolite References |
Not Available |
|
Enzyme 50
[top]
|
| Enzyme 50 ID |
10418 |
| Enzyme 50 Name |
Selenocysteine lyase |
| Enzyme 50 Synonyms |
- hSCL
|
| Enzyme 50 Gene Name |
SCLY |
| Enzyme 50 Protein Sequence |
>Selenocysteine lyase
MEAAVAPGRDAPAPAASQPSGCGKHNSPERKVYMDYNATTPLEPEVIQAMTKAMWEAWGN
PSSPYSAGRKAKDIINAARESLAKMIGGKPQDIIFTSGGTESNNLVIHSVVKHFHANQTS
KGHTGGHHSPVKGAKPHFITSSVEHDSIRLPLEHLVEEQVAAVTFVPVSKVSGQAEVDDI
LAAVRPTTRLVTIMLANNETGIVMPVPEISQRIKALNQERVAAGLPPILVHTDAAQALGK
QRVDVEDLGVDFLTIVGHKFYGPRIGALYIRGLGEFTPLYPMLFGGGQERNFRPGTENTP
MIAGLGKAAELVTQNCEAYEAHMRDVRDYLEERLEAEFGQKRIHLNSQFPGTQRLPNTCN
FSIRGPRLQGHVVLAQCRVLMASVGAACHSDHGDQPSPVLLSYGVPFDVARNALRLSVGR
STTRAEVDLVVQDLKQAVAQLEDQA
|
| Enzyme 50 Number of Residues |
445 |
| Enzyme 50 Molecular Weight |
48148.4 |
| Enzyme 50 Theoretical pI |
7.13 |
| Enzyme 50 GO Classification |
| Function |
- binding
- catalytic activity
- cofactor binding
- pyridoxal phosphate binding
|
| Process |
|
| Component |
| — |
|
| Enzyme 50 General Function |
Involved in metabolic process |
| Enzyme 50 Specific Function |
Catalyzes the decomposition of L-selenocysteine to L- alanine and elemental selenium |
| Enzyme 50 Pathways |
Not Available |
| Enzyme 50 Reactions |
- L-selenocysteine + reduced acceptor = selenide + L-alanine + acceptor [RN:R03598]
|
| Enzyme 50 Pfam Domain Function |
|
| Enzyme 50 Signals |
|
| Enzyme 50 Transmembrane Regions |
|
| Enzyme 50 Essentiality |
Not Available |
| Enzyme 50 GenBank ID Protein |
156713448  |
| Enzyme 50 UniProtKB/Swiss-Prot ID |
Q96I15  |
| Enzyme 50 UniProtKB/Swiss-Prot Entry Name |
SCLY_HUMAN  |
| Enzyme 50 PDB ID |
Not Available |
| Enzyme 50 Cellular Location |
Not Available |
| Enzyme 50 Gene Sequence |
>1338 bp
ATGGAGGCGGCCGTGGCGCCGGGGAGGGATGCGCCGGCACCCGCGGCGAGTCAGCCCAGC
GGCTGCGGGAAACACAACTCGCCGGAGAGGAAAGTTTATATGGACTATAATGCAACGACT
CCCCTGGAGCCAGAAGTTATCCAGGCCATGACCAAGGCCATGTGGGAAGCCTGGGGAAAT
CCCAGCAGCCCGTATTCAGCAGGAAGAAAGGCCAAGGATATTATAAATGCAGCTCGGGAA
AGCCTCGCGAAGATGATAGGGGGGAAACCTCAAGATATAATCTTCACTTCCGGGGGCACT
GAGTCAAATAATTTAGTAATCCATTCTGTGGTGAAACATTTCCACGCAAACCAGACCTCA
AAGGGACACACAGGTGGGCACCACAGCCCAGTGAAGGGGGCCAAGCCCCATTTCATTACT
TCCTCGGTGGAACACGACTCCATCCGGCTGCCCCTGGAGCACCTGGTGGAAGAACAAGTG
GCAGCGGTCACCTTTGTCCCGGTGTCCAAGGTGAGCGGGCAGGCAGAGGTGGACGACATC
CTCGCGGCAGTCCGCCCGACCACACGCCTCGTGACCATCATGCTGGCCAACAATGAGACT
GGCATTGTCATGCCTGTCCCTGAAATCAGTCAGCGCATTAAAGCCCTGAACCAGGAACGG
GTGGCAGCTGGGCTACCTCCCATCCTCGTGCACACGGATGCTGCACAGGCCTTGGGGAAG
CAGCGCGTGGATGTGGAGGACCTGGGCGTGGACTTCCTTACAATCGTGGGGCACAAGTTT
TATGGTCCCAGGATTGGCGCACTTTATATACGAGGACTTGGTGAATTTACCCCTCTCTAC
CCTATGCTATTTGGAGGTGGACAAGAACGGAATTTCAGGCCAGGGACAGAGAACACCCCA
ATGATTGCTGGCCTTGGGAAGGCCGCGGAGCTGGTGACCCAGAACTGCGAGGCTTATGAG
GCCCACATGAGGGACGTCCGCGACTACCTGGAAGAGAGGCTGGAAGCTGAATTCGGTCAG
AAGAGAATCCATCTGAATAGCCAGTTTCCAGGCACCCAGCGGCTTCCCAATACCTGTAAC
TTTTCCATCCGGGGACCCCGGCTTCAAGGCCACGTGGTGCTTGCGCAGTGCCGAGTGCTG
ATGGCCAGTGTGGGGGCCGCGTGCCACTCGGACCACGGGGACCAGCCGTCCCCAGTGCTG
CTGAGCTACGGTGTCCCCTTCGACGTGGCCAGGAACGCGCTCCGGCTCAGCGTGGGCCGC
AGCACCACCAGGGCCGAGGTGGACCTCGTCGTGCAGGACCTGAAGCAGGCCGTGGCGCAG
CTGGAGGACCAGGCCTAG
|
| Enzyme 50 GenBank Gene ID |
NM_016510.4  |
| Enzyme 50 GeneCard ID |
SCLY  |
| Enzyme 50 GenAtlas ID |
SCLY  |
| Enzyme 50 HGNC ID |
HGNC:18161  |
| Enzyme 50 Chromosome Location |
2 |
| Enzyme 50 Locus |
2q37.3 |
| Enzyme 50 SNPs |
SNPJam Report  |
| Enzyme 50 General References |
- Mihara H, Kurihara T, Watanabe T, Yoshimura T, Esaki N: cDNA cloning, purification, and characterization of mouse liver selenocysteine lyase. Candidate for selenium delivery protein in selenoprotein synthesis. J Biol Chem. 2000 Mar 3;275(9):6195-200. [PubMed
]
- Hillier LW, Graves TA, Fulton RS, Fulton LA, Pepin KH, Minx P, Wagner-McPherson C, Layman D, Wylie K, Sekhon M, Becker MC, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Kremitzki C, Oddy L, Du H, Sun H, Bradshaw-Cordum H, Ali J, Carter J, Cordes M, Harris A, Isak A, van Brunt A, Nguyen C, Du F, Courtney L, Kalicki J, Ozersky P, Abbott S, Armstrong J, Belter EA, Caruso L, Cedroni M, Cotton M, Davidson T, Desai A, Elliott G, Erb T, Fronick C, Gaige T, Haakenson W, Haglund K, Holmes A, Harkins R, Kim K, Kruchowski SS, Strong CM, Grewal N, Goyea E, Hou S, Levy A, Martinka S, Mead K, McLellan MD, Meyer R, Randall-Maher J, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Shah N, Swearengen-Shahid S, Snider J, Strong JT, Thompson J, Yoakum M, Leonard S, Pearman C, Trani L, Radionenko M, Waligorski JE, Wang C, Rock SM, Tin-Wollam AM, Maupin R, Latreille P, Wendl MC, Yang SP, Pohl C, Wallis JW, Spieth J, Bieri TA, Berkowicz N, Nelson JO, Osborne J, Ding L, Meyer R, Sabo A, Shotland Y, Sinha P, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Jones TA, She X, Ciccarelli FD, Izaurralde E, Taylor J, Schmutz J, Myers RM, Cox DR, Huang X, McPherson JD, Mardis ER, Clifton SW, Warren WC, Chinwalla AT, Eddy SR, Marra MA, Ovcharenko I, Furey TS, Miller W, Eichler EE, Bork P, Suyama M, Torrents D, Waterston RH, Wilson RK: Generation and annotation of the DNA sequences of human chromosomes 2 and 4. Nature. 2005 Apr 7;434(7034):724-31. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
- Jafari C, Panzer U, Steinmetz OM, Zahner G, Stahl RA, Harendza S: Enhanced expression of selenocysteine lyase in acute glomerulonephritis and its regulation by AP-1. Cell Mol Biol Lett. 2006;11(3):424-37. [PubMed
]
- Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed
]
|
| Enzyme 50 Metabolite References |
Not Available |
|
Enzyme 51
[top]
|
| Enzyme 51 ID |
12977 |
| Enzyme 51 Name |
Alanine aminotransferase |
| Enzyme 51 Synonyms |
Not Available |
| Enzyme 51 Gene Name |
GPT |
| Enzyme 51 Protein Sequence |
>Alanine aminotransferase
MASSTGDRSQAVRHGLRAKVLTLDGMNPRVRRVEYAVRGPIVQRALELEQELRQGVKKPF
TEVIRANIGDAQAMGQRPITFLRQVLALCVNPDLLSSPNFPDDAKKRAERILQACGGHSL
GAYSVSSGIQLIREDVARYIERRDGGIPADPNNVFLSTGASDAIVTVLKLLVAGEGHTRT
GVLIPIPQYPLYSATLAELGAVQVDYYLDEERAWALDVAELHRALGQARDHCRPRALCVI
NPGNPTGQVQTRECIEAVIRFAFEERLFLLADEVYQDNVYAAGSQFHSFKKVLMEMGPPY
AGQQELASFHSTSKGYMGECGFRGGYVEVVNMDAAVQQQMLKLMSVRLCPPVPGQALLDL
VVSPPAPTDPSFAQFQAEKQAVLAELAAKAKLTEQVFNEAPGISCNPVQGAMYSFPRVQL
PPRAVERAQELGLAPDMFFCLRLLEETGICVVPGSGFGQREGTYHFRMTILPPLEKLRLL
LEKLSRFHAKFTLEYS
|
| Enzyme 51 Number of Residues |
496 |
| Enzyme 51 Molecular Weight |
54637 |
| Enzyme 51 Theoretical pI |
Not Available |
| Enzyme 51 GO Classification |
Not Available |
| Enzyme 51 General Function |
Not Available |
| Enzyme 51 Specific Function |
Not Available |
| Enzyme 51 Pathways |
Not Available |
| Enzyme 51 Reactions |
Not Available |
| Enzyme 51 Pfam Domain Function |
Not Available |
| Enzyme 51 Signals |
|
| Enzyme 51 Transmembrane Regions |
|
| Enzyme 51 Essentiality |
Not Available |
| Enzyme 51 GenBank ID Protein |
Not Available |
| Enzyme 51 UniProtKB/Swiss-Prot ID |
B0YJ18  |
| Enzyme 51 UniProtKB/Swiss-Prot Entry Name |
B0YJ18_HUMAN  |
| Enzyme 51 PDB ID |
Not Available |
| Enzyme 51 Cellular Location |
Not Available |
| Enzyme 51 Gene Sequence |
Not Available |
| Enzyme 51 GenBank Gene ID |
Not Available |
| Enzyme 51 GeneCard ID |
B0YJ18  |
| Enzyme 51 GenAtlas ID |
Not Available |
| Enzyme 51 HGNC ID |
Not Available |
| Enzyme 51 Chromosome Location |
Not Available |
| Enzyme 51 Locus |
Not Available |
| Enzyme 51 SNPs |
SNPJam Report  |
| Enzyme 51 General References |
Not Available |
| Enzyme 51 Metabolite References |
Not Available |
|
Enzyme 52
[top]
|
| Enzyme 52 ID |
13019 |
| Enzyme 52 Name |
cDNA FLJ75824, highly similar to Homo sapiens serine dehydratase |
| Enzyme 52 Synonyms |
- SDS, mRNA
- Serine dehydratase, isoform CRA_a
|
| Enzyme 52 Gene Name |
SDS |
| Enzyme 52 Protein Sequence |
>cDNA FLJ75824, highly similar to Homo sapiens serine dehydratase
MMSGEPLHVKTPIRDSMALSKMAGTSVYLKMDSAQPSGSFKIRGIGHFCKRWAKQGCAHF
VCSSAGNAGMAAAYAARQLGVPATIVVPSTTPALTIERLKNEGATVKVVGELLDEAFELA
KALAKNNPGWVYIPPFDDPLIWEGHASIVKELKETLWEKPGAIALSVGGGGLLCGVVQGL
QEVGWGDVPVIAMETFGAHSFHAATTAGKLVSLPKITSVAKALGVKTVGAQALKLFQEHP
IFSEVISDQEAVAAIEKFVDDEKILVEPACGAALAAVYSHVIQKLQLEGNLRTPLPSLVV
IVCGGSNISLAQLRALKEQLGMTNRLPK
|
| Enzyme 52 Number of Residues |
328 |
| Enzyme 52 Molecular Weight |
34626 |
| Enzyme 52 Theoretical pI |
8.14 |
| Enzyme 52 GO Classification |
Not Available |
| Enzyme 52 General Function |
Amino acid transport and metabolism |
| Enzyme 52 Specific Function |
Not Available |
| Enzyme 52 Pathways |
Not Available |
| Enzyme 52 Reactions |
Not Available |
| Enzyme 52 Pfam Domain Function |
Not Available |
| Enzyme 52 Signals |
|
| Enzyme 52 Transmembrane Regions |
|
| Enzyme 52 Essentiality |
Not Available |
| Enzyme 52 GenBank ID Protein |
158258957  |
| Enzyme 52 UniProtKB/Swiss-Prot ID |
A8K9P5  |
| Enzyme 52 UniProtKB/Swiss-Prot Entry Name |
A8K9P5_HUMAN  |
| Enzyme 52 PDB ID |
1P5J  |
| Enzyme 52 PDB File |
Show |
| Enzyme 52 3D Structure |
|
| Enzyme 52 Cellular Location |
Not Available |
| Enzyme 52 Gene Sequence |
Not Available |
| Enzyme 52 GenBank Gene ID |
AK292760  |
| Enzyme 52 GeneCard ID |
A8K9P5  |
| Enzyme 52 GenAtlas ID |
Not Available |
| Enzyme 52 HGNC ID |
Not Available |
| Enzyme 52 Chromosome Location |
Not Available |
| Enzyme 52 Locus |
Not Available |
| Enzyme 52 SNPs |
SNPJam Report  |
| Enzyme 52 General References |
Not Available |
| Enzyme 52 Metabolite References |
Not Available |
|
Enzyme 53
[top]
|
| Enzyme 53 ID |
13053 |
| Enzyme 53 Name |
Phosphoserine aminotransferase 1 |
| Enzyme 53 Synonyms |
- Phosphoserine aminotransferase 1, isoform CRA_a
|
| Enzyme 53 Gene Name |
PSAT1 |
| Enzyme 53 Protein Sequence |
>Phosphoserine aminotransferase 1
MDAPRQVVNFGPGPAKLPHSVLLEIQKELLDYKGVGISVLEMSHRSSDFAKIINNTENLV
RELLAVPDNYKVIFLQGGGCGQFSAVPLNLIGLKAGRCADYVVTGAWSAKAAEEAKKFGT
INIVHPKLGSYTKIPDPSTWNLNPDASYVYYCANETVHGVEFDFIPDVKGAVLVCDMSSN
FLSKPVDVSKFGVIFAGAQKNVGSAGVTVVIVRDDLLGFALRECPSVLEYKVQAGNSSLY
NTPPCFSIYVMGLVLEWIKNNGGAAAMEKLSSIKSQTIYEIIDNSQGFYVSVGGIRASLY
NAVTIEDVQKLAAFMKKFLEMHQL
|
| Enzyme 53 Number of Residues |
324 |
| Enzyme 53 Molecular Weight |
35189 |
| Enzyme 53 Theoretical pI |
6.66 |
| Enzyme 53 GO Classification |
| Function |
- catalytic activity
- transaminase activity
- transferase activity
- transferase activity, transferring nitrogenous groups
|
| Process |
- L-serine biosynthesis
- L-serine metabolism
- amino acid and derivative metabolism
- amino acid metabolism
- cellular metabolism
- metabolism
- physiological process
- serine family amino acid metabolism
|
| Component |
| — |
|
| Enzyme 53 General Function |
Coenzyme transport and metabolism |
| Enzyme 53 Specific Function |
Not Available |
| Enzyme 53 Pathways |
Not Available |
| Enzyme 53 Reactions |
Not Available |
| Enzyme 53 Pfam Domain Function |
|
| Enzyme 53 Signals |
|
| Enzyme 53 Transmembrane Regions |
|
| Enzyme 53 Essentiality |
Not Available |
| Enzyme 53 GenBank ID Protein |
Not Available |
| Enzyme 53 UniProtKB/Swiss-Prot ID |
Q5T7G5  |
| Enzyme 53 UniProtKB/Swiss-Prot Entry Name |
Q5T7G5_HUMAN  |
| Enzyme 53 PDB ID |
Not Available |
| Enzyme 53 Cellular Location |
Not Available |
| Enzyme 53 Gene Sequence |
Not Available |
| Enzyme 53 GenBank Gene ID |
AL353594  |
| Enzyme 53 GeneCard ID |
Q5T7G5  |
| Enzyme 53 GenAtlas ID |
PSAT1  |
| Enzyme 53 HGNC ID |
HGNC:19129  |
| Enzyme 53 Chromosome Location |
Not Available |
| Enzyme 53 Locus |
Not Available |
| Enzyme 53 SNPs |
SNPJam Report  |
| Enzyme 53 General References |
Not Available |
| Enzyme 53 Metabolite References |
Not Available |
|
Enzyme 54
[top]
|
| Enzyme 54 ID |
13054 |
| Enzyme 54 Name |
Phosphatidylserine decarboxylase |
| Enzyme 54 Synonyms |
- SubName: Phosphatidylserine decarboxylase, isoform CRA_a
|
| Enzyme 54 Gene Name |
PISD |
| Enzyme 54 Protein Sequence |
>Phosphatidylserine decarboxylase
MMCQSEARQGPELRAAKWLHFPQLALRRRLGQLSCMSRPALKLRSWPLTVLYYLLPFGAL
RPLSRVGWRPVSRVALYKSVPTRLLSRAWGRLNQVELPHWLRRPVYSLYIWTFGVNMKEA
AVEDLHHYRNLSEFFRRKLKPQARPVCGLHSVISPSDGRILNFGQVKNCEVEQVKGVTYS
LESFLGPRMCTEDLPFPPAASCDSFKNQLVTREGNELYHCVIYLAPGDYHCFHSPTDWTV
SHRRHFPGSLMSVNPGMARWIKELFCHNERVVLTGDWKHGFFSLTAVGATNVGSIRIYFD
RDLHTNSPRHSKGSYNDFSFVTHTNREGVPMRKGEHLGEFNLGSTIVLIFEAPKDFNFQL
KTGQKIRFGEALGSL
|
| Enzyme 54 Number of Residues |
375 |
| Enzyme 54 Molecular Weight |
43046.3 |
| Enzyme 54 Theoretical pI |
10.14 |
| Enzyme 54 GO Classification |
| Function |
- carbon-carbon lyase activity
- carboxy-lyase activity
- catalytic activity
- lyase activity
- phosphatidylserine decarboxylase activity
|
| Process |
- metabolic process
- organophosphate metabolic process
- phospholipid biosynthetic process
- phospholipid metabolic process
|
| Component |
| — |
|
| Enzyme 54 General Function |
Involved in phosphatidylserine decarboxylase activity |
| Enzyme 54 Specific Function |
Not Available |
| Enzyme 54 Pathways |
Not Available |
| Enzyme 54 Reactions |
Not Available |
| Enzyme 54 Pfam Domain Function |
|
| Enzyme 54 Signals |
|
| Enzyme 54 Transmembrane Regions |
|
| Enzyme 54 Essentiality |
Not Available |
| Enzyme 54 GenBank ID Protein |
5921491  |
| Enzyme 54 UniProtKB/Swiss-Prot ID |
B1AKM7  |
| Enzyme 54 UniProtKB/Swiss-Prot Entry Name |
B1AKM7_HUMAN  |
| Enzyme 54 PDB ID |
Not Available |
| Enzyme 54 Cellular Location |
Not Available |
| Enzyme 54 Gene Sequence |
>1128 bp
ATGATGTGTCAGTCAGAGGCGCGGCAAGGACCAGAGCTCCGCGCGGCGAAATGGTTGCAC
TTCCCCCAGCTGGCCCTGAGGCGGAGGCTGGGGCAGCTGAGCTGCATGTCCAGACCCGCT
CTGAAACTGCGCTCCTGGCCCTTGACCGTCCTCTACTACCTCCTGCCCTTCGGCGCCCTC
AGACCGCTCAGCCGGGTGGGATGGAGGCCCGTAAGCAGGGTGGCTTTGTACAAGTCAGTG
CCAACGCGCTTGCTGTCACGGGCCTGGGGTCGCCTCAATCAGGTGGAGCTGCCACACTGG
CTGCGCAGGCCCGTCTACAGCCTGTACATCTGGACGTTTGGGGTGAACATGAAAGAGGCC
GCTGTGGAGGACCTGCATCACTACCGCAACCTCAGCGAGTTCTTCCGGCGCAAGCTGAAG
CCGCAGGCCCGGCCTGTCTGTGGCCTGCACAGCGTGATTAGCCCATCGGATGGAAGGATC
CTCAACTTTGGGCAGGTGAAGAACTGTGAGGTGGAGCAGGTAAAGGGGGTCACCTACTCC
CTGGAGTCGTTCCTGGGCCCGCGTATGTGCACAGAGGACCTGCCCTTCCCACCAGCCGCG
TCGTGTGACTCCTTCAAGAACCAGCTGGTCACCCGGGAAGGGAATGAGCTCTATCACTGT
GTCATCTACCTGGCCCCTGGGGACTACCACTGCTTCCACTCCCCCACCGACTGGACTGTG
TCCCACCGGCGCCACTTCCCAGGCTCCCTGATGTCAGTGAACCCTGGCATGGCTCGCTGG
ATCAAAGAGCTCTTCTGCCATAACGAGCGGGTGGTCCTGACGGGGGACTGGAAACATGGC
TTCTTCTCACTGACAGCTGTGGGGGCCACCAACGTGGGCTCCATTCGCATCTACTTTGAC
CGGGACCTGCACACAAACAGCCCAAGGCACAGCAAGGGCTCCTACAATGACTTCAGCTTC
GTGACGCACACCAATAGAGAGGGCGTCCCCATGCGTAAGGGCGAGCACCTGGGCGAGTTC
AACCTGGGCTCCACCATCGTGCTCATCTTCGAGGCCCCCAAGGACTTCAATTTCCAGCTG
AAAACAGGACAGAAAATCCGCTTTGGGGAAGCCCTGGGCTCGCTCTAG
|
| Enzyme 54 GenBank Gene ID |
AL096768  |
| Enzyme 54 GeneCard ID |
PISD  |
| Enzyme 54 GenAtlas ID |
PISD  |
| Enzyme 54 HGNC ID |
HGNC:8999  |
| Enzyme 54 Chromosome Location |
2 |
| Enzyme 54 Locus |
22q12.2 |
| Enzyme 54 SNPs |
SNPJam Report  |
| Enzyme 54 General References |
Not Available |
| Enzyme 54 Metabolite References |
Not Available |
|
Enzyme 55
[top]
|
| Enzyme 55 ID |
13055 |
| Enzyme 55 Name |
Glycine dehydrogenase |
| Enzyme 55 Synonyms |
- Decarboxylating
- Glycine dehydrogenase
- Decarboxylating
- glycine decarboxylase, glycine cleavage system protein P, isoform CRA_b
|
| Enzyme 55 Gene Name |
GLDC |
| Enzyme 55 Protein Sequence |
>Glycine dehydrogenase
MQSCARAWGLRLGRGVGGGRRLAGGSGPCWAPRSRDSSSGGGDSAAAGASRLLERLLPRH
DDFARRHIGPGDKDQREMLQTLGLASIDELIEKTVPANIRLKRPLKMEDPVCENEILATL
HAISSKNQIWRSYIGMGYYNCSVPQTILRNLLENSGWITQYTPYQPEVSQGRLESLLNYQ
TMVCDITGLDMANASLLDEGTAAAEALQLCYRHNKRRKFLVDPRCHPQTIAVVQTRAKYT
GVLTELKLPCEMDFSGKDVSGVLFQYPDTEGKVEDFTELVERAHQSGSLACCATDLLALC
ILRPPGEFGVDIALGSSQRFGVPLGYGGPHAAFFAVRESLVRMMPGRMVGVTRDATGKEV
YRLALQTREQHIRRDKATSNICTAQALLANMAAMFAIYHGSHGLEHIARRVHNATLILSE
GLKRAGHQLQHDLFFDTLKIQCGCSVKEVLGRAAQRQINFRLFEDGTLGISLDETVNEKD
LDDLLWIFGCESSAELVAESMGEECRGIPGSVFKRTSPFLTHQVFNSYHSETNIVRYMKK
LENKDISLVHSMIPLGSCTMKLNSSSELAPITWKEFANIHPFVPLDQAQGYQQLFRELEK
DLCELTGYDQVCFQPNSGAQGEYAGLATIRAYLNQKGEGHRTVCLIPKSAHGTNPASAHM
AGMKIQPVEVDKYGNIDAVHLKAMVDKHKENLAAIMITYPSTNGVFEENISDVCDLIHQH
GGQVYLDGANMNAQVGICRPGDFGSDVSHLNLHKTFCIPHGGGGPGMGPIGVKKHLAPFL
PNHPVISLKRNEDACPVGTVSAAPWGSSSILPISWAYIKMMGGKGLKQATETAILNANYM
AKRLETHYRILFRGARGYVGHEFILDTRPFKKSANIEAVDVAKRLQDYGFHAPTMSWPVA
GTLMVEPTESEDKAELDRFCDAMISIRQEIADIEEGRIDPRVNPLKMSPHSLTCVTSSHW
DRPYSREVAAFPLPFVKPENKFWPTIARIDDIYGDQHLVCTCPPMEVYESPFSEQKRASS
|
| Enzyme 55 Number of Residues |
1020 |
| Enzyme 55 Molecular Weight |
112731 |
| Enzyme 55 Theoretical pI |
7.11 |
| Enzyme 55 GO Classification |
| Function |
- catalytic activity
- glycine dehydrogenase (decarboxylating) activity
- oxidoreductase activity
- oxidoreductase activity, acting on the CH-NH2 group of donors
- oxidoreductase activity, acting on the CH-NH2 group of donors, disulfide as acceptor
|
| Process |
- amino acid and derivative metabolism
- amino acid metabolism
- cellular metabolism
- glycine metabolism
- metabolism
- physiological process
- serine family amino acid metabolism
|
| Component |
- glycine dehydrogenase complex (decarboxylating)
- protein complex
|
|
| Enzyme 55 General Function |
Amino acid transport and metabolism |
| Enzyme 55 Specific Function |
Not Available |
| Enzyme 55 Pathways |
Not Available |
| Enzyme 55 Reactions |
Not Available |
| Enzyme 55 Pfam Domain Function |
|
| Enzyme 55 Signals |
|
| Enzyme 55 Transmembrane Regions |
|
| Enzyme 55 Essentiality |
Not Available |
| Enzyme 55 GenBank ID Protein |
85566653  |
| Enzyme 55 UniProtKB/Swiss-Prot ID |
Q2M2F8  |
| Enzyme 55 UniProtKB/Swiss-Prot Entry Name |
Q2M2F8_HUMAN  |
| Enzyme 55 PDB ID |
Not Available |
| Enzyme 55 Cellular Location |
Not Available |
| Enzyme 55 Gene Sequence |
Not Available |
| Enzyme 55 GenBank Gene ID |
BC111993  |
| Enzyme 55 GeneCard ID |
Q2M2F8  |
| Enzyme 55 GenAtlas ID |
GLDC  |
| Enzyme 55 HGNC ID |
HGNC:4313  |
| Enzyme 55 Chromosome Location |
Not Available |
| Enzyme 55 Locus |
Not Available |
| Enzyme 55 SNPs |
SNPJam Report  |
| Enzyme 55 General References |
- Strausberg RL, Feingold EA, Grouse LH, Derge JG, Klausner RD, Collins FS, Wagner L, Shenmen CM, Schuler GD, Altschul SF, Zeeberg B, Buetow KH, Schaefer CF, Bhat NK, Hopkins RF, Jordan H, Moore T, Max SI, Wang J, Hsieh F, Diatchenko L, Marusina K, Farmer AA, Rubin GM, Hong L, Stapleton M, Soares MB, Bonaldo MF, Casavant TL, Scheetz TE, Brownstein MJ, Usdin TB, Toshiyuki S, Carninci P, Prange C, Raha SS, Loquellano NA, Peters GJ, Abramson RD, Mullahy SJ, Bosak SA, McEwan PJ, McKernan KJ, Malek JA, Gunaratne PH, Richards S, Worley KC, Hale S, Garcia AM, Gay LJ, Hulyk SW, Villalon DK, Muzny DM, Sodergren EJ, Lu X, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madan A, Young AC, Shevchenko Y, Bouffard GG, Blakesley RW, Touchman JW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Krzywinski MI, Skalska U, Smailus DE, Schnerch A, Schein JE, Jones SJ, Marra MA: Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. Proc Natl Acad Sci U S A. 2002 Dec 24;99(26):16899-903. Epub 2002 Dec 11. [PubMed
]
|
| Enzyme 55 Metabolite References |
Not Available |
|
Enzyme 56
[top]
|
| Enzyme 56 ID |
13103 |
| Enzyme 56 Name |
cDNA FLJ75707, highly similar to Homo sapiens serine palmitoyltransferase, long chain base subunit 1 |
| Enzyme 56 Synonyms |
- SPTLC1, transcript variant 1, mRNA
- Serine palmitoyltransferase, long chain base subunit 1, isoform CRA_a
|
| Enzyme 56 Gene Name |
SPTLC1 |
| Enzyme 56 Protein Sequence |
>cDNA FLJ75707, highly similar to Homo sapiens serine palmitoyltransferase, long chain base subunit 1
MATATEQWVLVEMVQALYEAPAYHLILEGILILWIIRLLFSKTYKLQERSDLTVKEKEEL
IEEWQPEPLVPPVPKDHPALNYNIVSGPPSHKTVVNGKECINFASFNFLGLLDNPRVKAA
ALASLKKYGVGTCGPRGFYGTFDVHLDLEDRLAKFMKTEEAIIYSYGFATIASAIPAYSK
RGDIVFVDRAACFAIQKGLQASRSDIKLFKHNDMADLERLLKEQEIEDQKNPRKARVTRR
FIVVEGLYMNTGTICPLPELVKLKYKYKARIFLEESLSFGVLGEHGRGVTEHYGINIDDI
DLISANMENALASIGGFCCGRSFVIDHQRLSGQGYCFSASLPPLLAAAAIEALNIMEENP
GIFAVLKEKCGQIHKALQGISGLKVVGESLSPAFHLQLEESTGSREQDVRLLQEIVDQCM
NRSIALTQARYLEKEEKCLPPPSIRVVVTVEQTEEELERAASTIKEVAQAVLL
|
| Enzyme 56 Number of Residues |
473 |
| Enzyme 56 Molecular Weight |
52745 |
| Enzyme 56 Theoretical pI |
5.87 |
| Enzyme 56 GO Classification |
Not Available |
| Enzyme 56 General Function |
Coenzyme transport and metabolism |
| Enzyme 56 Specific Function |
Not Available |
| Enzyme 56 Pathways |
Not Available |
| Enzyme 56 Reactions |
Not Available |
| Enzyme 56 Pfam Domain Function |
Not Available |
| Enzyme 56 Signals |
|
| Enzyme 56 Transmembrane Regions |
|
| Enzyme 56 Essentiality |
Not Available |
| Enzyme 56 GenBank ID Protein |
158256524  |
| Enzyme 56 UniProtKB/Swiss-Prot ID |
A8K681  |
| Enzyme 56 UniProtKB/Swiss-Prot Entry Name |
A8K681_HUMAN  |
| Enzyme 56 PDB ID |
Not Available |
| Enzyme 56 Cellular Location |
Not Available |
| Enzyme 56 Gene Sequence |
Not Available |
| Enzyme 56 GenBank Gene ID |
AK291546  |
| Enzyme 56 GeneCard ID |
A8K681  |
| Enzyme 56 GenAtlas ID |
Not Available |
| Enzyme 56 HGNC ID |
Not Available |
| Enzyme 56 Chromosome Location |
Not Available |
| Enzyme 56 Locus |
Not Available |
| Enzyme 56 SNPs |
SNPJam Report  |
| Enzyme 56 General References |
Not Available |
| Enzyme 56 Metabolite References |
Not Available |
|
Enzyme 57
[top]
|
| Enzyme 57 ID |
13118 |
| Enzyme 57 Name |
Kynureninase (L-kynurenine hydrolase) |
| Enzyme 57 Synonyms |
- SubName: Kynureninase (L-kynurenine hydrolase), isoform CRA_a
|
| Enzyme 57 Gene Name |
KYNU |
| Enzyme 57 Protein Sequence |
>Kynureninase (L-kynurenine hydrolase)
MEPSSLELPADTVQRIAAELKCHPTDERVALHLDEEDKLRHFRECFYIPKIQDLPPVDLS
LVNKDENAIYFLGNSLGLQPKMVKTYLEEELDKWAKIAAYGHEVGKRPWITGDESIVGLM
KDIVGANEKEIALMNALTVNLHLLMLSFFKPTPKRYKILLEAKAFPSDHYAIESQLQLHG
LNIEESMRMIKPREGEETLRIEDILEVIEKEGDSIAVILFSGVHFYTGQHFNIPAITKAG
QAKGCYVGFDLAHAVGNVELYLHDWGVDFACWCSYKYLNAGAGGIAGAFIHEKHAHTIKP
ARSEFFN
|
| Enzyme 57 Number of Residues |
307 |
| Enzyme 57 Molecular Weight |
34634.5 |
| Enzyme 57 Theoretical pI |
5.71 |
| Enzyme 57 GO Classification |
| Function |
- binding
- catalytic activity
- cofactor binding
- hydrolase activity
- hydrolase activity, acting on acid carbon-carbon bonds
- hydrolase activity, acting on acid carbon-carbon bonds, in ketonic substances
- kynureninase activity
- pyridoxal phosphate binding
|
| Process |
- NAD biosynthetic process
- cellular amino acid and derivative metabolic process
- cellular amino acid derivative metabolic process
- cellular biogenic amine metabolic process
- cellular metabolic process
- coenzyme biosynthetic process
- coenzyme metabolic process
- cofactor metabolic process
- indolalkylamine metabolic process
- metabolic process
- nicotinamide nucleotide biosynthetic process
- pyridine nucleotide biosynthetic process
- tryptophan catabolic process
- tryptophan metabolic process
|
| Component |
- cell part
- cytoplasm
- intracellular part
|
|
| Enzyme 57 General Function |
Involved in metabolic process |
| Enzyme 57 Specific Function |
Not Available |
| Enzyme 57 Pathways |
Not Available |
| Enzyme 57 Reactions |
Not Available |
| Enzyme 57 Pfam Domain Function |
|
| Enzyme 57 Signals |
|
| Enzyme 57 Transmembrane Regions |
|
| Enzyme 57 Essentiality |
Not Available |
| Enzyme 57 GenBank ID Protein |
12654129  |
| Enzyme 57 UniProtKB/Swiss-Prot ID |
Q9BVW3  |
| Enzyme 57 UniProtKB/Swiss-Prot Entry Name |
Q9BVW3_HUMAN  |
| Enzyme 57 PDB ID |
Not Available |
| Enzyme 57 Cellular Location |
Not Available |
| Enzyme 57 Gene Sequence |
>924 bp
ATGGAGCCTTCATCTCTTGAGCTGCCGGCTGACACAGTGCAGCGCATTGCGGCTGAACTC
AAATGCCACCCAACGGATGAGAGGGTGGCTCTCCACCTAGATGAGGAAGATAAGCTGAGG
CACTTCAGGGAGTGCTTTTATATTCCCAAAATACAGGATCTGCCTCCAGTTGATTTATCA
TTAGTGAATAAAGATGAAAATGCCATCTATTTCTTGGGAAATTCTCTTGGCCTTCAACCA
AAAATGGTTAAAACATATCTTGAAGAAGAACTAGATAAGTGGGCCAAAATAGCAGCCTAT
GGTCATGAAGTGGGGAAGCGTCCTTGGATTACAGGAGATGAGAGTATTGTAGGCCTTATG
AAGGACATTGTAGGAGCCAATGAGAAAGAAATAGCCCTAATGAATGCTTTGACTGTAAAT
TTACATCTTCTAATGTTATCATTTTTTAAGCCTACGCCAAAACGATATAAAATTCTTCTA
GAAGCCAAAGCCTTCCCTTCTGATCATTATGCTATTGAGTCACAACTACAACTTCACGGA
CTTAACATTGAAGAAAGTATGCGGATGATAAAGCCAAGAGAGGGGGAAGAAACCTTAAGA
ATAGAGGATATCCTTGAAGTAATTGAGAAGGAAGGAGACTCAATTGCAGTGATCCTGTTC
AGTGGGGTGCATTTTTACACTGGACAGCACTTTAATATTCCTGCCATCACAAAAGCTGGA
CAAGCGAAGGGTTGTTATGTTGGCTTTGATCTAGCACATGCAGTTGGAAATGTTGAACTC
TACTTACATGACTGGGGAGTTGATTTTGCCTGCTGGTGTTCCTACAAGTATTTAAATGCA
GGAGCAGGAGGAATTGCTGGTGCCTTCATTCATGAAAAGCATGCCCATACGATTAAACCT
GCGAGATCGGAGTTCTTTAATTAG
|
| Enzyme 57 GenBank Gene ID |
BC000879  |
| Enzyme 57 GeneCard ID |
KYNU  |
| Enzyme 57 GenAtlas ID |
KYNU  |
| Enzyme 57 HGNC ID |
HGNC:6469  |
| Enzyme 57 Chromosome Location |
2 |
| Enzyme 57 Locus |
2q22.2 |
| Enzyme 57 SNPs |
SNPJam Report  |
| Enzyme 57 General References |
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Venter JC, Adams MD, Myers EW, Li PW, Mural RJ, Sutton GG, Smith HO, Yandell M, Evans CA, Holt RA, Gocayne JD, Amanatides P, Ballew RM, Huson DH, Wortman JR, Zhang Q, Kodira CD, Zheng XH, Chen L, Skupski M, Subramanian G, Thomas PD, Zhang J, Gabor Miklos GL, Nelson C, Broder S, Clark AG, Nadeau J, McKusick VA, Zinder N, Levine AJ, Roberts RJ, Simon M, Slayman C, Hunkapiller M, Bolanos R, Delcher A, Dew I, Fasulo D, Flanigan M, Florea L, Halpern A, Hannenhalli S, Kravitz S, Levy S, Mobarry C, Reinert K, Remington K, Abu-Threideh J, Beasley E, Biddick K, Bonazzi V, Brandon R, Cargill M, Chandramouliswaran I, Charlab R, Chaturvedi K, Deng Z, Di Francesco V, Dunn P, Eilbeck K, Evangelista C, Gabrielian AE, Gan W, Ge W, Gong F, Gu Z, Guan P, Heiman TJ, Higgins ME, Ji RR, Ke Z, Ketchum KA, Lai Z, Lei Y, Li Z, Li J, Liang Y, Lin X, Lu F, Merkulov GV, Milshina N, Moore HM, Naik AK, Narayan VA, Neelam B, Nusskern D, Rusch DB, Salzberg S, Shao W, Shue B, Sun J, Wang Z, Wang A, Wang X, Wang J, Wei M, Wides R, Xiao C, Yan C, Yao A, Ye J, Zhan M, Zhang W, Zhang H, Zhao Q, Zheng L, Zhong F, Zhong W, Zhu S, Zhao S, Gilbert D, Baumhueter S, Spier G, Carter C, Cravchik A, Woodage T, Ali F, An H, Awe A, Baldwin D, Baden H, Barnstead M, Barrow I, Beeson K, Busam D, Carver A, Center A, Cheng ML, Curry L, Danaher S, Davenport L, Desilets R, Dietz S, Dodson K, Doup L, Ferriera S, Garg N, Gluecksmann A, Hart B, Haynes J, Haynes C, Heiner C, Hladun S, Hostin D, Houck J, Howland T, Ibegwam C, Johnson J, Kalush F, Kline L, Koduru S, Love A, Mann F, May D, McCawley S, McIntosh T, McMullen I, Moy M, Moy L, Murphy B, Nelson K, Pfannkoch C, Pratts E, Puri V, Qureshi H, Reardon M, Rodriguez R, Rogers YH, Romblad D, Ruhfel B, Scott R, Sitter C, Smallwood M, Stewart E, Strong R, Suh E, Thomas R, Tint NN, Tse S, Vech C, Wang G, Wetter J, Williams S, Williams M, Windsor S, Winn-Deen E, Wolfe K, Zaveri J, Zaveri K, Abril JF, Guigo R, Campbell MJ, Sjolander KV, Karlak B, Kejariwal A, Mi H, Lazareva B, Hatton T, Narechania A, Diemer K, Muruganujan A, Guo N, Sato S, Bafna V, Istrail S, Lippert R, Schwartz R, Walenz B, Yooseph S, Allen D, Basu A, Baxendale J, Blick L, Caminha M, Carnes-Stine J, Caulk P, Chiang YH, Coyne M, Dahlke C, Mays A, Dombroski M, Donnelly M, Ely D, Esparham S, Fosler C, Gire H, Glanowski S, Glasser K, Glodek A, Gorokhov M, Graham K, Gropman B, Harris M, Heil J, Henderson S, Hoover J, Jennings D, Jordan C, Jordan J, Kasha J, Kagan L, Kraft C, Levitsky A, Lewis M, Liu X, Lopez J, Ma D, Majoros W, McDaniel J, Murphy S, Newman M, Nguyen T, Nguyen N, Nodell M, Pan S, Peck J, Peterson M, Rowe W, Sanders R, Scott J, Simpson M, Smith T, Sprague A, Stockwell T, Turner R, Venter E, Wang M, Wen M, Wu D, Wu M, Xia A, Zandieh A, Zhu X: The sequence of the human genome. Science. 2001 Feb 16;291(5507):1304-51. [PubMed
]
|
| Enzyme 57 Metabolite References |
Not Available |
|
Enzyme 58
[top]
|
| Enzyme 58 ID |
13123 |
| Enzyme 58 Name |
cDNA, FLJ96771, Homo sapiens ornithine decarboxylase-like protein (ODC-p), mRNA (Arginine decarboxylase, isoform CRA_d) |
| Enzyme 58 Synonyms |
Not Available |
| Enzyme 58 Gene Name |
ADC |
| Enzyme 58 Protein Sequence |
>cDNA, FLJ96771, Homo sapiens ornithine decarboxylase-like protein (ODC-p)
MAGYLSESDFVMVEEGFSTRDLLKELTLGASQATTDEVAAFFVADLGAIVRKHFCFLKCL
PRVRPFYAVKCNSSPGVLKVLAQLGLGFSCANKAEMELVQHIGIPASKIICANPCKQIAQ
IKYAAKHGIQLLSFDNEMELAKVVKSHPSAKMVLCIATDDSHSLSCLSLKFGVSLKSCRH
LLENAKKHHVEVVGVSFHIGSGCPDPQAYAQSIADARLVFEMGTELGHKMHVLDLGGGFP
GTEGAKVRFEEIASVINSALDLYFPEGCGVDIFAELGRYYVTSAFTVAVSIIAKKEVLLD
QPGREEENGSTSKTIVYHLDEGVYGIFNSVLFDNICPTPILQKKPSTEQPLYSSSLWGPA
VDGCDCVAEGLWLPQLHVGDWLVFDNMGAYTVGMGSPFWGTQACHITYAMSRVAWEALRR
QLMAAEQEDDVEGVCKPLSCGWEITDTLCVGPVFTPASIM
|
| Enzyme 58 Number of Residues |
460 |
| Enzyme 58 Molecular Weight |
49980 |
| Enzyme 58 Theoretical pI |
Not Available |
| Enzyme 58 GO Classification |
Not Available |
| Enzyme 58 General Function |
Not Available |
| Enzyme 58 Specific Function |
Not Available |
| Enzyme 58 Pathways |
Not Available |
| Enzyme 58 Reactions |
Not Available |
| Enzyme 58 Pfam Domain Function |
Not Available |
| Enzyme 58 Signals |
|
| Enzyme 58 Transmembrane Regions |
|
| Enzyme 58 Essentiality |
Not Available |
| Enzyme 58 GenBank ID Protein |
Not Available |
| Enzyme 58 UniProtKB/Swiss-Prot ID |
B2RDU5  |
| Enzyme 58 UniProtKB/Swiss-Prot Entry Name |
B2RDU5_HUMAN  |
| Enzyme 58 PDB ID |
Not Available |
| Enzyme 58 Cellular Location |
Not Available |
| Enzyme 58 Gene Sequence |
Not Available |
| Enzyme 58 GenBank Gene ID |
Not Available |
| Enzyme 58 GeneCard ID |
B2RDU5  |
| Enzyme 58 GenAtlas ID |
Not Available |
| Enzyme 58 HGNC ID |
Not Available |
| Enzyme 58 Chromosome Location |
Not Available |
| Enzyme 58 Locus |
Not Available |
| Enzyme 58 SNPs |
SNPJam Report  |
| Enzyme 58 General References |
Not Available |
| Enzyme 58 Metabolite References |
Not Available |
|
Enzyme 59
[top]
|
| Enzyme 59 ID |
14513 |
| Enzyme 59 Name |
Pyridoxal phosphate phosphatase PHOSPHO2 |
| Enzyme 59 Synonyms |
Not Available |
| Enzyme 59 Gene Name |
PHOSPHO2 |
| Enzyme 59 Protein Sequence |
>Pyridoxal phosphate phosphatase PHOSPHO2
MKILLVFDFDNTIIDDNSDTWIVQCAPNKKLPIELRDSYRKGFWTEFMGRVFKYLGDKGV
REHEMKRAVTSLPFTPGMVELFNFIRKNKDKFDCIIISDSNSVFIDWVLEAASFHDIFDK
VFTNPAAFNSNGHLTVENYHTHSCNRCPKNLCKKVVLIEFVDKQLQQGVNYTQIVYIGDG
GNDVCPVTFLKNDDVAMPRKGYTLQKTLSRMSQNLEPMEYSVVVWSSGVDIISHLQFLIK
D
|
| Enzyme 59 Number of Residues |
241 |
| Enzyme 59 Molecular Weight |
27768.7 |
| Enzyme 59 Theoretical pI |
6.78 |
| Enzyme 59 GO Classification |
| Function |
- catalytic activity
- hydrolase activity
- hydrolase activity, acting on ester bonds
- phosphatase activity
- phosphoric ester hydrolase activity
|
| Process |
|
| Component |
| — |
|
| Enzyme 59 General Function |
Involved in phosphatase activity |
| Enzyme 59 Specific Function |
Phosphatase that has high activity toward pyridoxal 5'- phosphate (PLP). Also active at much lower level toward pyrophosphate, phosphoethanolamine (PEA), phosphocholine (PCho), phospho-l-tyrosine, fructose-6-phosphate, p-nitrophenyl phosphate, and h-glycerophosphate |
| Enzyme 59 Pathways |
|
| Enzyme 59 Reactions |
- pyridoxal 5'-phosphate + H2O = pyridoxal + phosphate [RN:R00173]
|
| Enzyme 59 Pfam Domain Function |
|
| Enzyme 59 Signals |
|
| Enzyme 59 Transmembrane Regions |
|
| Enzyme 59 Essentiality |
Not Available |
| Enzyme 59 GenBank ID Protein |
56606064  |
| Enzyme 59 UniProtKB/Swiss-Prot ID |
Q8TCD6  |
| Enzyme 59 UniProtKB/Swiss-Prot Entry Name |
PHOP2_HUMAN  |
| Enzyme 59 PDB ID |
Not Available |
| Enzyme 59 Cellular Location |
Not Available |
| Enzyme 59 Gene Sequence |
>726 bp
ATGAAAATTTTGCTAGTTTTTGACTTTGACAATACAATCATAGATGACAATAGTGACACT
TGGATTGTACAATGTGCTCCCAACAAAAAGCTTCCTATTGAACTACGTGATTCTTATCGA
AAAGGATTTTGGACAGAATTTATGGGCAGAGTCTTTAAGTATTTGGGAGATAAGGGTGTA
AGAGAACATGAAATGAAAAGAGCAGTGACATCATTGCCTTTCACTCCAGGGATGGTGGAA
CTCTTCAACTTTATAAGAAAGAATAAGGATAAATTTGACTGCATTATTATTTCAGATTCA
AATTCGGTCTTCATAGATTGGGTTTTAGAAGCTGCCAGTTTTCATGACATATTTGATAAA
GTGTTTACAAATCCAGCAGCTTTTAATAGCAATGGTCATCTCACTGTTGAAAATTATCAT
ACTCATTCTTGCAATAGATGCCCAAAGAATCTTTGCAAAAAGGTAGTTTTGATAGAATTT
GTAGATAAACAGTTACAACAGGGAGTGAATTATACACAAATTGTTTATATTGGTGATGGT
GGAAATGATGTCTGTCCAGTCACCTTTTTAAAGAATGATGATGTTGCCATGCCACGGAAA
GGATATACCTTACAGAAAACTCTTTCCAGAATGTCTCAAAATCTTGAGCCTATGGAATAT
TCTGTTGTAGTTTGGTCCTCAGGTGTTGATATAATTTCTCATTTACAATTTCTAATAAAG
GATTAA
|
| Enzyme 59 GenBank Gene ID |
NM_001008489.2  |
| Enzyme 59 GeneCard ID |
PHOSPHO2  |
| Enzyme 59 GenAtlas ID |
PHOSPHO2  |
| Enzyme 59 HGNC ID |
HGNC:28316  |
| Enzyme 59 Chromosome Location |
2 |
| Enzyme 59 Locus |
2q31.1 |
| Enzyme 59 SNPs |
SNPJam Report  |
| Enzyme 59 General References |
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
- Hillier LW, Graves TA, Fulton RS, Fulton LA, Pepin KH, Minx P, Wagner-McPherson C, Layman D, Wylie K, Sekhon M, Becker MC, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Kremitzki C, Oddy L, Du H, Sun H, Bradshaw-Cordum H, Ali J, Carter J, Cordes M, Harris A, Isak A, van Brunt A, Nguyen C, Du F, Courtney L, Kalicki J, Ozersky P, Abbott S, Armstrong J, Belter EA, Caruso L, Cedroni M, Cotton M, Davidson T, Desai A, Elliott G, Erb T, Fronick C, Gaige T, Haakenson W, Haglund K, Holmes A, Harkins R, Kim K, Kruchowski SS, Strong CM, Grewal N, Goyea E, Hou S, Levy A, Martinka S, Mead K, McLellan MD, Meyer R, Randall-Maher J, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Shah N, Swearengen-Shahid S, Snider J, Strong JT, Thompson J, Yoakum M, Leonard S, Pearman C, Trani L, Radionenko M, Waligorski JE, Wang C, Rock SM, Tin-Wollam AM, Maupin R, Latreille P, Wendl MC, Yang SP, Pohl C, Wallis JW, Spieth J, Bieri TA, Berkowicz N, Nelson JO, Osborne J, Ding L, Meyer R, Sabo A, Shotland Y, Sinha P, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Jones TA, She X, Ciccarelli FD, Izaurralde E, Taylor J, Schmutz J, Myers RM, Cox DR, Huang X, McPherson JD, Mardis ER, Clifton SW, Warren WC, Chinwalla AT, Eddy SR, Marra MA, Ovcharenko I, Furey TS, Miller W, Eichler EE, Bork P, Suyama M, Torrents D, Waterston RH, Wilson RK: Generation and annotation of the DNA sequences of human chromosomes 2 and 4. Nature. 2005 Apr 7;434(7034):724-31. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Roberts SJ, Stewart AJ, Schmid R, Blindauer CA, Bond SR, Sadler PJ, Farquharson C: Probing the substrate specificities of human PHOSPHO1 and PHOSPHO2. Biochim Biophys Acta. 2005 Aug 31;1752(1):73-82. [PubMed
]
|
| Enzyme 59 Metabolite References |
Not Available |
|
Enzyme 60
[top]
|
| Enzyme 60 ID |
14699 |
| Enzyme 60 Name |
Putative aspartate aminotransferase, cytoplasmic 2 |
| Enzyme 60 Synonyms |
- Glutamate oxaloacetate transaminase 1-like protein 1
- Transaminase A-like protein 1
|
| Enzyme 60 Gene Name |
GOT1L1 |
| Enzyme 60 Protein Sequence |
>Putative aspartate aminotransferase, cytoplasmic 2
MPTLSVFMDVPLAHKLEGSLLKTYKQDDYPNKIFLAYRVCMTNEGHPWVSLVVQKTRLQI
SQDPSLNYEYLPTMGLKSFIQASLALLFGKHSQAIVENRVGGVHTVGDSGAFQLGVQFLR
AWHKDARIVYIISSQKELHGLVFQDMGFTVYEYSVWDPKKLCMDPDILLNVVEQIPHGCV
LVMGNIIDCKLTPSGWAKLMSMIKSKQIFPFFDIPCQGLYTSDLEEDTRILQYFVSQGFE
FFCSQSLSKNFGIYDEGVGMLVVVAVNNQQLLCVLSQLEGLAQALWLNPPNTGARVITSI
LCNPALLGEWKQSLKEVVENIMLTKEKVKEKLQLLGTPGSWGHITEQSGTHGYLGLNSQQ
VEYLVRKKHIYIPKNGQINFSCINANNINYITEGINEAVLLTESSEMCLPKEKKTLIGIK
L
|
| Enzyme 60 Number of Residues |
421 |
| Enzyme 60 Molecular Weight |
47304.7 |
| Enzyme 60 Theoretical pI |
7.02 |
| Enzyme 60 GO Classification |
| Function |
- binding
- catalytic activity
- cofactor binding
- pyridoxal phosphate binding
- transaminase activity
- transferase activity
- transferase activity, transferring nitrogenous groups
|
| Process |
- biosynthetic process
- cellular amino acid and derivative metabolic process
- cellular amino acid metabolic process
- cellular metabolic process
- metabolic process
|
| Component |
| — |
|
| Enzyme 60 General Function |
Involved in transferase activity, transferring nitrogenous groups |
| Enzyme 60 Specific Function |
L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate |
| Enzyme 60 Pathways |
Not Available |
| Enzyme 60 Reactions |
Not Available |
| Enzyme 60 Pfam Domain Function |
|
| Enzyme 60 Signals |
|
| Enzyme 60 Transmembrane Regions |
|
| Enzyme 60 Essentiality |
Not Available |
| Enzyme 60 GenBank ID Protein |
117414139  |
| Enzyme 60 UniProtKB/Swiss-Prot ID |
Q8NHS2  |
| Enzyme 60 UniProtKB/Swiss-Prot Entry Name |
AATC2_HUMAN  |
| Enzyme 60 PDB ID |
Not Available |
| Enzyme 60 Cellular Location |
Not Available |
| Enzyme 60 Gene Sequence |
>1266 bp
ATGCCCACCCTTTCAGTGTTCATGGATGTGCCCCTCGCCCACAAGCTAGAGGGCAGCTTG
TTAAAGACCTACAAACAAGATGATTACCCGAACAAGATATTCTTAGCCTATAGAGTCTGC
ATGACAAATGAAGGCCATCCCTGGGTTTCTCTCGTGGTGCAGAAGACTCGACTACAGATT
TCACAGGATCCCTCCCTGAATTATGAGTACTTGCCCACCATGGGCCTGAAATCATTCATC
CAGGCCTCTCTAGCACTCCTCTTTGGAAAGCACAGCCAAGCCATTGTGGAGAACAGGGTA
GGGGGTGTACACACTGTTGGTGACAGTGGTGCCTTCCAGCTTGGCGTCCAGTTTCTCAGA
GCTTGGCATAAGGATGCTCGTATAGTTTACATCATCTCTTCTCAAAAAGAACTGCATGGA
CTCGTCTTCCAGGACATGGGCTTTACAGTTTATGAATACTCTGTCTGGGACCCCAAGAAG
CTATGCATGGACCCCGACATACTCCTCAATGTGGTGGAGCAGATCCCACATGGCTGTGTC
CTTGTGATGGGGAACATTATCGACTGCAAGTTGACACCAAGTGGGTGGGCAAAGTTGATG
TCCATGATAAAGAGCAAGCAGATATTCCCATTTTTTGATATTCCCTGTCAAGGTTTATAC
ACCAGTGACTTGGAAGAAGATACTAGAATCTTACAATACTTTGTGTCTCAAGGCTTTGAG
TTCTTCTGCAGCCAGTCTCTGTCCAAGAATTTTGGCATTTATGATGAAGGAGTGGGGATG
CTAGTGGTGGTGGCAGTCAACAACCAGCAGCTGCTGTGTGTCCTCTCCCAGCTGGAAGGA
TTAGCCCAGGCCCTGTGGCTAAACCCCCCCAACACGGGTGCACGTGTCATCACCTCCATC
CTCTGCAACCCTGCTCTGCTGGGAGAATGGAAGCAGAGTCTAAAAGAAGTTGTAGAGAAC
ATCATGCTAACCAAGGAAAAAGTGAAGGAGAAACTCCAGCTCCTGGGAACCCCTGGGTCC
TGGGGTCACATCACCGAGCAGAGTGGGACCCACGGCTATCTTGGACTCAACTCCCAGCAG
GTGGAATACCTGGTCAGGAAGAAGCACATCTATATCCCCAAGAACGGTCAGATTAACTTC
AGCTGTATCAATGCCAACAACATAAATTACATCACTGAGGGCATCAATGAGGCTGTCCTC
CTCACAGAGAGCTCAGAGATGTGTCTTCCAAAGGAAAAAAAAACACTGATTGGAATAAAA
CTTTAG
|
| Enzyme 60 GenBank Gene ID |
NM_152413.2  |
| Enzyme 60 GeneCard ID |
GOT1L1  |
| Enzyme 60 GenAtlas ID |
GOT1L1  |
| Enzyme 60 HGNC ID |
HGNC:28487  |
| Enzyme 60 Chromosome Location |
8 |
| Enzyme 60 Locus |
8p11.23 |
| Enzyme 60 SNPs |
SNPJam Report  |
| Enzyme 60 General References |
- Nusbaum C, Mikkelsen TS, Zody MC, Asakawa S, Taudien S, Garber M, Kodira CD, Schueler MG, Shimizu A, Whittaker CA, Chang JL, Cuomo CA, Dewar K, FitzGerald MG, Yang X, Allen NR, Anderson S, Asakawa T, Blechschmidt K, Bloom T, Borowsky ML, Butler J, Cook A, Corum B, DeArellano K, DeCaprio D, Dooley KT, Dorris L 3rd, Engels R, Glockner G, Hafez N, Hagopian DS, Hall JL, Ishikawa SK, Jaffe DB, Kamat A, Kudoh J, Lehmann R, Lokitsang T, Macdonald P, Major JE, Matthews CD, Mauceli E, Menzel U, Mihalev AH, Minoshima S, Murayama Y, Naylor JW, Nicol R, Nguyen C, O'Leary SB, O'Neill K, Parker SC, Polley A, Raymond CK, Reichwald K, Rodriguez J, Sasaki T, Schilhabel M, Siddiqui R, Smith CL, Sneddon TP, Talamas JA, Tenzin P, Topham K, Venkataraman V, Wen G, Yamazaki S, Young SK, Zeng Q, Zimmer AR, Rosenthal A, Birren BW, Platzer M, Shimizu N, Lander ES: DNA sequence and analysis of human chromosome 8. Nature. 2006 Jan 19;439(7074):331-5. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
|
| Enzyme 60 Metabolite References |
Not Available |
|
Enzyme 61
[top]
|
| Enzyme 61 ID |
14700 |
| Enzyme 61 Name |
Alanine--glyoxylate aminotransferase 2-like 2 |
| Enzyme 61 Synonyms |
Not Available |
| Enzyme 61 Gene Name |
AGXT2L2 |
| Enzyme 61 Protein Sequence |
>Alanine--glyoxylate aminotransferase 2-like 2
MAADQRPKADTLALRQRLISSSCRLFFPEDPVKIVRAQGQYMYDEQGAEYIDCISNVAHV
GHCHPLVVQAAHEQNQVLNTNSRYLHDNIVDYAQRLSETLPEQLCVFYFLNSGSEANDLA
LRLARHYTGHQDVVVLDHAYHGHLSSLIDISPYKFRNLDGQKEWVHVAPLPDTYRGPYRE
DHPNPAMAYANEVKRVVSSAQEKGRKIAAFFAESLPSVGGQIIPPAGYFSQVAEHIRKAG
GVFVADEIQVGFGRVGKHFWAFQLQGKDFVPDIVTMGKSIGNGHPVACVAATQPVARAFE
ATGVEYFNTFGGSPVSCAVGLAVLNVLEKEQLQDHATSVGSFLMQLLGQQKIKHPIVGDV
RGVGLFIGVDLIKDEATRTPATEEAAYLVSRLKENYVLLSTDGPGRNILKFKPPMCFSLD
NARQVVAKLDAILTDMEEKVRSCETLRLQP
|
| Enzyme 61 Number of Residues |
450 |
| Enzyme 61 Molecular Weight |
49710.2 |
| Enzyme 61 Theoretical pI |
6.76 |
| Enzyme 61 GO Classification |
| Function |
- binding
- catalytic activity
- cofactor binding
- pyridoxal phosphate binding
- transaminase activity
- transferase activity
- transferase activity, transferring nitrogenous groups
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 61 General Function |
Involved in transaminase activity |
| Enzyme 61 Specific Function |
Not Available |
| Enzyme 61 Pathways |
Not Available |
| Enzyme 61 Reactions |
Not Available |
| Enzyme 61 Pfam Domain Function |
|
| Enzyme 61 Signals |
|
| Enzyme 61 Transmembrane Regions |
|
| Enzyme 61 Essentiality |
Not Available |
| Enzyme 61 GenBank ID Protein |
24119277  |
| Enzyme 61 UniProtKB/Swiss-Prot ID |
Q8IUZ5  |
| Enzyme 61 UniProtKB/Swiss-Prot Entry Name |
AT2L2_HUMAN  |
| Enzyme 61 PDB ID |
Not Available |
| Enzyme 61 Cellular Location |
Not Available |
| Enzyme 61 Gene Sequence |
>1353 bp
ATGGCCGCAGACCAGCGCCCGAAGGCCGACACGCTGGCCCTGAGGCAACGGCTCATCAGC
TCTTCCTGCAGACTCTTTTTTCCCGAGGATCCTGTTAAGATTGTCCGGGCCCAAGGGCAG
TACATGTACGATGAACAGGGGGCAGAATACATCGATTGCATCAGCAATGTGGCGCACGTT
GGGCACTGCCACCCTCTCGTGGTCCAAGCAGCACATGAGCAGAACCAGGTGCTCAACACC
AACAGCCGGTACCTGCATGACAACATCGTGGACTATGCGCAGAGGCTGTCAGAGACCCTG
CCGGAGCAGCTCTGTGTGTTCTATTTCCTGAATTCTGGGTCAGAAGCCAATGACCTGGCC
CTGAGGCTGGCTCGCCACTACACGGGACACCAGGACGTGGTGGTATTAGATCATGCGTAT
CACGGCCACCTGAGCTCCCTGATTGACATCAGTCCCTACAAGTTCCGCAACCTGGATGGC
CAGAAGGAGTGGGTCCACGTGGCACCTCTCCCAGACACCTACCGGGGCCCCTACCGGGAG
GACCACCCCAACCCAGCTATGGCCTATGCCAACGAGGTGAAACGTGTGGTCAGCAGTGCA
CAGGAGAAGGGCAGGAAGATTGCAGCCTTCTTCGCTGAGTCTCTGCCCAGTGTGGGAGGG
CAGATCATTCCCCCTGCTGGCTACTTCTCCCAAGTGGCAGAGCACATCCGCAAGGCCGGA
GGGGTCTTTGTTGCAGATGAGATCCAGGTTGGCTTTGGCCGGGTAGGCAAGCACTTCTGG
GCCTTCCAGCTCCAGGGAAAAGACTTCGTCCCTGACATCGTCACCATGGGCAAGTCCATT
GGCAACGGCCACCCTGTTGCCTGCGTGGCCGCAACCCAGCCTGTGGCGAGGGCATTTGAA
GCCACCGGCGTTGAGTACTTCAACACGTTTGGGGGCAGCCCAGTGTCCTGCGCTGTGGGG
CTGGCCGTCCTGAATGTCTTGGAGAAGGAGCAGCTCCAGGATCATGCCACCAGTGTAGGC
AGCTTCCTGATGCAGCTCCTCGGGCAGCAAAAAATCAAACATCCCATCGTCGGGGATGTC
AGGGGTGTTGGGCTCTTCATTGGTGTGGATCTGATCAAAGATGAGGCCACAAGGACACCA
GCAACTGAAGAGGCTGCCTACTTGGTATCAAGGCTGAAGGAGAACTACGTTTTGCTGAGC
ACTGATGGCCCTGGGAGGAACATCCTGAAGTTTAAGCCCCCAATGTGCTTCAGCCTGGAC
AATGCACGGCAGGTGGTGGCAAAGCTGGATGCCATTCTGACTGACATGGAAGAGAAGGTG
AGAAGTTGTGAAACGCTGAGGCTCCAGCCCTAA
|
| Enzyme 61 GenBank Gene ID |
NM_153373.2  |
| Enzyme 61 GeneCard ID |
AGXT2L2  |
| Enzyme 61 GenAtlas ID |
AGXT2L2  |
| Enzyme 61 HGNC ID |
HGNC:28249  |
| Enzyme 61 Chromosome Location |
5 |
| Enzyme 61 Locus |
5q35.3 |
| Enzyme 61 SNPs |
SNPJam Report  |
| Enzyme 61 General References |
- Wan D, Gong Y, Qin W, Zhang P, Li J, Wei L, Zhou X, Li H, Qiu X, Zhong F, He L, Yu J, Yao G, Jiang H, Qian L, Yu Y, Shu H, Chen X, Xu H, Guo M, Pan Z, Chen Y, Ge C, Yang S, Gu J: Large-scale cDNA transfection screening for genes related to cancer development and progression. Proc Natl Acad Sci U S A. 2004 Nov 2;101(44):15724-9. Epub 2004 Oct 21. [PubMed
]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
|
| Enzyme 61 Metabolite References |
Not Available |
|
Enzyme 62
[top]
|
| Enzyme 62 ID |
14701 |
| Enzyme 62 Name |
Glutamate decarboxylase-like protein 1 |
| Enzyme 62 Synonyms |
Not Available |
| Enzyme 62 Gene Name |
GADL1 |
| Enzyme 62 Protein Sequence |
>Glutamate decarboxylase-like protein 1
MSSDSDRQCPVDGDIDQQEMIPSKKNAVLVDGVVLNGPTTDAKAGEKFVEEACRLIMEEV
VLKATDVNEKVCEWRPPEQLKQLLDLEMRDSGEPPHKLLELCRDVIHYSVKTNHPRFFNQ
LYAGLDYYSLVARFMTEALNPSVYTYEVSPVFLLVEEAVLKKMIEFIGWKEGDGIFNPGG
SVSNMYAMNLARYKYCPDIKEKGLSGSPRLILFTSAECHYSMKKAASFLGIGTENVCFVE
TDGRGKMIPEELEKQVWQARKEGAAPFLVCATSGTTVLGAFDPLDEIADICERHSLWLHV
DASWGGSALMSRKHRKLLHGIHRADSVAWNPHKMLMAGIQCCALLVKDKSDLLKKCYSAK
ASYLFQQDKFYDVSYDTGDKSIQCSRRPDAFKFWMTWKALGTLGLEERVNRALALSRYLV
DEIKKREGFKLLMEPEYANICFWYIPPSLREMEEGPEFWAKLNLVAPAIKERMMKKGSLM
LGYQPHRGKVNFFRQVVISPQVSREDMDFLLDEIDLLGKDM
|
| Enzyme 62 Number of Residues |
521 |
| Enzyme 62 Molecular Weight |
59245.9 |
| Enzyme 62 Theoretical pI |
6.30 |
| Enzyme 62 GO Classification |
| Function |
- binding
- carbon-carbon lyase activity
- carboxy-lyase activity
- catalytic activity
- cofactor binding
- lyase activity
- pyridoxal phosphate binding
|
| Process |
- carboxylic acid metabolic process
- cellular metabolic process
- metabolic process
- organic acid metabolic process
- oxoacid metabolic process
|
| Component |
| — |
|
| Enzyme 62 General Function |
Involved in carboxy-lyase activity |
| Enzyme 62 Specific Function |
Not Available |
| Enzyme 62 Pathways |
Not Available |
| Enzyme 62 Reactions |
Not Available |
| Enzyme 62 Pfam Domain Function |
|
| Enzyme 62 Signals |
|
| Enzyme 62 Transmembrane Regions |
|
| Enzyme 62 Essentiality |
Not Available |
| Enzyme 62 GenBank ID Protein |
197383062  |
| Enzyme 62 UniProtKB/Swiss-Prot ID |
Q6ZQY3  |
| Enzyme 62 UniProtKB/Swiss-Prot Entry Name |
GADL1_HUMAN  |
| Enzyme 62 PDB ID |
Not Available |
| Enzyme 62 Cellular Location |
Not Available |
| Enzyme 62 Gene Sequence |
>1566 bp
ATGAGCAGCGACTCGGACCGCCAGTGTCCTGTGGACGGAGATATTGATCAACAAGAGATG
ATTCCAAGTAAGAAGAATGCTGTTCTTGTGGATGGGGTTGTGCTGAATGGTCCTACAACA
GATGCAAAAGCTGGAGAAAAATTTGTTGAAGAGGCCTGTAGGCTAATAATGGAAGAGGTG
GTTTTGAAAGCTACAGATGTCAATGAGAAGGTGTGTGAATGGAGGCCTCCTGAACAACTG
AAACAGCTTCTTGATTTGGAGATGAGAGACTCAGGCGAGCCACCCCATAAACTATTGGAA
CTCTGTCGGGATGTCATACACTACAGTGTCAAAACTAACCACCCAAGATTTTTCAACCAA
TTGTATGCTGGACTTGATTATTACTCCTTGGTGGCCCGATTTATGACCGAAGCATTGAAT
CCAAGTGTTTATACGTATGAGGTGTCCCCAGTGTTTCTGTTAGTGGAAGAAGCGGTTCTG
AAGAAAATGATTGAATTTATTGGCTGGAAAGAAGGGGATGGAATATTTAACCCAGGTGGC
TCAGTGTCCAATATGTATGCAATGAATTTAGCTAGATACAAATATTGTCCTGATATTAAG
GAAAAGGGGCTGTCTGGTTCGCCAAGATTAATCCTTTTCACATCTGCAGAGTGTCATTAC
TCTATGAAGAAGGCAGCCTCTTTTCTTGGGATTGGCACTGAGAATGTTTGCTTTGTGGAA
ACAGATGGAAGAGGTAAAATGATACCTGAGGAACTGGAGAAGCAAGTCTGGCAAGCCAGA
AAAGAGGGGGCAGCACCGTTTCTTGTCTGTGCCACTTCTGGTACAACTGTGTTGGGAGCT
TTTGACCCTCTGGATGAAATAGCAGACATCTGCGAGAGGCACAGCCTCTGGCTTCATGTA
GATGCTTCTTGGGGTGGCTCAGCTTTGATGTCGAGGAAGCACCGCAAGCTTCTGCATGGC
ATCCACAGGGCTGACTCTGTGGCCTGGAACCCACACAAGATGCTGATGGCTGGGATCCAG
TGCTGTGCTCTCCTTGTGAAAGACAAATCTGATCTTCTTAAAAAATGCTACTCTGCCAAG
GCATCTTACCTCTTCCAGCAGGATAAATTCTATGATGTGAGCTATGACACAGGAGACAAG
TCTATCCAGTGTAGCAGAAGACCAGATGCATTCAAGTTCTGGATGACCTGGAAGGCCCTG
GGTACATTAGGCCTTGAAGAAAGAGTTAATCGTGCTCTTGCTTTATCTAGGTACCTAGTA
GATGAAATCAAGAAAAGAGAAGGATTCAAGTTACTGATGGAACCTGAATATGCCAATATT
TGCTTTTGGTACATTCCACCGAGCCTCAGAGAGATGGAAGAAGGACCCGAGTTCTGGGCA
AAACTTAATTTGGTGGCCCCAGCCATTAAGGAGAGGATGATGAAGAAGGGAAGCTTGATG
CTGGGCTACCAGCCGCACCGGGGAAAGGTCAACTTCTTCCGCCAGGTGGTGATCAGCCCT
CAAGTGAGCCGGGAGGACATGGACTTCCTCCTGGATGAGATAGACTTACTGGGTAAAGAC
ATGTAG
|
| Enzyme 62 GenBank Gene ID |
NM_207359.2  |
| Enzyme 62 GeneCard ID |
GADL1  |
| Enzyme 62 GenAtlas ID |
GADL1  |
| Enzyme 62 HGNC ID |
HGNC:27949  |
| Enzyme 62 Chromosome Location |
3 |
| Enzyme 62 Locus |
3p24.1-p23 |
| Enzyme 62 SNPs |
SNPJam Report  |
| Enzyme 62 General References |
- Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed
]
- Muzny DM, Scherer SE, Kaul R, Wang J, Yu J, Sudbrak R, Buhay CJ, Chen R, Cree A, Ding Y, Dugan-Rocha S, Gill R, Gunaratne P, Harris RA, Hawes AC, Hernandez J, Hodgson AV, Hume J, Jackson A, Khan ZM, Kovar-Smith C, Lewis LR, Lozado RJ, Metzker ML, Milosavljevic A, Miner GR, Morgan MB, Nazareth LV, Scott G, Sodergren E, Song XZ, Steffen D, Wei S, Wheeler DA, Wright MW, Worley KC, Yuan Y, Zhang Z, Adams CQ, Ansari-Lari MA, Ayele M, Brown MJ, Chen G, Chen Z, Clendenning J, Clerc-Blankenburg KP, Chen R, Chen Z, Davis C, Delgado O, Dinh HH, Dong W, Draper H, Ernst S, Fu G, Gonzalez-Garay ML, Garcia DK, Gillett W, Gu J, Hao B, Haugen E, Havlak P, He X, Hennig S, Hu S, Huang W, Jackson LR, Jacob LS, Kelly SH, Kube M, Levy R, Li Z, Liu B, Liu J, Liu W, Lu J, Maheshwari M, Nguyen BV, Okwuonu GO, Palmeiri A, Pasternak S, Perez LM, Phelps KA, Plopper FJ, Qiang B, Raymond C, Rodriguez R, Saenphimmachak C, Santibanez J, Shen H, Shen Y, Subramanian S, Tabor PE, Verduzco D, Waldron L, Wang J, Wang J, Wang Q, Williams GA, Wong GK, Yao Z, Zhang J, Zhang X, Zhao G, Zhou J, Zhou Y, Nelson D, Lehrach H, Reinhardt R, Naylor SL, Yang H, Olson M, Weinstock G, Gibbs RA: The DNA sequence, annotation and analysis of human chromosome 3. Nature. 2006 Apr 27;440(7088):1194-8. [PubMed
]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
|
| Enzyme 62 Metabolite References |
Not Available |
|
Enzyme 63
[top]
|
| Enzyme 63 ID |
14702 |
| Enzyme 63 Name |
Kynurenine--oxoglutarate transaminase 3 |
| Enzyme 63 Synonyms |
- Cysteine-S-conjugate beta-lyase 2
- Kynurenine aminotransferase III
- KATIII
- Kynurenine--glyoxylate transaminase
- Kynurenine--oxoglutarate transaminase III
|
| Enzyme 63 Gene Name |
CCBL2 |
| Enzyme 63 Protein Sequence |
>Kynurenine--oxoglutarate transaminase 3
MFLAQRSLCSLSGRAKFLKTISSSKILGFSTSAKMSLKFTNAKRIEGLDSNVWIEFTKLA
ADPSVVNLGQGFPDISPPTYVKEELSKIAAIDSLNQYTRGFGHPSLVKALSYLYEKLYQK
QIDSNKEILVTVGAYGSLFNTIQALIDEGDEVILIVPFYDCYEPMVRMAGATPVFIPLRS
KPVYGKRWSSSDWTLDPQELESKFNSKTKAIILNTPHNPLGKVYNREELQVIADLCIKYD
TLCISDEVYEWLVYSGNKHLKIATFPGMWERTITIGSAGKTFSVTGWKLGWSIGPNHLIK
HLQTVQQNTIYTCATPLQEALAQAFWIDIKRMDDPECYFNSLPKELEVKRDRMVRLLESV
GLKPIVPDGGYFIIADVSLLDPDLSDMKNNEPYDYKFVKWMTKHKKLSAIPVSAFCNSET
KSQFEKFVRFCFIKKDSTLDAAEEIIKAWSVQKS
|
| Enzyme 63 Number of Residues |
454 |
| Enzyme 63 Molecular Weight |
51399.9 |
| Enzyme 63 Theoretical pI |
8.34 |
| Enzyme 63 GO Classification |
| Function |
- binding
- catalytic activity
- cofactor binding
- pyridoxal phosphate binding
- transferase activity
- transferase activity, transferring nitrogenous groups
|
| Process |
- biosynthetic process
- metabolic process
|
| Component |
| — |
|
| Enzyme 63 General Function |
Involved in transferase activity, transferring nitrogenous groups |
| Enzyme 63 Specific Function |
Catalyzes the irreversible transamination of the L- tryptophan metabolite L-kynurenine to form kynurenic acid (KA). May catalyze the beta-elimination of S-conjugates and Se- conjugates of L-(seleno)cysteine, resulting in the cleavage of the C-S or C-Se bond. Has transaminase activity towards L-kynurenine, tryptophan, phenylalanine, serine, cysteine, methionine, histidine, glutamine and asparagine with glyoxylate as an amino group acceptor (in vitro). Has lower activity with 2- oxoglutarate as amino group acceptor (in vitro) |
| Enzyme 63 Pathways |
|
| Enzyme 63 Reactions |
- RS-CH2-CH(NH3+)COO- = RSH + NH3 + pyruvate [RN:R03528]
|
| Enzyme 63 Pfam Domain Function |
|
| Enzyme 63 Signals |
|
| Enzyme 63 Transmembrane Regions |
|
| Enzyme 63 Essentiality |
Not Available |
| Enzyme 63 GenBank ID Protein |
Not Available |
| Enzyme 63 UniProtKB/Swiss-Prot ID |
Q6YP21  |
| Enzyme 63 UniProtKB/Swiss-Prot Entry Name |
KAT3_HUMAN  |
| Enzyme 63 PDB ID |
Not Available |
| Enzyme 63 Cellular Location |
Not Available |
| Enzyme 63 Gene Sequence |
>1365 bp
ATGTTTTTGGCCCAGAGGAGCCTCTGCTCTCTTAGCGGTAGAGCAAAATTCCTGAAGACA
ATTTCTTCTTCCAAAATCCTCGGATTCTCTACTTCTGCTAAAATGTCACTGAAATTCACA
AATGCAAAACGGATTGAAGGACTTGATAGTAATGTGTGGATTGAATTTACCAAATTGGCT
GCAGACCCTTCTGTTGTGAATCTTGGCCAAGGCTTTCCAGATATATCCCCTCCTACATAT
GTAAAAGAAGAATTATCAAAGATTGCAGCAATCGATAGCCTGAATCAGTATACACGAGGC
TTTGGCCATCCATCACTTGTGAAAGCTCTGTCCTATCTGTATGAAAAGCTTTATCAAAAG
CAAATTGATTCAAATAAAGAAATCCTTGTGACAGTAGGAGCATATGGATCTCTTTTTAAC
ACCATTCAAGCATTAATTGATGAGGGAGATGAAGTCATACTAATAGTGCCTTTCTATGAC
TGCTATGAGCCCATGGTGAGAATGGCTGGAGCAACACCTGTTTTTATTCCCCTGAGATCT
AAACCTGTTTATGGAAAAAGATGGTCTAGTTCTGACTGGACATTAGATCCTCAAGAACTG
GAAAGTAAATTTAATTCCAAAACCAAAGCTATTATACTAAATACTCCACATAACCCACTT
GGCAAGGTGTATAACAGAGAGGAACTGCAAGTAATTGCTGACCTTTGCATCAAATATGAC
ACACTCTGCATCAGCGATGAGGTTTATGAATGGCTTGTATATTCTGGAAATAAGCACTTA
AAAATAGCTACTTTTCCAGGTATGTGGGAGAGAACAATAACAATAGGAAGTGCTGGAAAG
ACTTTCAGTGTAACTGGCTGGAAGCTTGGCTGGTCCATTGGTCCAAATCATTTGATAAAA
CATTTACAGACAGTTCAACAAAACACGATTTATACTTGTGCAACTCCTTTACAGGAAGCC
TTGGCTCAAGCTTTCTGGATTGACATCAAGCGCATGGATGACCCAGAATGTTACTTTAAT
TCTTTGCCAAAAGAGTTAGAAGTAAAAAGAGATCGGATGGTACGTTTACTTGAAAGTGTT
GGCCTAAAACCCATAGTTCCTGATGGAGGATACTTCATCATCGCTGATGTGTCTTTGCTA
GATCCAGACCTCTCTGATATGAAGAATAATGAGCCTTATGACTATAAGTTTGTGAAATGG
ATGACTAAACATAAGAAACTATCAGCCATCCCCGTTTCAGCATTCTGTAACTCAGAGACT
AAATCACAGTTTGAGAAGTTTGTGCGTTTTTGCTTCATTAAAAAAGACAGCACACTGGAT
GCTGCTGAAGAAATCATCAAGGCATGGAGTGTACAGAAGTCTTGA
|
| Enzyme 63 GenBank Gene ID |
AY028624  |
| Enzyme 63 GeneCard ID |
CCBL2  |
| Enzyme 63 GenAtlas ID |
CCBL2  |
| Enzyme 63 HGNC ID |
HGNC:33238  |
| Enzyme 63 Chromosome Location |
1 |
| Enzyme 63 Locus |
1p22.2 |
| Enzyme 63 SNPs |
SNPJam Report  |
| Enzyme 63 General References |
- Yu P, Li Z, Zhang L, Tagle DA, Cai T: Characterization of kynurenine aminotransferase III, a novel member of a phylogenetically conserved KAT family. Gene. 2006 Jan 3;365:111-8. Epub 2006 Jan 10. [PubMed
]
- Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed
]
- Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed
]
|
| Enzyme 63 Metabolite References |
Not Available |
|
Enzyme 64
[top]
|
| Enzyme 64 ID |
14703 |
| Enzyme 64 Name |
Molybdenum cofactor sulfurase |
| Enzyme 64 Synonyms |
- MCS
- MOS
- MoCo sulfurase
- hMCS
|
| Enzyme 64 Gene Name |
MOCOS |
| Enzyme 64 Protein Sequence |
>Molybdenum cofactor sulfurase
MAGAAAESGRELWTFAGSRDPSAPRLAYGYGPGSLRELRAREFSRLAGTVYLDHAGATLF
SQSQLESFTSDLMENTYGNPHSQNISSKLTHDTVEQVRYRILAHFHTTAEDYTVIFTAGS
TAALKLVAEAFPWVSQGPESSGSRFCYLTDSHTSVVGMRNVTMAINVISTPVRPEDLWSA
EERSASASNPDCQLPHLFCYPAQSNFSGVRYPLSWIEEVKSGRLHPVSTPGKWFVLLDAA
SYVSTSPLDLSAHQADFVPISFYKIFGFPTGLGALLVHNRAAPLLRKTYFGGGTASAYLA
GEDFYIPRQSVAQRFEDGTISFLDVIALKHGFDTLERLTGGMENIKQHTFTLAQYTYVAL
SSLQYPNGAPVVRIYSDSEFSSPEVQGPIINFNVLDDKGNIIGYSQVDKMASLYNIHLRT
GCFCNTGACQRHLGISNEMVRKHFQAGHVCGDNMDLIDGQPTGSVRISFGYMSTLDDVQA
FLRFIIDTRLHSSGDWPVPQAHADTGETGAPSADSQADVIPAVMGRRSLSPQEDALTGSR
VWNNSSTVNAVPVAPPVCDVARTQPTPSEKAAGVLEGALGPHVVTNLYLYPIKSCAAFEV
TRWPVGNQGLLYDRSWMVVNHNGVCLSQKQEPRLCLIQPFIDLRQRIMVIKAKGMEPIEV
PLEENSERTQIRQSRVCADRVSTYDCGEKISSWLSTFFGRPCHLIKQSSNSQRNAKKKHG
KDQLPGTMATLSLVNEAQYLLINTSSILELHRQLNTSDENGKEELFSLKDLSLRFRANII
INGKRAFEEEKWDEISIGSLRFQVLGPCHRCQMICIDQQTGQRNQHVFQKLSESRETKVN
FGMYLMHASLDLSSPCFLSVGSQVLPVLKENVEGHDLPASEKHQDVTS
|
| Enzyme 64 Number of Residues |
888 |
| Enzyme 64 Molecular Weight |
98119.0 |
| Enzyme 64 Theoretical pI |
6.68 |
| Enzyme 64 GO Classification |
| Function |
- binding
- catalytic activity
- cation binding
- cofactor binding
- ion binding
- metal ion binding
- molybdenum ion binding
- pyridoxal phosphate binding
- transition metal ion binding
|
| Process |
|
| Component |
| — |
|
| Enzyme 64 General Function |
Involved in metabolic process |
| Enzyme 64 Specific Function |
Sulfurates the molybdenum cofactor. Sulfation of molybdenum is essential for xanthine dehydrogenase (XDH) and aldehyde oxidase (ADO) enzymes in which molybdenum cofactor is liganded by 1 oxygen and 1 sulfur atom in active form |
| Enzyme 64 Pathways |
Not Available |
| Enzyme 64 Reactions |
Not Available |
| Enzyme 64 Pfam Domain Function |
|
| Enzyme 64 Signals |
|
| Enzyme 64 Transmembrane Regions |
|
| Enzyme 64 Essentiality |
Not Available |
| Enzyme 64 GenBank ID Protein |
157388923  |
| Enzyme 64 UniProtKB/Swiss-Prot ID |
Q96EN8  |
| Enzyme 64 UniProtKB/Swiss-Prot Entry Name |
MOCOS_HUMAN  |
| Enzyme 64 PDB ID |
Not Available |
| Enzyme 64 Cellular Location |
Not Available |
| Enzyme 64 Gene Sequence |
>2667 bp
ATGGCCGGCGCGGCGGCGGAGTCAGGGCGGGAGCTGTGGACCTTCGCGGGTTCCCGGGAC
CCGAGCGCACCGCGGCTAGCCTACGGCTACGGCCCGGGCAGCCTGCGCGAGCTGCGGGCG
CGCGAGTTCAGCCGCCTGGCAGGAACTGTCTATCTTGACCATGCAGGTGCCACCTTGTTC
TCCCAGAGCCAGCTCGAAAGCTTCACTAGTGATCTCATGGAAAACACTTATGGTAATCCT
CACAGCCAGAACATCAGCAGCAAGCTCACCCATGACACTGTGGAGCAGGTGCGCTACAGA
ATCCTGGCGCACTTCCACACCACCGCAGAAGACTACACTGTGATCTTCACTGCCGGGAGC
ACGGCTGCTCTCAAACTGGTGGCAGAGGCCTTTCCATGGGTGTCCCAGGGCCCAGAGAGC
AGTGGGAGTCGCTTCTGTTACCTCACCGACAGCCACACCTCCGTAGTGGGTATGCGGAAC
GTGACCATGGCTATAAATGTCATATCCACCCCGGTCAGGCCAGAGGACCTGTGGTCTGCA
GAGGAACGTAGTGCTTCAGCCAGCAACCCAGACTGCCAGCTGCCGCATCTCTTCTGCTAC
CCAGCTCAGAGTAACTTTTCTGGAGTCAGATACCCCCTGTCCTGGATAGAAGAGGTCAAG
TCTGGGCGGTTGCACCCTGTGAGCACGCCTGGGAAGTGGTTTGTGCTGCTGGATGCAGCC
TCCTACGTGAGCACCTCGCCTTTGGACCTGTCAGCTCACCAGGCCGACTTTGTCCCCATC
TCCTTCTATAAGATCTTCGGGTTTCCTACAGGCCTGGGCGCTCTGCTGGTCCATAATCGT
GCGGCTCCTCTACTGAGGAAGACCTACTTTGGAGGAGGGACAGCCTCTGCGTACCTAGCA
GGAGAAGACTTCTACATCCCGAGGCAGTCGGTAGCTCAGAGGTTTGAAGATGGCACCATC
TCATTCCTTGATGTTATCGCGCTAAAACATGGATTTGACACCCTAGAGCGCCTCACAGGT
GGAATGGAGAATATAAAGCAGCACACCTTCACCTTGGCTCAGTATACCTACGTGGCCCTG
TCCTCTCTCCAGTACCCCAATGGAGCCCCTGTGGTGCGGATTTACAGCGATTCTGAGTTC
AGCAGCCCTGAGGTTCAGGGCCCAATCATCAATTTTAATGTGCTGGATGACAAAGGGAAC
ATCATTGGTTACTCCCAGGTGGACAAAATGGCCAGTCTTTACAACATCCACCTGCGAACT
GGCTGCTTCTGTAACACTGGGGCCTGCCAGAGGCACCTGGGCATAAGCAACGAGATGGTC
AGGAAGCATTTTCAGGCTGGTCATGTCTGTGGGGACAATATGGACCTCATAGATGGGCAG
CCCACAGGATCTGTGAGGATTTCATTTGGATACATGTCGACGCTGGATGATGTCCAGGCC
TTTCTTAGGTTCATCATAGACACTCGCCTGCACTCATCAGGGGACTGGCCTGTCCCTCAG
GCCCATGCTGACACCGGGGAGACTGGAGCCCCATCAGCAGACAGCCAGGCTGATGTTATA
CCTGCTGTCATGGGCAGACGTAGCCTCTCGCCTCAGGAAGATGCCCTCACAGGCTCCAGG
GTTTGGAACAACTCGTCTACTGTGAATGCTGTGCCTGTGGCCCCACCTGTGTGTGATGTC
GCCAGAACCCAGCCGACTCCTTCAGAGAAAGCTGCAGGAGTCCTGGAGGGGGCCCTTGGG
CCACATGTTGTCACTAACCTTTATCTCTATCCAATCAAATCCTGTGCTGCATTTGAGGTG
ACCAGGTGGCCTGTAGGAAACCAAGGGCTGCTATATGACCGGAGCTGGATGGTTGTGAAT
CACAATGGTGTTTGCCTGAGTCAGAAGCAGGAACCCCGGCTCTGCCTGATCCAGCCCTTC
ATCGACTTGCGGCAAAGGATCATGGTCATCAAAGCCAAAGGGATGGAGCCTATAGAGGTG
CCTCTTGAGGAAAATAGTGAACGGACTCAGATTCGCCAAAGCAGGGTCTGTGCTGACAGA
GTAAGTACTTATGATTGTGGAGAAAAAATTTCAAGCTGGTTGTCAACATTTTTTGGCCGT
CCTTGTCATTTGATCAAACAAAGTTCAAACTCTCAAAGGAATGCAAAGAAGAAACATGGA
AAAGATCAACTTCCTGGTACAATGGCCACCCTTTCTCTGGTGAATGAGGCACAGTATCTG
CTGATCAACACATCCAGTATTTTGGAACTTCACCGGCAACTAAACACCAGTGATGAGAAT
GGAAAGGAGGAATTATTCTCACTGAAGGATCTCAGCTTGCGTTTTCGTGCCAATATTATT
ATCAATGGAAAAAGGGCTTTTGAAGAAGAGAAATGGGATGAGATTTCAATTGGCTCTTTG
CGTTTCCAGGTTTTGGGGCCTTGTCACAGATGCCAGATGATTTGCATCGACCAGCAAACT
GGGCAACGAAACCAGCATGTTTTCCAAAAACTTTCTGAGAGTCGTGAAACAAAGGTGAAC
TTTGGCATGTACCTGATGCATGCATCATTGGATTTATCCTCCCCATGTTTCCTGTCTGTA
GGATCTCAGGTGCTCCCTGTGTTGAAAGAGAATGTGGAAGGTCATGATTTACCTGCATCT
GAGAAACACCAGGATGTTACCTCCTAA
|
| Enzyme 64 GenBank Gene ID |
NM_017947.2  |
| Enzyme 64 GeneCard ID |
MOCOS  |
| Enzyme 64 GenAtlas ID |
MOCOS  |
| Enzyme 64 HGNC ID |
HGNC:18234  |
| Enzyme 64 Chromosome Location |
1 |
| Enzyme 64 Locus |
18q12 |
| Enzyme 64 SNPs |
SNPJam Report  |
| Enzyme 64 General References |
- Ichida K, Matsumura T, Sakuma R, Hosoya T, Nishino T: Mutation of human molybdenum cofactor sulfurase gene is responsible for classical xanthinuria type II. Biochem Biophys Res Commun. 2001 Apr 20;282(5):1194-200. [PubMed
]
- Nusbaum C, Zody MC, Borowsky ML, Kamal M, Kodira CD, Taylor TD, Whittaker CA, Chang JL, Cuomo CA, Dewar K, FitzGerald MG, Yang X, Abouelleil A, Allen NR, Anderson S, Bloom T, Bugalter B, Butler J, Cook A, DeCaprio D, Engels R, Garber M, Gnirke A, Hafez N, Hall JL, Norman CH, Itoh T, Jaffe DB, Kuroki Y, Lehoczky J, Lui A, Macdonald P, Mauceli E, Mikkelsen TS, Naylor JW, Nicol R, Nguyen C, Noguchi H, O'Leary SB, O'Neill K, Piqani B, Smith CL, Talamas JA, Topham K, Totoki Y, Toyoda A, Wain HM, Young SK, Zeng Q, Zimmer AR, Fujiyama A, Hattori M, Birren BW, Sakaki Y, Lander ES: DNA sequence and analysis of human chromosome 18. Nature. 2005 Sep 22;437(7058):551-5. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed
]
- Beausoleil SA, Jedrychowski M, Schwartz D, Elias JE, Villen J, Li J, Cohn MA, Cantley LC, Gygi SP: Large-scale characterization of HeLa cell nuclear phosphoproteins. Proc Natl Acad Sci U S A. 2004 Aug 17;101(33):12130-5. Epub 2004 Aug 9. [PubMed
]
- Beausoleil SA, Villen J, Gerber SA, Rush J, Gygi SP: A probability-based approach for high-throughput protein phosphorylation analysis and site localization. Nat Biotechnol. 2006 Oct;24(10):1285-92. Epub 2006 Sep 10. [PubMed
]
- Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed
]
- Yamamoto T, Moriwaki Y, Takahashi S, Tsutsumi Z, Tuneyoshi K, Matsui K, Cheng J, Hada T: Identification of a new point mutation in the human molybdenum cofactor sulferase gene that is responsible for xanthinuria type II. Metabolism. 2003 Nov;52(11):1501-4. [PubMed
]
- Peretz H, Naamati MS, Levartovsky D, Lagziel A, Shani E, Horn I, Shalev H, Landau D: Identification and characterization of the first mutation (Arg776Cys) in the C-terminal domain of the Human Molybdenum Cofactor Sulfurase (HMCS) associated with type II classical xanthinuria. Mol Genet Metab. 2007 May;91(1):23-9. Epub 2007 Mar 23. [PubMed
]
|
| Enzyme 64 Metabolite References |
Not Available |
|
Enzyme 65
[top]
|
| Enzyme 65 ID |
14704 |
| Enzyme 65 Name |
Pyridoxal-dependent decarboxylase domain-containing protein 1 |
| Enzyme 65 Synonyms |
Not Available |
| Enzyme 65 Gene Name |
PDXDC1 |
| Enzyme 65 Protein Sequence |
>Pyridoxal-dependent decarboxylase domain-containing protein 1
MDASLEKIADPTLAEMGKNLKEAVKMLEDSQRRTEEENGKKLISGDIPGPLQGSGQDMVS
ILQLVQNLMHGDEDEEPQSPRIQNIGEQGHMALLGHSLGAYISTLDKEKLRKLTTRILSD
TTLWLCRIFRYENGCAYFHEEEREGLAKICRLAIHSRYEDFVVDGFNVLYNKKPVIYLSA
AARPGLGQYLCNQLGLPFPCLCRVPCNTVFGSQHQMDVAFLEKLIKDDIERGRLPLLLVA
NAGTAAVGHTDKIGRLKELCEQYGIWLHVEGVNLATLALGYVSSSVLAAAKCDSMTMTPG
PWLGLPAVPAVTLYKHDDPALTLVAGLTSNKPTDKLRALPLWLSLQYLGLDGFVERIKHA
CQLSQRLQESLKKVNYIKILVEDELSSPVVVFRFFQELPGSDPVFKAVPVPNMTPSGVGR
ERHSCDALNRWLGEQLKQLVPASGLTVMDLEAEGTCLRFSPLMTAAVLGTRGEDVDQLVA
CIESKLPVLCCTLQLREEFKQEVEATAGLLYVDDPNWSGIGVVRYEHANDDKSSLKSDPE
GENIHAGLLKKLNELESDLTFKIGPEYKSMKSCLYVGMASDNVDAAELVETIAATAREIE
ENSRLLENMTEVVRKGIQEAQVELQKASEERLLEEGVLRQIPVVGSVLNWFSPVQALQKG
RTFNLTAGSLESTEPIYVYKAQGAGVTLPPTPSGSRTKQRLPGQKPFKRSLRGSDALSET
SSVSHIEDLEKVERLSSGPEQITLEASSTEGHPGAPSPQHTDQTEAFQKGVPHPEDDHSQ
VEGPESLR
|
| Enzyme 65 Number of Residues |
788 |
| Enzyme 65 Molecular Weight |
86706.1 |
| Enzyme 65 Theoretical pI |
5.05 |
| Enzyme 65 GO Classification |
| Function |
- binding
- carbon-carbon lyase activity
- carboxy-lyase activity
- catalytic activity
- cofactor binding
- lyase activity
- pyridoxal phosphate binding
|
| Process |
- carboxylic acid metabolic process
- cellular metabolic process
- metabolic process
- organic acid metabolic process
- oxoacid metabolic process
|
| Component |
| — |
|
| Enzyme 65 General Function |
Involved in carboxy-lyase activity |
| Enzyme 65 Specific Function |
Not Available |
| Enzyme 65 Pathways |
Not Available |
| Enzyme 65 Reactions |
Not Available |
| Enzyme 65 Pfam Domain Function |
|
| Enzyme 65 Signals |
|
| Enzyme 65 Transmembrane Regions |
|
| Enzyme 65 Essentiality |
Not Available |
| Enzyme 65 GenBank ID Protein |
190341074  |
| Enzyme 65 UniProtKB/Swiss-Prot ID |
Q6P996  |
| Enzyme 65 UniProtKB/Swiss-Prot Entry Name |
PDXD1_HUMAN  |
| Enzyme 65 PDB ID |
Not Available |
| Enzyme 65 Cellular Location |
Not Available |
| Enzyme 65 Gene Sequence |
>2367 bp
ATGGACGCGTCCCTGGAGAAGATAGCAGACCCCACGTTAGCTGAAATGGGAAAAAACTTG
AAGGAGGCAGTGAAGATGCTGGAGGACAGTCAGAGAAGAACAGAAGAGGAAAATGGAAAG
AAGCTCATATCCGGAGATATTCCAGGCCCACTCCAGGGCAGTGGGCAAGATATGGTGAGC
ATCCTCCAGTTAGTTCAGAATCTCATGCATGGAGATGAAGATGAGGAGCCCCAGAGCCCC
AGAATCCAAAATATTGGAGAACAAGGTCATATGGCTTTGTTGGGACATAGTCTGGGAGCT
TATATTTCAACTCTGGACAAAGAGAAGCTGAGAAAACTTACAACTAGGATACTTTCAGAT
ACCACCTTATGGCTATGCAGAATTTTCAGATATGAAAATGGGTGTGCTTATTTCCACGAA
GAGGAAAGAGAAGGACTTGCAAAGATATGTAGGCTTGCCATTCATTCTCGATATGAAGAC
TTCGTAGTGGATGGCTTCAATGTGTTATATAACAAGAAGCCTGTCATATATCTTAGTGCT
GCTGCTAGACCTGGCCTGGGCCAATACCTTTGTAATCAGCTCGGCTTGCCCTTCCCCTGC
TTGTGCCGTGTACCCTGTAACACTGTGTTTGGATCCCAGCATCAGATGGATGTTGCCTTC
CTGGAGAAACTGATTAAAGATGATATAGAGCGAGGAAGACTGCCCCTGTTGCTTGTCGCA
AATGCAGGAACGGCAGCAGTAGGACACACAGACAAGATTGGGAGATTGAAAGAACTCTGT
GAGCAGTATGGCATATGGCTTCATGTGGAGGGTGTGAATCTGGCAACATTGGCTCTGGGT
TATGTCTCCTCATCAGTGCTGGCTGCAGCCAAATGTGATAGCATGACGATGACTCCTGGC
CCGTGGCTGGGTTTGCCAGCTGTTCCTGCGGTGACACTGTATAAACACGATGACCCTGCC
TTGACTTTAGTTGCTGGTCTTACATCAAATAAGCCCACAGACAAACTCCGTGCCCTGCCT
CTGTGGTTATCTTTACAATACTTGGGACTTGATGGGTTTGTGGAGAGGATCAAGCATGCC
TGTCAACTGAGTCAACGGTTGCAGGAAAGTTTGAAGAAAGTGAATTACATCAAAATCTTG
GTGGAAGATGAGCTCAGCTCCCCAGTGGTGGTGTTCAGATTTTTCCAGGAATTACCAGGC
TCAGATCCGGTGTTTAAAGCCGTCCCAGTGCCCAACATGACACCTTCAGGAGTCGGCCGG
GAGAGGCACTCGTGTGACGCGCTGAATCGCTGGCTGGGAGAACAGCTGAAGCAGCTGGTG
CCTGCAAGCGGCCTCACAGTCATGGATCTGGAAGCTGAGGGCACGTGTTTGCGGTTCAGC
CCTTTGATGACCGCAGCAGTTTTAGGAACTCGGGGAGAGGATGTGGATCAGCTCGTAGCC
TGCATAGAAAGCAAACTGCCAGTGCTGTGCTGTACGCTCCAGTTGCGTGAAGAGTTCAAG
CAGGAAGTGGAAGCAACAGCAGGTCTCCTATATGTTGATGACCCTAACTGGTCTGGAATA
GGGGTTGTCAGGTATGAACATGCTAATGATGATAAGAGCAGTTTGAAATCAGATCCCGAA
GGGGAAAACATCCATGCTGGACTCCTGAAGAAGTTAAATGAACTGGAATCTGACCTAACC
TTTAAAATAGGCCCTGAGTATAAGAGCATGAAGAGCTGCCTTTATGTCGGCATGGCGAGC
GACAACGTCGATGCTGCTGAGCTCGTGGAGACCATTGCGGCCACAGCCCGGGAGATAGAG
GAGAACTCGAGGCTTCTGGAAAACATGACAGAAGTGGTTCGGAAAGGCATTCAGGAAGCT
CAAGTGGAGCTGCAGAAGGCAAGTGAAGAACGGCTTCTGGAAGAGGGGGTGTTGCGGCAG
ATCCCTGTAGTGGGCTCCGTGCTGAATTGGTTTTCTCCGGTCCAGGCTTTACAGAAGGGA
AGAACTTTTAACTTGACAGCAGGCTCTCTGGAGTCCACAGAACCCATATATGTCTACAAA
GCACAAGGTGCAGGAGTCACGCTGCCTCCAACGCCCTCGGGCAGTCGCACCAAGCAGAGG
CTTCCAGGCCAGAAGCCTTTTAAAAGGTCCCTGCGAGGTTCAGATGCTTTGAGTGAGACC
AGCTCAGTCAGTCACATTGAAGACTTAGAAAAGGTGGAGCGCCTATCCAGTGGGCCGGAG
CAGATCACCCTCGAGGCCAGCAGCACTGAGGGACACCCAGGGGCTCCCAGCCCTCAGCAC
ACCGACCAGACCGAGGCCTTCCAGAAAGGGGTCCCACACCCAGAAGATGACCACTCACAG
GTAGAAGGACCGGAGAGCTTAAGATGA
|
| Enzyme 65 GenBank Gene ID |
NM_015027.2  |
| Enzyme 65 GeneCard ID |
PDXDC1  |
| Enzyme 65 GenAtlas ID |
PDXDC1  |
| Enzyme 65 HGNC ID |
HGNC:28995  |
| Enzyme 65 Chromosome Location |
1 |
| Enzyme 65 Locus |
16p13.11 |
| Enzyme 65 SNPs |
SNPJam Report  |
| Enzyme 65 General References |
- Nagase T, Seki N, Ishikawa K, Ohira M, Kawarabayasi Y, Ohara O, Tanaka A, Kotani H, Miyajima N, Nomura N: Prediction of the coding sequences of unidentified human genes. VI. The coding sequences of 80 new genes (KIAA0201-KIAA0280) deduced by analysis of cDNA clones from cell line KG-1 and brain. DNA Res. 1996 Oct 31;3(5):321-9, 341-54. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed
]
- Beausoleil SA, Villen J, Gerber SA, Rush J, Gygi SP: A probability-based approach for high-throughput protein phosphorylation analysis and site localization. Nat Biotechnol. 2006 Oct;24(10):1285-92. Epub 2006 Sep 10. [PubMed
]
- Matsuoka S, Ballif BA, Smogorzewska A, McDonald ER 3rd, Hurov KE, Luo J, Bakalarski CE, Zhao Z, Solimini N, Lerenthal Y, Shiloh Y, Gygi SP, Elledge SJ: ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage. Science. 2007 May 25;316(5828):1160-6. [PubMed
]
- Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed
]
|
| Enzyme 65 Metabolite References |
Not Available |
|
Enzyme 66
[top]
|
| Enzyme 66 ID |
14705 |
| Enzyme 66 Name |
Pyridoxal-dependent decarboxylase domain-containing protein 2 |
| Enzyme 66 Synonyms |
Not Available |
| Enzyme 66 Gene Name |
PDXDC2 |
| Enzyme 66 Protein Sequence |
>Pyridoxal-dependent decarboxylase domain-containing protein 2
MDASLEKIADPTLAEMGKNLKEAVKMLEDSQRRTEEENGKKLISRDIPGPLQGSGQDMVS
ILQLVQNLMHGDEDEEPQSPRIQNIGEQGHVAVLGHSLGAYILTLDEEKLRKLTTRILSD
TTLWLCRIFRYENGCAYFHEEEREGLAKICRLAIHSQYEDFVVDGFSGLYNKKPVIYLSA
AARPGLGQYLCNQLGLPFPCLCRVPCNTMFGSQHQMDVAFLEKLIKDDIERGRLPLLLVA
NAGTAAVGHTDKIGRLKELCEQYGIWLHVEGVNLATLALGYVSSSVLAAAKCDSMTMTPG
PWLGLPAVPAVTLYKHDPALTLVAGLISNKPTDKLRALPLWLSLQYLGLDGFVERIKHAC
QLSQWLQESLKKVNYIKILVEDELSSPVVVFRFFQELPGSDPVFKAVPVPNMTPSAVGRE
RHSCDALNLWLGEQLKQLVPASGLTVMDLEAEGTCLRFSPLMTAAGMIS
|
| Enzyme 66 Number of Residues |
469 |
| Enzyme 66 Molecular Weight |
51809.5 |
| Enzyme 66 Theoretical pI |
5.81 |
| Enzyme 66 GO Classification |
| Function |
- binding
- carbon-carbon lyase activity
- carboxy-lyase activity
- catalytic activity
- cofactor binding
- lyase activity
- pyridoxal phosphate binding
|
| Process |
- carboxylic acid metabolic process
- cellular metabolic process
- metabolic process
- organic acid metabolic process
- oxoacid metabolic process
|
| Component |
| — |
|
| Enzyme 66 General Function |
Involved in carboxy-lyase activity |
| Enzyme 66 Specific Function |
Not Available |
| Enzyme 66 Pathways |
Not Available |
| Enzyme 66 Reactions |
Not Available |
| Enzyme 66 Pfam Domain Function |
|
| Enzyme 66 Signals |
|
| Enzyme 66 Transmembrane Regions |
|
| Enzyme 66 Essentiality |
Not Available |
| Enzyme 66 GenBank ID Protein |
158259181  |
| Enzyme 66 UniProtKB/Swiss-Prot ID |
Q6P474  |
| Enzyme 66 UniProtKB/Swiss-Prot Entry Name |
PDXD2_HUMAN  |
| Enzyme 66 PDB ID |
Not Available |
| Enzyme 66 Cellular Location |
Not Available |
| Enzyme 66 Gene Sequence |
>1410 bp
ATGGACGCGTCCCTGGAGAAGATAGCAGACCCCACGTTAGCTGAAATGGGAAAAAACTTG
AAGGAGGCAGTGAAGATGCTGGAGGACAGTCAGAGAAGAACAGAAGAGGAAAATGGAAAG
AAGCTCATATCCAGAGATATTCCAGGCCCACTCCAGGGCAGTGGACAAGATATGGTGAGC
ATCCTCCAGTTAGTTCAGAATCTGATGCATGGAGATGAAGATGAGGAGCCCCAGAGCCCC
AGAATCCAAAATATTGGAGAACAAGGTCATGTGGCTGTGTTGGGACATAGTCTGGGAGCT
TATATTTTGACTCTGGACGAAGAGAAGCTGAGAAAACTTACAACTAGGATACTTTCAGAT
ACCACCTTATGGCTATGCAGAATTTTCAGATATGAAAATGGGTGTGCTTATTTCCACGAA
GAGGAAAGAGAAGGACTTGCAAAGATATGTAGGCTTGCCATTCATTCTCAATATGAAGAC
TTCGTAGTGGATGGCTTCAGTGGGTTATATAACAAGAAGCCTGTCATATATCTTAGTGCT
GCTGCTAGACCTGGCCTGGGCCAATACCTTTGTAATCAGCTCGGCTTGCCCTTCCCCTGC
TTGTGCCGTGTACCCTGTAACACTATGTTTGGATCCCAGCATCAGATGGATGTTGCCTTC
CTGGAGAAACTGATTAAAGATGATATAGAGCGAGGAAGACTGCCCCTGTTGCTTGTCGCA
AATGCAGGAACGGCAGCAGTAGGACACACAGACAAGATTGGGAGATTGAAAGAACTCTGT
GAGCAGTATGGCATATGGCTTCATGTGGAGGGTGTGAATCTGGCAACATTGGCTCTGGGT
TATGTCTCCTCATCAGTGCTGGCTGCAGCCAAATGTGATAGCATGACGATGACTCCTGGC
CCGTGGCTGGGTTTGCCAGCTGTTCCTGCGGTGACACTGTATAAACACGACCCTGCCTTG
ACTTTAGTTGCTGGTCTTATATCAAATAAGCCCACAGACAAACTCCGTGCCCTGCCTCTG
TGGTTATCTTTACAATACTTGGGACTTGATGGGTTTGTGGAGAGGATCAAGCATGCCTGT
CAACTGAGTCAATGGTTGCAGGAAAGTTTGAAGAAAGTGAATTACATCAAAATCTTGGTG
GAAGATGAGCTCAGCTCCCCAGTGGTGGTGTTCAGATTTTTCCAAGAATTACCAGGCTCA
GATCCAGTGTTTAAAGCCGTCCCAGTGCCCAACATGACACCTTCAGCAGTCGGCCGGGAG
AGGCACTCGTGTGATGCGCTGAATCTCTGGCTGGGAGAACAGCTGAAGCAGCTGGTGCCT
GCGAGCGGCCTCACAGTCATGGATCTGGAAGCTGAGGGCACGTGTTTGCGGTTCAGCCCT
TTGATGACCGCAGCAGGTATGATCTCGTGA
|
| Enzyme 66 GenBank Gene ID |
AK292860  |
| Enzyme 66 GeneCard ID |
PDXDC2  |
| Enzyme 66 GenAtlas ID |
PDXDC2  |
| Enzyme 66 HGNC ID |
HGNC:27559  |
| Enzyme 66 Chromosome Location |
1 |
| Enzyme 66 Locus |
16q22.1 |
| Enzyme 66 SNPs |
SNPJam Report  |
| Enzyme 66 General References |
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
- Martin J, Han C, Gordon LA, Terry A, Prabhakar S, She X, Xie G, Hellsten U, Chan YM, Altherr M, Couronne O, Aerts A, Bajorek E, Black S, Blumer H, Branscomb E, Brown NC, Bruno WJ, Buckingham JM, Callen DF, Campbell CS, Campbell ML, Campbell EW, Caoile C, Challacombe JF, Chasteen LA, Chertkov O, Chi HC, Christensen M, Clark LM, Cohn JD, Denys M, Detter JC, Dickson M, Dimitrijevic-Bussod M, Escobar J, Fawcett JJ, Flowers D, Fotopulos D, Glavina T, Gomez M, Gonzales E, Goodstein D, Goodwin LA, Grady DL, Grigoriev I, Groza M, Hammon N, Hawkins T, Haydu L, Hildebrand CE, Huang W, Israni S, Jett J, Jewett PB, Kadner K, Kimball H, Kobayashi A, Krawczyk MC, Leyba T, Longmire JL, Lopez F, Lou Y, Lowry S, Ludeman T, Manohar CF, Mark GA, McMurray KL, Meincke LJ, Morgan J, Moyzis RK, Mundt MO, Munk AC, Nandkeshwar RD, Pitluck S, Pollard M, Predki P, Parson-Quintana B, Ramirez L, Rash S, Retterer J, Ricke DO, Robinson DL, Rodriguez A, Salamov A, Saunders EH, Scott D, Shough T, Stallings RL, Stalvey M, Sutherland RD, Tapia R, Tesmer JG, Thayer N, Thompson LS, Tice H, Torney DC, Tran-Gyamfi M, Tsai M, Ulanovsky LE, Ustaszewska A, Vo N, White PS, Williams AL, Wills PL, Wu JR, Wu K, Yang J, Dejong P, Bruce D, Doggett NA, Deaven L, Schmutz J, Grimwood J, Richardson P, Rokhsar DS, Eichler EE, Gilna P, Lucas SM, Myers RM, Rubin EM, Pennacchio LA: The sequence and analysis of duplication-rich human chromosome 16. Nature. 2004 Dec 23;432(7020):988-94. [PubMed
]
|
| Enzyme 66 Metabolite References |
Not Available |
|
Enzyme 67
[top]
|
| Enzyme 67 ID |
14706 |
| Enzyme 67 Name |
Serine dehydratase-like |
| Enzyme 67 Synonyms |
- L-serine deaminase
- L-serine dehydratase/L-threonine deaminase
- L-threonine dehydratase
- TDH
- Serine dehydratase 2
- SDH 2
|
| Enzyme 67 Gene Name |
SDSL |
| Enzyme 67 Protein Sequence |
>Serine dehydratase-like
MDGPVAEHAKQEPFHVVTPLLESWALSQVAGMPVFLKCENVQPSGSFKIRGIGHFCQEMA
KKGCRHLVCSSGGNAGIAAAYAARKLGIPATIVLPESTSLQVVQRLQGEGAEVQLTGKVW
DEANLRAQELAKRDGWENVPPFDHPLIWKGHASLVQELKAVLRTPPGALVLAVGGGGLLA
GVVAGLLEVGWQHVPIIAMETHGAHCFNAAITAGKLVTLPDITSVAKSLGAKTVAARALE
CMQVCKIHSEVVEDTEAVSAVQQLLDDERMLVEPACGAALAAIYSGLLRRLQAEGCLPPS
LTSVVVIVCGGNNINSRELQALKTHLGQV
|
| Enzyme 67 Number of Residues |
329 |
| Enzyme 67 Molecular Weight |
34674.0 |
| Enzyme 67 Theoretical pI |
6.88 |
| Enzyme 67 GO Classification |
| Function |
- binding
- catalytic activity
- cofactor binding
- pyridoxal phosphate binding
|
| Process |
- cellular amino acid and derivative metabolic process
- cellular amino acid metabolic process
- cellular metabolic process
- metabolic process
|
| Component |
| — |
|
| Enzyme 67 General Function |
Involved in catalytic activity |
| Enzyme 67 Specific Function |
Has low serine dehydratase and threonine dehydratase activity |
| Enzyme 67 Pathways |
Not Available |
| Enzyme 67 Reactions |
- L-threonine = 2-oxobutanoate + NH3 [RN:R00996]
|
| Enzyme 67 Pfam Domain Function |
|
| Enzyme 67 Signals |
|
| Enzyme 67 Transmembrane Regions |
|
| Enzyme 67 Essentiality |
Not Available |
| Enzyme 67 GenBank ID Protein |
Not Available |
| Enzyme 67 UniProtKB/Swiss-Prot ID |
Q96GA7  |
| Enzyme 67 UniProtKB/Swiss-Prot Entry Name |
SDSL_HUMAN  |
| Enzyme 67 PDB ID |
Not Available |
| Enzyme 67 Cellular Location |
Not Available |
| Enzyme 67 Gene Sequence |
>990 bp
ATGGACGGCCCTGTGGCAGAGCATGCCAAGCAGGAGCCCTTTCACGTGGTCACACCTCTG
TTGGAGAGCTGGGCGCTGTCCCAGGTGGCGGGCATGCCTGTCTTCCTCAAGTGTGAGAAT
GTGCAGCCCAGCGGCTCCTTCAAGATTCGGGGCATTGGGCATTTCTGCCAGGAGATGGCC
AAGAAGGGATGCAGACACCTGGTGTGCTCCTCAGGGGGTAATGCGGGCATCGCTGCTGCC
TATGCTGCTAGGAAGCTGGGCATTCCTGCCACCATCGTGCTCCCCGAGAGCACCTCCCTG
CAGGTGGTGCAGAGGCTGCAGGGGGAGGGGGCCGAGGTTCAGCTGACTGGAAAGGTCTGG
GACGAGGCCAATCTGAGGGCGCAAGAGTTGGCCAAGAGGGACGGCTGGGAGAATGTCCCC
CCGTTTGACCACCCCCTAATATGGAAAGGCCACGCCAGCCTGGTGCAGGAGCTGAAAGCA
GTGCTGAGGACCCCACCAGGTGCCCTGGTGCTGGCAGTTGGGGGTGGGGGTCTCCTGGCC
GGGGTGGTGGCTGGCCTGCTGGAGGTGGGCTGGCAGCATGTACCCATCATTGCCATGGAG
ACCCATGGGGCACACTGCTTCAATGCGGCCATCACAGCCGGCAAGCTGGTCACACTTCCA
GACATCACCAGTGTGGCCAAGAGCCTGGGTGCCAAGACGGTGGCCGCTCGGGCCCTGGAG
TGCATGCAGGTGTGCAAGATTCACTCTGAAGTGGTGGAGGACACCGAGGCTGTGAGCGCT
GTGCAGCAGCTCCTGGATGATGAGCGTATGCTGGTGGAGCCTGCCTGTGGGGCAGCCTTA
GCAGCCATCTACTCAGGCCTCCTGCGGAGGCTCCAGGCCGAGGGCTGCCTGCCCCCTTCC
CTGACTTCAGTTGTGGTAATCGTGTGTGGAGGCAACAACATCAACAGCCGAGAGCTGCAG
GCTTTGAAAACCCACCTGGGCCAGGTCTGA
|
| Enzyme 67 GenBank Gene ID |
AF134473  |
| Enzyme 67 GeneCard ID |
SDSL  |
| Enzyme 67 GenAtlas ID |
SDSL  |
| Enzyme 67 HGNC ID |
HGNC:30404  |
| Enzyme 67 Chromosome Location |
1 |
| Enzyme 67 Locus |
12q24.13 |
| Enzyme 67 SNPs |
SNPJam Report  |
| Enzyme 67 General References |
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Yamada T, Komoto J, Kasuya T, Takata Y, Ogawa H, Mori H, Takusagawa F: A catalytic mechanism that explains a low catalytic activity of serine dehydratase like-1 from human cancer cells: crystal structure and site-directed mutagenesis studies. Biochim Biophys Acta. 2008 May;1780(5):809-18. Epub 2008 Feb 19. [PubMed
]
|
| Enzyme 67 Metabolite References |
Not Available |
|
Enzyme 68
[top]
|
| Enzyme 68 ID |
14707 |
| Enzyme 68 Name |
O-phosphoseryl-tRNA(Sec) selenium transferase |
| Enzyme 68 Synonyms |
- Liver-pancreas antigen
- LP
- SLA-p35
- SLA/LP autoantigen
- Selenocysteine synthase
- Sec synthase
- Selenocysteinyl-tRNA(Sec) synthase
- Sep-tRNA:Sec-tRNA synthase
- SepSecS
- Soluble liver antigen
- SLA
- UGA suppressor tRNA-associated protein
- tRNA(Ser/Sec)-associated antigenic protein
|
| Enzyme 68 Gene Name |
SEPSECS |
| Enzyme 68 Protein Sequence |
>O-phosphoseryl-tRNA(Sec) selenium transferase
MNRESFAAGERLVSPAYVRQGCEARRSHEHLIRLLLEKGKCPENGWDESTLELFLHELAI
MDSNNFLGNCGVGEREGRVASALVARRHYRFIHGIGRSGDISAVQPKAAGSSLLNKITNS
LVLDIIKLAGVHTVANCFVVPMATGMSLTLCFLTLRHKRPKAKYIIWPRIDQKSCFKSMI
TAGFEPVVIENVLEGDELRTDLKAVEAKVQELGPDCILCIHSTTSCFAPRVPDRLEELAV
ICANYDIPHIVNNAYGVQSSKCMHLIQQGARVGRIDAFVQSLDKNFMVPVGGAIIAGFND
SFIQEISKMYPGRASASPSLDVLITLLSLGSNGYKKLLKERKEMFSYLSNQIKKLSEAYN
ERLLHTPHNPISLAMTLKTLDEHRDKAVTQLGSMLFTRQVSGARVVPLGSMQTVSGYTFR
GFMSHTNNYPCAYLNAASAIGMKMQDVDLFIKRLDRCLKAVRKERSKESDDNYDKTEDVD
IEEMALKLDNVLLDTYQDASS
|
| Enzyme 68 Number of Residues |
501 |
| Enzyme 68 Molecular Weight |
55725.7 |
| Enzyme 68 Theoretical pI |
8.13 |
| Enzyme 68 GO Classification |
Not Available |
| Enzyme 68 General Function |
Involved in catalytic activity |
| Enzyme 68 Specific Function |
Converts O-phosphoseryl-tRNA(Sec) to selenocysteinyl- tRNA(Sec) required for selenoprotein biosynthesis |
| Enzyme 68 Pathways |
Not Available |
| Enzyme 68 Reactions |
- O-phospho-L-seryl-tRNASec + selenophosphate = L-selenocysteinyl-tRNASec + phosphate [RN:R08224]
|
| Enzyme 68 Pfam Domain Function |
|
| Enzyme 68 Signals |
|
| Enzyme 68 Transmembrane Regions |
|
| Enzyme 68 Essentiality |
Not Available |
| Enzyme 68 GenBank ID Protein |
267844904  |
| Enzyme 68 UniProtKB/Swiss-Prot ID |
Q9HD40  |
| Enzyme 68 UniProtKB/Swiss-Prot Entry Name |
SPCS_HUMAN  |
| Enzyme 68 PDB ID |
Not Available |
| Enzyme 68 Cellular Location |
Not Available |
| Enzyme 68 Gene Sequence |
>1506 bp
ATGAACCGCGAGAGCTTCGCGGCGGGAGAGCGGCTGGTGTCGCCGGCTTACGTGCGGCAG
GGCTGTGAGGCCCGCCGCTCGCATGAGCACCTCATACGGCTGCTTCTGGAGAAGGGCAAG
TGTCCAGAGAATGGCTGGGATGAAAGTACACTTGAACTCTTTTTACATGAACTTGCAATC
ATGGACAGCAACAATTTCTTAGGCAATTGTGGTGTGGGAGAAAGGGAAGGGAGAGTGGCA
TCCGCACTGGTTGCTCGTCGTCATTACAGGTTCATTCATGGCATTGGACGATCCGGTGAT
ATTTCTGCTGTGCAACCAAAAGCTGCAGGCTCTAGCCTTTTGAACAAAATTACCAATTCT
TTGGTCCTGGACATTATAAAGCTGGCTGGTGTCCATACAGTAGCCAACTGCTTTGTAGTT
CCTATGGCAACTGGTATGAGTCTAACTCTGTGTTTCTTAACATTACGACACAAAAGACCA
AAGGCAAAGTATATTATATGGCCACGAATAGACCAGAAGTCCTGCTTTAAATCCATGATC
ACTGCAGGTTTTGAGCCTGTGGTGATAGAAAATGTTTTGGAAGGTGACGAGCTGCGTACA
GACCTGAAAGCAGTGGAGGCTAAAGTCCAGGAACTTGGGCCTGATTGCATTCTGTGTATT
CATTCTACTACATCCTGTTTTGCTCCAAGGGTGCCTGATAGATTAGAAGAACTGGCTGTG
ATTTGTGCTAATTATGACATTCCACATATAGTTAATAATGCTTATGGAGTGCAGTCTTCA
AAGTGTATGCATCTCATTCAGCAGGGGGCTCGAGTTGGTAGAATAGATGCTTTTGTTCAG
AGCTTGGACAAAAATTTTATGGTTCCAGTAGGTGGTGCTATAATTGCTGGCTTTAATGAT
TCATTCATTCAGGAAATCAGCAAGATGTATCCAGGAAGAGCTTCAGCTTCACCTTCTTTA
GATGTCCTTATTACTTTATTGTCACTTGGATCAAATGGCTATAAGAAGCTACTAAAAGAA
AGAAAGGAAATGTTTTCATATTTGTCCAACCAAATAAAGAAGTTGTCAGAAGCCTACAAT
GAAAGACTGTTGCATACACCTCACAATCCCATATCTTTAGCTATGACACTTAAAACACTA
GATGAACACCGTGACAAAGCTGTCACTCAGCTTGGCTCGATGCTTTTTACCAGACAGGTT
TCTGGAGCCAGGGTTGTGCCTCTTGGGTCCATGCAAACTGTGAGTGGCTATACTTTCAGA
GGCTTTATGTCACATACAAATAATTACCCTTGTGCTTACCTCAATGCTGCATCAGCCATC
GGAATGAAGATGCAGGATGTGGACCTGTTCATAAAGAGACTTGACAGGTGTTTAAAGGCA
GTAAGAAAAGAACGAAGTAAAGAGAGTGATGACAATTATGACAAAACTGAAGATGTGGAT
ATTGAAGAAATGGCTTTAAAACTAGATAATGTACTTCTTGACACATACCAGGATGCTTCT
TCATGA
|
| Enzyme 68 GenBank Gene ID |
NM_016955.3  |
| Enzyme 68 GeneCard ID |
SEPSECS  |
| Enzyme 68 GenAtlas ID |
SEPSECS  |
| Enzyme 68 HGNC ID |
HGNC:30605  |
| Enzyme 68 Chromosome Location |
4 |
| Enzyme 68 Locus |
4p15.2 |
| Enzyme 68 SNPs |
SNPJam Report  |
| Enzyme 68 General References |
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
- Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed
]
- Hillier LW, Graves TA, Fulton RS, Fulton LA, Pepin KH, Minx P, Wagner-McPherson C, Layman D, Wylie K, Sekhon M, Becker MC, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Kremitzki C, Oddy L, Du H, Sun H, Bradshaw-Cordum H, Ali J, Carter J, Cordes M, Harris A, Isak A, van Brunt A, Nguyen C, Du F, Courtney L, Kalicki J, Ozersky P, Abbott S, Armstrong J, Belter EA, Caruso L, Cedroni M, Cotton M, Davidson T, Desai A, Elliott G, Erb T, Fronick C, Gaige T, Haakenson W, Haglund K, Holmes A, Harkins R, Kim K, Kruchowski SS, Strong CM, Grewal N, Goyea E, Hou S, Levy A, Martinka S, Mead K, McLellan MD, Meyer R, Randall-Maher J, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Shah N, Swearengen-Shahid S, Snider J, Strong JT, Thompson J, Yoakum M, Leonard S, Pearman C, Trani L, Radionenko M, Waligorski JE, Wang C, Rock SM, Tin-Wollam AM, Maupin R, Latreille P, Wendl MC, Yang SP, Pohl C, Wallis JW, Spieth J, Bieri TA, Berkowicz N, Nelson JO, Osborne J, Ding L, Meyer R, Sabo A, Shotland Y, Sinha P, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Jones TA, She X, Ciccarelli FD, Izaurralde E, Taylor J, Schmutz J, Myers RM, Cox DR, Huang X, McPherson JD, Mardis ER, Clifton SW, Warren WC, Chinwalla AT, Eddy SR, Marra MA, Ovcharenko I, Furey TS, Miller W, Eichler EE, Bork P, Suyama M, Torrents D, Waterston RH, Wilson RK: Generation and annotation of the DNA sequences of human chromosomes 2 and 4. Nature. 2005 Apr 7;434(7034):724-31. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Wies I, Brunner S, Henninger J, Herkel J, Kanzler S, Meyer zum Buschenfelde KH, Lohse AW: Identification of target antigen for SLA/LP autoantibodies in autoimmune hepatitis. Lancet. 2000 Apr 29;355(9214):1510-5. [PubMed
]
- Costa M, Rodriguez-Sanchez JL, Czaja AJ, Gelpi C: Isolation and characterization of cDNA encoding the antigenic protein of the human tRNP(Ser)Sec complex recognized by autoantibodies from patients withtype-1 autoimmune hepatitis. Clin Exp Immunol. 2000 Aug;121(2):364-74. [PubMed
]
- Volkmann M, Martin L, Baurle A, Heid H, Strassburg CP, Trautwein C, Fiehn W, Manns MP: Soluble liver antigen: isolation of a 35-kd recombinant protein (SLA-p35) specifically recognizing sera from patients with autoimmune hepatitis. Hepatology. 2001 Mar;33(3):591-6. [PubMed
]
- Herkel J, Heidrich B, Nieraad N, Wies I, Rother M, Lohse AW: Fine specificity of autoantibodies to soluble liver antigen and liver/pancreas. Hepatology. 2002 Feb;35(2):403-8. [PubMed
]
- Yuan J, Palioura S, Salazar JC, Su D, O'Donoghue P, Hohn MJ, Cardoso AM, Whitman WB, Soll D: RNA-dependent conversion of phosphoserine forms selenocysteine in eukaryotes and archaea. Proc Natl Acad Sci U S A. 2006 Dec 12;103(50):18923-7. Epub 2006 Dec 1. [PubMed
]
- Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed
]
|
| Enzyme 68 Metabolite References |
Not Available |
|
Enzyme 69
[top]
|
| Enzyme 69 ID |
14708 |
| Enzyme 69 Name |
Serine palmitoyltransferase 3 |
| Enzyme 69 Synonyms |
- Long chain base biosynthesis protein 2b
- LCB2b
- Long chain base biosynthesis protein 3
- LCB 3
- Serine-palmitoyl-CoA transferase 3
- SPT 3
|
| Enzyme 69 Gene Name |
SPTLC3 |
| Enzyme 69 Protein Sequence |
>Serine palmitoyltransferase 3
MANPGGGAVCNGKLHNHKKQSNGSQSRNCTKNGIVKEAQQNGKPHFYDKLIVESFEEAPL
HVMVFTYMGYGIGTLFGYLRDFLRNWGIEKCNAAVERKEQKDFVPLYQDFENFYTRNLYM
RIRDNWNRPICSAPGPLFDLMERVSDDYNWTFRFTGRVIKDVINMGSYNFLGLAAKYDES
MRTIKDVLEVYGTGVASTRHEMGTLDKHKELEDLVAKFLNVEAAMVFGMGFATNSMNIPA
LVGKGCLILSDELNHTSLVLGARLSGATIRIFKHNNTQSLEKLLRDAVIYGQPRTRRAWK
KILILVEGVYSMEGSIVHLPQIIALKKKYKAYLYIDEAHSIGAVGPTGRGVTEFFGLDPH
EVDVLMGTFTKSFGASGGYIAGRKDLVDYLRVHSHSAVYASSMSPPIAEQIIRSLKLIMG
LDGTTQGLQRVQQLAKNTRYFRQRLQEMGFIIYGNENASVVPLLLYMPGKVAAFARHMLE
KKIGVVVVGFPATPLAEARARFCVSAAHTREMLDTVLEALDEMGDLLQLKYSRHKKSARP
ELYDETSFELED
|
| Enzyme 69 Number of Residues |
552 |
| Enzyme 69 Molecular Weight |
62049.0 |
| Enzyme 69 Theoretical pI |
9.05 |
| Enzyme 69 GO Classification |
| Function |
- binding
- catalytic activity
- cofactor binding
- pyridoxal phosphate binding
- transferase activity
- transferase activity, transferring nitrogenous groups
|
| Process |
- biosynthetic process
- metabolic process
|
| Component |
| — |
|
| Enzyme 69 General Function |
Involved in transferase activity |
| Enzyme 69 Specific Function |
Serine palmitoyltransferase (SPT). The heterodimer formed with LCB1/SPTLC1 constitutes the catalytic core. The composition of the serine palmitoyltransferase (SPT) complex determines the substrate preference. The SPTLC1-SPTLC3-SSSPTA isozyme uses both C14-CoA and C16-CoA as substrates, while the SPTLC1-SPTLC3-SSSPTB has the ability to use a broader range of acyl-CoAs without apparent preference |
| Enzyme 69 Pathways |
|
| Enzyme 69 Reactions |
- palmitoyl-CoA + L-serine = CoA + 3-dehydro-D-sphinganine + CO2 [RN:R01281]
|
| Enzyme 69 Pfam Domain Function |
|
| Enzyme 69 Signals |
|
| Enzyme 69 Transmembrane Regions |
|
| Enzyme 69 Essentiality |
Not Available |
| Enzyme 69 GenBank ID Protein |
119220554  |
| Enzyme 69 UniProtKB/Swiss-Prot ID |
Q9NUV7  |
| Enzyme 69 UniProtKB/Swiss-Prot Entry Name |
SPTC3_HUMAN  |
| Enzyme 69 PDB ID |
Not Available |
| Enzyme 69 Cellular Location |
Not Available |
| Enzyme 69 Gene Sequence |
>1659 bp
ATGGCTAACCCTGGAGGTGGTGCTGTTTGCAACGGGAAACTTCACAATCACAAGAAACAG
AGCAATGGCTCACAAAGCAGAAACTGCACAAAGAATGGAATAGTGAAGGAAGCCCAGCAA
AATGGGAAGCCACATTTTTATGATAAGCTCATTGTTGAATCGTTTGAGGAAGCACCCCTT
CATGTTATGGTTTTCACTTACATGGGATATGGAATTGGAACCCTGTTTGGCTATCTCAGA
GACTTTTTAAGAAACTGGGGAATAGAAAAATGCAACGCAGCTGTGGAACGAAAAGAACAA
AAAGATTTTGTGCCACTGTATCAAGACTTTGAAAATTTTTATACAAGAAACCTTTACATG
CGAATCAGAGACAACTGGAACCGGCCCATCTGCAGTGCCCCAGGGCCTCTGTTTGATTTG
ATGGAGAGGGTATCAGACGACTATAACTGGACGTTTAGGTTTACTGGAAGAGTCATCAAA
GATGTCATCAACATGGGCTCCTATAACTTCCTTGGTCTTGCAGCCAAGTATGATGAGTCT
ATGAGGACAATAAAGGATGTTTTAGAGGTGTATGGCACAGGCGTGGCCAGCACCAGGCAT
GAAATGGGCACCTTGGATAAGCACAAGGAGTTGGAGGACCTTGTGGCTAAGTTCCTGAAT
GTGGAAGCAGCTATGGTCTTTGGGATGGGATTCGCAACTAACTCAATGAATATCCCAGCA
TTAGTTGGAAAGGGATGCCTCATTTTAAGTGATGAGTTAAACCACACATCGCTTGTGCTT
GGGGCCCGACTCTCAGGTGCAACCATAAGAATCTTCAAACACAACAACACACAAAGCCTA
GAGAAGCTCCTGAGAGATGCTGTCATCTATGGCCAGCCTCGAACCCGCAGAGCTTGGAAA
AAGATTCTCATCCTGGTGGAGGGTGTCTACAGCATGGAAGGTTCCATCGTGCATCTGCCC
CAGATCATAGCTCTAAAGAAGAAATACAAGGCTTACCTCTACATAGATGAAGCTCACAGT
ATTGGGGCCGTGGGCCCAACCGGCCGGGGTGTCACGGAGTTCTTTGGACTAGACCCTCAT
GAAGTTGATGTGCTCATGGGCACATTCACCAAAAGTTTTGGAGCTTCAGGAGGTTACATA
GCTGGAAGGAAGGACCTCGTGGATTATTTACGGGTTCACTCGCATAGTGCTGTTTATGCT
TCATCCATGAGCCCACCGATAGCAGAGCAAATCATCAGATCACTAAAACTTATCATGGGA
CTGGATGGGACCACTCAAGGGCTGCAGAGAGTACAGCAACTTGCGAAAAACACAAGATAC
TTCAGACAAAGACTGCAGGAAATGGGATTCATTATCTATGGCAATGAGAATGCTTCTGTT
GTTCCTCTGCTTCTTTATATGCCTGGTAAAGTAGCGGCTTTTGCAAGGCATATGCTAGAG
AAAAAAATTGGAGTGGTGGTCGTGGGATTTCCAGCCACTCCCCTCGCAGAAGCTCGGGCT
CGGTTTTGTGTTTCAGCGGCACATACCCGGGAGATGTTAGACACGGTTTTAGAAGCTCTT
GATGAAATGGGTGATCTCTTGCAACTGAAATATTCCCGGCACAAGAAGTCAGCACGTCCT
GAGCTCTATGATGAGACGAGCTTTGAACTCGAAGATTAA
|
| Enzyme 69 GenBank Gene ID |
NM_018327.2  |
| Enzyme 69 GeneCard ID |
SPTLC3  |
| Enzyme 69 GenAtlas ID |
SPTLC3  |
| Enzyme 69 HGNC ID |
HGNC:16253  |
| Enzyme 69 Chromosome Location |
2 |
| Enzyme 69 Locus |
20p12.1 |
| Enzyme 69 SNPs |
SNPJam Report  |
| Enzyme 69 General References |
- Hornemann T, Richard S, Rutti MF, Wei Y, von Eckardstein A: Cloning and initial characterization of a new subunit for mammalian serine-palmitoyltransferase. J Biol Chem. 2006 Dec 8;281(49):37275-81. Epub 2006 Oct 4. [PubMed
]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
- Deloukas P, Matthews LH, Ashurst J, Burton J, Gilbert JG, Jones M, Stavrides G, Almeida JP, Babbage AK, Bagguley CL, Bailey J, Barlow KF, Bates KN, Beard LM, Beare DM, Beasley OP, Bird CP, Blakey SE, Bridgeman AM, Brown AJ, Buck D, Burrill W, Butler AP, Carder C, Carter NP, Chapman JC, Clamp M, Clark G, Clark LN, Clark SY, Clee CM, Clegg S, Cobley VE, Collier RE, Connor R, Corby NR, Coulson A, Coville GJ, Deadman R, Dhami P, Dunn M, Ellington AG, Frankland JA, Fraser A, French L, Garner P, Grafham DV, Griffiths C, Griffiths MN, Gwilliam R, Hall RE, Hammond S, Harley JL, Heath PD, Ho S, Holden JL, Howden PJ, Huckle E, Hunt AR, Hunt SE, Jekosch K, Johnson CM, Johnson D, Kay MP, Kimberley AM, King A, Knights A, Laird GK, Lawlor S, Lehvaslaiho MH, Leversha M, Lloyd C, Lloyd DM, Lovell JD, Marsh VL, Martin SL, McConnachie LJ, McLay K, McMurray AA, Milne S, Mistry D, Moore MJ, Mullikin JC, Nickerson T, Oliver K, Parker A, Patel R, Pearce TA, Peck AI, Phillimore BJ, Prathalingam SR, Plumb RW, Ramsay H, Rice CM, Ross MT, Scott CE, Sehra HK, Shownkeen R, Sims S, Skuce CD, Smith ML, Soderlund C, Steward CA, Sulston JE, Swann M, Sycamore N, Taylor R, Tee L, Thomas DW, Thorpe A, Tracey A, Tromans AC, Vaudin M, Wall M, Wallis JM, Whitehead SL, Whittaker P, Willey DL, Williams L, Williams SA, Wilming L, Wray PW, Hubbard T, Durbin RM, Bentley DR, Beck S, Rogers J: The DNA sequence and comparative analysis of human chromosome 20. Nature. 2001 Dec 20-27;414(6866):865-71. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Han G, Gupta SD, Gable K, Niranjanakumari S, Moitra P, Eichler F, Brown RH Jr, Harmon JM, Dunn TM: Identification of small subunits of mammalian serine palmitoyltransferase that confer distinct acyl-CoA substrate specificities. Proc Natl Acad Sci U S A. 2009 May 19;106(20):8186-91. Epub 2009 May 5. [PubMed
]
|
| Enzyme 69 Metabolite References |
Not Available |
|
Enzyme 70
[top]
|
| Enzyme 70 ID |
14709 |
| Enzyme 70 Name |
Serine racemase |
| Enzyme 70 Synonyms |
Not Available |
| Enzyme 70 Gene Name |
SRR |
| Enzyme 70 Protein Sequence |
>Serine racemase
MCAQYCISFADVEKAHINIRDSIHLTPVLTSSILNQLTGRNLFFKCELFQKTGSFKIRGA
LNAVRSLVPDALERKPKAVVTHSSGNHGQALTYAAKLEGIPAYIVVPQTAPDCKKLAIQA
YGASIVYCEPSDESRENVAKRVTEETEGIMVHPNQEPAVIAGQGTIALEVLNQVPLVDAL
VVPVGGGGMLAGIAITVKALKPSVKVYAAEPSNADDCYQSKLKGKLMPNLYPPETIADGV
KSSIGLNTWPIIRDLVDDIFTVTEDEIKCATQLVWERMKLLIEPTAGVGVAAVLSQHFQT
VSPEVKNICIVLSGGNVDLTSSITWVKQAERPASYQSVSV
|
| Enzyme 70 Number of Residues |
340 |
| Enzyme 70 Molecular Weight |
36565.9 |
| Enzyme 70 Theoretical pI |
6.51 |
| Enzyme 70 GO Classification |
| Function |
- binding
- catalytic activity
- cofactor binding
- pyridoxal phosphate binding
|
| Process |
- cellular amino acid and derivative metabolic process
- cellular amino acid metabolic process
- cellular metabolic process
- metabolic process
|
| Component |
| — |
|
| Enzyme 70 General Function |
Involved in catalytic activity |
| Enzyme 70 Specific Function |
Catalyzes the synthesis of D-serine from L-serine |
| Enzyme 70 Pathways |
Not Available |
| Enzyme 70 Reactions |
- L-serine = D-serine [RN:R00589]
|
| Enzyme 70 Pfam Domain Function |
|
| Enzyme 70 Signals |
|
| Enzyme 70 Transmembrane Regions |
|
| Enzyme 70 Essentiality |
Not Available |
| Enzyme 70 GenBank ID Protein |
Not Available |
| Enzyme 70 UniProtKB/Swiss-Prot ID |
Q9GZT4  |
| Enzyme 70 UniProtKB/Swiss-Prot Entry Name |
SRR_HUMAN  |
| Enzyme 70 PDB ID |
Not Available |
| Enzyme 70 Cellular Location |
Not Available |
| Enzyme 70 Gene Sequence |
>1023 bp
ATGTGTGCTCAGTATTGCATCTCCTTTGCTGATGTTGAAAAAGCTCATATCAACATTCGA
GATTCTATCCACCTCACACCAGTGCTAACAAGCTCCATTTTGAATCAACTAACAGGGCGC
AATCTTTTCTTCAAATGTGAACTCTTCCAGAAAACAGGATCTTTTAAGATTCGTGGTGCT
CTCAATGCCGTCAGAAGCTTGGTTCCTGATGCTTTAGAAAGGAAGCCGAAAGCTGTTGTT
ACTCACAGCAGTGGAAACCATGGCCAGGCTCTCACCTATGCTGCCAAATTGGAAGGAATT
CCTGCTTATATTGTGGTGCCCCAGACAGCTCCAGACTGTAAAAAACTTGCAATACAAGCC
TACGGAGCGTCAATTGTATACTGTGAACCTAGTGATGAGTCCAGAGAAAATGTTGCAAAA
AGAGTTACAGAAGAAACAGAAGGCATCATGGTACATCCCAACCAGGAGCCTGCAGTGATA
GCTGGACAAGGGACAATTGCCCTGGAAGTGCTGAACCAGGTTCCTTTGGTGGATGCACTG
GTGGTACCTGTAGGTGGAGGAGGAATGCTTGCTGGAATAGCAATTACAGTTAAGGCTCTG
AAACCTAGTGTGAAGGTATATGCTGCTGAACCCTCAAATGCAGATGACTGCTACCAGTCC
AAGCTGAAGGGGAAACTGATGCCCAATCTTTATCCTCCAGAAACCATAGCAGATGGTGTC
AAATCCAGCATTGGCTTGAACACCTGGCCTATTATCAGGGACCTTGTGGATGATATCTTC
ACTGTCACAGAGGATGAAATTAAGTGTGCAACCCAGCTGGTGTGGGAGAGGATGAAACTA
CTCATTGAACCTACAGCTGGTGTTGGAGTGGCTGCTGTGCTGTCTCAACATTTTCAAACT
GTTTCCCCAGAAGTAAAGAACATTTGTATTGTGCTCAGTGGTGGAAATGTAGACTTAACC
TCCTCCATAACTTGGGTGAAGCAGGCTGAAAGGCCAGCTTCTTATCAGTCTGTTTCTGTT
TAA
|
| Enzyme 70 GenBank Gene ID |
AF169974  |
| Enzyme 70 GeneCard ID |
SRR  |
| Enzyme 70 GenAtlas ID |
SRR  |
| Enzyme 70 HGNC ID |
HGNC:14398  |
| Enzyme 70 Chromosome Location |
1 |
| Enzyme 70 Locus |
17p13 |
| Enzyme 70 SNPs |
SNPJam Report  |
| Enzyme 70 General References |
- De Miranda J, Santoro A, Engelender S, Wolosker H: Human serine racemase: moleular cloning, genomic organization and functional analysis. Gene. 2000 Oct 3;256(1-2):183-8. [PubMed
]
- Xia M, Liu Y, Figueroa DJ, Chiu CS, Wei N, Lawlor AM, Lu P, Sur C, Koblan KS, Connolly TM: Characterization and localization of a human serine racemase. Brain Res Mol Brain Res. 2004 Jun 18;125(1-2):96-104. [PubMed
]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Baumgart F, Rodriguez-Crespo I: D-amino acids in the brain: the biochemistry of brain serine racemase. FEBS J. 2008 Jul;275(14):3538-45. [PubMed
]
|
| Enzyme 70 Metabolite References |
Not Available |
|
Enzyme 71
[top]
|
| Enzyme 71 ID |
14710 |
| Enzyme 71 Name |
Threonine synthase-like 2 |
| Enzyme 71 Synonyms |
- TSH2
|
| Enzyme 71 Gene Name |
THNSL2 |
| Enzyme 71 Protein Sequence |
>Threonine synthase-like 2
MWYVSTRGVAPRVNFEGALFSGYAPDGGLFMPEELPQLDRETLCQWSTLSYPGLVKELCA
LFIGSELLPKDELNDLIDRAFSRFRHREVVHLSRLRNGLNVLELWHGVTYAFKDLSLSCT
TQFLQYFLEKREKHVTVVVGTSGDTGSAAIESVQGAKNMDIIVLLPKGHCTKIQELQMTT
VLKQNVHVFGVEGNSDELDEPIKTVFADVAFVKKHNLMSLNSINWSRVLVQMAHHFFAYF
QCTPSLDTHPLPLVEVVVPTGAAGNLAAGYIAQKIGLPIRLVVAVNRNDIIHRTVQQGDF
SLSEAVKSTLASAMDIQVPYNMERVFWLLSGSDSQVTRALMEQFERTQSVNLPKELHSKL
SEAVTSVSVSDEAITQTMGRCWDENQYLLCPHSAVAVNYHYQQIDRQQPSTPRCCLAPAS
AAKFPEAVLAAGLTPETPAEIVALEHKETRCTLMRRGDNWMLMLRDTIEDLSRQWRSHAL
NTSQ
|
| Enzyme 71 Number of Residues |
484 |
| Enzyme 71 Molecular Weight |
54187.6 |
| Enzyme 71 Theoretical pI |
6.41 |
| Enzyme 71 GO Classification |
| Function |
- binding
- catalytic activity
- cofactor binding
- pyridoxal phosphate binding
|
| Process |
|
| Component |
| — |
|
| Enzyme 71 General Function |
Involved in catalytic activity |
| Enzyme 71 Specific Function |
Acts as a catabolic phospho-lyase on both gamma- and beta-phosphorylated substrates. Degrades O-phospho-threonine (PThr) to alpha-ketobutyrate, ammonia and phosphate |
| Enzyme 71 Pathways |
Not Available |
| Enzyme 71 Reactions |
Not Available |
| Enzyme 71 Pfam Domain Function |
|
| Enzyme 71 Signals |
|
| Enzyme 71 Transmembrane Regions |
|
| Enzyme 71 Essentiality |
Not Available |
| Enzyme 71 GenBank ID Protein |
149193323  |
| Enzyme 71 UniProtKB/Swiss-Prot ID |
Q86YJ6  |
| Enzyme 71 UniProtKB/Swiss-Prot Entry Name |
THNS2_HUMAN  |
| Enzyme 71 PDB ID |
Not Available |
| Enzyme 71 Cellular Location |
Not Available |
| Enzyme 71 Gene Sequence |
>1455 bp
ATGTGGTATGTCAGCACCAGGGGCGTAGCCCCACGGGTCAACTTTGAGGGGGCCCTCTTC
TCTGGCTATGCACCTGACGGGGGCCTCTTTATGCCTGAAGAGCTCCCACAGTTGGACAGA
GGGACCCTGTGCCAGTGGAGCACACTCTCCTATCCTGGCCTGGTGAAGGAGCTGTGTGCC
CTCTTCATTGGCTCTGAGCTCCTTCCAAAAGATGAATTAAATGATCTGATCGACCGAGCC
TTCAGCAGATTCCGTCACAGAGAAGTGGTCCATCTGTCCAGGTTGAGGAATGGGCTGAAC
GTGTTGGAGCTGTGGCATGGCGTCACATATGCATTTAAGGACCTGTCCCTGTCCTGCACA
ACACAGTTCCTGCAGTACTTCCTGGAGAAGAGGGAGAAGCACGTCACTGTGGTTGTAGGA
ACATCTGGGGACACAGGAAGTGCTGCCATTGAGAGTGTTCAAGGGGCAAAGAACATGGAC
ATTATCGTTCTGCTGCCCAAAGGTCACTGCACAAAGATTCAGGAGCTCCAGATGACAACG
GTGCTGAAGCAGAACGTACATGTGTTTGGAGTGGAGGGAAACAGCGATGAGCTCGATGAG
CCGATCAAGACTGTGTTTGCCGATGTGGCTTTTGTCAAGAAGCACAATCTGATGAGCCTG
AATTCGATCAACTGGTCCCGGGTCCTGGTGCAGATGGCCCATCACTTCTTTGCTTACTTC
CAGTGTACGCCATCCTTGGACACACATCCCCTACCCCTGGTGGAGGTGGTTGTGCCAACA
GGGGCTGCCGGTAACCTTGCAGCTGGGTACATTGCTCAAAAGATAGGCCTGCCCATCCGT
CTGGTCGTGGCAGTGAACCGCAATGACATCATCCACAGGACTGTCCAGCAGGGAGACTTC
TCTCTCTCTGAGGCTGTTAAATCAACCTTGGCATCAGCTATGGACATTCAGGTGCCCTAC
AACATGGAGAGGGTGTTCTGGCTGCTCTCTGGCTCTGACAGCCAGGTGACAAGAGCCCTC
ATGGAGCAGTTTGAAAGGACCCAAAGTGTGAATCTGCCCAAGGAACTGCACAGCAAGCTT
TCAGAGGCAGTGACATCCGTGTCAGTGTCGGATGAAGCCATCACCCAGACCATGGGCCGC
TGCTGGGATGAGAACCAGTACTTGCTGTGCCCCCACTCAGCGGTGGCCGTGAACTACCAT
TACCAGCAGATAGACAGGCAGCAGCCCAGCACTCCCCGGTGCTGCCTCGCCCCTGCCTCT
GCAGCCAAGTTCCCGGAAGCTGTCCTGGCTGCTGGCCTGACCCCTGAGACTCCCGCGGAG
ATCGTAGCCCTGGAGCACAAGGAGACACGCTGCACCCTGATGCGGAGAGGTGACAACTGG
ATGCTGATGCTTCGGGACACCATTGAGGACCTTAGCCGACAGTGGAGGAGTCATGCCCTC
AACACCTCCCAGTAG
|
| Enzyme 71 GenBank Gene ID |
NM_018271.3  |
| Enzyme 71 GeneCard ID |
THNSL2  |
| Enzyme 71 GenAtlas ID |
THNSL2  |
| Enzyme 71 HGNC ID |
HGNC:25602  |
| Enzyme 71 Chromosome Location |
2 |
| Enzyme 71 Locus |
2p11.2 |
| Enzyme 71 SNPs |
SNPJam Report  |
| Enzyme 71 General References |
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
- Hillier LW, Graves TA, Fulton RS, Fulton LA, Pepin KH, Minx P, Wagner-McPherson C, Layman D, Wylie K, Sekhon M, Becker MC, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Kremitzki C, Oddy L, Du H, Sun H, Bradshaw-Cordum H, Ali J, Carter J, Cordes M, Harris A, Isak A, van Brunt A, Nguyen C, Du F, Courtney L, Kalicki J, Ozersky P, Abbott S, Armstrong J, Belter EA, Caruso L, Cedroni M, Cotton M, Davidson T, Desai A, Elliott G, Erb T, Fronick C, Gaige T, Haakenson W, Haglund K, Holmes A, Harkins R, Kim K, Kruchowski SS, Strong CM, Grewal N, Goyea E, Hou S, Levy A, Martinka S, Mead K, McLellan MD, Meyer R, Randall-Maher J, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Shah N, Swearengen-Shahid S, Snider J, Strong JT, Thompson J, Yoakum M, Leonard S, Pearman C, Trani L, Radionenko M, Waligorski JE, Wang C, Rock SM, Tin-Wollam AM, Maupin R, Latreille P, Wendl MC, Yang SP, Pohl C, Wallis JW, Spieth J, Bieri TA, Berkowicz N, Nelson JO, Osborne J, Ding L, Meyer R, Sabo A, Shotland Y, Sinha P, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Jones TA, She X, Ciccarelli FD, Izaurralde E, Taylor J, Schmutz J, Myers RM, Cox DR, Huang X, McPherson JD, Mardis ER, Clifton SW, Warren WC, Chinwalla AT, Eddy SR, Marra MA, Ovcharenko I, Furey TS, Miller W, Eichler EE, Bork P, Suyama M, Torrents D, Waterston RH, Wilson RK: Generation and annotation of the DNA sequences of human chromosomes 2 and 4. Nature. 2005 Apr 7;434(7034):724-31. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
|
| Enzyme 71 Metabolite References |
Not Available |
|
Enzyme 72
[top]
|
| Enzyme 72 ID |
14711 |
| Enzyme 72 Name |
Histidine decarboxylase |
| Enzyme 72 Synonyms |
Not Available |
| Enzyme 72 Gene Name |
HDC |
| Enzyme 72 Protein Sequence |
>Histidine decarboxylase
MMEPEEYRERGREMVDYICQYLSTVRERRVMPDVQPGYLRAQLPESAPEDPDSWDSIFGD
IERIIMPGVVHWQSPHMHAYYPALTSWPSLLGDMLADAINCLGFTWASSPACTELEMNVM
DWLAKMLGLPEHFLHHHPSSQGGGVLQSTVSESTLIALLAARKNKILEMKTSEPDADESC
LNARLVAYASDQAHSSVEKAGLISLVKMKFLPVDDNFSLRGEALQKAIEEDKQRGLVPVF
VCATLGTTGVCAFDCLSELGPICAREGLWLHIDAAYAGTAFLCPEFRGFLKGIEYADSFT
FNPSKWMMVHFDCTGFWVKDKYKLQQTFSVNPIYLRHANSGVATDFMHWQIPLSRRFRSV
KLWFVIRSFGVKNLQAHVRHGTEMAKYFESLVRNDPSFEIPAKRHLGLVVFRLKGPNCLT
ENVLKEIAKAGRLFLIPATIQDKLIIRFTVTSQFTTRDDILRDWNLIRDAATLILSQHCT
SQPSPRVGNLISQIRGARAWACGTSLQSVSGAGDDPVQARKIIKQPQRVGAGPMKRENGL
HLETLLDPVDDCFSEEAPDATKHKLSSFLFSYLSVQTKKKTVRSLSCNSVPVSAQKPLPT
EASVKNGGSSRVRIFSRFPEDMMMLKKSAFKKLIKFYSVPSFPECSSQCGLQLPCCPLQA
MV
|
| Enzyme 72 Number of Residues |
662 |
| Enzyme 72 Molecular Weight |
74171 |
| Enzyme 72 Theoretical pI |
8.06 |
| Enzyme 72 GO Classification |
| Function |
- carbon-carbon lyase activity
- carboxy-lyase activity
- catalytic activity
- lyase activity
|
| Process |
- amino acid and derivative metabolism
- amino acid metabolism
- cellular metabolism
- metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 72 General Function |
Amino acid transport and metabolism |
| Enzyme 72 Specific Function |
Not Available |
| Enzyme 72 Pathways |
Not Available |
| Enzyme 72 Reactions |
Not Available |
| Enzyme 72 Pfam Domain Function |
|
| Enzyme 72 Signals |
|
| Enzyme 72 Transmembrane Regions |
|
| Enzyme 72 Essentiality |
Not Available |
| Enzyme 72 GenBank ID Protein |
120660080  |
| Enzyme 72 UniProtKB/Swiss-Prot ID |
A1L4G0  |
| Enzyme 72 UniProtKB/Swiss-Prot Entry Name |
A1L4G0_HUMAN  |
| Enzyme 72 PDB ID |
Not Available |
| Enzyme 72 Cellular Location |
Not Available |
| Enzyme 72 Gene Sequence |
>1989 bp
ATGATGGAGCCTGAGGAGTACAGAGAGAGAGGGAGAGAGATGGTGGATTACATCTGCCAG
TACCTGAGCACTGTGCGGGAGAGACGTGTGATGCCAGACGTGCAGCCTGGCTACCTGCGA
GCCCAGCTGCCTGAGAGTGCTCCTGAGGACCCCGACAGCTGGGACAGCATCTTTGGGGAC
ATTGAACGAATCATCATGCCTGGGGTGGTACATTGGCAGAGCCCCCATATGCACGCCTAC
TACCCAGCCCTCACCTCTTGGCCCTCCCTGCTAGGAGACATGCTGGCTGATGCCATCAAC
TGCTTGGGATTCACCTGGGCATCCAGCCCTGCGTGTACAGAGCTGGAGATGAACGTCATG
GACTGGTTGGCAAAAATGCTGGGACTTCCAGAGCACTTCTTGCACCACCACCCCAGCAGC
CAGGGCGGAGGCGTCCTGCAGAGCACGGTCAGTGAATCCACTTTGATTGCCCTGCTGGCA
GCAAGGAAGAACAAAATCCTGGAAATGAAAACGTCTGAGCCCGATGCTGATGAGTCCTGC
CTAAATGCCCGACTCGTGGCCTATGCCTCTGACCAGGCTCACTCCTCTGTGGAAAAGGCT
GGTTTGATTTCCCTTGTGAAGATGAAATTTCTGCCTGTGGATGACAACTTCTCACTCCGA
GGGGAAGCTCTTCAGAAGGCCATCGAGGAAGACAAGCAGCGGGGCTTGGTGCCCGTCTTT
GTCTGTGCAACACTAGGGACCACTGGGGTCTGTGCATTTGACTGCCTGTCAGAGCTGGGC
CCCATCTGTGCCCGTGAGGGGCTGTGGCTCCACATCGATGCTGCTTATGCAGGCACTGCC
TTCCTGTGCCCCGAGTTCCGGGGGTTTCTGAAGGGGATTGAGTATGCCGACTCCTTCACC
TTTAATCCTTCCAAGTGGATGATGGTGCATTTTGACTGTACTGGGTTCTGGGTCAAGGAC
AAGTACAAGCTGCAGCAGACCTTCAGTGTGAATCCCATCTACCTCAGGCATGCCAACTCA
GGCGTGGCCACCGACTTCATGCACTGGCAGATCCCCCTGAGCCGACGGTTTCGCTCTGTT
AAACTCTGGTTCGTGATTCGGTCCTTCGGGGTGAAGAATCTTCAAGCACATGTCAGACAT
GGTACTGAAATGGCTAAATATTTTGAATCTCTGGTCAGAAACGACCCTTCCTTTGAAATT
CCTGCCAAGAGGCACCTTGGCCTGGTGGTTTTTCGTCTAAAGGGTCCTAATTGTCTCACA
GAAAATGTGTTAAAGGAAATAGCTAAAGCTGGCCGTCTCTTCCTCATCCCGGCCACTATC
CAGGACAAGTTAATCATCCGTTTCACTGTGACATCCCAGTTTACCACTAGGGATGACATC
CTGAGAGACTGGAATCTCATTCGAGATGCTGCCACTCTCATCCTGAGTCAGCACTGTACT
TCCCAACCCAGCCCTCGGGTTGGGAACCTCATCTCCCAAATCAGGGGTGCCAGAGCCTGG
GCCTGTGGAACGTCCCTTCAGTCTGTCAGTGGGGCAGGAGATGATCCAGTCCAGGCCAGG
AAGATCATCAAGCAGCCTCAGCGTGTGGGAGCCGGTCCCATGAAAAGGGAAAATGGCCTC
CATCTTGAAACCCTGCTGGACCCAGTTGATGACTGCTTTTCAGAAGAGGCCCCAGATGCC
ACCAAGCACAAGCTGTCCTCCTTCCTGTTCAGTTACTTGTCTGTGCAGACTAAGAAGAAG
ACGGTGCGCTCCCTCAGTTGCAACAGTGTGCCAGTGAGTGCTCAGAAGCCACTGCCCACA
GAGGCCTCTGTGAAGAATGGGGGCTCCTCCAGGGTCAGAATCTTTTCCAGGTTTCCAGAA
GACATGATGATGCTGAAGAAAAGTGCCTTCAAAAAACTCATCAAATTCTACAGCGTCCCC
AGCTTTCCTGAATGCAGCTCTCAATGTGGACTCCAGCTGCCCTGTTGCCCTCTGCAGGCC
ATGGTTTAG
|
| Enzyme 72 GenBank Gene ID |
BC130527  |
| Enzyme 72 GeneCard ID |
A1L4G0  |
| Enzyme 72 GenAtlas ID |
Not Available |
| Enzyme 72 HGNC ID |
Not Available |
| Enzyme 72 Chromosome Location |
15 |
| Enzyme 72 Locus |
15q21-q22 |
| Enzyme 72 SNPs |
SNPJam Report  |
| Enzyme 72 General References |
- Strausberg RL, Feingold EA, Grouse LH, Derge JG, Klausner RD, Collins FS, Wagner L, Shenmen CM, Schuler GD, Altschul SF, Zeeberg B, Buetow KH, Schaefer CF, Bhat NK, Hopkins RF, Jordan H, Moore T, Max SI, Wang J, Hsieh F, Diatchenko L, Marusina K, Farmer AA, Rubin GM, Hong L, Stapleton M, Soares MB, Bonaldo MF, Casavant TL, Scheetz TE, Brownstein MJ, Usdin TB, Toshiyuki S, Carninci P, Prange C, Raha SS, Loquellano NA, Peters GJ, Abramson RD, Mullahy SJ, Bosak SA, McEwan PJ, McKernan KJ, Malek JA, Gunaratne PH, Richards S, Worley KC, Hale S, Garcia AM, Gay LJ, Hulyk SW, Villalon DK, Muzny DM, Sodergren EJ, Lu X, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madan A, Young AC, Shevchenko Y, Bouffard GG, Blakesley RW, Touchman JW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Krzywinski MI, Skalska U, Smailus DE, Schnerch A, Schein JE, Jones SJ, Marra MA: Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. Proc Natl Acad Sci U S A. 2002 Dec 24;99(26):16899-903. Epub 2002 Dec 11. [PubMed
]
|
| Enzyme 72 Metabolite References |
Not Available |
|
Enzyme 73
[top]
|
| Enzyme 73 ID |
14712 |
| Enzyme 73 Name |
Tyrosine aminotransferase |
| Enzyme 73 Synonyms |
Not Available |
| Enzyme 73 Gene Name |
TAT |
| Enzyme 73 Protein Sequence |
>Tyrosine aminotransferase
MDPYMIQMSSKGNLSSILDVHVNVGGRSSVPGKMKGRKARWSVRPSDMAKKTFNPIRAIV
DNMKVKPNPNKTMISLSIGDPTVFGNLPTDPEVTQAMKDALDSGKYNGYAPSIGFLSSRE
EIASYYHCPEAPLEAKDVILTSGCSQAIDLCLAVLANPGQNILVPRPGFSLYKTLAESMG
IEVKLYNLLPEKSWEIDLKQLEYLIDEKTACLIVNNPSNPCGSVFSKRHLQKILAVAARQ
CVPILADEIYGDMVFSDCKYEPLATLSTDVPILSCGGLAKRWLVPGWRLGWILIHDRRDI
FGNEIRDGLVKLSQRILGPCTIVQGALKSILCRTPGEFYHNTLSFLKSNADLCYGALAAI
PGLRPVRPSGAMYLMVGIEMEHFPEFENDVEFTERLVAEQSVHCLPATCFEYPNFIRVVI
TVPEVMMLEACSRIQEFCEQHYHCAEGSQEECDK
|
| Enzyme 73 Number of Residues |
454 |
| Enzyme 73 Molecular Weight |
50388.9 |
| Enzyme 73 Theoretical pI |
6.24 |
| Enzyme 73 GO Classification |
| Function |
- 1-aminocyclopropane-1-carboxylate synthase activity
- L-tyrosine aminotransferase activity
- L-tyrosine:2-oxoglutarate aminotransferase activity
- binding
- carbon-sulfur lyase activity
- catalytic activity
- cofactor binding
- lyase activity
- pyridoxal phosphate binding
- transaminase activity
- transferase activity
- transferase activity, transferring nitrogenous groups
|
| Process |
- aromatic amino acid family catabolic process
- aromatic amino acid family metabolic process
- biosynthetic process
- cellular amino acid and derivative metabolic process
- cellular amino acid catabolic process
- cellular amino acid metabolic process
- cellular metabolic process
- metabolic process
|
| Component |
| — |
|
| Enzyme 73 General Function |
Involved in 1-aminocyclopropane-1-carboxylate synthase activity |
| Enzyme 73 Specific Function |
Not Available |
| Enzyme 73 Pathways |
Not Available |
| Enzyme 73 Reactions |
Not Available |
| Enzyme 73 Pfam Domain Function |
|
| Enzyme 73 Signals |
|
| Enzyme 73 Transmembrane Regions |
|
| Enzyme 73 Essentiality |
Not Available |
| Enzyme 73 GenBank ID Protein |
120660410  |
| Enzyme 73 UniProtKB/Swiss-Prot ID |
A1L4G7  |
| Enzyme 73 UniProtKB/Swiss-Prot Entry Name |
A1L4G7_HUMAN  |
| Enzyme 73 PDB ID |
Not Available |
| Enzyme 73 Cellular Location |
Not Available |
| Enzyme 73 Gene Sequence |
>1365 bp
ATGGACCCATACATGATTCAGATGAGCAGCAAAGGCAACCTCTCCTCAATTCTGGACGTG
CATGTCAACGTTGGTGGGAGAAGCTCTGTGCCGGGAAAAATGAAAGGCAGAAAGGCCAGG
TGGTCTGTGAGGCCCTCAGACATGGCCAAGAAAACTTTCAACCCCATCCGAGCCATTGTG
GACAACATGAAGGTGAAACCAAATCCAAACAAAACCATGATTTCCCTGTCCATTGGGGAC
CCTACTGTGTTTGGAAACCTGCCTACAGACCCTGAAGTTACCCAGGCAATGAAAGATGCC
CTGGACTCGGGCAAATATAATGGCTATGCCCCATCCATCGGCTTCCTATCCAGTCGGGAG
GAGATTGCTTCTTATTACCACTGTCCTGAGGCACCCCTAGAAGCTAAGGACGTCATTCTG
ACAAGTGGCTGCAGCCAAGCTATTGACCTTTGTTTAGCTGTGTTGGCCAACCCAGGGCAA
AACATCCTGGTTCCAAGACCTGGTTTCTCTCTCTACAAGACTCTGGCTGAGTCTATGGGA
ATTGAGGTCAAACTCTACAATTTGTTGCCAGAGAAATCTTGGGAAATTGACCTGAAACAA
CTGGAATATCTAATTGATGAAAAGACAGCTTGTCTCATTGTCAATAATCCATCAAACCCC
TGTGGGTCAGTGTTCAGCAAACGTCATCTTCAGAAGATTCTGGCAGTGGCTGCACGGCAG
TGTGTCCCCATCTTAGCTGATGAGATCTATGGAGACATGGTGTTTTCGGATTGCAAATAT
GAACCACTGGCCACCCTCAGCACCGATGTCCCCATCCTGTCCTGTGGAGGGCTGGCCAAG
CGCTGGCTGGTTCCTGGCTGGAGGTTGGGCTGGATCCTCATTCATGACCGAAGAGACATT
TTTGGCAATGAGATCCGAGATGGGCTGGTGAAGCTGAGTCAGCGCATTTTGGGACCCTGT
ACCATTGTCCAGGGAGCTCTGAAAAGCATCCTATGTCGCACCCCGGGAGAGTTTTACCAC
AACACTCTGAGCTTCCTCAAGTCCAATGCTGATCTCTGTTATGGGGCGTTGGCTGCCATC
CCTGGACTCCGGCCAGTCCGCCCTTCTGGGGCTATGTACCTCATGGTTGGAATTGAGATG
GAACATTTCCCAGAATTTGAGAACGATGTGGAGTTCACGGAGCGGTTAGTTGCTGAGCAG
TCTGTCCACTGCCTCCCAGCAACGTGCTTTGAGTACCCGAATTTCATCCGAGTGGTCATC
ACAGTCCCCGAGGTGATGATGCTGGAGGCGTGCAGCCGGATCCAGGAGTTCTGTGAGCAG
CACTACCATTGTGCTGAAGGCAGCCAGGAGGAGTGTGATAAATAG
|
| Enzyme 73 GenBank Gene ID |
BC130534  |
| Enzyme 73 GeneCard ID |
TAT  |
| Enzyme 73 GenAtlas ID |
TAT  |
| Enzyme 73 HGNC ID |
HGNC:11573  |
| Enzyme 73 Chromosome Location |
1 |
| Enzyme 73 Locus |
16q22.1 |
| Enzyme 73 SNPs |
SNPJam Report  |
| Enzyme 73 General References |
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
|
| Enzyme 73 Metabolite References |
Not Available |
|
Enzyme 74
[top]
|
| Enzyme 74 ID |
14713 |
| Enzyme 74 Name |
Phosphorylase |
| Enzyme 74 Synonyms |
Not Available |
| Enzyme 74 Gene Name |
PYGM |
| Enzyme 74 Protein Sequence |
>Phosphorylase
MSRPLSDQEKRKQISVRGLAGVENVTELKKNFNRHLHFTLVKDRNVATPRDYYFALAHTV
RDHLVGRWIRTQQHYYEKDPKKISGGWQMEEADDWLRYGNPWEKARPEFTLPVHFYGHVE
HTSQGAKWVDTQVVLAMPYDTPVPGYRNNVVNTMRLWSAKAPNDFNLKDFNVGGYIQAVL
DRNLAENISRVLYPNDNFFEGKELRLKQEYFVVAATLQDIIRRFKSSKFGCRDPVRTNFD
AFPDKVAIQLNDTHPSLAIPELMRILVDLERMDWDKAWDVTVRTCAYTNHTVLPEALERW
PVHLLETLLPRHLQIIYEINQRFLNRVAAAFPGDVDRLRRMSLVEEGAVKRINMAHLCIA
GSHAVNGVARIHSEILKKTIFKDFYELEPHKFQNKTNGITPRRWLVLCNPGLAEVIAERI
GEDFISDLDQLRKLLSFVDDEAFIRDVAKVKQENKLKFAAYLEREYKVHINPNSLFDIQV
KRIHEYKRQLLNCLHVITLYNRIKREPNKFFVPRTVMIGGKAAPGYHMAKMIIRLVTAIG
DVVNHDPAVGDRLRVIFLENYRVSLAEKVIPAADLSEQISTAGTEASGTGNMKFMLNGAL
TIGTMDGANVEMAEEAGEENFFIFGMRVEDVDKLDQRGYNAQEYYDRIPELRQVIEQLSS
GFFSPKQPDLFKDIVNMLMHHDRFKVFADYEDYIKCQEKVSALYKNPREWTRMVIRNIAT
SGKFSSDRTIAQYAREIWGVEPSRQRLPAPDEAI
|
| Enzyme 74 Number of Residues |
754 |
| Enzyme 74 Molecular Weight |
87316.4 |
| Enzyme 74 Theoretical pI |
8.63 |
| Enzyme 74 GO Classification |
| Function |
- binding
- catalytic activity
- cofactor binding
- phosphorylase activity
- pyridoxal phosphate binding
- transferase activity
- transferase activity, transferring glycosyl groups
- transferase activity, transferring hexosyl groups
|
| Process |
- carbohydrate metabolic process
- metabolic process
- primary metabolic process
|
| Component |
| — |
|
| Enzyme 74 General Function |
Involved in phosphorylase activity |
| Enzyme 74 Specific Function |
Phosphorylase is an important allosteric enzyme in carbohydrate metabolism. Enzymes from different sources differ in their regulatory mechanisms and in their natural substrates. However, all known phosphorylases share catalytic and structural properties |
| Enzyme 74 Pathways |
|
| Enzyme 74 Reactions |
- [(1->4)-alpha-D-glucosyl]n + phosphate = [(1->4)-alpha-D-glucosyl]n-1 + alpha-D-glucose 1-phosphate [RN:R01821 R06050]
|
| Enzyme 74 Pfam Domain Function |
|
| Enzyme 74 Signals |
|
| Enzyme 74 Transmembrane Regions |
|
| Enzyme 74 Essentiality |
Not Available |
| Enzyme 74 GenBank ID Protein |
193786479  |
| Enzyme 74 UniProtKB/Swiss-Prot ID |
A6NDY6  |
| Enzyme 74 UniProtKB/Swiss-Prot Entry Name |
A6NDY6_HUMAN  |
| Enzyme 74 PDB ID |
1XL1  |
| Enzyme 74 PDB File |
Show |
| Enzyme 74 3D Structure |
|
| Enzyme 74 Cellular Location |
Not Available |
| Enzyme 74 Gene Sequence |
>2265 bp
ATGTCCCGGCCCCTGTCAGACCAAGAGAAAAGAAAGCAAATCAGTGTGCGTGGCCTGGCC
GGCGTGGAGAACGTGACTGAGCTGAAAAAGAACTTCAACCGGCACCTGCATTTCACACTC
GTAAAGGACCGCAATGTGGCCACCCCACGAGACTACTACTTTGCTCTGGCCCATACCGTG
CGCGACCACCTCGTGGGGCGCTGGATCCGCACGCAGCAGCACTACTATGAGAAGGACCCC
AAGAAGATCTCCGGGGGCTGGCAGATGGAGGAGGCCGATGACTGGCTTCGCTACGGCAAC
CCCTGGGAGAAGGCCCGGCCCGAGTTCACGCTACCTGTGCACTTCTACGGCCATGTGGAG
CACACCAGCCAGGGTGCCAAGTGGGTGGACACACAGGTGGTACTGGCCATGCCCTACGAT
ACGCCCGTGCCTGGCTATCGCAACAATGTTGTCAACACCATGCGCCTCTGGTCTGCCAAG
GCTCCCAATGACTTCAACCTCAAGGACTTCAATGTCGGTGGCTACATCCAGGCTGTGTTG
GACCGAAACCTGGCGGAGAACATCTCTCGTGTCCTGTACCCCAATGATAATTTCTTCGAA
GGGAAGGAGCTGCGGCTGAAGCAGGAGTATTTCGTGGTGGCTGCCACCCTCCAGGACATC
ATCCGTCGCTTCAAGTCTTCCAAGTTCGGCTGCCGTGATCCCGTGCGCACGAACTTCGAT
GCCTTCCCAGATAAGGTGGCCATCCAGCTCAATGACACCCACCCCTCCCTGGCCATCCCC
GAGCTGATGAGGATCCTGGTGGACCTGGAACGGATGGACTGGGACAAGGCGTGGGATGTG
ACAGTGAGGACCTGTGCCTACACCAACCACACGGTGCTGCCCGAGGCCCTGGAGCGCTGG
CCGGTGCACCTCTTGGAGACGCTGCTGCCGCGGCACCTCCAGATCATCTACGAGATCAAC
CAGCGCTTCCTCAACCGGGTGGCGGCCGCATTCCCAGGGGACGTAGACCGGCTGCGGCGC
ATGTCGCTGGTGGAGGAGGGCGCAGTGAAGCGCATCAACATGGCACACCTGTGCATCGCG
GGGTCGCACGCCGTCAACGGCGTGGCGCGCATCCACTCCGAGATCCTCAAGAAGACCATC
TTCAAAGACTTCTATGAGCTGGAGCCTCATAAGTTCCAGAATAAGACCAACGGCATCACC
CCTCGGCGCTGGCTGGTTCTGTGTAACCCCGGGCTGGCAGAGGTCATTGCTGAGCGCATC
GGGGAGGACTTCATCTCTGACCTGGACCAGCTGCGCAAACTGCTCTCCTTTGTGGATGAT
GAAGCTTTCATTCGGGATGTGGCCAAAGTGAAGCAGGAAAACAAGTTGAAGTTTGCTGCC
TACCTAGAGAGGGAATACAAAGTCCACATCAACCCCAACTCACTCTTCGACATCCAGGTG
AAGCGGATTCACGAATATAAACGACAGCTCCTCAACTGCCTCCATGTCATCACCCTGTAC
AACCGCATCAAGAGGGAGCCCAATAAGTTTTTTGTGCCTCGGACTGTGATGATTGGAGGG
AAGGCTGCACCTGGGTACCACATGGCCAAGATGATCATCAGACTCGTCACAGCCATCGGG
GATGTGGTCAACCATGACCCGGCAGTGGGTGACCGCCTCCGTGTCATCTTCCTGGAGAAC
TACCGAGTCTCACTGGCCGAGAAAGTGATCCCAGCTGCAGACCTCTCTGAGCAGATCTCC
ACTGCGGGCACTGAAGCCTCAGGCACCGGCAACATGAAGTTCATGCTCAACGGGGCTCTG
ACCATTGGCACCATGGACGGGGCCAATGTGGAGATGGCAGAAGAGGCGGGAGAGGAAAAC
TTCTTCATCTTTGGCATGCGGGTGGAGGATGTGGATAAGCTTGACCAAAGAGGGTACAAT
GCCCAGGAGTACTACGATCGCATTCCTGAGCTTCGGCAGGTCATTGAGCAGCTGAGCAGT
GGCTTCTTCTCCCCCAAACAGCCCGACCTGTTCAAGGACATTGTCAATATGCTCATGCAC
CATGACCGGTTTAAAGTCTTCGCAGATTATGAAGACTACATTAAATGCCAGGAGAAAGTC
AGCGCCTTGTACAAGAACCCAAGAGAGTGGACGCGGATGGTGATCCGGAACATAGCCACC
TCTGGCAAGTTCTCCAGTGACCGCACCATTGCCCAGTATGCCCGGGAGATCTGGGGTGTG
GAGCCTTCCCGCCAGCGCCTGCCAGCCCCGGATGAGGCCATCTGA
|
| Enzyme 74 GenBank Gene ID |
AK056607  |
| Enzyme 74 GeneCard ID |
PYGM  |
| Enzyme 74 GenAtlas ID |
PYGM  |
| Enzyme 74 HGNC ID |
HGNC:9726  |
| Enzyme 74 Chromosome Location |
1 |
| Enzyme 74 Locus |
11q12-q13.2 |
| Enzyme 74 SNPs |
SNPJam Report  |
| Enzyme 74 General References |
- Taylor TD, Noguchi H, Totoki Y, Toyoda A, Kuroki Y, Dewar K, Lloyd C, Itoh T, Takeda T, Kim DW, She X, Barlow KF, Bloom T, Bruford E, Chang JL, Cuomo CA, Eichler E, FitzGerald MG, Jaffe DB, LaButti K, Nicol R, Park HS, Seaman C, Sougnez C, Yang X, Zimmer AR, Zody MC, Birren BW, Nusbaum C, Fujiyama A, Hattori M, Rogers J, Lander ES, Sakaki Y: Human chromosome 11 DNA sequence and analysis including novel gene identification. Nature. 2006 Mar 23;440(7083):497-500. [PubMed
]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
|
| Enzyme 74 Metabolite References |
Not Available |
|
Enzyme 75
[top]
|
| Enzyme 75 ID |
14714 |
| Enzyme 75 Name |
Putative uncharacterized protein DDC |
| Enzyme 75 Synonyms |
Not Available |
| Enzyme 75 Gene Name |
DDC |
| Enzyme 75 Protein Sequence |
>Putative uncharacterized protein DDC
MNASEFRRRGKEMVDYMANYMEGIEGRQVYPDVEPGYLRPLIPAAAPQEPDTFEDIINDV
EKIIMPGVTHWHSPYFFAYFPTASSYPAMLADMLCGAIGCIGFSWAASPACTELETVMMD
WLGKMLELPKAFLNEKAGEGGGVIQGSASEATLVALLAARTKVIHRLQAASPELTQAAIM
EKLVAYSSDQAHSSVERAGLIGGVKLKAIPSDGNFAMRASALQEALERDKAAGLIPFFMV
ATLGTTTCCSFDNLLEVGPICNKEDIWLHVDAAYAGSAFICPEFRHLLNGVEFADSFNFN
PHKWLLVNFDCSAMWVKKRTDLTGAFRLDPTYLKHSHQDSDVLVSFQHWQIPLGRRFRSL
KMWFVFRMYGVKGLQAYIRKHVQLSHEFESLVRQDPRFEICVEVILGLVCFRLKGSNKVN
EALLQRINSAKKIHLVPCHLRDKFVLRFAICSRTVESAHVQRAWEHIKELAADVLRAERE
|
| Enzyme 75 Number of Residues |
480 |
| Enzyme 75 Molecular Weight |
53895.8 |
| Enzyme 75 Theoretical pI |
7.07 |
| Enzyme 75 GO Classification |
| Function |
- binding
- carbon-carbon lyase activity
- carboxy-lyase activity
- catalytic activity
- cofactor binding
- lyase activity
- pyridoxal phosphate binding
|
| Process |
- carboxylic acid metabolic process
- cellular amino acid and derivative metabolic process
- cellular metabolic process
- metabolic process
- organic acid metabolic process
- oxoacid metabolic process
|
| Component |
| — |
|
| Enzyme 75 General Function |
Involved in carboxy-lyase activity |
| Enzyme 75 Specific Function |
Not Available |
| Enzyme 75 Pathways |
Not Available |
| Enzyme 75 Reactions |
Not Available |
| Enzyme 75 Pfam Domain Function |
|
| Enzyme 75 Signals |
|
| Enzyme 75 Transmembrane Regions |
|
| Enzyme 75 Essentiality |
Not Available |
| Enzyme 75 GenBank ID Protein |
41393464  |
| Enzyme 75 UniProtKB/Swiss-Prot ID |
A6NI93  |
| Enzyme 75 UniProtKB/Swiss-Prot Entry Name |
A6NI93_HUMAN  |
| Enzyme 75 PDB ID |
Not Available |
| Enzyme 75 Cellular Location |
Not Available |
| Enzyme 75 Gene Sequence |
>1443 bp
ATGAACGCAAGTGAATTCCGAAGGAGAGGGAAGGAGATGGTGGATTACATGGCCAACTAC
ATGGAAGGCATTGAGGGACGCCAGGTCTACCCTGACGTGGAGCCCGGGTACCTGCGGCCG
CTGATCCCTGCCGCTGCCCCTCAGGAGCCAGACACGTTTGAGGACATCATCAACGACGTT
GAGAAGATAATCATGCCTGGGGTGACGCACTGGCACAGCCCCTACTTCTTCGCCTACTTC
CCCACTGCCAGCTCGTACCCGGCCATGCTTGCGGACATGCTGTGCGGGGCCATTGGCTGC
ATCGGCTTCTCCTGGGCGGCAAGCCCAGCATGCACAGAGCTGGAGACTGTGATGATGGAC
TGGCTCGGGAAGATGCTGGAACTACCAAAGGCATTTTTGAATGAGAAAGCTGGAGAAGGG
GGAGGAGTGATCCAGGGAAGTGCCAGTGAAGCCACCCTGGTGGCCCTGCTGGCCGCTCGG
ACCAAAGTGATCCATCGGCTGCAGGCAGCGTCCCCAGAGCTCACACAGGCCGCTATCATG
GAGAAGCTGGTGGCTTACTCATCCGATCAGGCACACTCCTCAGTGGAAAGAGCTGGGTTA
ATTGGTGGAGTGAAATTAAAAGCCATCCCCTCAGATGGCAACTTCGCCATGCGTGCGTCT
GCCCTGCAGGAAGCCCTGGAGAGAGACAAAGCGGCTGGCCTGATTCCTTTCTTTATGGTT
GCCACCCTGGGGACCACAACATGCTGCTCCTTTGACAATCTCTTAGAAGTCGGTCCTATC
TGCAACAAGGAAGACATATGGCTGCACGTTGATGCAGCCTACGCAGGCAGTGCATTCATC
TGCCCTGAGTTCCGGCACCTTCTGAATGGAGTGGAGTTTGCAGATTCATTCAACTTTAAT
CCCCACAAATGGCTATTGGTGAATTTTGACTGTTCTGCCATGTGGGTGAAAAAGAGAACA
GACTTAACGGGAGCCTTTAGACTGGACCCCACTTACCTGAAGCACAGCCATCAGGATTCA
GGGCTTATCACTGACTACCGGCATTGGCAGATACCACTGGGCAGAAGATTTCGCTCTTTG
AAAATGTGGTTTGTATTTAGGATGTATGGAGTCAAAGGACTGCAGGCTTATATCCGCAAG
CATGTCCAGCTGTCCCATGAGTTTGAGTCACTGGTGCGCCAGGATCCCCGCTTTGAAATC
TGTGTGGAAGTCATTCTGGGGCTTGTCTGCTTTCGGCTAAAGGGTTCCAACAAAGTGAAT
GAAGCTCTTCTGCAAAGAATAAACAGTGCCAAAAAAATCCACTTGGTTCCATGTCACCTC
AGGGACAAGTTTGTCCTGCGCTTTGCCATCTGTTCTCGCACGGTGGAATCTGCCCATGTG
CAGCGGGCCTGGGAACACATCAAAGAGCTGGCGGCCGACGTGCTGCGAGCAGAGAGGGAG
TAG
|
| Enzyme 75 GenBank Gene ID |
AC018705  |
| Enzyme 75 GeneCard ID |
DDC  |
| Enzyme 75 GenAtlas ID |
DDC  |
| Enzyme 75 HGNC ID |
HGNC:2719  |
| Enzyme 75 Chromosome Location |
7 |
| Enzyme 75 Locus |
7p12.2 |
| Enzyme 75 SNPs |
SNPJam Report  |
| Enzyme 75 General References |
- Hillier LW, Fulton RS, Fulton LA, Graves TA, Pepin KH, Wagner-McPherson C, Layman D, Maas J, Jaeger S, Walker R, Wylie K, Sekhon M, Becker MC, O'Laughlin MD, Schaller ME, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Cordes M, Du H, Sun H, Edwards J, Bradshaw-Cordum H, Ali J, Andrews S, Isak A, Vanbrunt A, Nguyen C, Du F, Lamar B, Courtney L, Kalicki J, Ozersky P, Bielicki L, Scott K, Holmes A, Harkins R, Harris A, Strong CM, Hou S, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Leonard S, Rohlfing T, Rock SM, Tin-Wollam AM, Abbott A, Minx P, Maupin R, Strowmatt C, Latreille P, Miller N, Johnson D, Murray J, Woessner JP, Wendl MC, Yang SP, Schultz BR, Wallis JW, Spieth J, Bieri TA, Nelson JO, Berkowicz N, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Bedell JA, Mardis ER, Clifton SW, Chissoe SL, Marra MA, Raymond C, Haugen E, Gillett W, Zhou Y, James R, Phelps K, Iadanoto S, Bubb K, Simms E, Levy R, Clendenning J, Kaul R, Kent WJ, Furey TS, Baertsch RA, Brent MR, Keibler E, Flicek P, Bork P, Suyama M, Bailey JA, Portnoy ME, Torrents D, Chinwalla AT, Gish WR, Eddy SR, McPherson JD, Olson MV, Eichler EE, Green ED, Waterston RH, Wilson RK: The DNA sequence of human chromosome 7. Nature. 2003 Jul 10;424(6945):157-64. [PubMed
]
|
| Enzyme 75 Metabolite References |
Not Available |
|
Enzyme 76
[top]
|
| Enzyme 76 ID |
14715 |
| Enzyme 76 Name |
cDNA FLJ75452, highly similar to Homo sapiens cysteine sulfinic acid decarboxylase-related protein 2 |
| Enzyme 76 Synonyms |
- CSADmRNA
- Cysteine sulfinic acid decarboxylase, isoform CRA_d
|
| Enzyme 76 Gene Name |
CSAD |
| Enzyme 76 Protein Sequence |
>cDNA FLJ75452, highly similar to Homo sapiens cysteine sulfinic acid decarboxylase-related protein 2
MADSEALPSLAGDPVAVEALLRAVFGVVVDEAIQKGTSVSQKCHYSIQKGAAFLGLGTDS
VRVVKADERGKMVPEDLERQIGMAEAEGAVPFLVSATSGTTVLGAFDPLEAIADVCQRHG
LWLHVDAAWGGSVLLSQTHRHLLDGIQRADSVAWNPHKLLAAGLQCSALLLQDTSNLLKR
CHGSQASYLFQQDKFYDVALDTGDKVVQCGRRVDCLKLWLMWKAQGDQGLERRIDQAFVL
ARYLVEEMKKREGFELVMEPEFVNVCFWFVPPSLRGKQESPDYHERLSKVAPVLKERMVK
EGSMMIGYQPHGTRGNFFRVVVANSALTCADMDFLLNELERLGQDL
|
| Enzyme 76 Number of Residues |
346 |
| Enzyme 76 Molecular Weight |
38232 |
| Enzyme 76 Theoretical pI |
5.85 |
| Enzyme 76 GO Classification |
Not Available |
| Enzyme 76 General Function |
Amino acid transport and metabolism |
| Enzyme 76 Specific Function |
Not Available |
| Enzyme 76 Pathways |
Not Available |
| Enzyme 76 Reactions |
Not Available |
| Enzyme 76 Pfam Domain Function |
Not Available |
| Enzyme 76 Signals |
|
| Enzyme 76 Transmembrane Regions |
|
| Enzyme 76 Essentiality |
Not Available |
| Enzyme 76 GenBank ID Protein |
158260341  |
| Enzyme 76 UniProtKB/Swiss-Prot ID |
A8K0U4  |
| Enzyme 76 UniProtKB/Swiss-Prot Entry Name |
A8K0U4_HUMAN  |
| Enzyme 76 PDB ID |
Not Available |
| Enzyme 76 Cellular Location |
Not Available |
| Enzyme 76 Gene Sequence |
>1041 bp
ATGGCTGACTCAGAAGCACTCCCCTCCCTTGCTGGGGACCCAGTGGCTGTGGAAGCCTTG
CTCCGGGCCGTGTTTGGGGTTGTTGTGGATGAGGCCATTCAGAAAGGAACCAGTGTCTCC
CAGAAGTGTCACTACTCCATCCAGAAGGGAGCTGCGTTTCTGGGACTTGGCACCGACAGT
GTCCGAGTGGTCAAGGCTGATGAGAGAGGGAAAATGGTCCCCGAGGATCTGGAGAGGCAG
ATTGGTATGGCTGAGGCTGAGGGTGCTGTGCCGTTCCTGGTCAGTGCCACCTCTGGCACC
ACTGTGCTAGGGGCCTTTGACCCCCTGGAGGCAATTGCTGATGTGTGCCAGCGTCATGGG
CTATGGCTGCATGTGGATGCTGCCTGGGGTGGGAGCGTCCTGCTGTCACAGACACACAGG
CATCTCCTGGATGGGATCCAGAGGGCTGACTCTGTGGCCTGGAATCCCCACAAGCTCCTC
GCAGCAGGCCTGCAATGCTCTGCACTTCTTCTCCAGGATACCTCGAACCTGCTCAAGCGC
TGCCATGGGTCCCAGGCCAGCTACCTTTTCCAGCAGGACAAGTTCTACGATGTGGCTCTG
GACACGGGAGACAAGGTGGTGCAGTGTGGCCGCCGTGTGGACTGTCTGAAGCTGTGGCTC
ATGTGGAAGGCACAGGGCGATCAAGGGCTGGAGCGGCGCATCGACCAGGCCTTTGTCCTT
GCCCGGTACCTGGTGGAGGAAATGAAGAAGCGGGAAGGGTTTGAGCTAGTCATGGAGCCT
GAGTTTGTCAATGTGTGTTTCTGGTTCGTACCCCCCAGCCTGCGAGGGAAGCAGGAGAGT
CCAGATTACCACGAAAGGCTGTCAAAGGTGGCCCCCGTGCTCAAGGAGCGCATGGTGAAG
GAGGGCTCCATGATGATTGGCTACCAGCCCCACGGGACCCGGGGCAACTTCTTCCGTGTG
GTTGTGGCCAACTCTGCACTGACCTGTGCTGATATGGACTTCCTCCTCAACGAGCTGGAG
CGGCTAGGCCAGGACCTGTGA
|
| Enzyme 76 GenBank Gene ID |
AK289659  |
| Enzyme 76 GeneCard ID |
A8K0U4  |
| Enzyme 76 GenAtlas ID |
Not Available |
| Enzyme 76 HGNC ID |
Not Available |
| Enzyme 76 Chromosome Location |
12 |
| Enzyme 76 Locus |
12q13.11-q14.3 |
| Enzyme 76 SNPs |
SNPJam Report  |
| Enzyme 76 General References |
Not Available |
| Enzyme 76 Metabolite References |
Not Available |
|
Enzyme 77
[top]
|
| Enzyme 77 ID |
14716 |
| Enzyme 77 Name |
cDNA FLJ77874, highly similar to Homo sapiens glycine C-acetyltransferase (2-amino-3-ketobutyrate coenzyme A ligase), mRNA |
| Enzyme 77 Synonyms |
Not Available |
| Enzyme 77 Gene Name |
Not Available |
| Enzyme 77 Protein Sequence |
>cDNA FLJ77874, highly similar to Homo sapiens glycine C-acetyltransferase (2-amino-3-ketobutyrate coenzyme A ligase), mRNA
MWPGNAWRAALFWVPRGRRAQSALAQLRGILEGELEGICGAGTWKSERVITSRQGPHIRV
DGVSGGILNFCANNYLGLSSHPEVIQAGLQALEEFGAGLSSVRFICGTQSIHKNLEAKIA
RFHQREDAILYPSCYDANAGLFEALLTPEDAVLSDELNHASIIDGIRLCKAHKYRYRHLD
MADLEAKLQEAQKHRLRLVATDGAFSMDGDIAPLQEICCLASRYGALVFMDECHATGFLG
PTGRGTDELLGVMDQVTIINSTLGKALGGASGGYTTGPGPLVSLLRQRARPYLFSNSLPP
AVVGCASKALDLLMGSNTIVQSMAAKTQRFRSKMEAAGFTISGASHPICPVMLGDARLAS
RMADDMLKRGIFVIGFSYPVVPKGKARIRVQTSAVHSEEDIDRCVEAFVEVGRLHGALP
|
| Enzyme 77 Number of Residues |
419 |
| Enzyme 77 Molecular Weight |
45219.5 |
| Enzyme 77 Theoretical pI |
7.90 |
| Enzyme 77 GO Classification |
| Function |
- C-acetyltransferase activity
- acetyltransferase activity
- acyltransferase activity
- binding
- catalytic activity
- cofactor binding
- glycine C-acetyltransferase activity
- pyridoxal phosphate binding
- transferase activity
- transferase activity, transferring acyl groups
- transferase activity, transferring acyl groups other than amino-acyl groups
- transferase activity, transferring nitrogenous groups
|
| Process |
- biosynthetic process
- metabolic process
|
| Component |
| — |
|
| Enzyme 77 General Function |
Involved in glycine C-acetyltransferase activity |
| Enzyme 77 Specific Function |
Not Available |
| Enzyme 77 Pathways |
Not Available |
| Enzyme 77 Reactions |
Not Available |
| Enzyme 77 Pfam Domain Function |
|
| Enzyme 77 Signals |
|
| Enzyme 77 Transmembrane Regions |
|
| Enzyme 77 Essentiality |
Not Available |
| Enzyme 77 GenBank ID Protein |
158261209  |
| Enzyme 77 UniProtKB/Swiss-Prot ID |
A8K228  |
| Enzyme 77 UniProtKB/Swiss-Prot Entry Name |
A8K228_HUMAN  |
| Enzyme 77 PDB ID |
Not Available |
| Enzyme 77 Cellular Location |
Not Available |
| Enzyme 77 Gene Sequence |
>1260 bp
ATGTGGCCTGGGAACGCCTGGCGCGCCGCACTCTTCTGGGTGCCCCGCGGCCGCCGCGCA
CAGTCAGCGCTGGCCCAGCTGCGTGGCATTCTGGAGGGGGAGCTGGAAGGCATCTGCGGA
GCTGGCACTTGGAAGAGTGAGCGGGTCATCACGTCCCGTCAGGGGCCGCACATCCGCGTG
GACGGCGTCTCCGGAGGAATCCTTAACTTCTGTGCCAACAACTACCTGGGCCTGAGCAGC
CACCCTGAGGTGATCCAGGCAGGTCTGCAGGCTCTGGAGGAGTTTGGAGCTGGCCTCAGC
TCTGTCCGCTTTATCTGTGGAACCCAGAGCATCCACAAGAATCTAGAAGCAAAAATAGCC
CGCTTCCACCAGCGGGAGGATGCCATCCTCTATCCCAGCTGTTATGACGCCAACGCCGGC
CTCTTTGAGGCCCTGCTGACCCCAGAGGACGCAGTCCTGTCGGACGAGCTGAACCATGCC
TCCATCATCGACGGCATCCGGCTGTGCAAGGCCCACAAGTACCGCTATCGCCACCTGGAC
ATGGCCGACCTAGAAGCCAAGCTGCAGGAGGCCCAGAAGCATCGGCTGCGCCTGGTGGCC
ACTGATGGGGCCTTTTCCATGGATGGCGACATCGCACCCCTGCAGGAGATCTGCTGCCTC
GCCTCTAGATATGGTGCCCTGGTCTTCATGGATGAATGCCATGCCACTGGCTTCCTGGGG
CCCACAGGACGGGGCACAGATGAGCTGCTGGGTGTGATGGACCAGGTCACCATCATCAAC
TCCACCCTGGGGAAGGCCCTGGGTGGAGCATCAGGGGGCTACACGACAGGGCCTGGGCCC
CTGGTGTCCCTGCTGCGGCAGCGCGCCCGGCCATACCTCTTCTCCAACAGTCTGCCACCT
GCTGTCGTTGGCTGCGCCTCCAAGGCCCTAGATCTGCTGATGGGGAGTAACACCATTGTC
CAGTCTATGGCTGCCAAGACCCAGAGGTTCCGTAGTAAGATGGAAGCTGCTGGCTTCACT
ATCTCGGGAGCCAGTCACCCCATCTGCCCTGTGATGCTGGGTGATGCCCGGCTGGCCTCT
CGCATGGCGGATGACATGCTGAAGAGAGGCATCTTTGTCATCGGGTTCAGCTACCCCGTG
GTCCCCAAGGGCAAGGCCCGGATCCGGGTACAGACCTCAGCAGTGCATAGCGAGGAAGAC
ATTGACCGCTGCGTGGAGGCCTTCGTGGAAGTGGGGCGACTGCACGGGGCACTGCCCTGA
|
| Enzyme 77 GenBank Gene ID |
AK290093  |
| Enzyme 77 GeneCard ID |
Not Available |
| Enzyme 77 GenAtlas ID |
Not Available |
| Enzyme 77 HGNC ID |
HGNC:4188  |
| Enzyme 77 Chromosome Location |
Not Available |
| Enzyme 77 Locus |
Not Available |
| Enzyme 77 SNPs |
Not Available |
| Enzyme 77 General References |
Not Available |
| Enzyme 77 Metabolite References |
Not Available |
|
Enzyme 78
[top]
|
| Enzyme 78 ID |
14717 |
| Enzyme 78 Name |
Aminolevulinate, delta-, synthase 2 (Sideroblastic/hypochromic anemia), isoform CRA_c |
| Enzyme 78 Synonyms |
- SubName: cDNA FLJ78080, highly similar to Human ALAS 5-aminolevulinate synthase
- SubName: cDNA, FLJ93603, highly similar to Homo sapiens aminolevulinate, delta-, synthase 2 (sideroblastic/hypochromic anemia) (ALAS2), nuclear gene encoding mitochondrial protein, mRNA
|
| Enzyme 78 Gene Name |
ALAS2 |
| Enzyme 78 Protein Sequence |
>Aminolevulinate, delta-, synthase 2 (Sideroblastic/hypochromic anemia), isoform CRA_c
MVTAAMLLQCCPVLARGPTSLLGKVVKTHQFLFGIGRCPILATQGPNCSQIHLKATKAGG
DSPSWAKGHCPFMLSELQDGKSKIVQKAAPEVQEDVKAFKTDLPSSLVSVSLRKPFSGPQ
EQEQISGKVTHLIQNNMPGNYVFSYDQFFRDKIMEKKQDHTYRVFKTVNRWADAYPFAQH
FSEASVASKDVSVWCSNDYLGMSRHPQVLQATQETLQRHGAGAGGTRNISGTSKFHVELE
QELAELHQKDSALLFSSCFVANDSTLFTLAKILPGCEIYSDAGNHASMIQGIRNSGAAKF
VFRHNDPDHLKKLLEKSNPKIPKIVAFETVHSMDGAICPLEELCDVSHQYGALTFVDEVH
AVGLYGSRGAGIGERDGIMHKIDIISGTLGKAFGCVGGYIASTRDLVDMVRSYAAGFIFT
TSLPPMVLSGALESVRLLKGEEGQALRRAHQRNVKHMRQLLMDRGLPVIPCPSHIIPIRV
GNAALNSKLCDLLLSKHGIYVQAINYPTVPRGEELLRLAPSPHHSPQMMEDFVEKLLLAW
TAVGLPLQDVSVAACNFCRRPVHFELMSEWERSYFGNMGPQYVTTYA
|
| Enzyme 78 Number of Residues |
587 |
| Enzyme 78 Molecular Weight |
64632.9 |
| Enzyme 78 Theoretical pI |
8.19 |
| Enzyme 78 GO Classification |
| Function |
- 5-aminolevulinate synthase activity
- N-acyltransferase activity
- N-succinyltransferase activity
- acyltransferase activity
- binding
- catalytic activity
- cofactor binding
- pyridoxal phosphate binding
- transferase activity
- transferase activity, transferring acyl groups
- transferase activity, transferring acyl groups other than amino-acyl groups
- transferase activity, transferring nitrogenous groups
|
| Process |
- biosynthetic process
- cellular biosynthetic process
- heterocycle biosynthetic process
- metabolic process
- nitrogen compound metabolic process
- porphyrin metabolic process
- tetrapyrrole biosynthetic process
- tetrapyrrole metabolic process
|
| Component |
- cell part
- cytoplasmic part
- intracellular part
- mitochondrial matrix
- mitochondrial part
|
|
| Enzyme 78 General Function |
Involved in 5-aminolevulinate synthase activity |
| Enzyme 78 Specific Function |
Not Available |
| Enzyme 78 Pathways |
Not Available |
| Enzyme 78 Reactions |
Not Available |
| Enzyme 78 Pfam Domain Function |
|
| Enzyme 78 Signals |
|
| Enzyme 78 Transmembrane Regions |
|
| Enzyme 78 Essentiality |
Not Available |
| Enzyme 78 GenBank ID Protein |
158254562  |
| Enzyme 78 UniProtKB/Swiss-Prot ID |
A8K3F0  |
| Enzyme 78 UniProtKB/Swiss-Prot Entry Name |
A8K3F0_HUMAN  |
| Enzyme 78 PDB ID |
Not Available |
| Enzyme 78 Cellular Location |
Not Available |
| Enzyme 78 Gene Sequence |
>1764 bp
ATGGTGACTGCAGCCATGCTGCTACAGTGCTGCCCAGTGCTTGCCCGGGGCCCCACAAGC
CTCCTAGGCAAGGTGGTTAAGACTCACCAGTTCCTGTTTGGTATTGGACGCTGTCCCATC
CTGGCTACCCAAGGACCAAACTGTTCTCAAATCCACCTTAAGGCAACAAAGGCTGGAGGA
GATTCTCCATCTTGGGCGAAGGGCCACTGTCCCTTCATGCTGTCGGAACTCCAGGATGGG
AAGAGCAAGATTGTGCAGAAGGCAGCCCCAGAAGTCCAGGAAGATGTGAAGGCTTTCAAG
ACAGATCTGCCTAGCTCCCTGGTCTCAGTCAGCCTAAGGAAGCCATTTTCCGGTCCCCAG
GAGCAGGAGCAGATCTCTGGGAAGGTCACACACCTGATTCAGAACAATATGCCTGGAAAC
TATGTCTTCAGTTATGACCAGTTTTTCAGGGACAAGATCATGGAGAAGAAACAGGATCAC
ACCTACCGTGTGTTCAAGACTGTGAACCGCTGGGCTGATGCATATCCCTTTGCCCAACAT
TTCTCTGAGGCATCTGTGGCCTCAAAGGATGTGTCCGTCTGGTGTAGTAATGATTACCTG
GGCATGAGCCGACACCCTCAGGTCTTGCAAGCCACACAGGAGACCCTGCAGCGTCATGGT
GCTGGAGCTGGTGGCACCCGCAACATCTCAGGCACCAGTAAGTTTCATGTGGAGCTTGAG
CAGGAGCTGGCTGAGCTGCACCAGAAGGACTCAGCCCTGCTCTTCTCCTCCTGCTTTGTT
GCCAATGACTCTACTCTCTTCACCTTGGCCAAGATCCTGCCAGGGTGCGAGATTTACTCA
GACGCAGGCAACCATGCTTCCATGATCCAAGGTATCCGTAACAGTGGAGCAGCCAAGTTT
GTCTTCAGGCACAATGACCCTGACCACCTAAAGAAACTTCTAGAGAAGTCTAACCCTAAG
ATACCCAAAATTGTGGCCTTTGAGACTGTCCACTCCATGGATGGTGCCATCTGTCCCCTC
GAGGAGTTGTGTGATGTGTCCCACCAGTATGGGGCCCTGACCTTCGTGGATGAGGTCCAT
GCTGTAGGACTGTATGGGTCCCGGGGCGCTGGGATTGGGGAGCGTGATGGAATTATGCAT
AAGATTGACATCATCTCTGGAACTCTTGGCAAGGCCTTTGGCTGTGTGGGCGGCTACATT
GCCAGCACCCGTGACTTGGTGGACATGGTGCGCTCCTATGCTGCAGGCTTCATCTTTACC
ACTTCTCTGCCCCCCATGGTGCTCTCTGGAGCTCTAGAATCTGTGCGGCTGCTCAAGGGA
GAGGAGGGCCAAGCCCTGAGGCGAGCCCACCAGCGCAATGTCAAGCACATGCGCCAGCTA
CTCATGGACAGGGGCCTTCCTGTCATCCCCTGCCCCAGCCACATCATCCCCATCCGGGTG
GGCAATGCAGCACTCAACAGCAAGCTCTGTGATCTCCTGCTCTCCAAGCATGGCATCTAT
GTGCAGGCCATCAACTACCCAACTGTCCCCCGGGGTGAAGAGCTCCTGCGCTTGGCACCC
TCCCCCCACCACAGCCCTCAGATGATGGAAGATTTTGTGGAGAAGCTGCTGCTGGCTTGG
ACTGCGGTGGGGCTGCCCCTCCAGGATGTGTCTGTGGCTGCCTGCAATTTCTGTCGCCGT
CCTGTACACTTTGAGCTCATGAGTGAGTGGGAACGTTCCTACTTCGGGAACATGGGGCCC
CAGTATGTCACCACCTATGCCTGA
|
| Enzyme 78 GenBank Gene ID |
AK290565  |
| Enzyme 78 GeneCard ID |
ALAS2  |
| Enzyme 78 GenAtlas ID |
ALAS2  |
| Enzyme 78 HGNC ID |
HGNC:397  |
| Enzyme 78 Chromosome Location |
Not Available |
| Enzyme 78 Locus |
Not Available |
| Enzyme 78 SNPs |
SNPJam Report  |
| Enzyme 78 General References |
Not Available |
| Enzyme 78 Metabolite References |
Not Available |
|
Enzyme 79
[top]
|
| Enzyme 79 ID |
14718 |
| Enzyme 79 Name |
Aspartate aminotransferase |
| Enzyme 79 Synonyms |
Not Available |
| Enzyme 79 Gene Name |
Not Available |
| Enzyme 79 Protein Sequence |
>Aspartate aminotransferase
MALLHSGRVLPGIAAAFHPGLAAAASARASSWWTHVEMGPPDPILGVTEAFKRDTNSKKM
NLGVGAYRDNNGKPYVLPSVRKAEAQIAAKNLDKEYLPIGGLAEFCKASAELALGENSKV
LKSGRFVTVQTISGTGASRIGASFLQRFFKFSRDVFLPKPTWGNHTPIFRDAGMQLQGYR
YYDPKTCGFDFTGAVEDISKIPEQSVLLLHACAHNPTGVDPRPEQWKEIATVVKKRNLFA
FFDMAYQGFANGDGDKDAWAVRHFIEQGINVCLCQSYAKNMGLYGERVGAFTMVCKDADE
AKRVESQLKILIRPMYSNPPLNGARIAAAILNTPDLRKQWLQEVKVMADRIIGMRTQLVS
NLKKEGSTHNWQHITDQIGMFCFTGLKPEQVERLIKEFSIYMTKDGRISVAGVTSSNVGY
LAHAIHQVTK
|
| Enzyme 79 Number of Residues |
430 |
| Enzyme 79 Molecular Weight |
47516.3 |
| Enzyme 79 Theoretical pI |
9.69 |
| Enzyme 79 GO Classification |
| Function |
- binding
- catalytic activity
- cofactor binding
- pyridoxal phosphate binding
- transaminase activity
- transferase activity
- transferase activity, transferring nitrogenous groups
|
| Process |
- biosynthetic process
- cellular amino acid and derivative metabolic process
- cellular amino acid metabolic process
- cellular metabolic process
- metabolic process
|
| Component |
| — |
|
| Enzyme 79 General Function |
Involved in transferase activity, transferring nitrogenous groups |
| Enzyme 79 Specific Function |
L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate |
| Enzyme 79 Pathways |
Not Available |
| Enzyme 79 Reactions |
- L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate [RN:R00355]
|
| Enzyme 79 Pfam Domain Function |
|
| Enzyme 79 Signals |
|
| Enzyme 79 Transmembrane Regions |
|
| Enzyme 79 Essentiality |
Not Available |
| Enzyme 79 GenBank ID Protein |
158255130  |
| Enzyme 79 UniProtKB/Swiss-Prot ID |
A8K482  |
| Enzyme 79 UniProtKB/Swiss-Prot Entry Name |
A8K482_HUMAN  |
| Enzyme 79 PDB ID |
Not Available |
| Enzyme 79 Cellular Location |
Not Available |
| Enzyme 79 Gene Sequence |
>1293 bp
ATGGCCCTGCTGCACTCCGGCCGCGTCCTCCCCGGGATCGCCGCCGCCTTCCACCCGGGC
CTCGCCGCCGCGGCCTCTGCCAGAGCCAGCTCCTGGTGGACCCATGTGGAAATGGGACCT
CCAGATCCCATTCTGGGAGTCACTGAAGCCTTTAAGAGGGACACCAATAGCAAAAAGATG
AATCTGGGAGTTGGTGCCTACCGGGATAATAATGGAAAGCCTTACGTTCTGCCTAGCGTC
CGCAAGGCAGAGGCCCAGATTGCCGCAAAAAATTTGGACAAGGAATACCTGCCCATTGGG
GGACTGGCTGAATTTTGCAAGGCATCTGCAGAACTAGCCCTGGGTGAGAACAGCAAAGTC
TTGAAGAGTGGCCGGTTTGTCACTGTGCAGACCATTTCTGGAACTGGAGCCTCAAGGATC
GGAGCCAGTTTTCTGCAAAGATTTTTTAAGTTCAGCCGAGATGTCTTTCTGCCCAAACCA
ACCTGGGGAAACCACACACCCATCTTCAGGGATGCTGGCATGCAGCTACAAGGTTATCGG
TATTATGACCCCAAGACTTGCGGTTTTGACTTCACAGGCGCTGTGGAGGATATTTCAAAA
ATACCAGAGCAGAGTGTTCTTCTTCTGCATGCCTGCGCCCACAATCCCACGGGAGTGGAC
CCGCGTCCGGAACAGTGGAAGGAAATAGCAACAGTGGTGAAGAAAAGGAATCTCTTTGCG
TTCTTTGACATGGCCTACCAAGGCTTTGCCAATGGTGATGGTGATAAGGATGCCTGGGCT
GTGCGCCACTTCATCGAACAGGGCATTAATGTTTGCCTCTGCCAATCATATGCCAAGAAC
ATGGGCTTATATGGTGAGCGTGTAGGAGCCTTCACTATGGTCTGCAAAGATGCGGATGAA
GCCAAAAGGGTAGAGTCACAGTTGAAGATCTTGATCCGTCCCATGTATTCCAACCCTCCC
CTCAATGGGGCCCGGATTGCTGCTGCCATTCTGAACACCCCAGATTTGCGAAAACAATGG
CTGCAAGAAGTGAAAGTCATGGCTGACCGCATCATTGGCATGCGGACTCAACTGGTCTCC
AACCTCAAGAAGGAGGGTTCCACCCACAATTGGCAACACATCACCGACCAAATTGGCATG
TTCTGTTTCACAGGGCTAAAGCCTGAACAGGTGGAGCGGCTGATCAAGGAGTTCTCCATC
TACATGACAAAAGATGGCCGCATCTCTGTGGCAGGGGTCACCTCCAGCAACGTGGGCTAC
CTTGCCCATGCCATTCACCAGGTCACCAAGTAA
|
| Enzyme 79 GenBank Gene ID |
AK290847  |
| Enzyme 79 GeneCard ID |
Not Available |
| Enzyme 79 GenAtlas ID |
Not Available |
| Enzyme 79 HGNC ID |
HGNC:4433  |
| Enzyme 79 Chromosome Location |
Not Available |
| Enzyme 79 Locus |
Not Available |
| Enzyme 79 SNPs |
Not Available |
| Enzyme 79 General References |
Not Available |
| Enzyme 79 Metabolite References |
Not Available |
|
Enzyme 80
[top]
|
| Enzyme 80 ID |
14719 |
| Enzyme 80 Name |
cDNA FLJ77623, highly similar to Homo sapiens glutamate decarboxylase 1 (brain, 67kDa) (GAD1), transcript variant GAD67, mRNA |
| Enzyme 80 Synonyms |
Not Available |
| Enzyme 80 Gene Name |
Not Available |
| Enzyme 80 Protein Sequence |
>cDNA FLJ77623, highly similar to Homo sapiens glutamate decarboxylase 1 (brain, 67kDa) (GAD1), transcript variant GAD67, mRNA
MASSTPSSSATSSNAGADPNTTNLRPTTYDTWCGVAHGCTRKLGLKICGFLQRTNSLEEK
SRLVSAFKERQSSKNLLSCENSDRDARFRRTETDFSNLFARDLLPAKNGEEQTVQFLLEV
VDILLNYVRKTFDRSTKVLDFHHPHQLLEGMEGFNLELSDHPESLEQILVDCRDTLKYGV
RTGHPRFFNQLSTGLDIIGLAGEWLTSTANTNMFTYEIAPVFVLMEQITLKKMREIVGWS
SKDGDGIFSPGGAISNMYSIMAARYKYFPEVKTKGMAAVPKLVLFTSEQSHYSIKKAGAA
LGFGTDNVILIKCNERGKIIPADFEAKILEAKQKGYVPFYVNATAGTTVYGAFDPIQEIA
DICEKYNLWLHVDAAWGGGLLMSRKHRHKLNGIERANSVTWNPHKMMGVLLQCSAILVKE
KGILQGCNQMCAGYLFQPDKQYDVSYDTGDKAIPCGRHVDIFKFWLMWKAKGTVGFENQI
NKCLELAEYLYAKIKNREEFEMVFNGEPEHTNVCFWYIPQSLRGVPDSPQRREKLHKVAP
KIKALMMESGTTMVGYQPQGDKANFFRMVISNPAATQSDIDFLIEEIERLGQDL
|
| Enzyme 80 Number of Residues |
594 |
| Enzyme 80 Molecular Weight |
66865.0 |
| Enzyme 80 Theoretical pI |
7.67 |
| Enzyme 80 GO Classification |
| Function |
- binding
- carbon-carbon lyase activity
- carboxy-lyase activity
- catalytic activity
- cofactor binding
- lyase activity
- pyridoxal phosphate binding
|
| Process |
- carboxylic acid metabolic process
- cellular metabolic process
- metabolic process
- organic acid metabolic process
- oxoacid metabolic process
|
| Component |
| — |
|
| Enzyme 80 General Function |
Involved in carboxy-lyase activity |
| Enzyme 80 Specific Function |
Not Available |
| Enzyme 80 Pathways |
Not Available |
| Enzyme 80 Reactions |
Not Available |
| Enzyme 80 Pfam Domain Function |
|
| Enzyme 80 Signals |
|
| Enzyme 80 Transmembrane Regions |
|
| Enzyme 80 Essentiality |
Not Available |
| Enzyme 80 GenBank ID Protein |
158258601  |
| Enzyme 80 UniProtKB/Swiss-Prot ID |
A8K967  |
| Enzyme 80 UniProtKB/Swiss-Prot Entry Name |
A8K967_HUMAN  |
| Enzyme 80 PDB ID |
Not Available |
| Enzyme 80 Cellular Location |
Not Available |
| Enzyme 80 Gene Sequence |
>1785 bp
ATGGCGTCTTCGACCCCATCTTCGTCCGCAACCTCCTCGAACGCGGGAGCGGACCCCAAT
ACCACTAACCTGCGCCCCACAACGTACGATACCTGGTGCGGCGTGGCCCACGGATGCACC
AGAAAACTGGGGCTCAAGATCTGCGGCTTCTTGCAAAGGACCAACAGCCTGGAAGAGAAG
AGTCGCCTTGTGAGTGCCTTCAAGGAGAGGCAATCCTCCAAGAACCTGCTTTCCTGTGAA
AACAGCGACCGGGATGCCCGCTTCCGGCGCACAGAGACTGACTTCTCTAATCTGTTTGCT
AGAGATCTGCTTCCGGCTAAGAACGGTGAGGAGCAAACCGTGCAATTCCTCCTGGAAGTG
GTGGACATACTCCTCAACTATGTCCGCAAGACATTTGATCGCTCCACCAAGGTGCTGGAC
TTTCATCACCCACACCAGTTGCTGGAAGGCATGGAGGGCTTCAACTTGGAGCTCTCTGAC
CACCCCGAGTCCCTGGAGCAGATCCTGGTTGACTGCAGAGACACCTTGAAGTATGGGGTT
CGCACAGGTCATCCTCGATTTTTCAACCAGCTCTCCACTGGATTGGATATTATTGGCCTA
GCTGGAGAATGGCTGACATCAACGGCCAATACCAACATGTTTACATATGAAATTGCACCA
GTGTTTGTCCTCATGGAACAAATAACACTTAAGAAGATGAGAGAGATAGTTGGATGGTCA
AGTAAAGATGGTGATGGGATATTTTCTCCTGGGGGCGCCATATCCAACATGTACAGCATC
ATGGCTGCTCGCTACAAGTACTTCCCGGAAGTTAAGACAAAGGGCATGGCGGCTGTGCCT
AAACTGGTCCTCTTCACCTCAGAACAGAGTCACTATTCCATAAAGAAAGCTGGGGCTGCA
CTTGGCTTTGGAACTGACAATGTGATTTTGATAAAGTGCAATGAAAGGGGGAAAATAATT
CCAGCTGATTTTGAGGCAAAAATTCTTGAAGCCAAACAGAAGGGATATGTTCCCTTTTAT
GTCAATGCAACTGCTGGCACGACTGTTTATGGAGCTTTTGATCCGATACAAGAGATTGCA
GATATATGTGAGAAATATAACCTTTGGTTGCATGTCGATGCTGCCTGGGGAGGTGGGCTG
CTCATGTCCAGGAAGCACCGCCATAAACTCAACGGCATAGAAAGGGCCAACTCAGTCACC
TGGAACCCTCACAAGATGATGGGCGTGCTGTTGCAGTGCTCTGCCATTCTCGTCAAGGAA
AAGGGTATACTCCAAGGATGCAACCAGATGTGTGCAGGATACCTCTTCCAGCCAGACAAG
CAGTATGATGTCTCCTACGACACCGGGGACAAGGCAATTCCGTGTGGCCGCCACGTGGAT
ATCTTCAAGTTCTGGCTGATGTGGAAAGCAAAGGGCACAGTGGGATTTGAAAACCAGATC
AACAAATGCCTGGAACTGGCTGAATACCTCTATGCCAAGATTAAAAACAGAGAAGAATTT
GAGATGGTTTTCAATGGCGAGCCTGAGCACACAAACGTCTGTTTTTGGTATATTCCACAA
AGCCTCAGGGGTGTGCCAGACAGCCCTCAACGACGGGAAAAGCTACACAAGGTGGCTCCA
AAAATCAAAGCCCTGATGATGGAGTCAGGTACGACCATGGTTGGCTACCAGCCCCAAGGG
GACAAGGCCAACTTCTTCCGGATGGTCATCTCCAACCCAGCCGCTACCCAGTCTGACATT
GACTTCCTCATTGAGGAGATAGAAAGACTGGGCCAGGATCTGTAA
|
| Enzyme 80 GenBank Gene ID |
AK292582  |
| Enzyme 80 GeneCard ID |
Not Available |
| Enzyme 80 GenAtlas ID |
Not Available |
| Enzyme 80 HGNC ID |
HGNC:4092  |
| Enzyme 80 Chromosome Location |
Not Available |
| Enzyme 80 Locus |
Not Available |
| Enzyme 80 SNPs |
Not Available |
| Enzyme 80 General References |
Not Available |
| Enzyme 80 Metabolite References |
Not Available |
|
Enzyme 81
[top]
|
| Enzyme 81 ID |
14720 |
| Enzyme 81 Name |
cDNA FLJ77209 |
| Enzyme 81 Synonyms |
Not Available |
| Enzyme 81 Gene Name |
Not Available |
| Enzyme 81 Protein Sequence |
>cDNA FLJ77209
MDASLEKIADPTLAEMGKNLKEAVKMLEDSQRRTEEENGKKLISRDIPGPLQGSGQDMVS
ILQLVQNLMHGDEDEEPQSPRIQNIGEQGHVAVLGHSLGAYILTLDEEKLRKLTTRILSD
TTLWLCRIFRYENGCAYFHEEEREGLAKICRLAIHSQYEDFVVDGFSGLYNKKPVIYLSA
AARPGLGQYLCNQLGLPFPCLCRVPCNTMFGSQHQMDVAFLEKLIKDDIERGRLPLLLVA
NAGTAAVGHTDKIGRLKELCEQYGIWLHVEGVNLATLALGYVSSSVLAAAKCDSMTMTPG
PWLGLPAVPAVTLYKHDPALTLVAGLISNKPTDKLRALPLWLSLQYLGLDGFVERIKHAC
QLSQWLQESLKKVNYIKILVEDELSSPVVVFRFFQELPGSDPVFKAVPVPNMTPSAVGRE
RHSCDALNLWLGEQLKQLVPASGLTVMDLEAEGTCLRFSPLMTAAGMIS
|
| Enzyme 81 Number of Residues |
469 |
| Enzyme 81 Molecular Weight |
51811 |
| Enzyme 81 Theoretical pI |
5.81 |
| Enzyme 81 GO Classification |
Not Available |
| Enzyme 81 General Function |
Amino acid transport and metabolism |
| Enzyme 81 Specific Function |
Not Available |
| Enzyme 81 Pathways |
Not Available |
| Enzyme 81 Reactions |
Not Available |
| Enzyme 81 Pfam Domain Function |
Not Available |
| Enzyme 81 Signals |
|
| Enzyme 81 Transmembrane Regions |
|
| Enzyme 81 Essentiality |
Not Available |
| Enzyme 81 GenBank ID Protein |
158259181  |
| Enzyme 81 UniProtKB/Swiss-Prot ID |
A8K9Z5  |
| Enzyme 81 UniProtKB/Swiss-Prot Entry Name |
A8K9Z5_HUMAN  |
| Enzyme 81 PDB ID |
Not Available |
| Enzyme 81 Cellular Location |
Not Available |
| Enzyme 81 Gene Sequence |
>1410 bp
ATGGACGCGTCCCTGGAGAAGATAGCAGACCCCACGTTAGCTGAAATGGGAAAAAACTTG
AAGGAGGCAGTGAAGATGCTGGAGGACAGTCAGAGAAGAACAGAAGAGGAAAATGGAAAG
AAGCTCATATCCAGAGATATTCCAGGCCCACTCCAGGGCAGTGGACAAGATATGGTGAGC
ATCCTCCAGTTAGTTCAGAATCTGATGCATGGAGATGAAGATGAGGAGCCCCAGAGCCCC
AGAATCCAAAATATTGGAGAACAAGGTCATGTGGCTGTGTTGGGACATAGTCTGGGAGCT
TATATTTTGACTCTGGACGAAGAGAAGCTGAGAAAACTTACAACTAGGATACTTTCAGAT
ACCACCTTATGGCTATGCAGAATTTTCAGATATGAAAATGGGTGTGCTTATTTCCACGAA
GAGGAAAGAGAAGGACTTGCAAAGATATGTAGGCTTGCCATTCATTCTCAATATGAAGAC
TTCGTAGTGGATGGCTTCAGTGGGTTATATAACAAGAAGCCTGTCATATATCTTAGTGCT
GCTGCTAGACCTGGCCTGGGCCAATACCTTTGTAATCAGCTCGGCTTGCCCTTCCCCTGC
TTGTGCCGTGTACCCTGTAACACTATGTTTGGATCCCAGCATCAGATGGATGTTGCCTTC
CTGGAGAAACTGATTAAAGATGATATAGAGCGAGGAAGACTGCCCCTGTTGCTTGTCGCA
AATGCAGGAACGGCAGCAGTAGGACACACAGACAAGATTGGGAGATTGAAAGAACTCTGT
GAGCAGTATGGCATATGGCTTCATGTGGAGGGTGTGAATCTGGCAACATTGGCTCTGGGT
TATGTCTCCTCATCAGTGCTGGCTGCAGCCAAATGTGATAGCATGACGATGACTCCTGGC
CCGTGGCTGGGTTTGCCAGCTGTTCCTGCGGTGACACTGTATAAACACGACCCTGCCTTG
ACTTTAGTTGCTGGTCTTATATCAAATAAGCCCACAGACAAACTCCGTGCCCTGCCTCTG
TGGTTATCTTTACAATACTTGGGACTTGATGGGTTTGTGGAGAGGATCAAGCATGCCTGT
CAACTGAGTCAATGGTTGCAGGAAAGTTTGAAGAAAGTGAATTACATCAAAATCTTGGTG
GAAGATGAGCTCAGCTCCCCAGTGGTGGTGTTCAGATTTTTCCAAGAATTACCAGGCTCA
GATCCAGTGTTTAAAGCCGTCCCAGTGCCCAACATGACACCTTCAGCAGTCGGCCGGGAG
AGGCACTCGTGTGATGCGCTGAATCTCTGGCTGGGAGAACAGCTGAAGCAGCTGGTGCCT
GCGAGCGGCCTCACAGTCATGGATCTGGAAGCTGAGGGCACGTGTTTGCGGTTCAGCCCT
TTGATGACCGCAGCAGGTATGATCTCGTGA
|
| Enzyme 81 GenBank Gene ID |
AK292860  |
| Enzyme 81 GeneCard ID |
A8K9Z5  |
| Enzyme 81 GenAtlas ID |
Not Available |
| Enzyme 81 HGNC ID |
Not Available |
| Enzyme 81 Chromosome Location |
Not Available |
| Enzyme 81 Locus |
Not Available |
| Enzyme 81 SNPs |
Not Available |
| Enzyme 81 General References |
Not Available |
| Enzyme 81 Metabolite References |
Not Available |
|
Enzyme 82
[top]
|
| Enzyme 82 ID |
14721 |
| Enzyme 82 Name |
Serine hydroxymethyltransferase |
| Enzyme 82 Synonyms |
Not Available |
| Enzyme 82 Gene Name |
SHMT1 |
| Enzyme 82 Protein Sequence |
>Serine hydroxymethyltransferase
MTMPVNGAHKDADLWSSHDKMLAQPLKDSDVEVYNIIKKESNRQRVGLELIASENFASRA
VLEALGSCLNNKYSEGYPGQRYYGGTEFIDELETLCQKRALQAYKLDPQCWGVNVQPYSG
SPANFAVYTALVEPHGRIMGLDLPDGGHLTHGFMTDKKKISATSIFFESMPYKVNPDTGY
INYDQLEENARLFHPKLIIAGTSCYSRNLEYARLRKIADENGAYLMADMAHISGLVAAGV
VPSPFEHCHVVTTTTHKTLRGCRAGMIFYRKGVKSVDPKTGKEILYNLESLINSAVFPGL
QGGPHNHAIAGVAVALKQAMTLEFKVYQHQVVANCRALSEALTELGYKIVTGGSDNHLIL
VDLRSKGTDGGRAEKVLEACSIACNKNTCPGIELTLQIQSDTGVRATLKEFKERLAGDKY
QAAVQALREEVESFASLFPLPGLPDF
|
| Enzyme 82 Number of Residues |
446 |
| Enzyme 82 Molecular Weight |
48998.5 |
| Enzyme 82 Theoretical pI |
7.01 |
| Enzyme 82 GO Classification |
| Function |
- binding
- catalytic activity
- cofactor binding
- glycine hydroxymethyltransferase activity
- methyltransferase activity
- pyridoxal phosphate binding
- transferase activity
- transferase activity, transferring one-carbon groups
|
| Process |
- L-serine metabolic process
- cellular amino acid and derivative metabolic process
- cellular amino acid metabolic process
- cellular metabolic process
- glycine metabolic process
- metabolic process
- serine family amino acid metabolic process
|
| Component |
| — |
|
| Enzyme 82 General Function |
Involved in catalytic activity |
| Enzyme 82 Specific Function |
Interconversion of serine and glycine |
| Enzyme 82 Pathways |
Not Available |
| Enzyme 82 Reactions |
- 5,10-methylenetetrahydrofolate + glycine + H2O = tetrahydrofolate + L-serine [RN:R00945]
|
| Enzyme 82 Pfam Domain Function |
|
| Enzyme 82 Signals |
|
| Enzyme 82 Transmembrane Regions |
|
| Enzyme 82 Essentiality |
Not Available |
| Enzyme 82 GenBank ID Protein |
22547186  |
| Enzyme 82 UniProtKB/Swiss-Prot ID |
A8MYA6  |
| Enzyme 82 UniProtKB/Swiss-Prot Entry Name |
A8MYA6_HUMAN  |
| Enzyme 82 PDB ID |
Not Available |
| Enzyme 82 Cellular Location |
Not Available |
| Enzyme 82 Gene Sequence |
>1452 bp
ATGACGATGCCAGTCAACGGGGCCCACAAGGATGCTGACCTGTGGTCCTCACATGACAAG
ATGCTGGCACAACCCCTCAAAGACAGTGATGTTGAGGTTTACAACATCATTAAGAAGGAG
AGTAACCGGCAGAGGGTTGGATTGGAGCTGATTGCCTCGGAGAATTTCGCCAGCCGAGCA
GTTTTGGAGGCCCTAGGCTCTTGCTTAAATAACAAATACTCTGAGGGGTACCCGGGCCAG
AGATACTATGGCGGGACTGAGTTTATTGATGAACTGGAGACCCTCTGTCAGAAGCGAGCC
CTGCAGGCCTATAAGCTGGACCCACAGTGCTGGGGGGTCAACGTCCAGCCCTACTCAGGC
TCCCCTGCAAACTTTGCTGTGTACACTGCCCTGGTGGAACCCCATGGGCGCATCATGGGC
CTGGACCTTCCGGATGGGGGCCACCTGACCCATGGGTTCATGACAGACAAGAAGAAAATC
TCTGCCACGTCCATCTTCTTTGAATCTATGCCCTACAAGGTGAACCCAGATACTGGCTAC
ATCAACTATGACCAGCTGGAGGAGAACGCACGCCTCTTCCACCCGAAGCTGATCATCGCA
GGAACCAGCTGCTACTCCCGAAACCTGGAATATGCCCGGCTACGGAAGATTGCAGATGAG
AACGGGGCGTATCTCATGGCGGACATGGCTCACATCAGCGGGCTGGTGGCGGCTGGCGTG
GTGCCCTCCCCATTTGAACACTGCCATGTGGTGACCACCACCACTCACAAGACCCTGCGA
GGCTGCCGAGCTGGCATGATCTTCTACAGGAAAGGAGTGAAAAGTGTGGATCCCAAGACT
GGCAAAGAGATTCTGTACAACCTGGAGTCTCTTATCAATTCTGCTGTGTTCCCTGGCCTG
CAGGGAGGTCCCCACAACCACGCCATTGCTGGGGTTGCTGTGGCACTGAAGCAAGCTATG
ACTCTGGAATTTAAAGTTTATCAACACCAGGTGGTGGCCAACTGCAGGGCTCTGTCTGAG
GCCCTGACGGAGCTGGGCTACAAAATAGTCACAGGTGGTTCTGACAACCATTTGATCCTT
GTGGATCTCCGTTCCAAAGGCACAGATGGTGGAAGGGCTGAGAAGGTGCTAGAAGCCTGT
TCTATTGCCTGCAACAAGAACACCTGTCCAGGTGACAGAAGCGCTCTGCGGCCCAGTGGA
CTGCGGCTGGGGACCCCAGCACTGACGTCCCGTGGACTTTTGGAAAAAGACTTCCAAAAA
GTAGCCCACTTTATTCACAGAGGGATAGAGCTGACCCTGCAGATCCAGAGCGACACTGGT
GTCAGAGCCACCCTGAAAGAGTTCAAGGAGAGACTGGCAGGGGATAAGTACCAGGCGGCC
GTGCAGGCTCTCCGGGAGGAGGTTGAGAGCTTCGCCTCTCTCTTCCCTCTGCCTGGCCTG
CCTGACTTCTAA
|
| Enzyme 82 GenBank Gene ID |
NM_004169  |
| Enzyme 82 GeneCard ID |
SHMT1  |
| Enzyme 82 GenAtlas ID |
SHMT1  |
| Enzyme 82 HGNC ID |
HGNC:10850  |
| Enzyme 82 Chromosome Location |
1 |
| Enzyme 82 Locus |
17p11.2 |
| Enzyme 82 SNPs |
SNPJam Report  |
| Enzyme 82 General References |
- Zody MC, Garber M, Adams DJ, Sharpe T, Harrow J, Lupski JR, Nicholson C, Searle SM, Wilming L, Young SK, Abouelleil A, Allen NR, Bi W, Bloom T, Borowsky ML, Bugalter BE, Butler J, Chang JL, Chen CK, Cook A, Corum B, Cuomo CA, de Jong PJ, DeCaprio D, Dewar K, FitzGerald M, Gilbert J, Gibson R, Gnerre S, Goldstein S, Grafham DV, Grocock R, Hafez N, Hagopian DS, Hart E, Norman CH, Humphray S, Jaffe DB, Jones M, Kamal M, Khodiyar VK, LaButti K, Laird G, Lehoczky J, Liu X, Lokyitsang T, Loveland J, Lui A, Macdonald P, Major JE, Matthews L, Mauceli E, McCarroll SA, Mihalev AH, Mudge J, Nguyen C, Nicol R, O'Leary SB, Osoegawa K, Schwartz DC, Shaw-Smith C, Stankiewicz P, Steward C, Swarbreck D, Venkataraman V, Whittaker CA, Yang X, Zimmer AR, Bradley A, Hubbard T, Birren BW, Rogers J, Lander ES, Nusbaum C: DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage. Nature. 2006 Apr 20;440(7087):1045-9. [PubMed
]
|
| Enzyme 82 Metabolite References |
Not Available |
|
Enzyme 83
[top]
|
| Enzyme 83 ID |
14722 |
| Enzyme 83 Name |
Aspartate aminotransferase |
| Enzyme 83 Synonyms |
Not Available |
| Enzyme 83 Gene Name |
GIG18 |
| Enzyme 83 Protein Sequence |
>Aspartate aminotransferase
MAPPSVFAEVPQAQPVLVFKLTADFREDPDPRKVNLGVGAYRTDDCHPWVLPVVKKVEQK
IANDNSLNHEYLPILGLAEFRSCASRLALEDDSPALKEKRVGGVQSLGGTGALRIGADFL
ARWYNGTNNKNTPVYVSSPTWENHNAVFSAAGFKDIRSYRYWDAEKRGLDLQGFLNDLEN
APEFSIVVLHACAHNPTGIDPTPEQWKQIASVMKHRFLFPFFDSAYQGFASGNLERDAWA
IRYFVSEGFEFFCAQSFSKNFGLYNERVGNLTVVGKEPESILQVLSQMEKIVRITWSNPP
AQGARIVASTLSNPELFEEWTGNVKTMADRILTMRSELRARLEALKTPGTWNHITDQIGM
FSFTGLNPKQVEYLVNEKHIYLLPSGRINVSGLTTKNLDYVATSIHEAVTKIQ
|
| Enzyme 83 Number of Residues |
413 |
| Enzyme 83 Molecular Weight |
46319.2 |
| Enzyme 83 Theoretical pI |
6.80 |
| Enzyme 83 GO Classification |
| Function |
- binding
- catalytic activity
- cofactor binding
- pyridoxal phosphate binding
- transaminase activity
- transferase activity
- transferase activity, transferring nitrogenous groups
|
| Process |
- biosynthetic process
- cellular amino acid and derivative metabolic process
- cellular amino acid metabolic process
- cellular metabolic process
- metabolic process
|
| Component |
| — |
|
| Enzyme 83 General Function |
Involved in transferase activity, transferring nitrogenous groups |
| Enzyme 83 Specific Function |
L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate |
| Enzyme 83 Pathways |
|
| Enzyme 83 Reactions |
- L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate [RN:R00355]
|
| Enzyme 83 Pfam Domain Function |
|
| Enzyme 83 Signals |
|
| Enzyme 83 Transmembrane Regions |
|
| Enzyme 83 Essentiality |
Not Available |
| Enzyme 83 GenBank ID Protein |
46981967  |
| Enzyme 83 UniProtKB/Swiss-Prot ID |
Q2TU84  |
| Enzyme 83 UniProtKB/Swiss-Prot Entry Name |
Q2TU84_HUMAN  |
| Enzyme 83 PDB ID |
1AJS  |
| Enzyme 83 PDB File |
Show |
| Enzyme 83 3D Structure |
|
| Enzyme 83 Cellular Location |
Not Available |
| Enzyme 83 Gene Sequence |
>1242 bp
ATGGCACCTCCGTCAGTCTTTGCCGAGGTTCCGCAGGCCCAGCCTGTCCTGGTCTTCAAG
CTCACTGCCGACTTCAGGGAGGATCCGGACCCCCGCAAGGTCAACCTGGGAGTGGGAGCA
TATCGCACGGATGACTGCCATCCCTGGGTTTTGCCAGTAGTGAAGAAAGTGGAGCAGAAG
ATTGCTAATGACAATAGCCTAAATCACGAGTATCTGCCAATCCTGGGCCTGGCTGAGTTC
CGGAGCTGTGCTTCTCGTCTTGCCCTTGAGGATGACAGCCCAGCACTCAAGGAGAAGCGG
GTAGGAGGTGTGCAATCTTTGGGGGGAACAGGTGCACTTCGAATTGGAGCTGATTTCTTA
GCGCGTTGGTACAATGGAACAAACAACAAGAACACACCTGTCTATGTGTCCTCACCAACC
TGGGAGAATCACAATGCTGTGTTTTCCGCTGCTGGTTTTAAAGACATTCGGTCCTATCGC
TACTGGGATGCAGAGAAGAGAGGATTGGACCTCCAGGGCTTCCTGAATGATCTGGAGAAT
GCTCCTGAGTTCTCCATTGTTGTCCTCCACGCCTGTGCACACAACCCAACTGGGATTGAC
CCAACTCCGGAGCAGTGGAAGCAGATTGCTTCTGTCATGAAGCACCGGTTTCTGTTCCCC
TTCTTTGACTCAGCCTATCAGGGCTTCGCATCTGGAAACCTGGAGAGAGATGCCTGGGCC
ATTCGCTATTTTGTGTCTGAAGGCTTCGAGTTCTTCTGTGCCCAGTCCTTCTCCAAGAAC
TTCGGGCTCTACAATGAGAGAGTCGGGAATCTGACTGTGGTTGGAAAAGAACCTGAGAGC
ATCCTGCAAGTCCTTTCCCAGATGGAGAAGATCGTGCGGATTACTTGGTCCAATCCCCCC
GCCCAGGGAGCACGAATTGTGGCCAGCACCCTCTCTAACCCTGAGCTCTTTGAGGAATGG
ACAGGTAATGTGAAGACAATGGCTGACCGGATTCTGACCATGAGATCTGAACTCAGGGCA
CGACTAGAAGCCCTCAAAACCCCTGGGACCTGGAACCACATCACTGATCAAATTGGCATG
TTCAGCTTCACTGGGTTGAACCCCAAGCAGGTTGAGTATCTGGTCAATGAAAAGCACATC
TACCTGCTGCCAAGTGGTCGAATCAACGTGAGTGGCTTAACCACCAAAAATCTAGATTAC
GTGGCCACCTCCATCCATGAAGCAGTCACCAAAATCCAGTGA
|
| Enzyme 83 GenBank Gene ID |
AY513279  |
| Enzyme 83 GeneCard ID |
GIG18  |
| Enzyme 83 GenAtlas ID |
GIG18  |
| Enzyme 83 HGNC ID |
HGNC:4432  |
| Enzyme 83 Chromosome Location |
Not Available |
| Enzyme 83 Locus |
Not Available |
| Enzyme 83 SNPs |
SNPJam Report  |
| Enzyme 83 General References |
Not Available |
| Enzyme 83 Metabolite References |
Not Available |
|
Enzyme 84
[top]
|
| Enzyme 84 ID |
14723 |
| Enzyme 84 Name |
GAD1 protein |
| Enzyme 84 Synonyms |
Not Available |
| Enzyme 84 Gene Name |
GAD1 |
| Enzyme 84 Protein Sequence |
>GAD1 protein
MASSTPSSSATSSNAGADPNTTNLRPTTYDTWCGVAHGCTRKLGLKICGFLQRTNSLEEK
SRLVSAFKERQSSKNLLSCENSDRDARFRRTETDFSNLFARDLLPAKNGEEQTVQFLLEV
VDILLNYVRKTFDRSTKVLDFHHPHQLLEGMEGFNLELSDHPESLEQILVDCRDTLKYGV
RTGHPRFFNQLSTGLDIIGLAGEWLTSTANTNMFTYEIAPVFVLMEQITLKKMREIVGWS
SKDGDGIFSPGGAISNMYSIMAARYKYFPEVKTKGMAAVPKLVLFTSEQSHYSIKKAGAA
LGFGTDNVILIKCNERGKIIPADFEAKILEAKQKGYVPFYVNATAGTTVYGAFDPIQEIA
DICEKYNLWLHVDGFNFSQLANRIICLATELMTNKGCVTWHPNYSVNMHHGCLGRWAAHV
QEAPP
|
| Enzyme 84 Number of Residues |
425 |
| Enzyme 84 Molecular Weight |
47439.6 |
| Enzyme 84 Theoretical pI |
7.30 |
| Enzyme 84 GO Classification |
| Function |
- binding
- carbon-carbon lyase activity
- carboxy-lyase activity
- catalytic activity
- cofactor binding
- lyase activity
- pyridoxal phosphate binding
|
| Process |
- carboxylic acid metabolic process
- cellular metabolic process
- metabolic process
- organic acid metabolic process
- oxoacid metabolic process
|
| Component |
| — |
|
| Enzyme 84 General Function |
Involved in carboxy-lyase activity |
| Enzyme 84 Specific Function |
Not Available |
| Enzyme 84 Pathways |
Not Available |
| Enzyme 84 Reactions |
Not Available |
| Enzyme 84 Pfam Domain Function |
|
| Enzyme 84 Signals |
|
| Enzyme 84 Transmembrane Regions |
|
| Enzyme 84 Essentiality |
Not Available |
| Enzyme 84 GenBank ID Protein |
71297135  |
| Enzyme 84 UniProtKB/Swiss-Prot ID |
Q49AK1  |
| Enzyme 84 UniProtKB/Swiss-Prot Entry Name |
Q49AK1_HUMAN  |
| Enzyme 84 PDB ID |
Not Available |
| Enzyme 84 Cellular Location |
Not Available |
| Enzyme 84 Gene Sequence |
>1278 bp
ATGGCGTCTTCGACCCCATCTTCGTCCGCAACCTCCTCGAACGCGGGAGCGGACCCCAAT
ACCACTAACCTGCGCCCCACAACGTACGATACCTGGTGCGGCGTGGCCCATGGATGCACC
AGAAAACTGGGGCTCAAGATCTGCGGCTTCTTGCAAAGGACCAACAGCCTGGAAGAGAAG
AGTCGCCTTGTGAGTGCCTTCAAGGAGAGGCAATCCTCCAAGAACCTGCTTTCCTGTGAA
AACAGCGACCGGGATGCCCGCTTCCGGCGCACAGAGACTGACTTCTCTAATCTGTTTGCT
AGAGATCTGCTTCCGGCTAAGAACGGTGAGGAGCAAACCGTGCAATTCCTCCTGGAAGTG
GTGGACATACTCCTCAACTATGTCCGCAAGACATTTGATCGCTCCACCAAGGTGCTGGAC
TTTCATCACCCACACCAGTTGCTGGAAGGCATGGAGGGCTTCAACTTGGAGCTCTCTGAC
CACCCCGAGTCCCTGGAGCAGATCCTGGTTGACTGCAGAGACACCTTGAAGTATGGGGTT
CGCACAGGTCATCCTCGATTTTTCAACCAGCTCTCCACTGGATTGGATATTATTGGCCTA
GCTGGAGAATGGCTGACATCAACGGCCAATACCAACATGTTTACATATGAAATTGCACCA
GTGTTTGTCCTCATGGAACAAATAACACTTAAGAAGATGAGAGAGATAGTTGGATGGTCA
AGTAAAGATGGTGATGGGATATTTTCTCCTGGGGGCGCCATATCCAACATGTACAGCATC
ATGGCTGCTCGCTACAAGTACTTCCCGGAAGTTAAGACAAAGGGCATGGCGGCTGTGCCT
AAACTGGTCCTCTTCACCTCAGAACAGAGTCACTATTCCATAAAGAAAGCTGGGGCTGCA
CTTGGCTTTGGAACTGACAATGTGATTTTGATAAAGTGCAATGAAAGGGGGAAAATAATT
CCAGCTGATTTTGAGGCAAAAATTCTTGAAGCCAAACAGAAGGGATATGTTCCCTTTTAT
GTCAATGCAACTGCTGGCACGACTGTTTATGGAGCTTTTGATCCGATACAAGAGATTGCA
GATATATGTGAGAAATATAACCTTTGGTTGCATGTCGATGGATTTAACTTCTCACAATTG
GCCAATAGGATCATCTGCCTTGCTACTGAACTAATGACTAACAAAGGCTGTGTCACGTGG
CATCCCAACTATTCAGTAAACATGCATCATGGCTGCCTGGGGAGGTGGGCTGCTCATGTC
CAGGAAGCACCACCATAA
|
| Enzyme 84 GenBank Gene ID |
BC036552  |
| Enzyme 84 GeneCard ID |
GAD1  |
| Enzyme 84 GenAtlas ID |
GAD1  |
| Enzyme 84 HGNC ID |
HGNC:4092  |
| Enzyme 84 Chromosome Location |
2 |
| Enzyme 84 Locus |
2q31 |
| Enzyme 84 SNPs |
SNPJam Report  |
| Enzyme 84 General References |
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
|
| Enzyme 84 Metabolite References |
Not Available |
|
Enzyme 85
[top]
|
| Enzyme 85 ID |
14724 |
| Enzyme 85 Name |
Serine hydroxymethyltransferase |
| Enzyme 85 Synonyms |
Not Available |
| Enzyme 85 Gene Name |
Not Available |
| Enzyme 85 Protein Sequence |
>Serine hydroxymethyltransferase
MLYFSLFWAARPLQRCGQLVRMAIRAQHSNAAQTQTGEANRGWTGQESLSDSDPEMWELL
QREKDRQCRGLELIASENFCSRAALEALGSCLNNKYSEGYPGKRYYGGAEVVDEIELLCQ
RRALEAFDLDPAQWGVNVQPYSGSPANLAVYTALLQPHDRIMGLDLPDGGHLTHGYMSDV
KRISATSIFFESMPYKLNPKTGLIDYNQLALTARLFRPRLIIAGTSAYARLIDYARMREV
CDEVKAHLLADMAHISGLVAAKVIPSPFKHADIVTTTTHKTLRGARSGLIFYRKGVKAVD
PKTGREIPYTFEDRINFAVFPSLQGGPHNHAIAAVAVALKQACTPMFREYSLQVLKNARA
MADALLERGYSLVSGGTDNHLVLVDLRPKGLDGARAERVLELVSITANKNTCPGDRSAIT
PGGLRLGAPALTSRQFHEDDFRRVVDFIDEGVNIGLEVKSKTAKLQDFKSFLLKDSETSQ
RLANLRQRVEQFARAFPMPGFDEH
|
| Enzyme 85 Number of Residues |
504 |
| Enzyme 85 Molecular Weight |
55973.3 |
| Enzyme 85 Theoretical pI |
8.53 |
| Enzyme 85 GO Classification |
| Function |
- binding
- catalytic activity
- cofactor binding
- glycine hydroxymethyltransferase activity
- methyltransferase activity
- pyridoxal phosphate binding
- transferase activity
- transferase activity, transferring one-carbon groups
|
| Process |
- L-serine metabolic process
- cellular amino acid and derivative metabolic process
- cellular amino acid metabolic process
- cellular metabolic process
- glycine metabolic process
- metabolic process
- serine family amino acid metabolic process
|
| Component |
| — |
|
| Enzyme 85 General Function |
Involved in catalytic activity |
| Enzyme 85 Specific Function |
Interconversion of serine and glycine |
| Enzyme 85 Pathways |
|
| Enzyme 85 Reactions |
- 5,10-methylenetetrahydrofolate + glycine + H2O = tetrahydrofolate + L-serine [RN:R00945]
|
| Enzyme 85 Pfam Domain Function |
|
| Enzyme 85 Signals |
|
| Enzyme 85 Transmembrane Regions |
|
| Enzyme 85 Essentiality |
Not Available |
| Enzyme 85 GenBank ID Protein |
Not Available |
| Enzyme 85 UniProtKB/Swiss-Prot ID |
Q53ET4  |
| Enzyme 85 UniProtKB/Swiss-Prot Entry Name |
Q53ET4_HUMAN  |
| Enzyme 85 PDB ID |
Not Available |
| Enzyme 85 Cellular Location |
Not Available |
| Enzyme 85 Gene Sequence |
>1515 bp
ATGCTGTACTTCTCTTTGTTTTGGGCGGCTCGGCCTCTGCAGAGATGTGGGCAGCTGGTC
AGGATGGCCATTCGGGCTCAGCACAGCAACGCAGCCCAGACTCAGACTGGGGAAGCAAAC
AGGGGCTGGACAGGCCAGGAGAGCCTGTCGGACAGTGATCCTGAGATGTGGGAGTTGCTG
CAGAGGGAGAAGGACAGGCAGTGTCGTGGCCTGGAGCTCATTGCCTCAGAGAACTTCTGC
AGCCGAGCTGCGCTGGAGGCCCTGGGGTCCTGTCTGAACAACAAGTACTCGGAGGGTTAT
CCTGGCAAGAGATACTATGGGGGAGCAGAGGTGGTGGATGAAATTGAGCTGCTGTGCCAG
CGCCGGGCCTTGGAAGCCTTTGACCTGGATCCTGCACAGTGGGGAGTCAATGTCCAGCCC
TACTCCGGGTCCCCAGCCAACCTGGCCGTCTACACAGCCCTTCTGCAACCTCACGACCGG
ATCATGGGGCTGGACCTGCCCGATGGGGGCCATCTCACCCACGGCTACATGTCTGACGTC
AAGCGGATATCAGCCACGTCCATCTTCTTCGAGTCTATGCCCTATAAGCTCAACCCCAAA
ACTGGCCTCATTGACTACAACCAGCTGGCACTGACTGCTCGACTTTTCCGGCCACGGCTC
ATCATAGCTGGCACCAGCGCCTATGCTCGCCTCATTGACTACGCCCGCATGAGAGAGGTG
TGTGATGAAGTCAAAGCACACCTGCTGGCAGACATGGCCCACATCAGTGGCCTGGTGGCT
GCCAAGGTGATTCCCTCGCCTTTCAAGCACGCGGACATCGTCACCACCACTACTCACAAG
ACTCTTCGAGGGGCCAGGTCAGGGCTCATCTTCTACCGGAAAGGGGTGAAGGCTGTGGAC
CCCAAGACTGGCCGGGAGATCCCTTACACATTTGAGGACCGAATCAACTTTGCCGTGTTC
CCATCCCTGCAGGGGGGCCCCCACAATCATGCCATTGCTGCAGTAGCTGTGGCCCTAAAG
CAGGCCTGCACCCCCATGTTCCGGGAGTACTCCCTGCAGGTTCTGAAGAATGCTCGGGCC
ATGGCAGATGCCCTGCTAGAGCGAGGCTACTCACTGGTATCAGGTGGTACTGACAACCAC
CTGGTGCTGGTGGACCTGCGGCCCAAGGGCCTGGATGGAGCTCGGGCTGAGCGGGTGCTA
GAGCTTGTATCCATCACTGCCAACAAGAACACCTGTCCTGGAGACCGAAGTGCCATCACA
CCGGGCGGCCTGCGGCTTGGGGCCCCAGCCTTAACTTCTCGACAGTTCCATGAGGATGAC
TTCCGGAGAGTTGTGGACTTTATAGATGAAGGGGTCAACATTGGCTTAGAGGTGAAGAGC
AAGACTGCCAAGCTCCAGGATTTCAAATCCTTCCTGCTTAAGGACTCAGAAACAAGTCAG
CGTCTGGCCAACCTCAGGCAACGGGTGGAGCAGTTTGCCAGGGCCTTCCCCATGCCTGGT
TTTGATGAGCATTGA
|
| Enzyme 85 GenBank Gene ID |
AK223555  |
| Enzyme 85 GeneCard ID |
Not Available |
| Enzyme 85 GenAtlas ID |
Not Available |
| Enzyme 85 HGNC ID |
HGNC:10852  |
| Enzyme 85 Chromosome Location |
Not Available |
| Enzyme 85 Locus |
Not Available |
| Enzyme 85 SNPs |
Not Available |
| Enzyme 85 General References |
- Maruyama K, Sugano S: Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides. Gene. 1994 Jan 28;138(1-2):171-4. [PubMed
]
- Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S: Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library. Gene. 1997 Oct 24;200(1-2):149-56. [PubMed
]
|
| Enzyme 85 Metabolite References |
Not Available |
|
Enzyme 86
[top]
|
| Enzyme 86 ID |
14725 |
| Enzyme 86 Name |
Serine hydroxymethyltransferase |
| Enzyme 86 Synonyms |
Not Available |
| Enzyme 86 Gene Name |
Not Available |
| Enzyme 86 Protein Sequence |
>Serine hydroxymethyltransferase
MTMPVNGAHKDADLWSSHDKMLAQPLKDSDVEVYNIIKKESNRQRVGLELIASENFASRA
VLEALGSCLNNKYSEGYPGQRYYGGTEFIDELETLCQKRALQAYKLDPQCWGVNVQPYSG
SPANFAVYTALVEPHGRIMGLDLPDGGHLTHGFMTDKKKISATSIFFESMPYKVNPDTGY
INYDQLEENARLFHPKLIIAGTSCYSRNLEYARLRKIADENGAYLMADMAHISGLVAAGV
VPSPFEHCHVVTTTTHKTLRGCRAGMIFYRKGVKSVDPKTGKEILYNLESLINSAVFPGL
QGGPHNHAIAEVAVALKQAMTLEFKVYQHQVVANCRALSEALTELGYKIVTGGSDNHLIL
VDLRSKGTDGGRAEKVLEACSIACNKNTCPGDRSALRPSGLRLGTPALTSRGLLEKDFQK
VAHFIHRGIELTLQIQSDTGVRATLKEFKERLAGDKYQAAVQALREEVESFASLFPLPGL
PDF
|
| Enzyme 86 Number of Residues |
483 |
| Enzyme 86 Molecular Weight |
53154.2 |
| Enzyme 86 Theoretical pI |
7.58 |
| Enzyme 86 GO Classification |
| Function |
- binding
- catalytic activity
- cofactor binding
- glycine hydroxymethyltransferase activity
- methyltransferase activity
- pyridoxal phosphate binding
- transferase activity
- transferase activity, transferring one-carbon groups
|
| Process |
- L-serine metabolic process
- cellular amino acid and derivative metabolic process
- cellular amino acid metabolic process
- cellular metabolic process
- glycine metabolic process
- metabolic process
- serine family amino acid metabolic process
|
| Component |
| — |
|
| Enzyme 86 General Function |
Involved in catalytic activity |
| Enzyme 86 Specific Function |
Interconversion of serine and glycine |
| Enzyme 86 Pathways |
|
| Enzyme 86 Reactions |
- 5,10-methylenetetrahydrofolate + glycine + H2O = tetrahydrofolate + L-serine [RN:R00945]
|
| Enzyme 86 Pfam Domain Function |
|
| Enzyme 86 Signals |
|
| Enzyme 86 Transmembrane Regions |
|
| Enzyme 86 Essentiality |
Not Available |
| Enzyme 86 GenBank ID Protein |
Not Available |
| Enzyme 86 UniProtKB/Swiss-Prot ID |
Q53ET7  |
| Enzyme 86 UniProtKB/Swiss-Prot Entry Name |
Q53ET7_HUMAN  |
| Enzyme 86 PDB ID |
1BJ4  |
| Enzyme 86 PDB File |
Show |
| Enzyme 86 3D Structure |
|
| Enzyme 86 Cellular Location |
Not Available |
| Enzyme 86 Gene Sequence |
>1452 bp
ATGACGATGCCAGTCAACGGGGCCCACAAGGATGCTGACCTGTGGTCCTCACATGACAAG
ATGCTGGCACAACCCCTCAAAGACAGTGATGTTGAGGTTTACAACATCATTAAGAAGGAG
AGTAACCGGCAGAGGGTTGGATTGGAGCTGATTGCCTCGGAGAATTTCGCCAGCCGAGCA
GTTTTGGAGGCCCTAGGCTCTTGCTTAAATAACAAATACTCTGAGGGGTACCCGGGCCAG
AGATACTATGGCGGGACTGAGTTTATTGATGAACTGGAGACCCTCTGTCAGAAGCGAGCC
CTGCAGGCCTATAAGCTGGACCCACAGTGCTGGGGGGTCAACGTCCAGCCCTACTCAGGC
TCCCCTGCAAACTTTGCTGTGTACACTGCCCTGGTGGAACCCCATGGGCGCATCATGGGC
CTGGACCTTCCGGATGGGGGCCACCTGACCCATGGGTTCATGACAGACAAGAAGAAAATC
TCTGCCACGTCCATCTTCTTTGAATCTATGCCCTACAAGGTGAACCCAGATACTGGCTAC
ATCAACTATGACCAGCTGGAGGAGAACGCACGCCTCTTCCACCCGAAGCTGATCATCGCA
GGAACCAGCTGCTACTCCCGAAACCTGGAATATGCCCGGCTACGGAAGATTGCAGATGAG
AACGGGGCGTATCTCATGGCGGACATGGCTCACATCAGCGGGCTGGTGGCGGCTGGCGTG
GTGCCCTCCCCATTTGAACACTGCCATGTGGTGACCACCACCACTCACAAGACCCTGCGA
GGCTGCCGAGCTGGCATGATCTTCTACAGGAAAGGAGTGAAAAGTGTGGATCCCAAGACT
GGCAAAGAGATTCTGTACAACCTGGAGTCTCTTATCAATTCTGCTGTGTTCCCTGGCCTG
CAGGGAGGTCCCCACAACCACGCCATTGCTGAGGTTGCTGTGGCACTGAAGCAAGCTATG
ACTCTGGAATTTAAAGTTTATCAACACCAGGTGGTGGCCAACTGCAGGGCTCTGTCTGAG
GCCCTGACGGAGCTGGGCTACAAAATAGTCACAGGTGGTTCTGACAACCATTTGATCCTT
GTGGATCTCCGTTCCAAAGGCACAGATGGTGGAAGGGCTGAGAAGGTGCTAGAAGCCTGT
TCTATTGCCTGCAACAAGAACACCTGTCCAGGTGACAGAAGCGCTCTGCGGCCCAGTGGA
CTGCGGCTGGGGACCCCAGCACTGACGTCCCGTGGACTTTTGGAAAAAGACTTCCAAAAA
GTAGCCCACTTTATTCACAGAGGGATAGAGCTGACCCTGCAGATCCAGAGCGACACTGGT
GTCAGAGCCACCCTGAAAGAGTTCAAGGAGAGACTGGCAGGGGATAAGTACCAGGCGGCC
GTGCAGGCTCTCCGGGAGGAGGTTGAGAGCTTCGCCTCTCTCTTCCCTCTGCCTGGCCTG
CCTGACTTCTAA
|
| Enzyme 86 GenBank Gene ID |
AK223552  |
| Enzyme 86 GeneCard ID |
Not Available |
| Enzyme 86 GenAtlas ID |
Not Available |
| Enzyme 86 HGNC ID |
HGNC:10850  |
| Enzyme 86 Chromosome Location |
Not Available |
| Enzyme 86 Locus |
Not Available |
| Enzyme 86 SNPs |
Not Available |
| Enzyme 86 General References |
- Maruyama K, Sugano S: Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides. Gene. 1994 Jan 28;138(1-2):171-4. [PubMed
]
- Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S: Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library. Gene. 1997 Oct 24;200(1-2):149-56. [PubMed
]
|
| Enzyme 86 Metabolite References |
Not Available |
|
Enzyme 87
[top]
|
| Enzyme 87 ID |
14726 |
| Enzyme 87 Name |
Dopa decarboxylase (Aromatic L-amino acid decarboxylase) |
| Enzyme 87 Synonyms |
- SubName: Dopa decarboxylase (Aromatic L-amino acid decarboxylase), isoform CRA_a
|
| Enzyme 87 Gene Name |
DDC |
| Enzyme 87 Protein Sequence |
>Dopa decarboxylase (Aromatic L-amino acid decarboxylase)
MNASEFRRRGKEMVDYVANYMEGIEGRQVYPDVEPGYLRPLIPAAAPQEPDTFEDIINDV
EKIIMPGVTHWHSPYFFAYFPTASSYPAMLADMLCGAIGCIGFSWAASPACTELETVMMD
WLGKMLELPKAFLNEKAGEGGGVIQGSASEATLVALLAARTKVIHRLQAASPELTQAAIM
EKLVAYSSDQAHSSVERAGLIGGVKLKAIPSDGNFAMRASALQEALERDKAAGLIPFFMV
ATLGTTTCCSFDNLLEVGPICNKEDIWLHVDAAYAGSAFICPEFRHLLNGVEFADSFNFN
PHKWLLVNFDCSAMWVKKRTDLTGAFRLDPTYLKHSHQDSGLITDYRHWQIPLGRRFRSL
KMWFVFRMYGVKGLQAYIRKHVQLSHEFESLVRQDPRFEICVEVILGLVCFRLKGSNKVN
EALLQRINSAKKIHLVPCHLRDKFVLRFAICSRTVESAHVQRAWEHIKELAADVLRAERE
|
| Enzyme 87 Number of Residues |
480 |
| Enzyme 87 Molecular Weight |
53893.8 |
| Enzyme 87 Theoretical pI |
7.21 |
| Enzyme 87 GO Classification |
| Function |
- binding
- carbon-carbon lyase activity
- carboxy-lyase activity
- catalytic activity
- cofactor binding
- lyase activity
- pyridoxal phosphate binding
|
| Process |
- carboxylic acid metabolic process
- cellular amino acid and derivative metabolic process
- cellular metabolic process
- metabolic process
- organic acid metabolic process
- oxoacid metabolic process
|
| Component |
| — |
|
| Enzyme 87 General Function |
Involved in carboxy-lyase activity |
| Enzyme 87 Specific Function |
Not Available |
| Enzyme 87 Pathways |
Not Available |
| Enzyme 87 Reactions |
Not Available |
| Enzyme 87 Pfam Domain Function |
|
| Enzyme 87 Signals |
|
| Enzyme 87 Transmembrane Regions |
|
| Enzyme 87 Essentiality |
Not Available |
| Enzyme 87 GenBank ID Protein |
30582857  |
| Enzyme 87 UniProtKB/Swiss-Prot ID |
Q53Y41  |
| Enzyme 87 UniProtKB/Swiss-Prot Entry Name |
Q53Y41_HUMAN  |
| Enzyme 87 PDB ID |
1JS3  |
| Enzyme 87 PDB File |
Show |
| Enzyme 87 3D Structure |
|
| Enzyme 87 Cellular Location |
Not Available |
| Enzyme 87 Gene Sequence |
>1443 bp
ATGAACGCAAGTGAATTCCGAAGGAGAGGGAAGGAGATGGTGGATTACGTGGCCAACTAC
ATGGAAGGCATTGAGGGACGCCAGGTCTACCCTGACGTGGAGCCCGGGTACCTGCGGCCG
CTGATCCCTGCCGCTGCCCCTCAGGAGCCAGACACGTTTGAGGACATCATCAACGACGTT
GAGAAGATAATCATGCCTGGGGTGACGCACTGGCACAGCCCCTACTTCTTCGCCTACTTC
CCCACTGCCAGCTCGTACCCGGCCATGCTTGCGGACATGCTGTGCGGGGCCATTGGCTGC
ATCGGCTTCTCCTGGGCGGCAAGCCCAGCATGCACAGAGCTGGAGACTGTGATGATGGAC
TGGCTCGGGAAGATGCTGGAACTACCAAAGGCATTTTTGAATGAGAAAGCTGGAGAAGGG
GGAGGAGTGATCCAGGGAAGTGCCAGTGAAGCCACCCTGGTGGCCCTGCTGGCCGCTCGG
ACCAAAGTGATCCATCGGCTGCAGGCAGCGTCCCCAGAGCTCACACAGGCCGCTATCATG
GAGAAGCTGGTGGCTTACTCATCCGATCAGGCACACTCCTCAGTGGAAAGAGCTGGGTTA
ATTGGTGGAGTGAAATTAAAAGCCATCCCCTCAGATGGCAACTTCGCCATGCGTGCGTCT
GCCCTGCAGGAAGCCCTGGAGAGAGACAAAGCGGCTGGCCTGATTCCTTTCTTTATGGTT
GCCACCCTGGGGACCACAACATGCTGCTCCTTTGACAATCTCTTAGAAGTCGGTCCTATC
TGCAACAAGGAAGACATATGGCTGCACGTTGATGCAGCCTACGCAGGCAGTGCATTCATC
TGCCCTGAGTTCCGGCACCTTCTGAATGGAGTGGAGTTTGCAGATTCATTCAACTTTAAT
CCCCACAAATGGCTATTGGTGAATTTTGACTGTTCTGCCATGTGGGTGAAAAAGAGAACA
GACTTAACGGGAGCCTTTAGACTGGACCCCACTTACCTGAAGCACAGCCATCAGGATTCA
GGGCTTATCACTGACTACCGGCATTGGCAGATACCACTGGGCAGAAGATTTCGCTCTTTG
AAAATGTGGTTTGTATTTAGGATGTATGGAGTCAAAGGACTGCAGGCTTATATCCGCAAG
CATGTCCAGCTGTCCCATGAGTTTGAGTCACTGGTGCGCCAGGATCCCCGCTTTGAAATC
TGTGTGGAAGTCATTCTGGGGCTTGTCTGCTTTCGGCTAAAGGGTTCCAACAAAGTGAAT
GAAGCTCTTCTGCAAAGAATAAACAGTGCCAAAAAAATCCACTTGGTTCCATGTCACCTC
AGGGACAAGTTTGTCCTGCGCTTTGCCATCTGTTCTCGCACGGTGGAATCTGCCCATGTG
CAGCGGGCCTGGGAACACATCAAAGAGCTGGCGGCCGACGTGCTGCGAGCAGAGAGGGAG
TAG
|
| Enzyme 87 GenBank Gene ID |
BT007009  |
| Enzyme 87 GeneCard ID |
DDC  |
| Enzyme 87 GenAtlas ID |
DDC  |
| Enzyme 87 HGNC ID |
HGNC:2719  |
| Enzyme 87 Chromosome Location |
7 |
| Enzyme 87 Locus |
7p12.2 |
| Enzyme 87 SNPs |
SNPJam Report  |
| Enzyme 87 General References |
- Venter JC, Adams MD, Myers EW, Li PW, Mural RJ, Sutton GG, Smith HO, Yandell M, Evans CA, Holt RA, Gocayne JD, Amanatides P, Ballew RM, Huson DH, Wortman JR, Zhang Q, Kodira CD, Zheng XH, Chen L, Skupski M, Subramanian G, Thomas PD, Zhang J, Gabor Miklos GL, Nelson C, Broder S, Clark AG, Nadeau J, McKusick VA, Zinder N, Levine AJ, Roberts RJ, Simon M, Slayman C, Hunkapiller M, Bolanos R, Delcher A, Dew I, Fasulo D, Flanigan M, Florea L, Halpern A, Hannenhalli S, Kravitz S, Levy S, Mobarry C, Reinert K, Remington K, Abu-Threideh J, Beasley E, Biddick K, Bonazzi V, Brandon R, Cargill M, Chandramouliswaran I, Charlab R, Chaturvedi K, Deng Z, Di Francesco V, Dunn P, Eilbeck K, Evangelista C, Gabrielian AE, Gan W, Ge W, Gong F, Gu Z, Guan P, Heiman TJ, Higgins ME, Ji RR, Ke Z, Ketchum KA, Lai Z, Lei Y, Li Z, Li J, Liang Y, Lin X, Lu F, Merkulov GV, Milshina N, Moore HM, Naik AK, Narayan VA, Neelam B, Nusskern D, Rusch DB, Salzberg S, Shao W, Shue B, Sun J, Wang Z, Wang A, Wang X, Wang J, Wei M, Wides R, Xiao C, Yan C, Yao A, Ye J, Zhan M, Zhang W, Zhang H, Zhao Q, Zheng L, Zhong F, Zhong W, Zhu S, Zhao S, Gilbert D, Baumhueter S, Spier G, Carter C, Cravchik A, Woodage T, Ali F, An H, Awe A, Baldwin D, Baden H, Barnstead M, Barrow I, Beeson K, Busam D, Carver A, Center A, Cheng ML, Curry L, Danaher S, Davenport L, Desilets R, Dietz S, Dodson K, Doup L, Ferriera S, Garg N, Gluecksmann A, Hart B, Haynes J, Haynes C, Heiner C, Hladun S, Hostin D, Houck J, Howland T, Ibegwam C, Johnson J, Kalush F, Kline L, Koduru S, Love A, Mann F, May D, McCawley S, McIntosh T, McMullen I, Moy M, Moy L, Murphy B, Nelson K, Pfannkoch C, Pratts E, Puri V, Qureshi H, Reardon M, Rodriguez R, Rogers YH, Romblad D, Ruhfel B, Scott R, Sitter C, Smallwood M, Stewart E, Strong R, Suh E, Thomas R, Tint NN, Tse S, Vech C, Wang G, Wetter J, Williams S, Williams M, Windsor S, Winn-Deen E, Wolfe K, Zaveri J, Zaveri K, Abril JF, Guigo R, Campbell MJ, Sjolander KV, Karlak B, Kejariwal A, Mi H, Lazareva B, Hatton T, Narechania A, Diemer K, Muruganujan A, Guo N, Sato S, Bafna V, Istrail S, Lippert R, Schwartz R, Walenz B, Yooseph S, Allen D, Basu A, Baxendale J, Blick L, Caminha M, Carnes-Stine J, Caulk P, Chiang YH, Coyne M, Dahlke C, Mays A, Dombroski M, Donnelly M, Ely D, Esparham S, Fosler C, Gire H, Glanowski S, Glasser K, Glodek A, Gorokhov M, Graham K, Gropman B, Harris M, Heil J, Henderson S, Hoover J, Jennings D, Jordan C, Jordan J, Kasha J, Kagan L, Kraft C, Levitsky A, Lewis M, Liu X, Lopez J, Ma D, Majoros W, McDaniel J, Murphy S, Newman M, Nguyen T, Nguyen N, Nodell M, Pan S, Peck J, Peterson M, Rowe W, Sanders R, Scott J, Simpson M, Smith T, Sprague A, Stockwell T, Turner R, Venter E, Wang M, Wen M, Wu D, Wu M, Xia A, Zandieh A, Zhu X: The sequence of the human genome. Science. 2001 Feb 16;291(5507):1304-51. [PubMed
]
- Scherer SW, Cheung J, MacDonald JR, Osborne LR, Nakabayashi K, Herbrick JA, Carson AR, Parker-Katiraee L, Skaug J, Khaja R, Zhang J, Hudek AK, Li M, Haddad M, Duggan GE, Fernandez BA, Kanematsu E, Gentles S, Christopoulos CC, Choufani S, Kwasnicka D, Zheng XH, Lai Z, Nusskern D, Zhang Q, Gu Z, Lu F, Zeesman S, Nowaczyk MJ, Teshima I, Chitayat D, Shuman C, Weksberg R, Zackai EH, Grebe TA, Cox SR, Kirkpatrick SJ, Rahman N, Friedman JM, Heng HH, Pelicci PG, Lo-Coco F, Belloni E, Shaffer LG, Pober B, Morton CC, Gusella JF, Bruns GA, Korf BR, Quade BJ, Ligon AH, Ferguson H, Higgins AW, Leach NT, Herrick SR, Lemyre E, Farra CG, Kim HG, Summers AM, Gripp KW, Roberts W, Szatmari P, Winsor EJ, Grzeschik KH, Teebi A, Minassian BA, Kere J, Armengol L, Pujana MA, Estivill X, Wilson MD, Koop BF, Tosi S, Moore GE, Boright AP, Zlotorynski E, Kerem B, Kroisel PM, Petek E, Oscier DG, Mould SJ, Dohner H, Dohner K, Rommens JM, Vincent JB, Venter JC, Li PW, Mural RJ, Adams MD, Tsui LC: Human chromosome 7: DNA sequence and biology. Science. 2003 May 2;300(5620):767-72. Epub 2003 Apr 10. [PubMed
]
|
| Enzyme 87 Metabolite References |
Not Available |
|
Enzyme 88
[top]
|
| Enzyme 88 ID |
14727 |
| Enzyme 88 Name |
Phosphorylase |
| Enzyme 88 Synonyms |
Not Available |
| Enzyme 88 Gene Name |
Not Available |
| Enzyme 88 Protein Sequence |
>Phosphorylase
IPAFACAAAFLLHLFSSASAGAMAKPLTDSEKRKQISVRGLAGLGDVAEVRKSFNRHLHF
TLVKDRNVATPRDYFFALAHTVRDHLVGRWIRTQQHYYERDPKRIYYLSLEFYMGRTLQN
TMVNLGLQNACDEAIYQLGLDLEELEEIEEDAGLGNGGLGRLAACFLDSMATLGLAAYGY
GIRYEFGIFNQKIVNGWQVEEADDWLRYGNPWEKARPEYMLPVHFYGRVEHTPDGVKWLD
TQVVLAMPYDTPVPGYKNNTVNTMRLWSAKAPNDFKLQDFNVGDYIEAVLDRNLAENISR
VLYPNDNFFEGKELRLKQEYFVVASTLQDIIRRFKSSKFGCRDPVRTCFETFPDKVAIQL
NDTHPALSIPELMRILVDVEKVDWDKAWEITKKTCAYTNHTVLPEALERWPVSMFEKLLP
RHLEIIYAINQRHLDHVAALFPGDVDRLRRMSVIEEGDCKRINMAHLCVIGSHAVNGVAR
IHSEIVKQSVFKDFYELEPEKFQNKTNGITPRRWLLLCNPGLANTIVEKIGEEFLTDLSQ
LKKLLPLVSDEVFIRDVAKVKQENKLKFSAFLEKEYKVKINPSSMFDVHVKRIHEYKRQL
LNCLHVVTLYNRIKRDPAKAFVPRTVMIGGKAAPGYHMAKLIIKLVTSIGDVVNHDPVVG
DRLKVIFLENYRVSLAEKVIPAADLSQQISTAGTEASGTGNMKFMLNGALTIGTMDGANV
EMAEEAGAENLFIFGLRVEDVEALDRKGYNAREYYDHLPELKQAVDQISSGFFSPKEPDC
FKDIVNMLMHHDRFKVFADYEAYMQCQAQVDQLYRNPKEWTKKVIRNIACSGKFSSDRTI
TEYAREIWGVEPSDLQIPPPNIPRD
|
| Enzyme 88 Number of Residues |
865 |
| Enzyme 88 Molecular Weight |
98828.6 |
| Enzyme 88 Theoretical pI |
6.95 |
| Enzyme 88 GO Classification |
| Function |
- binding
- catalytic activity
- cofactor binding
- phosphorylase activity
- pyridoxal phosphate binding
- transferase activity
- transferase activity, transferring glycosyl groups
- transferase activity, transferring hexosyl groups
|
| Process |
- carbohydrate metabolic process
- metabolic process
- primary metabolic process
|
| Component |
| — |
|
| Enzyme 88 General Function |
Involved in phosphorylase activity |
| Enzyme 88 Specific Function |
Phosphorylase is an important allosteric enzyme in carbohydrate metabolism. Enzymes from different sources differ in their regulatory mechanisms and in their natural substrates. However, all known phosphorylases share catalytic and structural properties |
| Enzyme 88 Pathways |
|
| Enzyme 88 Reactions |
- [(1->4)-alpha-D-glucosyl]n + phosphate = [(1->4)-alpha-D-glucosyl]n-1 + alpha-D-glucose 1-phosphate [RN:R01821 R06050]
|
| Enzyme 88 Pfam Domain Function |
|
| Enzyme 88 Signals |
|
| Enzyme 88 Transmembrane Regions |
|
| Enzyme 88 Essentiality |
Not Available |
| Enzyme 88 GenBank ID Protein |
62087740  |
| Enzyme 88 UniProtKB/Swiss-Prot ID |
Q59GM9  |
| Enzyme 88 UniProtKB/Swiss-Prot Entry Name |
Q59GM9_HUMAN  |
| Enzyme 88 PDB ID |
Not Available |
| Enzyme 88 Cellular Location |
Not Available |
| Enzyme 88 Gene Sequence |
>2599 bp
CATCCCGGCGTTCGCGTGTGCCGCCGCTTTCCTCCTCCATCTCTTTTCCTCCGCCTCCGC
CGGCGCGATGGCGAAGCCGCTGACGGACAGCGAGAAGCGGAAGCAGATCAGCGTGCGCGG
CCTGGCGGGGCTAGGCGACGTGGCCGAGGTGCGGAAGAGCTTCAACCGGCACTTGCACTT
CACGCTGGTCAAGGACCGCAATGTGGCCACGCCCCGCGACTACTTCTTCGCGCTGGCGCA
CACGGTGCGCGACCACCTCGTGGGCCGCTGGATCCGCACGCAGCAGCACTACTACGAGCG
CGACCCCAAGCGCATTTATTATCTTTCCCTGGAATTCTACATGGGTCGCACGCTGCAGAA
CACGATGGTGAACCTGGGCCTTCAGAATGCCTGCGATGAAGCCATCTATCAGTTGGGGTT
AGACTTGGAGGAACTCGAGGAGATAGAAGAAGATGCTGGCCTTGGGAATGGAGGCCTGGG
GAGGCTGGCAGCGTGTTTCCTTGACTCAATGGCTACCTTGGGCCTGGCAGCATACGGCTA
TGGAATCCGCTATGAATTTGGGATTTTTAACCAGAAGATTGTCAATGGCTGGCAGGTAGA
GGAGGCCGATGACTGGCTGCGCTACGGCAACCCCTGGGAGAAAGCGCGGCCTGAGTATAT
GCTTCCCGTGCACTTCTACGGACGCGTGGAGCACACCCCCGACGGCGTGAAGTGGCTGGA
CACACAGGTGGTGCTGGCCATGCCCTACGACACCCCAGTGCCCGGCTACAAGAACAACAC
CGTCAACACCATGCGGCTGTGGTCCGCCAAGGCTCCCAACGACTTCAAGCTGCAGGACTT
CAACGTGGGAGACTACATCGAGGCGGTCCTGGACCGGAACTTGGCTGAGAACATCTCCAG
GGTCCTGTATCCAAATGATAACTTCTTTGAGGGGAAGGAGCTGCGGCTGAAGCAGGAGTA
CTTCGTGGTGGCCTCCACGCTCCAGGACATCATCCGCCGCTTCAAGTCGTCCAAGTTCGG
CTGCCGGGACCCTGTGAGAACCTGTTTCGAGACGTTCCCAGACAAGGTGGCCATCCAGCT
GAACGACACCCACCCCGCCCTCTCCATCCCTGAGCTCATGCGGATCCTGGTGGACGTGGA
GAAGGTGGACTGGGACAAGGCCTGGGAAATCACGAAGAAGACCTGTGCGTACACCAACCA
CACTGTGCTGCCTGAGGCCTTGGAGCGCTGGCCCGTGTCCATGTTTGAGAAGCTGCTGCC
GCGGCACCTGGAGATAATCTATGCCATCAACCAGCGGCACCTGGACCACGTGGCCGCGCT
GTTTCCCGGCGATGTGGACCGCCTGCGCAGGATGTCTGTGATCGAGGAGGGGGACTGCAA
GCGGATCAACATGGCCCACCTGTGTGTGATTGGGTCCCATGCTGTCAATGGTGTGGCGAG
GATCCACTCGGAGATCGTGAAACAGTCGGTCTTTAAGGATTTTTATGAACTGGAGCCAGA
GAAGTTCCAGAATAAGACCAATGGCATCACCCCCCGCCGGTGGCTGCTGCTGTGCAACCC
GGGGCTGGCCAATACCATCGTGGAGAAAATTGGGGAGGAGTTCCTGACTGACCTGAGCCA
GCTGAAGAAGCTGCTGCCGCTGGTCAGTGACGAGGTGTTCATCAGGGACGTGGCCAAGGT
CAAACAGGAGAACAAGCTCAAGTTCTCGGCCTTCCTGGAGAAGGAGTACAAGGTGAAGAT
CAACCCCTCCTCCATGTTCGACGTGCATGTGAAGAGGATCCACGAGTACAAGCGGCAGCT
GCTCAACTGCCTGCACGTCGTCACCCTGTACAATCGAATCAAGAGAGACCCGGCCAAGGC
TTTTGTGCCCAGGACTGTTATGATTGGGGGCAAGGCAGCGCCCGGTTACCACATGGCCAA
GCTGATCATCAAGTTGGTCACCTCCATCGGCGACGTCGTCAATCATGACCCAGTTGTGGG
TGACAGGTTGAAAGTGATCTTCCTGGAGAACTACCGTGTGTCCTTGGCTGAGAAAGTGAT
CCCGGCCGCTGATCTGTCGCAGCAGATCTCCACTGCAGGCACCGAGGCCTCAGGCACAGG
CAACATGAAGTTCATGCTCAACGGGGCCCTCACCATCGGCACCATGGACGGCGCCAACGT
GGAGATGGCCGAGGAGGCCGGGGCCGAGAACCTCTTCATCTTCGGCCTGCGGGTGGAGGA
TGTCGAGGCCTTGGACCGGAAAGGGTACAATGCCAGGGAGTACTACGACCACCTGCCCGA
GCTGAAGCAGGCCGTGGACCAGATCAGCAGTGGCTTTTTTTCTCCCAAGGAGCCAGACTG
CTTCAAGGACATCGTGAACATGCTGATGCACCATGACAGGTTCAAGGTGTTTGCAGACTA
TGAAGCCTACATGCAGTGCCAGGCACAGGTGGACCAACTGTACCGGAACCCCAAGGAGTG
GACCAAGAAGGTCATCAGGAACATCGCCTGCTCGGGCAAGTTCTCCAGTGACCGGACCAT
CACGGAGTATGCACGGGAGATCTGGGGTGTGGAGCCCTCCGACCTGCAGATCCCGCCCCC
CAACATCCCCCGGGACTAG
|
| Enzyme 88 GenBank Gene ID |
AB209080  |
| Enzyme 88 GeneCard ID |
Not Available |
| Enzyme 88 GenAtlas ID |
Not Available |
| Enzyme 88 HGNC ID |
HGNC:9723  |
| Enzyme 88 Chromosome Location |
Not Available |
| Enzyme 88 Locus |
Not Available |
| Enzyme 88 SNPs |
Not Available |
| Enzyme 88 General References |
Not Available |
| Enzyme 88 Metabolite References |
Not Available |
|
Enzyme 89
[top]
|
| Enzyme 89 ID |
14728 |
| Enzyme 89 Name |
Serine hydroxymethyltransferase |
| Enzyme 89 Synonyms |
Not Available |
| Enzyme 89 Gene Name |
SHMT2 |
| Enzyme 89 Protein Sequence |
>Serine hydroxymethyltransferase
ELRCCTSLCFGRLGLCRDVGSWSGWPFGLSTATQPRLRLGKQTGAGQARRACRTVILRCG
SCCRGRRTGSVVAWSSLPQRYYGGAEVVDEIELLCQRRALEAFDLDPAQWGVNVQPYSGS
PANLAVYTALLQPHDRIMGLDLPDGGHLTHGYMSDVKRISATSIFFESMPYKLNPKTGLI
DYNQLALTARLFRPRLIIAGTSAYARLIDYARMREVCDEVKAHLLADMAHISGLVAAKVI
PSPFKHADIVTTTTHKTLRGARSGLIFYRKGVKAVDPKTGREIPYTFEDRINFAVFPSLQ
GGPHNHAIAAVAVALKQACTPMFREYSLQVLKNARAMADALLERGYSLVSGGTDNHLVLV
DLRPKGLDGARAERVLELVSITANKNTCPGDRSAITPGGLRLGAPALTSRQFREDDFRRV
VDFIDEGVNIGLEVKSKTAKLQDFKSFLLKDSETSQRLANLRQRVEQFARAFPMPGFDEH
|
| Enzyme 89 Number of Residues |
480 |
| Enzyme 89 Molecular Weight |
52909.3 |
| Enzyme 89 Theoretical pI |
9.66 |
| Enzyme 89 GO Classification |
| Function |
- binding
- catalytic activity
- cofactor binding
- glycine hydroxymethyltransferase activity
- methyltransferase activity
- pyridoxal phosphate binding
- transferase activity
- transferase activity, transferring one-carbon groups
|
| Process |
- L-serine metabolic process
- cellular amino acid and derivative metabolic process
- cellular amino acid metabolic process
- cellular metabolic process
- glycine metabolic process
- metabolic process
- serine family amino acid metabolic process
|
| Component |
| — |
|
| Enzyme 89 General Function |
Involved in catalytic activity |
| Enzyme 89 Specific Function |
Interconversion of serine and glycine |
| Enzyme 89 Pathways |
|
| Enzyme 89 Reactions |
- 5,10-methylenetetrahydrofolate + glycine + H2O = tetrahydrofolate + L-serine [RN:R00945]
|
| Enzyme 89 Pfam Domain Function |
|
| Enzyme 89 Signals |
|
| Enzyme 89 Transmembrane Regions |
|
| Enzyme 89 Essentiality |
Not Available |
| Enzyme 89 GenBank ID Protein |
60552225  |
| Enzyme 89 UniProtKB/Swiss-Prot ID |
Q5BJF5  |
| Enzyme 89 UniProtKB/Swiss-Prot Entry Name |
Q5BJF5_HUMAN  |
| Enzyme 89 PDB ID |
Not Available |
| Enzyme 89 Cellular Location |
Not Available |
| Enzyme 89 Gene Sequence |
>1445 bp
CCGAGTTGCGATGCTGTACTTCTCTTTGTTTTGGGCGGCTCGGCCTCTGCAGAGATGTGG
GCAGCTGGTCAGGATGGCCATTCGGGCTCAGCACAGCAACGCAGCCCAGACTCAGACTGG
GGAAGCAAACAGGGGCTGGACAGGCCAGGAGAGCCTGTCGGACAGTGATCCTGAGATGTG
GGAGTTGCTGCAGAGGGAGAAGGACAGGCAGTGTCGTGGCCTGGAGCTCATTGCCTCAGA
GATACTATGGGGGAGCAGAGGTGGTGGATGAAATTGAGCTGCTGTGCCAGCGCCGGGCCT
TGGAAGCCTTTGACCTGGATCCTGCACAGTGGGGAGTCAATGTCCAGCCCTACTCCGGGT
CCCCAGCCAACCTGGCCGTCTACACAGCCCTTCTGCAACCTCACGACCGGATCATGGGGC
TGGACCTGCCCGATGGGGGCCATCTCACCCACGGCTACATGTCTGACGTCAAGCGGATAT
CAGCCACGTCCATCTTCTTCGAGTCTATGCCCTATAAGCTCAACCCCAAAACTGGCCTCA
TTGACTACAACCAGCTGGCACTGACTGCTCGACTTTTCCGGCCACGGCTCATCATAGCTG
GCACCAGCGCCTATGCTCGCCTCATTGACTACGCCCGCATGAGAGAGGTGTGTGATGAAG
TCAAAGCACACCTGCTGGCAGACATGGCCCACATCAGTGGCCTGGTGGCTGCCAAGGTGA
TTCCCTCGCCTTTCAAGCACGCGGACATCGTCACCACCACTACTCACAAGACTCTTCGAG
GGGCCAGGTCAGGGCTCATCTTCTACCGGAAAGGGGTGAAGGCTGTGGACCCCAAGACTG
GCCGGGAGATCCCTTACACATTTGAGGACCGAATCAACTTTGCCGTGTTCCCATCCCTGC
AGGGGGGCCCCCACAATCATGCCATTGCTGCAGTAGCTGTGGCCCTAAAGCAGGCCTGCA
CCCCCATGTTCCGGGAGTACTCCCTGCAGGTTCTGAAGAATGCTCGGGCCATGGCAGATG
CCCTGCTAGAGCGAGGCTACTCACTGGTATCAGGTGGTACTGACAACCACCTGGTGCTGG
TGGACCTGCGGCCCAAGGGCCTGGATGGAGCTCGGGCTGAGCGGGTGCTAGAGCTTGTAT
CCATCACTGCCAACAAGAACACCTGTCCTGGAGACCGAAGTGCCATCACACCGGGCGGCC
TGCGGCTTGGGGCCCCAGCCTTAACTTCTCGACAGTTCCGTGAGGATGACTTCCGGAGAG
TTGTGGACTTTATAGATGAAGGGGTCAACATTGGCTTAGAGGTGAAGAGCAAGACTGCCA
AGCTCCAGGATTTCAAATCCTTCCTGCTTAAGGACTCAGAAACAAGTCAGCGTCTGGCCA
ACCTCAGGCAACGGGTGGAGCAGTTTGCCAGGGCCTTCCCCATGCCTGGTTTTGATGAGC
ATTGA
|
| Enzyme 89 GenBank Gene ID |
BC091501  |
| Enzyme 89 GeneCard ID |
SHMT2  |
| Enzyme 89 GenAtlas ID |
SHMT2  |
| Enzyme 89 HGNC ID |
HGNC:10852  |
| Enzyme 89 Chromosome Location |
1 |
| Enzyme 89 Locus |
12q12-q14 |
| Enzyme 89 SNPs |
SNPJam Report  |
| Enzyme 89 General References |
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
|
| Enzyme 89 Metabolite References |
Not Available |
|
Enzyme 90
[top]
|
| Enzyme 90 ID |
14729 |
| Enzyme 90 Name |
Serine hydroxymethyltransferase |
| Enzyme 90 Synonyms |
Not Available |
| Enzyme 90 Gene Name |
DKFZp686P09201 |
| Enzyme 90 Protein Sequence |
>Serine hydroxymethyltransferase
MAIRAQHSNAAQTQTGEANRGWTGQESLSDSDPEMWELLQREKDRQCRGLELIASENFCS
RAALEALGSCLNNKYPEGYPGKRYYGGAEVVDEIELLCQRRALEAFDLDPAQWGVNVQPY
SGSPANLAVYTALLQPHDRIMGLDLPDGGHLTHGYMSDVKRISATSIFFESMPYKLNPKT
GLIDYNQLALTARLFRPRLIIAGTSAYARLIDYARMREVCDEVKAHLLADMAHISGLVAA
KVIPSPFKHADIVTTTTHKTLRGARSGLIFYRKGVKAVDPKTGREIPYTFEDRINFAVFP
SLQGGPHNHAIAAVAVALKQACTPMFREYSLQVLKNARAMADALLERGYSLVSGGTDNHL
VLVDLRPKGLDGARAERVLELVSITANKNTCPGDRSAITPGGLRLGAPALTSRQFREDDF
RRVVDFIDEGVNIGLEVKSKTAKLQDFKSFLLKDSETSQRLANLRQRVEQFARAFPMPGF
DEH
|
| Enzyme 90 Number of Residues |
483 |
| Enzyme 90 Molecular Weight |
53464.4 |
| Enzyme 90 Theoretical pI |
8.27 |
| Enzyme 90 GO Classification |
| Function |
- binding
- catalytic activity
- cofactor binding
- glycine hydroxymethyltransferase activity
- methyltransferase activity
- pyridoxal phosphate binding
- transferase activity
- transferase activity, transferring one-carbon groups
|
| Process |
- L-serine metabolic process
- cellular amino acid and derivative metabolic process
- cellular amino acid metabolic process
- cellular metabolic process
- glycine metabolic process
- metabolic process
- serine family amino acid metabolic process
|
| Component |
| — |
|
| Enzyme 90 General Function |
Involved in catalytic activity |
| Enzyme 90 Specific Function |
Interconversion of serine and glycine |
| Enzyme 90 Pathways |
|
| Enzyme 90 Reactions |
- 5,10-methylenetetrahydrofolate + glycine + H2O = tetrahydrofolate + L-serine [RN:R00945]
|
| Enzyme 90 Pfam Domain Function |
|
| Enzyme 90 Signals |
|
| Enzyme 90 Transmembrane Regions |
|
| Enzyme 90 Essentiality |
Not Available |
| Enzyme 90 GenBank ID Protein |
57997528  |
| Enzyme 90 UniProtKB/Swiss-Prot ID |
Q5HYG8  |
| Enzyme 90 UniProtKB/Swiss-Prot Entry Name |
Q5HYG8_HUMAN  |
| Enzyme 90 PDB ID |
Not Available |
| Enzyme 90 Cellular Location |
Not Available |
| Enzyme 90 Gene Sequence |
>1452 bp
ATGGCCATTCGGGCTCAGCACAGCAACGCAGCCCAGACTCAGACTGGGGAAGCAAACAGG
GGCTGGACAGGCCAGGAGAGCCTGTCGGACAGTGATCCTGAGATGTGGGAGTTGCTGCAG
AGGGAGAAGGACAGGCAGTGTCGTGGCCTGGAGCTCATTGCCTCAGAGAACTTCTGCAGC
CGAGCTGCGCTGGAGGCCCTGGGGTCCTGTCTGAACAACAAGTACCCGGAGGGTTATCCT
GGCAAGAGATACTATGGGGGAGCAGAGGTGGTGGATGAAATTGAGCTGCTGTGCCAGCGC
CGGGCCTTGGAAGCCTTTGACCTGGATCCTGCACAGTGGGGAGTCAATGTCCAGCCCTAC
TCCGGGTCCCCAGCCAACCTGGCCGTCTACACAGCCCTTCTGCAACCTCACGACCGGATC
ATGGGGCTGGACCTGCCCGATGGGGGCCATCTCACCCACGGCTACATGTCTGACGTCAAG
CGGATATCAGCCACGTCCATCTTCTTCGAGTCTATGCCCTATAAGCTCAACCCCAAAACT
GGCCTCATTGACTACAACCAGCTGGCACTGACTGCTCGACTTTTCCGGCCACGGCTCATC
ATAGCTGGCACCAGCGCCTATGCTCGCCTCATTGACTACGCCCGCATGAGAGAGGTGTGT
GATGAAGTCAAAGCACACCTGCTGGCAGACATGGCCCACATCAGTGGCCTGGTGGCTGCC
AAGGTGATTCCCTCGCCTTTCAAGCACGCGGACATCGTCACCACCACTACTCACAAGACT
CTTCGAGGGGCCAGGTCAGGGCTCATCTTCTACCGGAAAGGGGTGAAGGCTGTGGACCCC
AAGACTGGCCGGGAGATCCCTTACACATTTGAGGACCGAATCAACTTTGCCGTGTTCCCA
TCCCTGCAGGGGGGCCCCCACAATCATGCCATTGCTGCAGTAGCTGTGGCCCTAAAGCAG
GCCTGCACCCCCATGTTCCGGGAGTACTCCCTGCAGGTTCTGAAGAATGCTCGGGCCATG
GCAGATGCCCTGCTAGAGCGAGGCTACTCACTGGTATCAGGTGGTACTGACAACCACCTG
GTGCTGGTGGACCTGCGGCCCAAGGGCCTGGATGGAGCTCGGGCTGAGCGGGTGCTAGAG
CTTGTATCCATCACTGCCAACAAGAACACCTGTCCTGGAGACCGAAGTGCCATCACACCG
GGCGGCCTGCGGCTTGGGGCCCCAGCCTTAACTTCTCGACAGTTCCGTGAGGATGACTTC
CGGAGAGTTGTGGACTTTATAGATGAAGGGGTCAACATTGGCTTAGAGGTGAAGAGCAAG
ACTGCCAAGCTCCAGGATTTCAAATCCTTCCTGCTTAAGGACTCAGAAACAAGTCAGCGT
CTGGCCAACCTCAGGCAACGGGTGGAGCAGTTTGCCAGGGCCTTCCCCATGCCTGGTTTT
GATGAGCATTGA
|
| Enzyme 90 GenBank Gene ID |
BX647711  |
| Enzyme 90 GeneCard ID |
DKFZp686P09201  |
| Enzyme 90 GenAtlas ID |
DKFZp686P09201  |
| Enzyme 90 HGNC ID |
HGNC:10852  |
| Enzyme 90 Chromosome Location |
Not Available |
| Enzyme 90 Locus |
Not Available |
| Enzyme 90 SNPs |
SNPJam Report  |
| Enzyme 90 General References |
Not Available |
| Enzyme 90 Metabolite References |
Not Available |
|
Enzyme 91
[top]
|
| Enzyme 91 ID |
14730 |
| Enzyme 91 Name |
Aminolevulinate, delta-, synthase 1, isoform CRA_a |
| Enzyme 91 Synonyms |
- SubName: Migration-inducing protein 4
- SubName: cDNA, FLJ92941, Homo sapiens aminolevulinate, delta-, synthase 1 (ALAS1), nuclear gene encoding mitochondrial protein, mRNA
|
| Enzyme 91 Gene Name |
ALAS1 |
| Enzyme 91 Protein Sequence |
>Aminolevulinate, delta-, synthase 1, isoform CRA_a
MESVVRRCPFLSRVPQAFLQKAGKSLLFYAQNCPKMMEVGAKPAPRALSTAAVHYQQIKE
TPPASEKDKTAKAKVQQTPDGSQQSPDGTQLPSGHPLPATSQGTASKCPFLAAQMNQRGS
SVFCKASLELQEDVQEMNAVRKEVAETSAGPSVVSVKTDGGDPSGLLKNFQDIMQKQRPE
RVSHLLQDNLPKSVSTFQYDRFFEKKIDEKKNDHTYRVFKTVNRRAHIFPMADDYSDSLI
TKKQVSVWCSNDYLGMSRHPRVCGAVMDTLKQHGAGAGGTRNISGTSKFHVDLERELADL
HGKDAALLFSSCFVANDSTLFTLAKMMPGCEIYSDSGNHASMIQGIRNSRVPKYIFRHND
VSHLRELLQRSDPSVPKIVAFETVHSMDGAVCPLEELCDVAHEFGAITFVDEVHAVGLYG
ARGGGIGDRDGVMPKMDIISGTLGKAFGCVGGYIASTSSLIDTVRSYAAGFIFTTSLPPM
LLAGALESVRILKSAEGRVLRRQHQRNVKLMRQMLMDAGLPVVHCPSHIIPVRVADAAKN
TEVCDELMSRHNIYVQAINYPTVPRGEELLRIAPTPHHTPQMMNYFLENLLVTWKQVGLE
LKPHSSAECNFCRRPLHFEVMSEREKSYFSGLSKLVSAQA
|
| Enzyme 91 Number of Residues |
640 |
| Enzyme 91 Molecular Weight |
70580.3 |
| Enzyme 91 Theoretical pI |
8.57 |
| Enzyme 91 GO Classification |
| Function |
- 5-aminolevulinate synthase activity
- N-acyltransferase activity
- N-succinyltransferase activity
- acyltransferase activity
- binding
- catalytic activity
- cofactor binding
- pyridoxal phosphate binding
- transferase activity
- transferase activity, transferring acyl groups
- transferase activity, transferring acyl groups other than amino-acyl groups
- transferase activity, transferring nitrogenous groups
|
| Process |
- biosynthetic process
- cellular biosynthetic process
- heterocycle biosynthetic process
- metabolic process
- nitrogen compound metabolic process
- porphyrin metabolic process
- tetrapyrrole biosynthetic process
- tetrapyrrole metabolic process
|
| Component |
- cell part
- cytoplasmic part
- intracellular part
- mitochondrial matrix
- mitochondrial part
|
|
| Enzyme 91 General Function |
Involved in 5-aminolevulinate synthase activity |
| Enzyme 91 Specific Function |
Not Available |
| Enzyme 91 Pathways |
Not Available |
| Enzyme 91 Reactions |
Not Available |
| Enzyme 91 Pfam Domain Function |
|
| Enzyme 91 Signals |
|
| Enzyme 91 Transmembrane Regions |
|
| Enzyme 91 Essentiality |
Not Available |
| Enzyme 91 GenBank ID Protein |
Not Available |
| Enzyme 91 UniProtKB/Swiss-Prot ID |
Q5JAM2  |
| Enzyme 91 UniProtKB/Swiss-Prot Entry Name |
Q5JAM2_HUMAN  |
| Enzyme 91 PDB ID |
Not Available |
| Enzyme 91 Cellular Location |
Not Available |
| Enzyme 91 Gene Sequence |
>1923 bp
ATGGAGAGTGTTGTTCGCCGCTGCCCATTCTTATCCCGAGTCCCCCAGGCCTTTCTGCAG
AAAGCAGGCAAATCTCTGTTGTTCTATGCCCAAAACTGCCCCAAGATGATGGAAGTTGGG
GCCAAGCCAGCCCCTCGGGCATTGTCCACTGCAGCAGTACACTACCAACAGATCAAAGAA
ACCCCTCCGGCCAGTGAGAAAGACAAAACTGCTAAGGCCAAGGTCCAACAGACTCCTGAT
GGATCCCAGCAGAGTCCAGATGGCACACAGCTTCCGTCTGGACACCCCTTGCCTGCCACA
AGCCAGGGCACTGCAAGCAAATGCCCTTTCCTGGCAGCACAGATGAATCAGAGAGGCAGC
AGTGTCTTCTGCAAAGCCAGTCTTGAGCTTCAGGAGGATGTGCAGGAAATGAATGCCGTG
AGGAAAGAGGTTGCTGAAACCTCAGCAGGCCCCAGTGTGGTTAGTGTGAAAACCGATGGA
GGGGATCCCAGTGGACTGCTGAAGAACTTCCAGGACATTATGCAAAAGCAAAGACCAGAA
AGAGTGTCTCATCTTCTTCAAGATAACTTGCCAAAATCTGTTTCCACTTTTCAGTATGAT
CGTTTCTTTGAGAAAAAAATTGATGAGAAAAAGAATGACCACACCTATCGAGTTTTTAAA
ACTGTGAACCGGCGAGCACACATCTTCCCCATGGCAGATGACTATTCAGACTCCCTCATC
ACCAAAAAGCAAGTGTCAGTCTGGTGCAGTAATGACTACCTAGGAATGAGTCGCCACCCA
CGGGTGTGTGGGGCAGTTATGGACACTTTGAAACAACATGGTGCTGGGGCAGGTGGTACT
AGAAATATTTCTGGAACTAGTAAATTCCATGTGGACTTAGAGCGGGAGCTGGCAGACCTC
CATGGGAAAGATGCCGCACTCTTGTTTTCCTCGTGCTTTGTGGCCAATGACTCAACCCTC
TTCACCCTGGCTAAGATGATGCCAGGCTGTGAGATTTACTCTGATTCTGGGAACCATGCC
TCCATGATCCAAGGGATTCGAAACAGCCGAGTGCCAAAGTACATCTTCCGCCACAATGAT
GTCAGCCACCTCAGAGAACTGCTGCAAAGATCTGACCCCTCAGTCCCCAAGATTGTGGCA
TTTGAAACTGTCCATTCAATGGATGGGGCGGTGTGCCCACTGGAAGAGCTGTGTGATGTG
GCCCATGAGTTTGGAGCAATCACCTTCGTGGATGAGGTCCACGCAGTGGGGCTTTATGGG
GCTCGAGGCGGAGGGATTGGGGATCGGGATGGAGTCATGCCAAAAATGGACATCATTTCT
GGAACACTTGGCAAAGCCTTTGGTTGTGTTGGAGGGTACATCGCCAGCACGAGTTCTCTG
ATTGACACCGTACGGTCCTATGCTGCTGGCTTCATCTTCACCACCTCTCTGCCACCCATG
CTGCTGGCTGGAGCCCTGGAGTCTGTGCGGATCCTGAAGAGCGCTGAGGGACGGGTGCTT
CGCCGCCAGCACCAGCGCAACGTCAAACTCATGAGACAGATGCTAATGGATGCCGGCCTC
CCTGTTGTCCACTGCCCCAGCCACATCATCCCTGTGCGGGTTGCAGATGCTGCTAAAAAC
ACAGAAGTCTGTGATGAACTAATGAGCAGACATAACATCTACGTGCAAGCAATCAATTAC
CCTACGGTGCCCCGGGGAGAAGAGCTCCTACGGATTGCCCCCACCCCTCACCACACACCC
CAGATGATGAACTACTTCCTTGAGAATCTGCTAGTCACATGGAAGCAAGTGGGGCTGGAA
CTGAAGCCTCATTCCTCAGCTGAGTGCAACTTCTGCAGGAGGCCACTGCATTTTGAAGTG
ATGAGTGAAAGAGAGAAGTCCTATTTCTCAGGCTTGAGCAAGTTGGTATCTGCTCAGGCC
TGA
|
| Enzyme 91 GenBank Gene ID |
AY260745  |
| Enzyme 91 GeneCard ID |
ALAS1  |
| Enzyme 91 GenAtlas ID |
ALAS1  |
| Enzyme 91 HGNC ID |
HGNC:396  |
| Enzyme 91 Chromosome Location |
3 |
| Enzyme 91 Locus |
3p21.1 |
| Enzyme 91 SNPs |
SNPJam Report  |
| Enzyme 91 General References |
- Venter JC, Adams MD, Myers EW, Li PW, Mural RJ, Sutton GG, Smith HO, Yandell M, Evans CA, Holt RA, Gocayne JD, Amanatides P, Ballew RM, Huson DH, Wortman JR, Zhang Q, Kodira CD, Zheng XH, Chen L, Skupski M, Subramanian G, Thomas PD, Zhang J, Gabor Miklos GL, Nelson C, Broder S, Clark AG, Nadeau J, McKusick VA, Zinder N, Levine AJ, Roberts RJ, Simon M, Slayman C, Hunkapiller M, Bolanos R, Delcher A, Dew I, Fasulo D, Flanigan M, Florea L, Halpern A, Hannenhalli S, Kravitz S, Levy S, Mobarry C, Reinert K, Remington K, Abu-Threideh J, Beasley E, Biddick K, Bonazzi V, Brandon R, Cargill M, Chandramouliswaran I, Charlab R, Chaturvedi K, Deng Z, Di Francesco V, Dunn P, Eilbeck K, Evangelista C, Gabrielian AE, Gan W, Ge W, Gong F, Gu Z, Guan P, Heiman TJ, Higgins ME, Ji RR, Ke Z, Ketchum KA, Lai Z, Lei Y, Li Z, Li J, Liang Y, Lin X, Lu F, Merkulov GV, Milshina N, Moore HM, Naik AK, Narayan VA, Neelam B, Nusskern D, Rusch DB, Salzberg S, Shao W, Shue B, Sun J, Wang Z, Wang A, Wang X, Wang J, Wei M, Wides R, Xiao C, Yan C, Yao A, Ye J, Zhan M, Zhang W, Zhang H, Zhao Q, Zheng L, Zhong F, Zhong W, Zhu S, Zhao S, Gilbert D, Baumhueter S, Spier G, Carter C, Cravchik A, Woodage T, Ali F, An H, Awe A, Baldwin D, Baden H, Barnstead M, Barrow I, Beeson K, Busam D, Carver A, Center A, Cheng ML, Curry L, Danaher S, Davenport L, Desilets R, Dietz S, Dodson K, Doup L, Ferriera S, Garg N, Gluecksmann A, Hart B, Haynes J, Haynes C, Heiner C, Hladun S, Hostin D, Houck J, Howland T, Ibegwam C, Johnson J, Kalush F, Kline L, Koduru S, Love A, Mann F, May D, McCawley S, McIntosh T, McMullen I, Moy M, Moy L, Murphy B, Nelson K, Pfannkoch C, Pratts E, Puri V, Qureshi H, Reardon M, Rodriguez R, Rogers YH, Romblad D, Ruhfel B, Scott R, Sitter C, Smallwood M, Stewart E, Strong R, Suh E, Thomas R, Tint NN, Tse S, Vech C, Wang G, Wetter J, Williams S, Williams M, Windsor S, Winn-Deen E, Wolfe K, Zaveri J, Zaveri K, Abril JF, Guigo R, Campbell MJ, Sjolander KV, Karlak B, Kejariwal A, Mi H, Lazareva B, Hatton T, Narechania A, Diemer K, Muruganujan A, Guo N, Sato S, Bafna V, Istrail S, Lippert R, Schwartz R, Walenz B, Yooseph S, Allen D, Basu A, Baxendale J, Blick L, Caminha M, Carnes-Stine J, Caulk P, Chiang YH, Coyne M, Dahlke C, Mays A, Dombroski M, Donnelly M, Ely D, Esparham S, Fosler C, Gire H, Glanowski S, Glasser K, Glodek A, Gorokhov M, Graham K, Gropman B, Harris M, Heil J, Henderson S, Hoover J, Jennings D, Jordan C, Jordan J, Kasha J, Kagan L, Kraft C, Levitsky A, Lewis M, Liu X, Lopez J, Ma D, Majoros W, McDaniel J, Murphy S, Newman M, Nguyen T, Nguyen N, Nodell M, Pan S, Peck J, Peterson M, Rowe W, Sanders R, Scott J, Simpson M, Smith T, Sprague A, Stockwell T, Turner R, Venter E, Wang M, Wen M, Wu D, Wu M, Xia A, Zandieh A, Zhu X: The sequence of the human genome. Science. 2001 Feb 16;291(5507):1304-51. [PubMed
]
|
| Enzyme 91 Metabolite References |
Not Available |
|
Enzyme 92
[top]
|
| Enzyme 92 ID |
14731 |
| Enzyme 92 Name |
Phosphorylase |
| Enzyme 92 Synonyms |
Not Available |
| Enzyme 92 Gene Name |
PYGB |
| Enzyme 92 Protein Sequence |
>Phosphorylase
KHHHTVPPSVTPKALDRSPPCPEMFTRAAPGYHMAKLIIKLVTSIGDVVNHDPVVGDRLK
VIFLENYRVSLAEKVIPAADLSQQISTAGTEASGTGNMKFMLNGALTIGTMDGANVEMAE
EAGAENLFIFGLRVEDVEALDRKGYNAREYYDHLPELKQAVDQISSGFFSPKEPDCFKDI
VNMLMHHDRFKVFADYEAYMQCQAQVDQLYRNPKEWTKKVIRNIACSGKFSSDRTITEYA
REIW
|
| Enzyme 92 Number of Residues |
244 |
| Enzyme 92 Molecular Weight |
27445.1 |
| Enzyme 92 Theoretical pI |
6.31 |
| Enzyme 92 GO Classification |
| Function |
- catalytic activity
- phosphorylase activity
- transferase activity
- transferase activity, transferring glycosyl groups
- transferase activity, transferring hexosyl groups
|
| Process |
- carbohydrate metabolic process
- metabolic process
- primary metabolic process
|
| Component |
| — |
|
| Enzyme 92 General Function |
Involved in phosphorylase activity |
| Enzyme 92 Specific Function |
Phosphorylase is an important allosteric enzyme in carbohydrate metabolism. Enzymes from different sources differ in their regulatory mechanisms and in their natural substrates. However, all known phosphorylases share catalytic and structural properties |
| Enzyme 92 Pathways |
|
| Enzyme 92 Reactions |
- [(1->4)-alpha-D-glucosyl]n + phosphate = [(1->4)-alpha-D-glucosyl]n-1 + alpha-D-glucose 1-phosphate [RN:R01821 R06050]
|
| Enzyme 92 Pfam Domain Function |
|
| Enzyme 92 Signals |
|
| Enzyme 92 Transmembrane Regions |
|
| Enzyme 92 Essentiality |
Not Available |
| Enzyme 92 GenBank ID Protein |
56203803  |
| Enzyme 92 UniProtKB/Swiss-Prot ID |
Q5JWL9  |
| Enzyme 92 UniProtKB/Swiss-Prot Entry Name |
Q5JWL9_HUMAN  |
| Enzyme 92 PDB ID |
Not Available |
| Enzyme 92 Cellular Location |
Not Available |
| Enzyme 92 Gene Sequence |
>734 bp
TGAAACATCACCACACAGTACCACCATCCGTCACACCTAAAGCATTGGACAGGAGTCCTC
CGTGTCCTGAAATGTTCACTCGGGCAGCGCCCGGTTACCACATGGCCAAGCTGATCATCA
AGTTGGTCACCTCCATCGGCGACGTCGTCAATCATGACCCAGTTGTGGGTGACAGGTTGA
AAGTGATCTTCCTGGAGAACTACCGTGTGTCCTTGGCTGAGAAAGTGATCCCGGCCGCTG
ATCTGTCGCAGCAGATCTCCACTGCAGGCACCGAGGCCTCAGGCACAGGCAACATGAAGT
TCATGCTCAACGGGGCCCTCACCATCGGCACCATGGACGGCGCCAACGTGGAGATGGCCG
AGGAGGCCGGGGCCGAGAACCTCTTCATCTTCGGCCTGCGGGTGGAGGATGTCGAGGCCT
TGGACCGGAAAGGGTACAATGCCAGGGAGTACTACGACCACCTGCCCGAGCTGAAGCAGG
CCGTGGACCAGATCAGCAGTGGCTTTTTTTCTCCCAAGGAGCCAGACTGCTTCAAGGACA
TCGTGAACATGCTGATGCACCATGACAGGTTCAAGGTGTTTGCAGACTATGAAGCCTACA
TGCAGTGCCAGGCACAGGTGGACCAGCTGTACCGGAACCCCAAGGAGTGGACCAAGAAGG
TCATCAGGAACATCGCCTGCTCGGGCAAGTTCTCCAGTGACCGGACCATCACGGAGTATG
CACGGGAGATCTGG
|
| Enzyme 92 GenBank Gene ID |
AL121772  |
| Enzyme 92 GeneCard ID |
PYGB  |
| Enzyme 92 GenAtlas ID |
PYGB  |
| Enzyme 92 HGNC ID |
HGNC:9723  |
| Enzyme 92 Chromosome Location |
2 |
| Enzyme 92 Locus |
20p11.2-p11.1 |
| Enzyme 92 SNPs |
SNPJam Report  |
| Enzyme 92 General References |
Not Available |
| Enzyme 92 Metabolite References |
Not Available |
|
Enzyme 93
[top]
|
| Enzyme 93 ID |
14732 |
| Enzyme 93 Name |
Aminolevulinate, delta-, synthase 2 |
| Enzyme 93 Synonyms |
- SubName: Aminolevulinate, delta-, synthase 2 (Sideroblastic/hypochromic anemia), isoform CRA_a
|
| Enzyme 93 Gene Name |
ALAS2 |
| Enzyme 93 Protein Sequence |
>Aminolevulinate, delta-, synthase 2
MRGGEVALGWNKKKRLFCEDFRFKMVTAAMLLQCCPVLARGPTSLLGKVVKTHQFLFGIG
RCPILATQGPNCSQIHLKATKAGGDSPSWAKGHCPFMLSELQDGKSKIVQKAAPEVQEDV
KAFKTGNYVFSYDQFFRDKIMEKKQDHTYRVFKTVNRWADAYPFAQHFSEASVASKDVSV
WCSNDYLGMSRHPQVLQATQETLQRHGAGAGGTRNISGTSKFHVELEQELAELHQKDSAL
LFSSCFVANDSTLFTLAKILPGCEIYSDAGNHASMIQGIRNSGAAKFVFRHNDPDHLKKL
LEKSNPKIPKIVAFETVHSMDGAICPLEELCDVSHQYGALTFVDEVHAVGLYGSRGAGIG
ERDGIMHKIDIISGTLGKAFGCVGGYIASTRDLVDMVRSYAAGFIFTTSLPPMVLSGALE
SVRLLKGEEGQALRRAHQRNVKHMRQLLMDRGLPVIPCPSHIIPIRVGNAALNSKLCDLL
LSKHGIYVQAINYPTVPRGEELLRLAPSPHHSPQMMEDFVEKLLLAWTAVGLPLQDVSVA
ACNFCRRPVHFELMSEWERSYFGNMGPQYVTTYA
|
| Enzyme 93 Number of Residues |
574 |
| Enzyme 93 Molecular Weight |
63486.7 |
| Enzyme 93 Theoretical pI |
8.52 |
| Enzyme 93 GO Classification |
| Function |
- 5-aminolevulinate synthase activity
- N-acyltransferase activity
- N-succinyltransferase activity
- acyltransferase activity
- binding
- catalytic activity
- cofactor binding
- pyridoxal phosphate binding
- transferase activity
- transferase activity, transferring acyl groups
- transferase activity, transferring acyl groups other than amino-acyl groups
- transferase activity, transferring nitrogenous groups
|
| Process |
- biosynthetic process
- cellular biosynthetic process
- heterocycle biosynthetic process
- metabolic process
- nitrogen compound metabolic process
- porphyrin metabolic process
- tetrapyrrole biosynthetic process
- tetrapyrrole metabolic process
|
| Component |
- cell part
- cytoplasmic part
- intracellular part
- mitochondrial matrix
- mitochondrial part
|
|
| Enzyme 93 General Function |
Involved in 5-aminolevulinate synthase activity |
| Enzyme 93 Specific Function |
Not Available |
| Enzyme 93 Pathways |
Not Available |
| Enzyme 93 Reactions |
Not Available |
| Enzyme 93 Pfam Domain Function |
|
| Enzyme 93 Signals |
|
| Enzyme 93 Transmembrane Regions |
|
| Enzyme 93 Essentiality |
Not Available |
| Enzyme 93 GenBank ID Protein |
220732257  |
| Enzyme 93 UniProtKB/Swiss-Prot ID |
Q5JZF5  |
| Enzyme 93 UniProtKB/Swiss-Prot Entry Name |
Q5JZF5_HUMAN  |
| Enzyme 93 PDB ID |
Not Available |
| Enzyme 93 Cellular Location |
Not Available |
| Enzyme 93 Gene Sequence |
>1725 bp
ATGAGAGGGGGAGAGGTTGCTCTGGGATGGAACAAGAAAAAGAGGTTGTTTTGTGAGGAC
TTTAGGTTCAAGATGGTGACTGCAGCCATGCTGCTACAGTGCTGCCCAGTGCTTGCCCGG
GGCCCCACAAGCCTCCTAGGCAAGGTGGTTAAGACTCACCAGTTCCTGTTTGGTATTGGA
CGCTGTCCCATCCTGGCTACCCAAGGACCAAACTGTTCTCAAATCCACCTTAAGGCAACA
AAGGCTGGAGGAGATTCTCCATCTTGGGCGAAGGGCCACTGTCCCTTCATGCTGTCGGAA
CTCCAGGATGGGAAGAGCAAGATTGTGCAGAAGGCAGCCCCAGAAGTCCAGGAAGATGTG
AAGGCTTTCAAGACAGGAAACTATGTCTTCAGTTATGACCAGTTTTTCAGGGACAAGATC
ATGGAGAAGAAACAGGATCACACCTACCGTGTGTTCAAGACTGTGAACCGCTGGGCTGAT
GCATATCCCTTTGCCCAACATTTCTCTGAGGCATCTGTGGCCTCAAAGGATGTGTCCGTC
TGGTGTAGTAATGATTACCTGGGCATGAGCCGACACCCTCAGGTCTTGCAAGCCACACAG
GAGACCCTGCAGCGTCATGGTGCTGGAGCTGGTGGCACCCGCAACATCTCAGGCACCAGT
AAGTTTCATGTGGAGCTTGAGCAGGAGCTGGCTGAGCTGCACCAGAAGGACTCAGCCCTG
CTCTTCTCCTCCTGCTTTGTTGCCAATGACTCTACTCTCTTCACCTTGGCCAAGATCCTG
CCAGGGTGCGAGATTTACTCAGACGCAGGCAACCATGCTTCCATGATCCAAGGTATCCGT
AACAGTGGAGCAGCCAAGTTTGTCTTCAGGCACAATGACCCTGACCACCTAAAGAAACTT
CTAGAGAAGTCTAACCCTAAGATACCCAAAATTGTGGCCTTTGAGACTGTCCACTCCATG
GATGGTGCCATCTGTCCCCTCGAGGAGTTGTGTGATGTGTCCCACCAGTATGGGGCCCTG
ACCTTCGTGGATGAGGTCCATGCTGTAGGACTGTATGGGTCCCGGGGCGCTGGGATTGGG
GAGCGTGATGGAATTATGCATAAGATTGACATCATCTCTGGAACTCTTGGCAAGGCCTTT
GGCTGTGTGGGCGGCTACATTGCCAGCACCCGTGACTTGGTGGACATGGTGCGCTCCTAT
GCTGCAGGCTTCATCTTTACCACTTCTCTGCCCCCCATGGTGCTCTCTGGAGCTCTAGAA
TCTGTGCGGCTGCTCAAGGGAGAGGAGGGCCAAGCCCTGAGGCGAGCCCACCAGCGCAAT
GTCAAGCACATGCGCCAGCTACTCATGGACAGGGGCCTTCCTGTCATCCCCTGCCCCAGC
CACATCATCCCCATCCGGGTGGGCAATGCAGCACTCAACAGCAAGCTCTGTGATCTCCTG
CTCTCCAAGCATGGCATCTATGTGCAGGCCATCAACTACCCAACTGTCCCCCGGGGTGAA
GAGCTCCTGCGCTTGGCACCCTCCCCCCACCACAGCCCTCAGATGATGGAAGATTTTGTG
GAGAAGCTGCTGCTGGCTTGGACTGCGGTGGGGCTGCCCCTCCAGGATGTGTCTGTGGCT
GCCTGCAATTTCTGTCGCCGTCCTGTACACTTTGAGCTCATGAGTGAGTGGGAACGTTCC
TACTTCGGGAACATGGGGCCCCAGTATGTCACCACCTATGCCTGA
|
| Enzyme 93 GenBank Gene ID |
AL020991  |
| Enzyme 93 GeneCard ID |
ALAS2  |
| Enzyme 93 GenAtlas ID |
ALAS2  |
| Enzyme 93 HGNC ID |
HGNC:397  |
| Enzyme 93 Chromosome Location |
Not Available |
| Enzyme 93 Locus |
Not Available |
| Enzyme 93 SNPs |
SNPJam Report  |
| Enzyme 93 General References |
Not Available |
| Enzyme 93 Metabolite References |
Not Available |
|
Enzyme 94
[top]
|
| Enzyme 94 ID |
14733 |
| Enzyme 94 Name |
Glutamate decarboxylase 2 (Pancreatic islets and brain, 65kDa) |
| Enzyme 94 Synonyms |
Not Available |
| Enzyme 94 Gene Name |
GAD2 |
| Enzyme 94 Protein Sequence |
>Glutamate decarboxylase 2 (Pancreatic islets and brain, 65kDa)
MNILLQYVVKSFDRSTKVIDFHYPNELLQEYNWELADQPQNLEEILMHCQTTLKYAIKTG
HPRYFNQLSTGLDMVGLAADWLTSTANTNMFTYEIAPVFVLLEYVTLKKMREIIGWPGGS
GDGIFSPGT
|
| Enzyme 94 Number of Residues |
129 |
| Enzyme 94 Molecular Weight |
14754.8 |
| Enzyme 94 Theoretical pI |
4.80 |
| Enzyme 94 GO Classification |
| Function |
- binding
- carbon-carbon lyase activity
- carboxy-lyase activity
- catalytic activity
- cofactor binding
- lyase activity
- pyridoxal phosphate binding
|
| Process |
- carboxylic acid metabolic process
- cellular metabolic process
- metabolic process
- organic acid metabolic process
- oxoacid metabolic process
|
| Component |
| — |
|
| Enzyme 94 General Function |
Involved in carboxy-lyase activity |
| Enzyme 94 Specific Function |
Not Available |
| Enzyme 94 Pathways |
Not Available |
| Enzyme 94 Reactions |
Not Available |
| Enzyme 94 Pfam Domain Function |
|
| Enzyme 94 Signals |
|
| Enzyme 94 Transmembrane Regions |
|
| Enzyme 94 Essentiality |
Not Available |
| Enzyme 94 GenBank ID Protein |
55662654  |
| Enzyme 94 UniProtKB/Swiss-Prot ID |
Q5VZ29  |
| Enzyme 94 UniProtKB/Swiss-Prot Entry Name |
Q5VZ29_HUMAN  |
| Enzyme 94 PDB ID |
Not Available |
| Enzyme 94 Cellular Location |
Not Available |
| Enzyme 94 Gene Sequence |
>390 bp
ATGAACATTTTACTTCAGTATGTGGTGAAAAGTTTCGATAGATCAACCAAAGTGATTGAT
TTCCATTATCCTAATGAGCTTCTCCAAGAATATAATTGGGAATTGGCAGACCAACCACAA
AATTTGGAGGAAATTTTGATGCATTGCCAAACAACTCTAAAATATGCAATTAAAACAGGG
CATCCTAGATACTTCAATCAACTTTCTACTGGTTTGGATATGGTTGGATTAGCAGCAGAC
TGGCTGACATCAACAGCAAATACTAACATGTTCACCTATGAAATTGCTCCAGTATTTGTG
CTTTTGGAATATGTCACACTAAAGAAAATGAGAGAAATCATTGGCTGGCCAGGGGGCTCT
GGCGATGGGATATTTTCTCCCGGTACATGA
|
| Enzyme 94 GenBank Gene ID |
AL162503  |
| Enzyme 94 GeneCard ID |
GAD2  |
| Enzyme 94 GenAtlas ID |
GAD2  |
| Enzyme 94 HGNC ID |
HGNC:4093  |
| Enzyme 94 Chromosome Location |
1 |
| Enzyme 94 Locus |
10p11.23 |
| Enzyme 94 SNPs |
SNPJam Report  |
| Enzyme 94 General References |
Not Available |
| Enzyme 94 Metabolite References |
Not Available |
|
Enzyme 95
[top]
|
| Enzyme 95 ID |
14734 |
| Enzyme 95 Name |
Glutamate decarboxylase 2 (Pancreatic islets and brain, 65kDa) |
| Enzyme 95 Synonyms |
- SubName: Glutamate decarboxylase 2 (Pancreatic islets and brain, 65kDa), isoform CRA_b
|
| Enzyme 95 Gene Name |
GAD2 |
| Enzyme 95 Protein Sequence |
>Glutamate decarboxylase 2 (Pancreatic islets and brain, 65kDa)
MASPGSGFWSFGSEDGSGDSENPGTARAWCQVAQKFTGGIGNKLCALLYGDAEKPAESGG
SQPPRAAARKAACACDQKPCSCSKVDVNYAFLHATDLLPACDGERPTLAFLQDVMNILLQ
YVVKSFDRSTKVIDFHYPNELLQEYNWELADQPQNLEEILMHCQTTLKYAIKTGHPRYFN
QLSTGLDMVGLAADWLTSTANTNMFTYEIAPVFVLLEYVTLKKMREIIGWPGGSGDGIFS
PGGAISNMYAMMIARFKMFPEVKEKGMAALPRLIAFTSEHSHFSLKKGAAALGIGTDSVI
LIKCDERGKMIPSDLERRILEAKQKGFVPFLVSATAGTTVYGAFDPLLAVADICKKYKIW
MHVDAAWGGGLLMSRKHKWKLSGVERANSVTWNPHKMMGVPLQCSALLVREEGLMQNCNQ
MHASYLFQQDKHYDLSYDTGDKALQCGRHVDVFKLWLMWRAKGTTGFEAHVDKCLELAEY
LYNIIKNREGYEMVFDGKPQHTNVCFWYIPPSLRTLEDNEERMSRLSKVAPVIKARMMEY
GTTMVSYQPLGDKVNFFRMVISNPAATHQDIDFLIEEIERLGQDL
|
| Enzyme 95 Number of Residues |
585 |
| Enzyme 95 Molecular Weight |
65410.8 |
| Enzyme 95 Theoretical pI |
6.89 |
| Enzyme 95 GO Classification |
| Function |
- binding
- carbon-carbon lyase activity
- carboxy-lyase activity
- catalytic activity
- cofactor binding
- lyase activity
- pyridoxal phosphate binding
|
| Process |
- carboxylic acid metabolic process
- cellular metabolic process
- metabolic process
- organic acid metabolic process
- oxoacid metabolic process
|
| Component |
| — |
|
| Enzyme 95 General Function |
Involved in carboxy-lyase activity |
| Enzyme 95 Specific Function |
Not Available |
| Enzyme 95 Pathways |
Not Available |
| Enzyme 95 Reactions |
Not Available |
| Enzyme 95 Pfam Domain Function |
|
| Enzyme 95 Signals |
|
| Enzyme 95 Transmembrane Regions |
|
| Enzyme 95 Essentiality |
Not Available |
| Enzyme 95 GenBank ID Protein |
118835509  |
| Enzyme 95 UniProtKB/Swiss-Prot ID |
Q5VZ30  |
| Enzyme 95 UniProtKB/Swiss-Prot Entry Name |
Q5VZ30_HUMAN  |
| Enzyme 95 PDB ID |
Not Available |
| Enzyme 95 Cellular Location |
Not Available |
| Enzyme 95 Gene Sequence |
>1758 bp
ATGGCATCTCCGGGCTCTGGCTTTTGGTCTTTCGGGTCGGAAGATGGCTCTGGGGATTCC
GAGAATCCCGGCACAGCGCGAGCCTGGTGCCAAGTGGCTCAGAAGTTCACGGGCGGCATC
GGAAACAAACTGTGCGCCCTGCTCTACGGAGACGCCGAGAAGCCGGCGGAGAGCGGCGGG
AGCCAACCCCCGCGGGCCGCCGCCCGGAAGGCCGCCTGCGCCTGCGACCAGAAGCCCTGC
AGCTGCTCCAAAGTGGATGTCAACTACGCGTTTCTCCATGCAACAGACCTGCTGCCGGCG
TGTGATGGAGAAAGGCCCACTTTGGCGTTTCTGCAAGATGTTATGAACATTTTACTTCAG
TATGTGGTGAAAAGTTTCGATAGATCAACCAAAGTGATTGATTTCCATTATCCTAATGAG
CTTCTCCAAGAATATAATTGGGAATTGGCAGACCAACCACAAAATTTGGAGGAAATTTTG
ATGCATTGCCAAACAACTCTAAAATATGCAATTAAAACAGGGCATCCTAGATACTTCAAT
CAACTTTCTACTGGTTTGGATATGGTTGGATTAGCAGCAGACTGGCTGACATCAACAGCA
AATACTAACATGTTCACCTATGAAATTGCTCCAGTATTTGTGCTTTTGGAATATGTCACA
CTAAAGAAAATGAGAGAAATCATTGGCTGGCCAGGGGGCTCTGGCGATGGGATATTTTCT
CCCGGTGGCGCCATATCTAACATGTATGCCATGATGATCGCACGCTTTAAGATGTTCCCA
GAAGTCAAGGAGAAAGGAATGGCTGCTCTTCCCAGGCTCATTGCCTTCACGTCTGAACAT
AGTCATTTTTCTCTCAAGAAGGGAGCTGCAGCCTTAGGGATTGGAACAGACAGCGTGATT
CTGATTAAATGTGATGAGAGAGGGAAAATGATTCCATCTGATCTTGAAAGAAGGATTCTT
GAAGCCAAACAGAAAGGGTTTGTTCCTTTCCTCGTGAGTGCCACAGCTGGAACCACCGTG
TACGGAGCATTTGACCCCCTCTTAGCTGTCGCTGACATTTGCAAAAAGTATAAGATCTGG
ATGCATGTGGATGCAGCTTGGGGTGGGGGATTACTGATGTCCCGAAAACACAAGTGGAAA
CTGAGTGGCGTGGAGAGGGCCAACTCTGTGACGTGGAATCCACACAAGATGATGGGAGTC
CCTTTGCAGTGCTCTGCTCTCCTGGTTAGAGAAGAGGGATTGATGCAGAATTGCAACCAA
ATGCATGCCTCCTACCTCTTTCAGCAAGATAAACATTATGACCTGTCCTATGACACTGGA
GACAAGGCCTTACAGTGCGGACGCCACGTTGATGTTTTTAAACTATGGCTGATGTGGAGG
GCAAAGGGGACTACCGGGTTTGAAGCGCATGTTGATAAATGTTTGGAGTTGGCAGAGTAT
TTATACAACATCATAAAAAACCGAGAAGGATATGAGATGGTGTTTGATGGGAAGCCTCAG
CACACAAATGTCTGCTTCTGGTACATTCCTCCAAGCTTGCGTACTCTGGAAGACAATGAA
GAGAGAATGAGTCGCCTCTCGAAGGTGGCTCCAGTGATTAAAGCCAGAATGATGGAGTAT
GGAACCACAATGGTCAGCTACCAACCCTTGGGAGACAAGGTCAATTTCTTCCGCATGGTC
ATCTCAAACCCAGCGGCAACTCACCAAGACATTGACTTCCTGATTGAAGAAATAGAACGC
CTTGGACAAGATTTATAA
|
| Enzyme 95 GenBank Gene ID |
BC126327  |
| Enzyme 95 GeneCard ID |
GAD2  |
| Enzyme 95 GenAtlas ID |
GAD2  |
| Enzyme 95 HGNC ID |
HGNC:4093  |
| Enzyme 95 Chromosome Location |
1 |
| Enzyme 95 Locus |
10p11.23 |
| Enzyme 95 SNPs |
SNPJam Report  |
| Enzyme 95 General References |
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Venter JC, Adams MD, Myers EW, Li PW, Mural RJ, Sutton GG, Smith HO, Yandell M, Evans CA, Holt RA, Gocayne JD, Amanatides P, Ballew RM, Huson DH, Wortman JR, Zhang Q, Kodira CD, Zheng XH, Chen L, Skupski M, Subramanian G, Thomas PD, Zhang J, Gabor Miklos GL, Nelson C, Broder S, Clark AG, Nadeau J, McKusick VA, Zinder N, Levine AJ, Roberts RJ, Simon M, Slayman C, Hunkapiller M, Bolanos R, Delcher A, Dew I, Fasulo D, Flanigan M, Florea L, Halpern A, Hannenhalli S, Kravitz S, Levy S, Mobarry C, Reinert K, Remington K, Abu-Threideh J, Beasley E, Biddick K, Bonazzi V, Brandon R, Cargill M, Chandramouliswaran I, Charlab R, Chaturvedi K, Deng Z, Di Francesco V, Dunn P, Eilbeck K, Evangelista C, Gabrielian AE, Gan W, Ge W, Gong F, Gu Z, Guan P, Heiman TJ, Higgins ME, Ji RR, Ke Z, Ketchum KA, Lai Z, Lei Y, Li Z, Li J, Liang Y, Lin X, Lu F, Merkulov GV, Milshina N, Moore HM, Naik AK, Narayan VA, Neelam B, Nusskern D, Rusch DB, Salzberg S, Shao W, Shue B, Sun J, Wang Z, Wang A, Wang X, Wang J, Wei M, Wides R, Xiao C, Yan C, Yao A, Ye J, Zhan M, Zhang W, Zhang H, Zhao Q, Zheng L, Zhong F, Zhong W, Zhu S, Zhao S, Gilbert D, Baumhueter S, Spier G, Carter C, Cravchik A, Woodage T, Ali F, An H, Awe A, Baldwin D, Baden H, Barnstead M, Barrow I, Beeson K, Busam D, Carver A, Center A, Cheng ML, Curry L, Danaher S, Davenport L, Desilets R, Dietz S, Dodson K, Doup L, Ferriera S, Garg N, Gluecksmann A, Hart B, Haynes J, Haynes C, Heiner C, Hladun S, Hostin D, Houck J, Howland T, Ibegwam C, Johnson J, Kalush F, Kline L, Koduru S, Love A, Mann F, May D, McCawley S, McIntosh T, McMullen I, Moy M, Moy L, Murphy B, Nelson K, Pfannkoch C, Pratts E, Puri V, Qureshi H, Reardon M, Rodriguez R, Rogers YH, Romblad D, Ruhfel B, Scott R, Sitter C, Smallwood M, Stewart E, Strong R, Suh E, Thomas R, Tint NN, Tse S, Vech C, Wang G, Wetter J, Williams S, Williams M, Windsor S, Winn-Deen E, Wolfe K, Zaveri J, Zaveri K, Abril JF, Guigo R, Campbell MJ, Sjolander KV, Karlak B, Kejariwal A, Mi H, Lazareva B, Hatton T, Narechania A, Diemer K, Muruganujan A, Guo N, Sato S, Bafna V, Istrail S, Lippert R, Schwartz R, Walenz B, Yooseph S, Allen D, Basu A, Baxendale J, Blick L, Caminha M, Carnes-Stine J, Caulk P, Chiang YH, Coyne M, Dahlke C, Mays A, Dombroski M, Donnelly M, Ely D, Esparham S, Fosler C, Gire H, Glanowski S, Glasser K, Glodek A, Gorokhov M, Graham K, Gropman B, Harris M, Heil J, Henderson S, Hoover J, Jennings D, Jordan C, Jordan J, Kasha J, Kagan L, Kraft C, Levitsky A, Lewis M, Liu X, Lopez J, Ma D, Majoros W, McDaniel J, Murphy S, Newman M, Nguyen T, Nguyen N, Nodell M, Pan S, Peck J, Peterson M, Rowe W, Sanders R, Scott J, Simpson M, Smith T, Sprague A, Stockwell T, Turner R, Venter E, Wang M, Wen M, Wu D, Wu M, Xia A, Zandieh A, Zhu X: The sequence of the human genome. Science. 2001 Feb 16;291(5507):1304-51. [PubMed
]
|
| Enzyme 95 Metabolite References |
Not Available |
|
Enzyme 96
[top]
|
| Enzyme 96 ID |
14735 |
| Enzyme 96 Name |
Putative L-Dopa decarboxylase |
| Enzyme 96 Synonyms |
Not Available |
| Enzyme 96 Gene Name |
DDC |
| Enzyme 96 Protein Sequence |
>Putative L-Dopa decarboxylase
MNASEFRRRGKEMVDYVANYMEGIEGRQVYPDVEPGYLRPLIPAAAPQEPDTFEDIINDV
EKIIMPGVTHWHSPYFFAYFPTASSYPAMLADMLCGAIGCIGFSWAASPACTELETVMMD
WLGKMLELPKAFLNEKAGEGGGVIQGSASEATLVALLAARTKVIHRLQAASPELTQAAIM
EKLVAYSSDQAHSSVERAGLIGGVKLKAIPSDGNFAMRASALQEALERDKAAGLIPFFMV
ATLGTTTCCSFDNLLEVGPICNKEDIWLHVDAAYAGSAFICPEFRHLLNGVEFADSFNFN
PHKWLLVNFDCSAMWSRQPVRMLRLKKTCLVSAVVRRS
|
| Enzyme 96 Number of Residues |
338 |
| Enzyme 96 Molecular Weight |
37085.4 |
| Enzyme 96 Theoretical pI |
5.41 |
| Enzyme 96 GO Classification |
| Function |
- binding
- carbon-carbon lyase activity
- carboxy-lyase activity
- catalytic activity
- cofactor binding
- lyase activity
- pyridoxal phosphate binding
|
| Process |
- carboxylic acid metabolic process
- cellular amino acid and derivative metabolic process
- cellular metabolic process
- metabolic process
- organic acid metabolic process
- oxoacid metabolic process
|
| Component |
| — |
|
| Enzyme 96 General Function |
Involved in carboxy-lyase activity |
| Enzyme 96 Specific Function |
Not Available |
| Enzyme 96 Pathways |
Not Available |
| Enzyme 96 Reactions |
Not Available |
| Enzyme 96 Pfam Domain Function |
|
| Enzyme 96 Signals |
|
| Enzyme 96 Transmembrane Regions |
|
| Enzyme 96 Essentiality |
Not Available |
| Enzyme 96 GenBank ID Protein |
54969713  |
| Enzyme 96 UniProtKB/Swiss-Prot ID |
Q5W5T9  |
| Enzyme 96 UniProtKB/Swiss-Prot Entry Name |
Q5W5T9_HUMAN  |
| Enzyme 96 PDB ID |
1JS3  |
| Enzyme 96 PDB File |
Show |
| Enzyme 96 3D Structure |
|
| Enzyme 96 Cellular Location |
Not Available |
| Enzyme 96 Gene Sequence |
>1017 bp
ATGAACGCAAGTGAATTCCGAAGGAGAGGGAAGGAGATGGTGGATTACGTGGCCAACTAC
ATGGAAGGCATTGAGGGACGCCAGGTCTACCCTGACGTGGAGCCCGGGTACCTGCGGCCG
CTGATCCCTGCCGCTGCCCCTCAGGAGCCAGACACGTTTGAGGACATCATCAACGACGTT
GAGAAGATAATCATGCCTGGGGTGACGCACTGGCACAGCCCCTACTTCTTCGCCTACTTC
CCCACTGCCAGCTCGTACCCGGCCATGCTTGCGGACATGCTGTGCGGGGCCATTGGCTGC
ATCGGCTTCTCCTGGGCGGCAAGCCCAGCATGCACAGAGCTGGAGACTGTGATGATGGAC
TGGCTCGGGAAGATGCTGGAACTACCAAAGGCATTTTTGAATGAGAAAGCTGGAGAAGGG
GGAGGAGTGATCCAGGGAAGTGCCAGTGAAGCCACCCTGGTGGCCCTGCTGGCCGCTCGG
ACCAAAGTGATCCATCGGCTGCAGGCAGCGTCCCCAGAGCTCACACAGGCCGCTATCATG
GAGAAGCTGGTGGCTTACTCATCCGATCAGGCACACTCCTCAGTGGAAAGAGCTGGGTTA
ATTGGTGGAGTGAAATTAAAAGCCATCCCCTCAGATGGCAACTTCGCCATGCGTGCGTCT
GCCCTGCAGGAAGCCCTGGAGAGAGACAAAGCGGCTGGCCTGATTCCTTTCTTTATGGTT
GCCACCCTGGGGACCACAACATGCTGCTCCTTTGACAATCTCTTAGAAGTCGGTCCTATC
TGCAACAAGGAAGACATATGGCTGCACGTTGATGCAGCCTACGCAGGCAGTGCATTCATC
TGCCCTGAGTTCCGGCACCTTCTGAATGGAGTGGAGTTTGCAGATTCATTCAACTTTAAT
CCCCACAAATGGCTATTGGTGAATTTTGACTGTTCTGCCATGTGGTCCAGACAACCAGTG
CGTATGTTAAGGCTGAAGAAAACCTGCTTAGTCAGTGCGGTGGTGAGAAGGAGTTGA
|
| Enzyme 96 GenBank Gene ID |
AJ310724  |
| Enzyme 96 GeneCard ID |
DDC  |
| Enzyme 96 GenAtlas ID |
DDC  |
| Enzyme 96 HGNC ID |
HGNC:2719  |
| Enzyme 96 Chromosome Location |
7 |
| Enzyme 96 Locus |
7p12.2 |
| Enzyme 96 SNPs |
SNPJam Report  |
| Enzyme 96 General References |
Not Available |
| Enzyme 96 Metabolite References |
Not Available |
|
Enzyme 97
[top]
|
| Enzyme 97 ID |
14736 |
| Enzyme 97 Name |
DDC protein |
| Enzyme 97 Synonyms |
Not Available |
| Enzyme 97 Gene Name |
DDC |
| Enzyme 97 Protein Sequence |
>DDC protein
MNASEFRRRGKEMVDYVANYMEGIEGRQVYPDVEPGYLRPLIPAAAPQEPDTFEDIINDV
EKIIMPGVTHWHSPYFFAYFPTASSYPAMLADMLCGAIGCIGFSWAASPACTELETVMMD
WLGKMLELPKAFLNEKAGEGGGVIQGSASEATLVALLAARTKVIHRLQAASPELTQAAIM
EKLVAYSSDQAHSSVERAGLIGGVKLKAIPSDGNFAMRASALQEALERDKAAGLIPFFMV
ATLGTTTCCSFDNLLEVGPICNKEDIWLHVDAAYAGSAFICPEFRHLLNGVEFADSFNFN
PHKWLLVNFDCSAMWVKKRTDLTGAFRLDPTYLKHSHQDSGLITDYRHWQIPLGRRFRSL
KMWFVFRMYGVKGLQAYIRKHVQLSHEFESLVRQDPRFEICVEVILGLVCFRLKGSNKVN
EALLQRINSAKKIHLVPCHLRDKFVLRFAICSRTVESAHVQRAWEHIKELAADVLRAERD
|
| Enzyme 97 Number of Residues |
480 |
| Enzyme 97 Molecular Weight |
53879.7 |
| Enzyme 97 Theoretical pI |
7.21 |
| Enzyme 97 GO Classification |
| Function |
- binding
- carbon-carbon lyase activity
- carboxy-lyase activity
- catalytic activity
- cofactor binding
- lyase activity
- pyridoxal phosphate binding
|
| Process |
- carboxylic acid metabolic process
- cellular amino acid and derivative metabolic process
- cellular metabolic process
- metabolic process
- organic acid metabolic process
- oxoacid metabolic process
|
| Component |
| — |
|
| Enzyme 97 General Function |
Involved in carboxy-lyase activity |
| Enzyme 97 Specific Function |
Not Available |
| Enzyme 97 Pathways |
Not Available |
| Enzyme 97 Reactions |
Not Available |
| Enzyme 97 Pfam Domain Function |
|
| Enzyme 97 Signals |
|
| Enzyme 97 Transmembrane Regions |
|
| Enzyme 97 Essentiality |
Not Available |
| Enzyme 97 GenBank ID Protein |
48145565  |
| Enzyme 97 UniProtKB/Swiss-Prot ID |
Q6IBS8  |
| Enzyme 97 UniProtKB/Swiss-Prot Entry Name |
Q6IBS8_HUMAN  |
| Enzyme 97 PDB ID |
1JS3  |
| Enzyme 97 PDB File |
Show |
| Enzyme 97 3D Structure |
|
| Enzyme 97 Cellular Location |
Not Available |
| Enzyme 97 Gene Sequence |
>1443 bp
ATGAACGCAAGTGAATTCCGAAGGAGAGGGAAGGAGATGGTGGATTACGTGGCCAACTAC
ATGGAAGGCATTGAGGGACGCCAGGTCTACCCTGACGTGGAGCCCGGGTACCTGCGGCCG
CTGATCCCTGCCGCTGCCCCTCAGGAGCCAGACACGTTTGAGGACATCATCAACGACGTT
GAGAAGATAATCATGCCTGGGGTGACGCACTGGCACAGCCCCTACTTCTTCGCCTACTTC
CCCACTGCCAGCTCGTACCCGGCCATGCTTGCGGACATGCTGTGCGGGGCCATTGGCTGC
ATCGGCTTCTCCTGGGCGGCAAGCCCAGCATGCACAGAGCTGGAGACTGTGATGATGGAC
TGGCTCGGGAAGATGCTGGAACTACCAAAGGCATTTTTGAATGAGAAAGCTGGAGAAGGG
GGAGGAGTGATCCAGGGAAGTGCCAGTGAAGCCACCCTGGTGGCCCTGCTGGCCGCTCGG
ACCAAAGTGATCCATCGGCTGCAGGCAGCGTCCCCAGAGCTCACACAGGCCGCTATCATG
GAGAAGCTGGTGGCTTACTCATCCGATCAGGCACACTCCTCAGTGGAAAGAGCTGGGTTA
ATTGGTGGAGTGAAATTAAAAGCCATCCCCTCAGATGGCAACTTCGCCATGCGTGCGTCT
GCCCTGCAGGAAGCCCTGGAGAGAGACAAAGCGGCTGGCCTGATTCCTTTCTTTATGGTT
GCCACCCTGGGGACCACAACATGCTGCTCCTTTGACAATCTCTTAGAAGTCGGTCCTATC
TGCAACAAGGAAGACATATGGCTGCACGTTGATGCAGCCTACGCAGGCAGTGCATTCATC
TGCCCTGAGTTCCGGCACCTTCTGAATGGAGTGGAGTTTGCAGATTCATTCAACTTTAAT
CCCCACAAATGGCTATTGGTGAATTTTGACTGTTCTGCCATGTGGGTGAAAAAGAGAACA
GACTTAACGGGAGCCTTTAGACTGGACCCCACTTACCTGAAGCACAGCCATCAGGATTCA
GGGCTTATCACTGACTACCGGCATTGGCAGATACCACTGGGCAGAAGATTTCGCTCTTTG
AAAATGTGGTTTGTATTTAGGATGTATGGAGTCAAAGGACTGCAGGCTTATATCCGCAAG
CATGTCCAGCTGTCCCATGAGTTTGAGTCACTGGTGCGCCAGGATCCCCGCTTTGAAATC
TGTGTGGAAGTCATTCTGGGGCTTGTCTGCTTTCGGCTAAAGGGTTCCAACAAAGTGAAT
GAAGCTCTTCTGCAAAGAATAAACAGTGCCAAAAAAATCCACTTGGTTCCATGTCACCTC
AGGGACAAGTTTGTCCTGCGCTTTGCCATCTGTTCTCGCACGGTGGAATCTGCCCATGTG
CAGCGGGCCTGGGAACACATCAAAGAGCTGGCGGCCGACGTGCTGCGAGCAGAGAGGGAT
TAA
|
| Enzyme 97 GenBank Gene ID |
CR456724  |
| Enzyme 97 GeneCard ID |
DDC  |
| Enzyme 97 GenAtlas ID |
DDC  |
| Enzyme 97 HGNC ID |
HGNC:2719  |
| Enzyme 97 Chromosome Location |
7 |
| Enzyme 97 Locus |
7p12.2 |
| Enzyme 97 SNPs |
SNPJam Report  |
| Enzyme 97 General References |
Not Available |
| Enzyme 97 Metabolite References |
Not Available |
|
Enzyme 98
[top]
|
| Enzyme 98 ID |
14737 |
| Enzyme 98 Name |
Putative uncharacterized protein DDC |
| Enzyme 98 Synonyms |
Not Available |
| Enzyme 98 Gene Name |
DDC |
| Enzyme 98 Protein Sequence |
>Putative uncharacterized protein DDC
MNASEFRRRGKEMVDYMANYMEGIEGRQVYPDVEPGYLRPLIPAAAPQEPDTFEDIINDV
EKIIMPGVTHWHSPYFFAYFPTASSYPAMLADMLCGAIGCIGFSWAASPACTELETVMMD
WLGKMLELPKAFLNEKAGEGGGVIQGSASEATLVALLAARTKVIHRLQAASPELTQAAIM
EKLVAYSSDQAHSSVERAGLIGGVKLKAIPSDGNFAMRASALQEALERDKAAGLIPFFMV
ATLGTTTCCSFDNLLEVGPICNKEDIWLHVDAAYAGSAFICPEFRHLLNGVEFADSFNFN
PHKWLLVNFDCSAMWVKKRTDLTGAFRLDPTYLKHSHQDSGLITDYRHWQIPLGRRFRSL
KMWFVFRMYGVKGLQAYIRKHVQLSHEFESLVRQDPRFEICVEVILGLVCFRLKGSNKVN
EALLQRINSAKKIHLVPCHLRDKFVLRFAICSRTVESAHVQRAWEHIKELAADVLRAERE
|
| Enzyme 98 Number of Residues |
480 |
| Enzyme 98 Molecular Weight |
53927 |
| Enzyme 98 Theoretical pI |
7.21 |
| Enzyme 98 GO Classification |
| Function |
- carbon-carbon lyase activity
- carboxy-lyase activity
- catalytic activity
- lyase activity
|
| Process |
- amino acid and derivative metabolism
- amino acid metabolism
- cellular metabolism
- metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 98 General Function |
Amino acid transport and metabolism |
| Enzyme 98 Specific Function |
Not Available |
| Enzyme 98 Pathways |
Not Available |
| Enzyme 98 Reactions |
Not Available |
| Enzyme 98 Pfam Domain Function |
|
| Enzyme 98 Signals |
|
| Enzyme 98 Transmembrane Regions |
|
| Enzyme 98 Essentiality |
Not Available |
| Enzyme 98 GenBank ID Protein |
41393464  |
| Enzyme 98 UniProtKB/Swiss-Prot ID |
Q75MJ6  |
| Enzyme 98 UniProtKB/Swiss-Prot Entry Name |
Q75MJ6_HUMAN  |
| Enzyme 98 PDB ID |
1JS3  |
| Enzyme 98 PDB File |
Show |
| Enzyme 98 3D Structure |
|
| Enzyme 98 Cellular Location |
Not Available |
| Enzyme 98 Gene Sequence |
>1443 bp
ATGAACGCAAGTGAATTCCGAAGGAGAGGGAAGGAGATGGTGGATTACATGGCCAACTAC
ATGGAAGGCATTGAGGGACGCCAGGTCTACCCTGACGTGGAGCCCGGGTACCTGCGGCCG
CTGATCCCTGCCGCTGCCCCTCAGGAGCCAGACACGTTTGAGGACATCATCAACGACGTT
GAGAAGATAATCATGCCTGGGGTGACGCACTGGCACAGCCCCTACTTCTTCGCCTACTTC
CCCACTGCCAGCTCGTACCCGGCCATGCTTGCGGACATGCTGTGCGGGGCCATTGGCTGC
ATCGGCTTCTCCTGGGCGGCAAGCCCAGCATGCACAGAGCTGGAGACTGTGATGATGGAC
TGGCTCGGGAAGATGCTGGAACTACCAAAGGCATTTTTGAATGAGAAAGCTGGAGAAGGG
GGAGGAGTGATCCAGGGAAGTGCCAGTGAAGCCACCCTGGTGGCCCTGCTGGCCGCTCGG
ACCAAAGTGATCCATCGGCTGCAGGCAGCGTCCCCAGAGCTCACACAGGCCGCTATCATG
GAGAAGCTGGTGGCTTACTCATCCGATCAGGCACACTCCTCAGTGGAAAGAGCTGGGTTA
ATTGGTGGAGTGAAATTAAAAGCCATCCCCTCAGATGGCAACTTCGCCATGCGTGCGTCT
GCCCTGCAGGAAGCCCTGGAGAGAGACAAAGCGGCTGGCCTGATTCCTTTCTTTATGGTT
GCCACCCTGGGGACCACAACATGCTGCTCCTTTGACAATCTCTTAGAAGTCGGTCCTATC
TGCAACAAGGAAGACATATGGCTGCACGTTGATGCAGCCTACGCAGGCAGTGCATTCATC
TGCCCTGAGTTCCGGCACCTTCTGAATGGAGTGGAGTTTGCAGATTCATTCAACTTTAAT
CCCCACAAATGGCTATTGGTGAATTTTGACTGTTCTGCCATGTGGGTGAAAAAGAGAACA
GACTTAACGGGAGCCTTTAGACTGGACCCCACTTACCTGAAGCACAGCCATCAGGATTCA
GGGCTTATCACTGACTACCGGCATTGGCAGATACCACTGGGCAGAAGATTTCGCTCTTTG
AAAATGTGGTTTGTATTTAGGATGTATGGAGTCAAAGGACTGCAGGCTTATATCCGCAAG
CATGTCCAGCTGTCCCATGAGTTTGAGTCACTGGTGCGCCAGGATCCCCGCTTTGAAATC
TGTGTGGAAGTCATTCTGGGGCTTGTCTGCTTTCGGCTAAAGGGTTCCAACAAAGTGAAT
GAAGCTCTTCTGCAAAGAATAAACAGTGCCAAAAAAATCCACTTGGTTCCATGTCACCTC
AGGGACAAGTTTGTCCTGCGCTTTGCCATCTGTTCTCGCACGGTGGAATCTGCCCATGTG
CAGCGGGCCTGGGAACACATCAAAGAGCTGGCGGCCGACGTGCTGCGAGCAGAGAGGGAG
TAG
|
| Enzyme 98 GenBank Gene ID |
AC018705  |
| Enzyme 98 GeneCard ID |
Q75MJ6  |
| Enzyme 98 GenAtlas ID |
DDC  |
| Enzyme 98 HGNC ID |
HGNC:2719  |
| Enzyme 98 Chromosome Location |
Not Available |
| Enzyme 98 Locus |
Not Available |
| Enzyme 98 SNPs |
SNPJam Report  |
| Enzyme 98 General References |
- Hillier LW, Fulton RS, Fulton LA, Graves TA, Pepin KH, Wagner-McPherson C, Layman D, Maas J, Jaeger S, Walker R, Wylie K, Sekhon M, Becker MC, O'Laughlin MD, Schaller ME, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Cordes M, Du H, Sun H, Edwards J, Bradshaw-Cordum H, Ali J, Andrews S, Isak A, Vanbrunt A, Nguyen C, Du F, Lamar B, Courtney L, Kalicki J, Ozersky P, Bielicki L, Scott K, Holmes A, Harkins R, Harris A, Strong CM, Hou S, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Leonard S, Rohlfing T, Rock SM, Tin-Wollam AM, Abbott A, Minx P, Maupin R, Strowmatt C, Latreille P, Miller N, Johnson D, Murray J, Woessner JP, Wendl MC, Yang SP, Schultz BR, Wallis JW, Spieth J, Bieri TA, Nelson JO, Berkowicz N, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Bedell JA, Mardis ER, Clifton SW, Chissoe SL, Marra MA, Raymond C, Haugen E, Gillett W, Zhou Y, James R, Phelps K, Iadanoto S, Bubb K, Simms E, Levy R, Clendenning J, Kaul R, Kent WJ, Furey TS, Baertsch RA, Brent MR, Keibler E, Flicek P, Bork P, Suyama M, Bailey JA, Portnoy ME, Torrents D, Chinwalla AT, Gish WR, Eddy SR, McPherson JD, Olson MV, Eichler EE, Green ED, Waterston RH, Wilson RK: The DNA sequence of human chromosome 7. Nature. 2003 Jul 10;424(6945):157-64. [PubMed
]
|
| Enzyme 98 Metabolite References |
Not Available |
|
Enzyme 99
[top]
|
| Enzyme 99 ID |
14738 |
| Enzyme 99 Name |
CSAD protein |
| Enzyme 99 Synonyms |
Not Available |
| Enzyme 99 Gene Name |
CSAD |
| Enzyme 99 Protein Sequence |
>CSAD protein
HGLRATEALPSVRTTLRSLGLAPTCQARPPAGSLAARRLLQAPAHPANPTAAAAPTGTEG
GSHLWSQHVGRPRSYLCTLPPALLSREILMADSEALPSLAGDPVAVEALLRAVFGVVVDE
AIQKGTSVSQKVCEWKEPEELKQLLDLELRSQGESQKQILERCRAVIRYSVKTGHPRFFN
QLFSGLDPHALAGRIITESLNTSQYTYEIAPVFVLMEEEVLRKLRALVGWSSGDGIFCPG
GSISNMYAVNLARYQRYPDCKQRGLRTLPPLALFTSKECHYSIQKGAAFLGLGTDSVRVV
KADERGKMVPEDLDRQIGMAEAEGAVPFLVSATSGTTVLGAFDPLEAIADVCQRHGLWLH
VDAAWGGSVLLSQTHRHLLDGIQRADSVAWNPHKLLAAGLQCSALLLQDTSNLLKRCHGS
QASYLFQQDKFYDVALDTGDKVVQCGRRVDCLKLWLMWKAQGDQGLERRIDQAFVLARYL
VEEMKKREGFELVMEPEFVNVCFWFVPPSLRGKQESPDYHERLSKVAPVLKERMVKEGSM
MIGYQPHGTRGNFFRVVVANSALTCADMDFLLNELERLGQDL
|
| Enzyme 99 Number of Residues |
582 |
| Enzyme 99 Molecular Weight |
64252.3 |
| Enzyme 99 Theoretical pI |
7.50 |
| Enzyme 99 GO Classification |
| Function |
- binding
- carbon-carbon lyase activity
- carboxy-lyase activity
- catalytic activity
- cofactor binding
- lyase activity
- pyridoxal phosphate binding
|
| Process |
- carboxylic acid metabolic process
- cellular metabolic process
- metabolic process
- organic acid metabolic process
- oxoacid metabolic process
|
| Component |
| — |
|
| Enzyme 99 General Function |
Involved in carboxy-lyase activity |
| Enzyme 99 Specific Function |
Not Available |
| Enzyme 99 Pathways |
Not Available |
| Enzyme 99 Reactions |
Not Available |
| Enzyme 99 Pfam Domain Function |
|
| Enzyme 99 Signals |
|
| Enzyme 99 Transmembrane Regions |
|
| Enzyme 99 Essentiality |
Not Available |
| Enzyme 99 GenBank ID Protein |
30354461  |
| Enzyme 99 UniProtKB/Swiss-Prot ID |
Q86V02  |
| Enzyme 99 UniProtKB/Swiss-Prot Entry Name |
Q86V02_HUMAN  |
| Enzyme 99 PDB ID |
Not Available |
| Enzyme 99 Cellular Location |
Not Available |
| Enzyme 99 Gene Sequence |
>1750 bp
CCACGGCTTGCGAGCTACTGAAGCGCTGCCGTCTGTACGGACGACGCTGCGGTCTTTGGG
GCTTGCTCCTACCTGCCAGGCGCGGCCTCCCGCTGGCTCCCTGGCCGCGCGGCGCCTCCT
CCAGGCCCCAGCACACCCTGCCAACCCCACCGCCGCGGCTGCCCCCACCGGGACCGAGGG
TGGCTCACACCTGTGGTCCCAGCACGTTGGGAGGCCGAGGAGCTACCTGTGCACCCTGCC
TCCGGCTCTCCTGAGCAGAGAGATCCTGATGGCTGACTCAGAAGCACTCCCCTCCCTTGC
TGGGGACCCAGTGGCTGTGGAAGCCTTGCTCCGGGCCGTGTTTGGGGTTGTTGTGGATGA
GGCCATTCAGAAAGGAACCAGTGTCTCCCAGAAGGTCTGTGAGTGGAAGGAGCCTGAGGA
GCTGAAGCAGCTGCTGGATTTGGAGCTGCGGAGCCAGGGCGAGTCACAGAAGCAGATCCT
GGAGCGGTGTCGGGCTGTGATTCGCTACAGTGTCAAGACTGGTCACCCTCGGTTCTTCAA
CCAGCTCTTCTCTGGGTTGGATCCCCATGCTCTGGCCGGGCGCATTATCACTGAGAGCCT
CAACACCAGCCAGTACACATATGAAATCGCCCCCGTGTTTGTGCTCATGGAAGAGGAGGT
GCTGAGGAAACTGCGGGCCCTGGTGGGCTGGAGCTCTGGGGACGGAATCTTCTGCCCTGG
TGGCTCCATCTCCAACATGTATGCTGTAAATCTGGCCCGCTATCAGCGCTACCCGGATTG
CAAGCAGAGGGGCCTCCGCACACTGCCGCCCCTGGCCCTATTCACATCGAAGGAGTGTCA
CTACTCCATCCAGAAGGGAGCTGCGTTTCTGGGACTTGGCACCGACAGTGTCCGAGTGGT
CAAGGCTGATGAGAGAGGGAAAATGGTCCCCGAGGATCTGGACAGGCAGATTGGTATGGC
CGAGGCTGAGGGTGCTGTGCCGTTCCTGGTCAGTGCCACCTCTGGCACCACTGTGCTAGG
GGCCTTTGACCCCCTGGAGGCAATTGCTGATGTGTGCCAGCGTCATGGGCTATGGCTGCA
TGTGGATGCTGCCTGGGGTGGGAGCGTCCTGCTGTCACAGACACACAGGCATCTCCTGGA
TGGGATCCAGAGGGCTGACTCTGTGGCCTGGAATCCCCACAAGCTCCTCGCAGCAGGCCT
GCAATGCTCTGCACTTCTTCTCCAGGATACCTCGAACCTGCTCAAGCGCTGCCATGGGTC
CCAGGCCAGCTACCTTTTCCAGCAGGACAAGTTCTACGATGTGGCTCTGGACACGGGAGA
CAAGGTGGTGCAGTGTGGCCGCCGTGTGGACTGTCTGAAGCTGTGGCTCATGTGGAAGGC
ACAGGGCGATCAAGGGCTGGAGCGGCGCATCGACCAGGCCTTTGTCCTTGCCCGGTACCT
GGTGGAGGAAATGAAGAAGCGGGAAGGGTTTGAGCTAGTCATGGAGCCTGAGTTTGTCAA
TGTGTGTTTCTGGTTCGTACCCCCCAGCCTGCGAGGGAAGCAGGAGAGTCCAGATTACCA
CGAAAGGCTGTCAAAGGTGGCCCCCGTGCTCAAGGAGCGCATGGTGAAGGAGGGCTCCAT
GATGATTGGCTACCAGCCCCACGGGACCCGGGGCAACTTCTTCCGTGTGGTTGTGGCCAA
CTCTGCACTGACCTGTGCTGATATGGACTTCCTCCTCAACGAGCTGGAGCGGCTAGGCCA
GGACCTGTGA
|
| Enzyme 99 GenBank Gene ID |
BC052249  |
| Enzyme 99 GeneCard ID |
CSAD  |
| Enzyme 99 GenAtlas ID |
CSAD  |
| Enzyme 99 HGNC ID |
HGNC:18966  |
| Enzyme 99 Chromosome Location |
1 |
| Enzyme 99 Locus |
12q13.11-q14.3 |
| Enzyme 99 SNPs |
SNPJam Report  |
| Enzyme 99 General References |
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
|
| Enzyme 99 Metabolite References |
Not Available |
|
Enzyme 100
[top]
|
| Enzyme 100 ID |
14739 |
| Enzyme 100 Name |
PDXDC1 protein |
| Enzyme 100 Synonyms |
Not Available |
| Enzyme 100 Gene Name |
PDXDC1 |
| Enzyme 100 Protein Sequence |
>PDXDC1 protein
MDASLEKIADPTLAEMGKNLKEAVKMLEDSQRRTEEENGKKLISGDIPGPLQGSGQDMVS
ILQLVQNLMHGDEDEEPQSPRIQNIGEQGHMALLGHSLGAYISTLDKEKLRKLTTRILSD
TTLWLCRIFRYENGCAYFHEEEREGLAKICRLAIHSRYEDFVVDGFNVLYNKKPVIYLSA
AARPGLGQYLCNQLGLPFPCLCRVPCNTVFGSQHQMDVAFLEKLIKDDIERGRLPLLLVA
NAGTAAVGHTDKIGRLKELCEQYGIWLHVEGVNLATLALGYVSSSVLAAAKCDSMTMTPG
PWLGLPAVPAVTLYKHDDPALTLVAGLTSNKPTDKLRALPLWLSLQYLGLDGFVERIKHA
CQLSQRLQESLKKVNYIKILVEDELSSPVVVFRFFQELPGSDPVFKAVPVPNMTPSGVGR
ERHSCDALNRWLGEQLKQLVPASGLTVMDLEAEGTCLRFSPLMTAAGWSHCGTTTRYDCV
RSRLTTRLPGSTGEQAPP
|
| Enzyme 100 Number of Residues |
498 |
| Enzyme 100 Molecular Weight |
54981.9 |
| Enzyme 100 Theoretical pI |
6.64 |
| Enzyme 100 GO Classification |
| Function |
- binding
- carbon-carbon lyase activity
- carboxy-lyase activity
- catalytic activity
- cofactor binding
- lyase activity
- pyridoxal phosphate binding
|
| Process |
- carboxylic acid metabolic process
- cellular metabolic process
- metabolic process
- organic acid metabolic process
- oxoacid metabolic process
|
| Component |
| — |
|
| Enzyme 100 General Function |
Involved in carboxy-lyase activity |
| Enzyme 100 Specific Function |
Not Available |
| Enzyme 100 Pathways |
Not Available |
| Enzyme 100 Reactions |
Not Available |
| Enzyme 100 Pfam Domain Function |
|
| Enzyme 100 Signals |
|
| Enzyme 100 Transmembrane Regions |
|
| Enzyme 100 Essentiality |
Not Available |
| Enzyme 100 GenBank ID Protein |
71052052  |
| Enzyme 100 UniProtKB/Swiss-Prot ID |
Q86XE2  |
| Enzyme 100 UniProtKB/Swiss-Prot Entry Name |
Q86XE2_HUMAN  |
| Enzyme 100 PDB ID |
Not Available |
| Enzyme 100 Cellular Location |
Not Available |
| Enzyme 100 Gene Sequence |
>1497 bp
ATGGACGCGTCCCTGGAGAAGATAGCAGACCCCACGTTAGCTGAAATGGGAAAAAACTTG
AAGGAGGCAGTGAAGATGCTGGAGGACAGTCAGAGAAGAACAGAAGAGGAAAATGGAAAG
AAGCTCATATCCGGAGATATTCCAGGCCCACTCCAGGGCAGTGGGCAAGATATGGTGAGC
ATCCTCCAGTTAGTTCAGAATCTCATGCATGGAGATGAAGATGAGGAGCCCCAGAGCCCC
AGAATCCAAAATATTGGAGAACAAGGTCATATGGCTTTGTTGGGACATAGTCTGGGAGCT
TATATTTCAACTCTGGACAAAGAGAAGCTGAGAAAACTTACAACTAGGATACTTTCAGAT
ACCACCTTATGGCTATGCAGAATTTTCAGATATGAAAATGGGTGTGCTTATTTCCACGAA
GAGGAAAGAGAAGGACTTGCAAAGATATGTAGGCTTGCCATTCATTCTCGATATGAAGAC
TTCGTAGTGGATGGCTTCAATGTGTTATATAACAAGAAGCCTGTCATATATCTTAGTGCT
GCTGCTAGACCTGGCCTGGGCCAATACCTTTGTAATCAGCTCGGCTTGCCCTTCCCCTGC
TTGTGCCGTGTACCCTGTAACACTGTGTTTGGATCCCAGCATCAGATGGATGTTGCCTTC
CTGGAGAAACTGATTAAAGATGATATAGAGCGAGGAAGACTGCCCCTGTTGCTTGTCGCA
AATGCAGGAACGGCAGCAGTAGGACACACAGACAAGATTGGGAGATTGAAAGAACTCTGT
GAGCAGTATGGCATATGGCTTCATGTGGAGGGTGTGAATCTGGCAACATTGGCTCTGGGT
TATGTCTCCTCATCAGTGCTGGCTGCAGCCAAATGTGATAGCATGACGATGACTCCTGGC
CCGTGGCTGGGTTTGCCAGCTGTTCCTGCGGTGACACTGTATAAACACGATGACCCTGCC
TTGACTTTAGTTGCTGGTCTTACATCAAATAAGCCCACAGACAAACTCCGTGCCCTGCCT
CTGTGGTTATCTTTACAATACTTGGGACTTGATGGGTTTGTGGAGAGGATCAAGCATGCC
TGTCAACTGAGTCAACGGTTGCAGGAAAGTTTGAAGAAAGTGAATTACATCAAAATCTTG
GTGGAAGATGAGCTCAGCTCCCCAGTGGTGGTGTTCAGATTTTTCCAGGAATTACCAGGC
TCAGATCCGGTGTTTAAAGCCGTCCCAGTGCCCAACATGACACCTTCAGGAGTCGGCCGG
GAGAGGCACTCGTGTGACGCGCTGAATCGCTGGCTGGGAGAACAGCTGAAGCAGCTGGTG
CCTGCAAGCGGCCTCACAGTCATGGATCTGGAAGCTGAGGGCACGTGTTTGCGGTTCAGC
CCTTTGATGACCGCAGCAGGGTGGTCCCACTGTGGGACCACAACCAGGTATGACTGTGTG
AGAAGCAGGCTCACTACCAGGCTACCAGGGAGCACAGGGGAGCAGGCGCCACCTTGA
|
| Enzyme 100 GenBank Gene ID |
BC045554  |
| Enzyme 100 GeneCard ID |
PDXDC1  |
| Enzyme 100 GenAtlas ID |
PDXDC1  |
| Enzyme 100 HGNC ID |
HGNC:28995  |
| Enzyme 100 Chromosome Location |
1 |
| Enzyme 100 Locus |
16p13.11 |
| Enzyme 100 SNPs |
SNPJam Report  |
| Enzyme 100 General References |
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
|
| Enzyme 100 Metabolite References |
Not Available |
|
Enzyme 101
[top]
|
| Enzyme 101 ID |
14740 |
| Enzyme 101 Name |
Glutamate decarboxylase 1 (Brain, 67kDa) |
| Enzyme 101 Synonyms |
Not Available |
| Enzyme 101 Gene Name |
GAD1 |
| Enzyme 101 Protein Sequence |
>Glutamate decarboxylase 1 (Brain, 67kDa)
MASSTPSSSATSSNAGADPNTTNLRPTTYDTWCGVAHGCTRKLGLKICGFLQRTNSLEEK
SRLVSAFKERQSSKNLLSCENSDRDARFRRTETDFSNLFARDLLPAKNGEEQTVQFLLEV
VDILLNYVRKTFDRSTKVLDFHHPHQLLEGMEGFNLELSDHPESLEQILVDCRDTLKYGV
RTGHPRFFNQLSTGLDIIGLAGEWLTSTANTNMFTYEIAPVFVLMEQITLKKMREIVGWS
SKDGDGIFSPGGAISNMYSIMAARYKYFPEVKTKGMAAVPKLVLFTSEQSRYSIKKAGAA
LGFGTDNVILIKCNERGEIIPADFEAKILEAKQKGYVPFYVNATAGTTVYGAFDPIQEIA
DICEKYNLWLHVDAAWGGGLLMSRKHRHKLNGIERANSVTWNPHKMMGVLLQCSAILVKE
KGILQGCNQMCAGYLFQPDKQYDVSYDTGDKAIQCGRHVDIFKFWLMWKAKGTVGFENQI
NKCLELAEYLYAKIKNREEFEMVFNGEPEHTNVCFWYIPQSLRGVPDSPQRREKLHKVAP
KIKALMMESGTTMVGYQPQGDKANFFRMVISNPAATQSDIDFLIEEIERLGQDL
|
| Enzyme 101 Number of Residues |
594 |
| Enzyme 101 Molecular Weight |
66916.0 |
| Enzyme 101 Theoretical pI |
7.48 |
| Enzyme 101 GO Classification |
| Function |
- binding
- carbon-carbon lyase activity
- carboxy-lyase activity
- catalytic activity
- cofactor binding
- lyase activity
- pyridoxal phosphate binding
|
| Process |
- carboxylic acid metabolic process
- cellular metabolic process
- metabolic process
- organic acid metabolic process
- oxoacid metabolic process
|
| Component |
| — |
|
| Enzyme 101 General Function |
Involved in carboxy-lyase activity |
| Enzyme 101 Specific Function |
Not Available |
| Enzyme 101 Pathways |
Not Available |
| Enzyme 101 Reactions |
Not Available |
| Enzyme 101 Pfam Domain Function |
|
| Enzyme 101 Signals |
|
| Enzyme 101 Transmembrane Regions |
|
| Enzyme 101 Essentiality |
Not Available |
| Enzyme 101 GenBank ID Protein |
23138819  |
| Enzyme 101 UniProtKB/Swiss-Prot ID |
Q8IVA8  |
| Enzyme 101 UniProtKB/Swiss-Prot Entry Name |
Q8IVA8_HUMAN  |
| Enzyme 101 PDB ID |
Not Available |
| Enzyme 101 Cellular Location |
Not Available |
| Enzyme 101 Gene Sequence |
>1785 bp
ATGGCGTCTTCGACCCCATCTTCGTCCGCAACCTCCTCGAACGCGGGAGCGGACCCCAAT
ACCACTAACCTGCGCCCCACAACGTACGATACCTGGTGCGGCGTGGCCCATGGATGCACC
AGAAAACTGGGGCTCAAGATCTGCGGCTTCTTGCAAAGGACCAACAGCCTGGAAGAGAAG
AGTCGCCTTGTGAGTGCCTTCAAGGAGAGGCAATCCTCCAAGAACCTGCTTTCCTGTGAA
AACAGCGACCGGGATGCCCGCTTCCGGCGCACAGAGACTGACTTCTCTAATCTGTTTGCT
AGAGATCTGCTTCCGGCTAAGAACGGTGAGGAGCAAACCGTGCAATTCCTCCTGGAAGTG
GTGGACATACTCCTCAACTATGTCCGCAAGACATTTGATCGCTCCACCAAGGTGCTGGAC
TTTCATCACCCACACCAGTTGCTGGAAGGCATGGAGGGCTTCAACTTGGAGCTCTCTGAC
CACCCCGAGTCCCTGGAGCAGATCCTGGTTGACTGCAGAGACACCTTGAAGTATGGGGTT
CGCACAGGTCATCCTCGATTTTTCAACCAGCTCTCCACTGGATTGGATATTATTGGCCTA
GCTGGAGAATGGCTGACATCAACGGCCAATACCAACATGTTTACATATGAAATTGCACCA
GTGTTTGTCCTCATGGAACAAATAACACTTAAGAAGATGAGAGAGATAGTTGGATGGTCA
AGTAAAGATGGTGATGGGATATTTTCTCCTGGGGGCGCCATATCCAACATGTACAGCATC
ATGGCTGCTCGCTACAAGTACTTCCCGGAAGTTAAGACAAAGGGCATGGCGGCTGTGCCT
AAACTGGTCCTCTTCACCTCAGAACAGAGTCGCTATTCCATAAAGAAAGCTGGGGCTGCA
CTTGGCTTTGGAACTGACAATGTGATTTTGATAAAGTGCAATGAAAGGGGGGAAATAATT
CCAGCTGATTTTGAGGCAAAAATTCTTGAAGCCAAACAGAAGGGATATGTTCCCTTTTAT
GTCAATGCAACTGCTGGCACGACTGTTTATGGAGCTTTTGATCCGATACAAGAGATTGCA
GATATATGTGAGAAATATAACCTTTGGTTGCATGTCGATGCTGCCTGGGGAGGTGGGCTG
CTCATGTCCAGGAAGCACCGCCATAAACTCAACGGCATAGAAAGGGCCAACTCAGTCACC
TGGAACCCTCACAAGATGATGGGCGTGCTGTTGCAGTGCTCTGCCATTCTCGTCAAGGAA
AAGGGTATACTCCAAGGATGCAACCAGATGTGTGCAGGATACCTCTTCCAGCCAGACAAG
CAGTATGATGTCTCCTACGACACCGGGGACAAGGCAATTCAGTGTGGCCGCCACGTGGAT
ATCTTCAAGTTCTGGCTGATGTGGAAAGCAAAGGGCACAGTGGGATTTGAAAACCAGATC
AACAAATGCCTGGAACTGGCTGAATACCTCTATGCCAAGATTAAAAACAGAGAAGAATTT
GAGATGGTTTTCAATGGCGAGCCTGAGCACACAAACGTCTGTTTTTGGTATATTCCACAA
AGCCTCAGGGGTGTGCCAGACAGCCCTCAACGACGGGAAAAGCTACACAAGGTGGCTCCA
AAAATCAAAGCCCTGATGATGGAGTCAGGTACGACCATGGTTGGCTACCAGCCCCAAGGG
GACAAGGCCAACTTCTTCCGGATGGTCATCTCCAACCCAGCCGCTACCCAGTCTGACATT
GACTTCCTCATTGAGGAGATAGAAAGACTGGGCCAGGATCTGTAA
|
| Enzyme 101 GenBank Gene ID |
BC037780  |
| Enzyme 101 GeneCard ID |
GAD1  |
| Enzyme 101 GenAtlas ID |
GAD1  |
| Enzyme 101 HGNC ID |
HGNC:4092  |
| Enzyme 101 Chromosome Location |
2 |
| Enzyme 101 Locus |
2q31 |
| Enzyme 101 SNPs |
SNPJam Report  |
| Enzyme 101 General References |
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
|
| Enzyme 101 Metabolite References |
Not Available |
|
Enzyme 102
[top]
|
| Enzyme 102 ID |
14741 |
| Enzyme 102 Name |
Serine hydroxymethyltransferase |
| Enzyme 102 Synonyms |
Not Available |
| Enzyme 102 Gene Name |
SHMT2 |
| Enzyme 102 Protein Sequence |
>Serine hydroxymethyltransferase
MLYFSLFWAARPLQRCGQLVRMAIRAQHSNAAQTQTGEANRGWTGQESLSDSDPEMWELL
QREKDRQCRGLELIASENFCSRAALEALGSCLNNKYSEGYPGKRYYGGAEVVDEIELLCQ
RRALEAFDLDPAQWGVNVQPYSGSPANLAVYTALLQPHDRIMGLDLPDGGHLTHGYMSDV
KRISATSIFFESMPYKLNLALTARLFRPRLIIAGTSAYARLIDYARMREVCDEVKAHLLA
DMAHISGLVAAKVIPSPFKHADIVTTTTHKTLRGARSGLIFYRKGVKAVDPKTGREIPYT
FEDRINFAVFPSLQGGPHNHAIAAVAVALKQACTPMFREYSLQVLKNARAMADALLERGY
SLVSGGTDNHLVLVDLRPKGLDGARAERVLELVSITANKNTCPGDRSAITPGGLRLGAPA
LTSRQFREDDFRRVVDFIDEGVNIGLEVKSKTAKLQDFKSFLLKDSETSQRLANLRQRVE
QFARAFPMPGFDEH
|
| Enzyme 102 Number of Residues |
494 |
| Enzyme 102 Molecular Weight |
54862.1 |
| Enzyme 102 Theoretical pI |
8.68 |
| Enzyme 102 GO Classification |
| Function |
- binding
- catalytic activity
- cofactor binding
- glycine hydroxymethyltransferase activity
- methyltransferase activity
- pyridoxal phosphate binding
- transferase activity
- transferase activity, transferring one-carbon groups
|
| Process |
- L-serine metabolic process
- cellular amino acid and derivative metabolic process
- cellular amino acid metabolic process
- cellular metabolic process
- glycine metabolic process
- metabolic process
- serine family amino acid metabolic process
|
| Component |
| — |
|
| Enzyme 102 General Function |
Involved in catalytic activity |
| Enzyme 102 Specific Function |
Interconversion of serine and glycine |
| Enzyme 102 Pathways |
|
| Enzyme 102 Reactions |
- 5,10-methylenetetrahydrofolate + glycine + H2O = tetrahydrofolate + L-serine [RN:R00945]
|
| Enzyme 102 Pfam Domain Function |
|
| Enzyme 102 Signals |
|
| Enzyme 102 Transmembrane Regions |
|
| Enzyme 102 Essentiality |
Not Available |
| Enzyme 102 GenBank ID Protein |
21619733  |
| Enzyme 102 UniProtKB/Swiss-Prot ID |
Q8N1A5  |
| Enzyme 102 UniProtKB/Swiss-Prot Entry Name |
Q8N1A5_HUMAN  |
| Enzyme 102 PDB ID |
Not Available |
| Enzyme 102 Cellular Location |
Not Available |
| Enzyme 102 Gene Sequence |
>1485 bp
ATGCTGTACTTCTCTTTGTTTTGGGCGGCTCGGCCTCTGCAGAGATGTGGGCAGCTGGTC
AGGATGGCCATTCGGGCTCAGCACAGCAACGCAGCCCAGACTCAGACTGGGGAAGCAAAC
AGGGGCTGGACAGGCCAGGAGAGCCTGTCGGACAGTGATCCTGAGATGTGGGAGTTGCTG
CAGAGGGAGAAGGACAGGCAGTGTCGTGGCCTGGAGCTCATTGCCTCAGAGAACTTCTGC
AGCCGAGCTGCGCTGGAGGCCCTGGGGTCCTGTCTGAACAACAAGTACTCGGAGGGTTAT
CCTGGCAAGAGATACTATGGGGGAGCAGAGGTGGTGGATGAAATTGAGCTGCTGTGCCAG
CGCCGGGCCTTGGAAGCCTTTGACCTGGATCCTGCACAGTGGGGAGTCAATGTCCAGCCC
TACTCCGGGTCCCCAGCCAACCTGGCCGTCTACACAGCCCTTCTGCAACCTCACGACCGG
ATCATGGGGCTGGACCTGCCCGATGGGGGCCATCTCACCCACGGCTACATGTCTGACGTC
AAGCGGATATCAGCCACGTCCATCTTCTTCGAGTCTATGCCCTATAAGCTCAACCTGGCA
CTGACTGCTCGACTTTTCCGGCCACGGCTCATCATAGCTGGCACCAGCGCCTATGCTCGC
CTCATTGACTACGCCCGCATGAGAGAGGTGTGTGATGAAGTCAAAGCACACCTGCTGGCA
GACATGGCCCACATCAGTGGCCTGGTGGCTGCCAAGGTGATTCCCTCGCCTTTCAAGCAC
GCGGACATCGTCACCACCACTACTCACAAGACTCTTCGAGGGGCCAGGTCAGGGCTCATC
TTCTACCGGAAAGGGGTGAAGGCTGTGGACCCCAAGACTGGCCGGGAGATCCCTTACACA
TTTGAGGACCGAATCAACTTTGCCGTGTTCCCATCCCTGCAGGGGGGCCCCCACAATCAT
GCCATTGCTGCAGTAGCTGTGGCCCTAAAGCAGGCCTGCACCCCCATGTTCCGGGAGTAC
TCCCTGCAGGTTCTGAAGAATGCTCGGGCCATGGCAGATGCCCTGCTAGAGCGAGGCTAC
TCACTGGTATCAGGTGGTACTGACAACCACCTGGTGCTGGTGGACCTGCGGCCCAAGGGC
CTGGATGGAGCTCGGGCTGAGCGGGTGCTAGAGCTTGTATCCATCACTGCCAACAAGAAC
ACCTGTCCTGGAGACCGAAGTGCCATCACACCGGGCGGCCTGCGGCTTGGGGCCCCAGCC
TTAACTTCTCGACAGTTCCGTGAGGATGACTTCCGGAGAGTTGTGGACTTTATAGATGAA
GGGGTCAACATTGGCTTAGAGGTGAAGAGCAAGACTGCCAAGCTCCAGGATTTCAAATCC
TTCCTGCTTAAGGACTCAGAAACAAGTCAGCGTCTGGCCAACCTCAGGCAACGGGTGGAG
CAGTTTGCCAGGGCCTTCCCCATGCCTGGTTTTGATGAGCATTGA
|
| Enzyme 102 GenBank Gene ID |
BC032584  |
| Enzyme 102 GeneCard ID |
SHMT2  |
| Enzyme 102 GenAtlas ID |
SHMT2  |
| Enzyme 102 HGNC ID |
HGNC:10852  |
| Enzyme 102 Chromosome Location |
1 |
| Enzyme 102 Locus |
12q12-q14 |
| Enzyme 102 SNPs |
SNPJam Report  |
| Enzyme 102 General References |
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
|
| Enzyme 102 Metabolite References |
Not Available |
|
Enzyme 103
[top]
|
| Enzyme 103 ID |
14742 |
| Enzyme 103 Name |
Aminolevulinate, delta-, synthase 2 |
| Enzyme 103 Synonyms |
Not Available |
| Enzyme 103 Gene Name |
ALAS2 |
| Enzyme 103 Protein Sequence |
>Aminolevulinate, delta-, synthase 2
MRGGEVALGWNKKKRLFCEDFRFKMVTAAMLLQCCPVLARGPTSLLGKVVKTHQFLFGIG
RCPILATQGPNCSQIHLKATKAGGDSPSWAKGHCPFMLSELQDGKSKIVQKAAPEVQEDV
KAFKTGNYVFSYDQFFRDKIMEKKQDHTYRVFKTVNRWADAYPFAQHFSEASVASKDVSV
WCSNDYLGMSRHPQVLQATQETLQRHGVGAGGTRNISGTSKFHVELEQELAELHQKDSAL
LFSSCFVANDSTLFTLAKILPGCEIYSDAGNHASMIQGIRNSGAAKFVFRHNDPDHLKKL
LEKSNPKIPKIVAFETVHSMDGAICPLEELCDVSHQYGALTFVDEVHAVGLYGSRGAGIG
ERDGIMHKIDIISGTLGKAFGCVGGYIASTRDLVDMVRSYAAGFIFTTSLPPMVLSGALE
SVRLLKGEEGQALRRAHQRNVKHMRQLLMDRGLPVIPCPSHIIPIRVGNAALNSKLCDLL
LSKHGIYVQAINYPTVPRGEELLRLAPSPHHSPQMMEDFVEKLLLAWTAVGLPLQDVSVA
ACNFCRRPVHFELMSEWERSYFGNMGPQYVTTYA
|
| Enzyme 103 Number of Residues |
574 |
| Enzyme 103 Molecular Weight |
63514.8 |
| Enzyme 103 Theoretical pI |
8.52 |
| Enzyme 103 GO Classification |
| Function |
- 5-aminolevulinate synthase activity
- N-acyltransferase activity
- N-succinyltransferase activity
- acyltransferase activity
- binding
- catalytic activity
- cofactor binding
- pyridoxal phosphate binding
- transferase activity
- transferase activity, transferring acyl groups
- transferase activity, transferring acyl groups other than amino-acyl groups
- transferase activity, transferring nitrogenous groups
|
| Process |
- biosynthetic process
- cellular biosynthetic process
- heterocycle biosynthetic process
- metabolic process
- nitrogen compound metabolic process
- porphyrin metabolic process
- tetrapyrrole biosynthetic process
- tetrapyrrole metabolic process
|
| Component |
- cell part
- cytoplasmic part
- intracellular part
- mitochondrial matrix
- mitochondrial part
|
|
| Enzyme 103 General Function |
Involved in 5-aminolevulinate synthase activity |
| Enzyme 103 Specific Function |
Not Available |
| Enzyme 103 Pathways |
Not Available |
| Enzyme 103 Reactions |
Not Available |
| Enzyme 103 Pfam Domain Function |
|
| Enzyme 103 Signals |
|
| Enzyme 103 Transmembrane Regions |
|
| Enzyme 103 Essentiality |
Not Available |
| Enzyme 103 GenBank ID Protein |
112180419  |
| Enzyme 103 UniProtKB/Swiss-Prot ID |
Q8N6H3  |
| Enzyme 103 UniProtKB/Swiss-Prot Entry Name |
Q8N6H3_HUMAN  |
| Enzyme 103 PDB ID |
Not Available |
| Enzyme 103 Cellular Location |
Not Available |
| Enzyme 103 Gene Sequence |
>1725 bp
ATGAGAGGGGGAGAGGTTGCTCTGGGATGGAACAAGAAAAAGAGGTTGTTTTGTGAGGAC
TTTAGGTTCAAGATGGTGACTGCAGCCATGCTGCTACAGTGCTGCCCAGTGCTTGCCCGG
GGCCCCACAAGCCTCCTAGGCAAGGTGGTTAAGACTCACCAGTTCCTGTTTGGTATTGGA
CGCTGTCCCATCCTGGCTACCCAAGGACCAAACTGTTCTCAAATCCACCTTAAGGCAACA
AAGGCTGGAGGAGATTCTCCATCTTGGGCGAAGGGCCACTGTCCCTTCATGCTGTCGGAA
CTCCAGGATGGGAAGAGCAAGATTGTGCAGAAGGCAGCCCCAGAAGTCCAGGAAGATGTG
AAGGCTTTCAAGACAGGAAACTATGTCTTCAGTTATGACCAGTTTTTCAGGGACAAGATC
ATGGAGAAGAAACAGGATCACACCTACCGTGTGTTCAAGACTGTGAACCGCTGGGCTGAT
GCATATCCCTTTGCCCAACATTTCTCTGAGGCATCTGTGGCCTCAAAGGATGTGTCCGTC
TGGTGTAGTAATGATTACCTGGGCATGAGCCGACACCCTCAGGTCTTGCAAGCCACACAG
GAGACCCTGCAGCGTCATGGTGTTGGAGCTGGTGGCACCCGCAACATCTCAGGCACCAGT
AAGTTTCATGTGGAGCTTGAGCAGGAGCTGGCTGAGCTGCACCAGAAGGACTCAGCCCTG
CTCTTCTCCTCCTGCTTTGTTGCCAATGACTCTACTCTCTTCACCTTGGCCAAGATCCTG
CCAGGGTGCGAGATTTACTCAGACGCAGGCAACCATGCTTCCATGATCCAAGGTATCCGT
AACAGTGGAGCAGCCAAGTTTGTCTTCAGGCACAATGACCCTGACCACCTAAAGAAACTT
CTAGAGAAGTCTAACCCTAAGATACCCAAAATTGTGGCCTTTGAGACTGTCCACTCCATG
GATGGTGCCATCTGTCCCCTCGAGGAGTTGTGTGATGTGTCCCACCAGTATGGGGCCCTG
ACCTTCGTGGATGAGGTCCATGCTGTAGGACTGTATGGGTCCCGGGGCGCTGGGATTGGG
GAGCGTGATGGAATTATGCATAAGATTGACATCATCTCTGGAACTCTTGGCAAGGCCTTT
GGCTGTGTGGGCGGCTACATTGCCAGCACCCGTGACTTGGTGGACATGGTGCGCTCCTAT
GCTGCAGGCTTCATCTTTACCACTTCTCTGCCCCCCATGGTGCTCTCTGGAGCTCTAGAA
TCTGTGCGGCTGCTCAAGGGAGAGGAGGGCCAAGCCCTGAGGCGAGCCCACCAGCGCAAT
GTCAAGCACATGCGCCAGCTACTCATGGACAGGGGCCTTCCTGTCATCCCCTGCCCCAGC
CACATCATCCCCATCCGGGTGGGCAATGCAGCACTCAACAGCAAGCTCTGTGATCTCCTG
CTCTCCAAGCATGGCATCTATGTGCAGGCCATCAACTACCCAACTGTCCCCCGGGGTGAA
GAGCTCCTGCGCTTGGCACCCTCCCCCCACCACAGCCCTCAGATGATGGAAGATTTTGTG
GAGAAGCTGCTGCTGGCTTGGACTGCGGTGGGGCTGCCCCTCCAGGATGTGTCTGTGGCT
GCCTGCAATTTCTGTCGCCGTCCTGTACACTTTGAGCTCATGAGTGAGTGGGAACGTTCC
TACTTCGGGAACATGGGGCCCCAGTATGTCACCACCTATGCCTGA
|
| Enzyme 103 GenBank Gene ID |
BC030230  |
| Enzyme 103 GeneCard ID |
ALAS2  |
| Enzyme 103 GenAtlas ID |
ALAS2  |
| Enzyme 103 HGNC ID |
HGNC:397  |
| Enzyme 103 Chromosome Location |
Not Available |
| Enzyme 103 Locus |
Not Available |
| Enzyme 103 SNPs |
SNPJam Report  |
| Enzyme 103 General References |
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
|
| Enzyme 103 Metabolite References |
Not Available |
|
Enzyme 104
[top]
|
| Enzyme 104 ID |
14743 |
| Enzyme 104 Name |
Phosphorylase |
| Enzyme 104 Synonyms |
Not Available |
| Enzyme 104 Gene Name |
Not Available |
| Enzyme 104 Protein Sequence |
>Phosphorylase
KVIFLENYRVSLAEKVIPAADLSQQISTAGTEASGTGNMKFMLNGALTIGTMDGANVEMA
EEAGAENLFIFGLRVEDVEALDRKGYNAREYYDHLPELKQAVDQISSGFFSPKEPDCFKD
IVNMLMHHDRFKVFADYEAYMQCQAQVDQLYRNPKEWTKKVIRNIACSGKFSSDRTITEY
AREIWGVEPSDLQIPPPNIPRD
|
| Enzyme 104 Number of Residues |
202 |
| Enzyme 104 Molecular Weight |
22840.6 |
| Enzyme 104 Theoretical pI |
4.64 |
| Enzyme 104 GO Classification |
| Function |
- catalytic activity
- phosphorylase activity
- transferase activity
- transferase activity, transferring glycosyl groups
- transferase activity, transferring hexosyl groups
|
| Process |
- carbohydrate metabolic process
- metabolic process
- primary metabolic process
|
| Component |
| — |
|
| Enzyme 104 General Function |
Involved in phosphorylase activity |
| Enzyme 104 Specific Function |
Phosphorylase is an important allosteric enzyme in carbohydrate metabolism. Enzymes from different sources differ in their regulatory mechanisms and in their natural substrates. However, all known phosphorylases share catalytic and structural properties |
| Enzyme 104 Pathways |
|
| Enzyme 104 Reactions |
- [(1->4)-alpha-D-glucosyl]n + phosphate = [(1->4)-alpha-D-glucosyl]n-1 + alpha-D-glucose 1-phosphate [RN:R01821 R06050]
|
| Enzyme 104 Pfam Domain Function |
|
| Enzyme 104 Signals |
|
| Enzyme 104 Transmembrane Regions |
|
| Enzyme 104 Essentiality |
Not Available |
| Enzyme 104 GenBank ID Protein |
19851938  |
| Enzyme 104 UniProtKB/Swiss-Prot ID |
Q8TDG6  |
| Enzyme 104 UniProtKB/Swiss-Prot Entry Name |
Q8TDG6_HUMAN  |
| Enzyme 104 PDB ID |
Not Available |
| Enzyme 104 Cellular Location |
Not Available |
| Enzyme 104 Gene Sequence |
>609 bp
AAAGTGATCTTCCTGGAGAACTACCGTGTGTCCTTGGCTGAGAAAGTGATCCCGGCCGCT
GATCTGTCGCAGCAGATCTCCACTGCAGGCACCGAGGCCTCAGGCACAGGCAACATGAAG
TTCATGCTCAACGGGGCCCTCACCATCGGCACCATGGACGGCGCCAACGTGGAGATGGCC
GAGGAGGCCGGGGCCGAGAACCTCTTCATCTTCGGCCTGCGGGTGGAGGATGTCGAGGCC
TTGGACCGGAAAGGGTACAATGCCAGGGAGTACTACGACCACCTGCCCGAGCTGAAGCAG
GCCGTGGACCAGATCAGCAGTGGCTTTTTTTCTCCCAAGGAGCCAGACTGCTTCAAGGAC
ATCGTGAACATGCTGATGCACCATGACAGGTTCAAGGTGTTTGCAGACTATGAAGCCTAC
ATGCAGTGCCAGGCACAGGTGGACCAGCTGTACCGGAACCCCAAGGAGTGGACCAAGAAG
GTCATCAGGAACATCGCCTGCTCGGGCAAGTTCTCCAGTGACCGGACCATCACGGAGTAT
GCACGGGAGATCTGGGGTGTGGAGCCCTCCGACCTGCAGATCCCGCCCCCCAACATCCCC
CGGGACTAG
|
| Enzyme 104 GenBank Gene ID |
AF432222  |
| Enzyme 104 GeneCard ID |
Not Available |
| Enzyme 104 GenAtlas ID |
Not Available |
| Enzyme 104 HGNC ID |
HGNC:9723  |
| Enzyme 104 Chromosome Location |
Not Available |
| Enzyme 104 Locus |
Not Available |
| Enzyme 104 SNPs |
Not Available |
| Enzyme 104 General References |
Not Available |
| Enzyme 104 Metabolite References |
Not Available |
|
Enzyme 105
[top]
|
| Enzyme 105 ID |
14744 |
| Enzyme 105 Name |
Serine hydroxymethyltransferase |
| Enzyme 105 Synonyms |
Not Available |
| Enzyme 105 Gene Name |
SHMT1 |
| Enzyme 105 Protein Sequence |
>Serine hydroxymethyltransferase
MTMPVNGAHKDADLWSSHDKMLAQPLKDSDVEVYNIIKKESNRQRVGLELIASENFASRA
VLEALGSCLNNKYSEGYPGQRYYGGTEFIDELETLCQKRALQAYKLDPQCWGVNVQPYSG
SPANFAVYTALVEPHGRIMGLDLPDGGHLTHGFMTDKKKISATSIFFESMPYKVNPDTGY
INYDQLEENARLFHPKLIIAGTSCYSRNLEYARLRKIADENGAYLMADMAHISGLVAAGV
VPSPFEHCHVVTTTTHKTLRGCRAGMIFYRKGVKSVDPKTGKEILYNLESLINSAVFPGL
QGGPHNHAIAGVAVALKQAMTLEFKVYQHQVVANCRALSEALTELGYKIVTGGSDNHLIL
VDLRSKGTDGGRAEKVLEACSIACNKNTCPGDRSALRPSGLRLGTPALTSRGLLEKDFQK
VAHFIHRGIELTLQIQSDTGVRATLKEFKERLAGDKYQAAVQALREEVESFASFFPLPGL
PDF
|
| Enzyme 105 Number of Residues |
483 |
| Enzyme 105 Molecular Weight |
53117 |
| Enzyme 105 Theoretical pI |
7.77 |
| Enzyme 105 GO Classification |
| Function |
- catalytic activity
- glycine hydroxymethyltransferase activity
- methyltransferase activity
- transferase activity
- transferase activity, transferring one-carbon groups
|
| Process |
- L-serine metabolism
- amino acid and derivative metabolism
- amino acid metabolism
- cellular metabolism
- glycine metabolism
- metabolism
- physiological process
- serine family amino acid metabolism
|
| Component |
| — |
|
| Enzyme 105 General Function |
Amino acid transport and metabolism |
| Enzyme 105 Specific Function |
Interconversion of serine and glycine |
| Enzyme 105 Pathways |
|
| Enzyme 105 Reactions |
- 5,10-methylenetetrahydrofolate + glycine + H2O = tetrahydrofolate + L-serine [RN:R00945] ALL_REAC R00945
- (other) R03284
|
| Enzyme 105 Pfam Domain Function |
|
| Enzyme 105 Signals |
|
| Enzyme 105 Transmembrane Regions |
|
| Enzyme 105 Essentiality |
Not Available |
| Enzyme 105 GenBank ID Protein |
14124914  |
| Enzyme 105 UniProtKB/Swiss-Prot ID |
Q96HY0  |
| Enzyme 105 UniProtKB/Swiss-Prot Entry Name |
Q96HY0_HUMAN  |
| Enzyme 105 PDB ID |
1BJ4  |
| Enzyme 105 PDB File |
Show |
| Enzyme 105 3D Structure |
|
| Enzyme 105 Cellular Location |
Not Available |
| Enzyme 105 Gene Sequence |
>1452 bp
ATGACGATGCCAGTCAACGGGGCCCACAAGGATGCTGACCTGTGGTCCTCACATGACAAG
ATGCTGGCACAACCCCTCAAAGACAGTGATGTTGAGGTTTACAACATCATTAAGAAGGAG
AGTAACCGGCAGAGGGTTGGATTGGAGCTGATTGCCTCGGAGAATTTCGCCAGCCGAGCA
GTTTTGGAGGCCCTAGGCTCTTGCTTAAATAACAAATACTCTGAGGGGTACCCGGGCCAG
AGATACTATGGCGGGACTGAGTTTATTGATGAACTGGAGACCCTCTGTCAGAAGCGAGCC
CTGCAGGCCTATAAGCTGGACCCACAGTGCTGGGGGGTCAACGTCCAGCCCTACTCAGGC
TCCCCTGCAAACTTTGCTGTGTACACTGCCCTGGTGGAACCCCATGGGCGCATCATGGGC
CTGGACCTTCCGGATGGGGGCCACCTGACCCATGGGTTCATGACAGACAAGAAGAAAATC
TCTGCCACGTCCATCTTCTTTGAATCTATGCCCTACAAGGTGAACCCAGATACTGGCTAC
ATCAACTATGACCAGCTGGAGGAGAACGCACGCCTCTTCCACCCGAAGCTGATCATCGCA
GGAACCAGCTGCTACTCCCGAAACCTGGAATATGCCCGGCTACGGAAGATTGCAGATGAG
AACGGGGCGTATCTCATGGCGGACATGGCTCACATCAGCGGGCTGGTGGCGGCTGGCGTG
GTGCCCTCCCCATTTGAACACTGCCATGTGGTGACCACCACCACTCACAAGACCCTGCGA
GGCTGCCGAGCTGGCATGATCTTCTACAGGAAAGGAGTGAAAAGTGTGGATCCCAAGACT
GGCAAAGAGATTCTGTACAACCTGGAGTCTCTTATCAATTCTGCTGTGTTCCCTGGCCTG
CAGGGAGGTCCCCACAACCACGCCATTGCTGGGGTTGCTGTGGCACTGAAGCAAGCTATG
ACTCTGGAATTTAAAGTTTATCAACACCAGGTGGTGGCCAACTGCAGGGCTCTGTCTGAG
GCCCTGACGGAGCTGGGCTACAAAATAGTCACAGGTGGTTCTGACAACCATTTGATCCTT
GTGGATCTCCGTTCCAAAGGCACAGATGGTGGAAGGGCTGAGAAGGTGCTAGAAGCCTGT
TCTATTGCCTGCAACAAGAACACCTGTCCAGGTGACAGAAGCGCTCTGCGGCCCAGTGGA
CTGCGGCTGGGGACCCCAGCACTGACGTCCCGTGGACTTTTGGAAAAAGACTTCCAAAAA
GTAGCCCACTTTATTCACAGAGGGATAGAGCTGACCCTGCAGATCCAGAGCGACACTGGT
GTCAGAGCCACCCTGAAAGAGTTCAAGGAGAGACTGGCAGGGGATAAGTACCAGGCGGCC
GTGCAGGCTCTCCGGGAGGAGGTTGAGAGCTTCGCCTCTTTCTTCCCTCTGCCTGGCCTG
CCTGACTTCTAA
|
| Enzyme 105 GenBank Gene ID |
BC007979  |
| Enzyme 105 GeneCard ID |
Q96HY0  |
| Enzyme 105 GenAtlas ID |
SHMT1  |
| Enzyme 105 HGNC ID |
HGNC:10850  |
| Enzyme 105 Chromosome Location |
17 |
| Enzyme 105 Locus |
17p11.2 |
| Enzyme 105 SNPs |
SNPJam Report  |
| Enzyme 105 General References |
- Strausberg RL, Feingold EA, Grouse LH, Derge JG, Klausner RD, Collins FS, Wagner L, Shenmen CM, Schuler GD, Altschul SF, Zeeberg B, Buetow KH, Schaefer CF, Bhat NK, Hopkins RF, Jordan H, Moore T, Max SI, Wang J, Hsieh F, Diatchenko L, Marusina K, Farmer AA, Rubin GM, Hong L, Stapleton M, Soares MB, Bonaldo MF, Casavant TL, Scheetz TE, Brownstein MJ, Usdin TB, Toshiyuki S, Carninci P, Prange C, Raha SS, Loquellano NA, Peters GJ, Abramson RD, Mullahy SJ, Bosak SA, McEwan PJ, McKernan KJ, Malek JA, Gunaratne PH, Richards S, Worley KC, Hale S, Garcia AM, Gay LJ, Hulyk SW, Villalon DK, Muzny DM, Sodergren EJ, Lu X, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madan A, Young AC, Shevchenko Y, Bouffard GG, Blakesley RW, Touchman JW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Krzywinski MI, Skalska U, Smailus DE, Schnerch A, Schein JE, Jones SJ, Marra MA: Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. Proc Natl Acad Sci U S A. 2002 Dec 24;99(26):16899-903. Epub 2002 Dec 11. [PubMed
]
|
| Enzyme 105 Metabolite References |
Not Available |
|
Enzyme 106
[top]
|
| Enzyme 106 ID |
14745 |
| Enzyme 106 Name |
P-selectin cytoplasmic tail-associated protein (PCAP) |
| Enzyme 106 Synonyms |
Not Available |
| Enzyme 106 Gene Name |
pcap |
| Enzyme 106 Protein Sequence |
>P-selectin cytoplasmic tail-associated protein (PCAP)
MGAVPFLVSATSGTTVLGAFDPLEAIADVCQRHGLWLHVDAAWGGSVLLSQTHRHLLDGI
QRADSVAWNPHKLLAAGLQCSALLLQDTSNLLKRCHGSQASYLFQQDKFYDVALDTGDKV
VQCGRRVDCLKLWLMWKAQGDQGLERRIDQAFVLARYLVEEMKKREGFELVMEPEFVNVC
FWFVPPSLRGKQESPDYHERLSKVAPVLKERMVKEGSMMIGYQPHGTRGNFFRVVVANSA
LTCADMDFLLNELERLGQDL
|
| Enzyme 106 Number of Residues |
260 |
| Enzyme 106 Molecular Weight |
29222.5 |
| Enzyme 106 Theoretical pI |
6.71 |
| Enzyme 106 GO Classification |
| Function |
- binding
- carbon-carbon lyase activity
- carboxy-lyase activity
- catalytic activity
- cofactor binding
- lyase activity
- pyridoxal phosphate binding
|
| Process |
- carboxylic acid metabolic process
- cellular metabolic process
- metabolic process
- organic acid metabolic process
- oxoacid metabolic process
|
| Component |
| — |
|
| Enzyme 106 General Function |
Involved in carboxy-lyase activity |
| Enzyme 106 Specific Function |
Not Available |
| Enzyme 106 Pathways |
Not Available |
| Enzyme 106 Reactions |
Not Available |
| Enzyme 106 Pfam Domain Function |
|
| Enzyme 106 Signals |
|
| Enzyme 106 Transmembrane Regions |
|
| Enzyme 106 Essentiality |
Not Available |
| Enzyme 106 GenBank ID Protein |
14495153  |
| Enzyme 106 UniProtKB/Swiss-Prot ID |
Q96JQ3  |
| Enzyme 106 UniProtKB/Swiss-Prot Entry Name |
Q96JQ3_HUMAN  |
| Enzyme 106 PDB ID |
Not Available |
| Enzyme 106 Cellular Location |
Not Available |
| Enzyme 106 Gene Sequence |
>783 bp
ATGGGTGCTGTGCCGTTCCTGGTCAGTGCCACCTCTGGCACCACTGTGCTAGGGGCCTTT
GACCCCCTGGAGGCAATTGCTGATGTGTGCCAGCGTCATGGGCTATGGCTGCATGTGGAT
GCTGCCTGGGGTGGGAGCGTCCTGCTGTCACAGACACACAGGCATCTCCTGGATGGGATC
CAGAGGGCTGACTCTGTGGCCTGGAATCCCCACAAGCTCCTCGCAGCAGGCCTGCAATGC
TCTGCACTTCTTCTCCAGGATACCTCGAACCTGCTCAAGCGCTGCCATGGGTCCCAGGCC
AGCTACCTTTTCCAGCAGGACAAGTTCTACGATGTGGCTCTGGACACGGGAGACAAGGTG
GTGCAGTGTGGCCGCCGTGTGGACTGTCTGAAGCTGTGGCTCATGTGGAAGGCACAGGGC
GATCAAGGGCTGGAGCGGCGCATCGACCAGGCCTTTGTCCTTGCCCGGTACCTGGTGGAG
GAAATGAAGAAGCGGGAAGGGTTTGAGCTAGTCATGGAGCCTGAGTTTGTCAATGTGTGT
TTCTGGTTCGTACCCCCCAGCCTGCGAGGGAAGCAGGAGAGTCCAGATTACCACGAAAGG
CTGTCAAAGGTGGCCCCCGTGCTCAAGGAGCGCATGGTGAAGGAGGGCTCCATGATGATT
GGCTACCAGCCCCACGGGACCCGGGGCAACTTCTTCCGTGTGGTTGTGGCCAACTCTGCA
CTGACCTGTGCTGATATGGACTTCCTCCTCAACGAGCTGGAGCGGCTAGGCCAGGACCTG
TGA
|
| Enzyme 106 GenBank Gene ID |
AB044561  |
| Enzyme 106 GeneCard ID |
pcap  |
| Enzyme 106 GenAtlas ID |
pcap  |
| Enzyme 106 HGNC ID |
HGNC:18966  |
| Enzyme 106 Chromosome Location |
1 |
| Enzyme 106 Locus |
1q42.2-q43 |
| Enzyme 106 SNPs |
SNPJam Report  |
| Enzyme 106 General References |
Not Available |
| Enzyme 106 Metabolite References |
Not Available |
|
Enzyme 107
[top]
|
| Enzyme 107 ID |
14746 |
| Enzyme 107 Name |
Glutamic acid decarboxylase |
| Enzyme 107 Synonyms |
Not Available |
| Enzyme 107 Gene Name |
GAD65 |
| Enzyme 107 Protein Sequence |
>Glutamic acid decarboxylase
LKYAIKTGHPRYFNQLSTGLDMVGLAADWLTSTANTNMFTYEIAPVFVLLEYVTLKKMRE
IIGWPGGSGDGIFSPGGAISNMYAMMIARFKMFPEVKEKGMAALPRLIAFTSEHSHFSLK
KGAAALGIGTDSVILIKCDERGKMIPSDLERRILEAKQKGFVPFLVSATAGTTVYGAFDP
LLAVADICKKYKIWMHVDAAWGGGLLMSRKHKWKLSGVERANSVTWNPHKMMGVPLQCSA
LLVREEGLMQNCNQMHASYLFQQDKHYDLSYDTGDKALQCGRHVDVFKLWLMWRAKGTTG
FEAHVDKCLELAEYLYNIIKNREGYEMVFDGKPQHTNVCFWYIPPSLRTLEDNEERMSRL
SKVAPVIKARMMEYGTTMVSYQPLGDKVNFFRMVISNPAATHQDIDFLIEEIERLGQDL
|
| Enzyme 107 Number of Residues |
419 |
| Enzyme 107 Molecular Weight |
47343.7 |
| Enzyme 107 Theoretical pI |
8.44 |
| Enzyme 107 GO Classification |
| Function |
- binding
- carbon-carbon lyase activity
- carboxy-lyase activity
- catalytic activity
- cofactor binding
- lyase activity
- pyridoxal phosphate binding
|
| Process |
- carboxylic acid metabolic process
- cellular metabolic process
- metabolic process
- organic acid metabolic process
- oxoacid metabolic process
|
| Component |
| — |
|
| Enzyme 107 General Function |
Involved in carboxy-lyase activity |
| Enzyme 107 Specific Function |
Not Available |
| Enzyme 107 Pathways |
|
| Enzyme 107 Reactions |
- L-glutamate = 4-aminobutanoate + CO2 [RN:R00261]
|
| Enzyme 107 Pfam Domain Function |
|
| Enzyme 107 Signals |
|
| Enzyme 107 Transmembrane Regions |
|
| Enzyme 107 Essentiality |
Not Available |
| Enzyme 107 GenBank ID Protein |
6562440  |
| Enzyme 107 UniProtKB/Swiss-Prot ID |
Q9UGI5  |
| Enzyme 107 UniProtKB/Swiss-Prot Entry Name |
Q9UGI5_HUMAN  |
| Enzyme 107 PDB ID |
Not Available |
| Enzyme 107 Cellular Location |
Not Available |
| Enzyme 107 Gene Sequence |
>1261 bp
TCTAAAATATGCAATTAAAACAGGGCATCCTAGATACTTCAATCAACTTTCTACTGGTTT
GGATATGGTTGGACTAGCAGCAGACTGGCTGACATCAACAGCAAATACTAACATGTTCAC
CTATGAAATTGCTCCAGTATTTGTGCTTTTGGAATATGTCACACTAAAGAAAATGAGAGA
AATCATTGGCTGGCCAGGGGGCTCTGGCGATGGGATATTTTCTCCCGGTGGCGCCATATC
TAACATGTATGCCATGATGATCGCACGCTTTAAGATGTTCCCAGAAGTCAAGGAGAAAGG
AATGGCTGCTCTTCCCAGGCTCATTGCCTTCACGTCTGAACATAGTCATTTTTCTCTCAA
GAAGGGAGCTGCAGCCTTAGGGATTGGAACAGACAGCGTGATTCTGATTAAATGTGATGA
GAGAGGGAAAATGATTCCATCTGATCTTGAAAGAAGGATTCTTGAAGCCAAACAGAAAGG
GTTTGTTCCTTTCCTCGTGAGTGCCACAGCTGGAACCACCGTGTACGGAGCATTTGACCC
CCTCTTAGCTGTCGCTGACATTTGCAAAAAGTATAAGATCTGGATGCATGTGGATGCAGC
TTGGGGTGGGGGATTACTGATGTCCCGAAAACACAAGTGGAAACTGAGTGGCGTGGAGAG
GGCCAACTCTGTGACGTGGAATCCACACAAGATGATGGGAGTCCCTTTGCAGTGCTCTGC
TCTCCTGGTTAGAGAAGAGGGATTGATGCAGAATTGCAACCAAATGCATGCCTCCTACCT
CTTTCAGCAAGATAAACATTATGACCTGTCCTATGACACTGGAGACAAGGCCTTACAGTG
CGGACGCCACGTTGATGTTTTTAAACTATGGCTGATGTGGAGGGCAAAGGGGACTACCGG
GTTTGAAGCGCATGTTGATAAATGTTTGGAGTTGGCAGAGTATTTATACAACATCATAAA
AAACCGAGAAGGATATGAGATGGTGTTTGATGGGAAGCCTCAGCACACAAATGTCTGCTT
CTGGTACATTCCTCCAAGCTTGCGTACTCTGGAAGACAATGAAGAGAGAATGAGTCGCCT
CTCGAAGGTGGCTCCAGTGATTAAAGCCAGAATGATGGAGTATGGAACCACAATGGTCAG
CTACCAACCCTTGGGAGACAAGGTCAATTTCTTCCGCATGGTCATCTCAAACCCAGCGGC
AACTCACCAAGACATTGACTTCCTGATTGAAGAAATAGAACGCCTTGGACAAGATTTATA
A
|
| Enzyme 107 GenBank Gene ID |
AJ251501  |
| Enzyme 107 GeneCard ID |
GAD65  |
| Enzyme 107 GenAtlas ID |
GAD65  |
| Enzyme 107 HGNC ID |
HGNC:4093  |
| Enzyme 107 Chromosome Location |
Not Available |
| Enzyme 107 Locus |
Not Available |
| Enzyme 107 SNPs |
SNPJam Report  |
| Enzyme 107 General References |
- Santos J, Anton EA, Buslje CM, Valdez SN, Villanueva AL, Sica M, Iacono R, Maffia P, Poskus E, Ermacora MR: Replacement of methionine-161 with threonine eliminates a major by-product of human glutamate decarboxylase 65-kDa variant expression in Escherichia coli. Biotechnol Appl Biochem. 2000 Jun;31 ( Pt 3):205-12. [PubMed
]
|
| Enzyme 107 Metabolite References |
Not Available |
|
Enzyme 108
[top]
|
| Enzyme 108 ID |
14747 |
| Enzyme 108 Name |
Cysteine sulfinic acid decarboxylase, isoform CRA_c |
| Enzyme 108 Synonyms |
- SubName: Cysteine sulfinic acid decarboxylase-related protein 1
|
| Enzyme 108 Gene Name |
CSAD |
| Enzyme 108 Protein Sequence |
>Cysteine sulfinic acid decarboxylase, isoform CRA_c
MADSEALPSLAGDPVAVEALLRAVFGVVVDEAIQKGTSVSQKVCEWKEPEELKQLLDLEL
RSQGESQKQILERCRAVIRYSVKTGHPRFFNQLFSGLDPHALAGRIITESLNTSQYTYEI
APVFVLMEEEVLRKLRALVGWSSGDGIFCPGGSISNMYAVNLARYQRYPDCKQRGLRTLP
PLALFTSKEVGKRHRPNPGLLILISSHVTTPSRRELRFWDLAPTVSEWSRLMREGKWSPR
IWRGRLVWPRLRVLCRSWSVPPLAPLC
|
| Enzyme 108 Number of Residues |
267 |
| Enzyme 108 Molecular Weight |
30263.8 |
| Enzyme 108 Theoretical pI |
9.85 |
| Enzyme 108 GO Classification |
| Function |
- binding
- carbon-carbon lyase activity
- carboxy-lyase activity
- catalytic activity
- cofactor binding
- lyase activity
- pyridoxal phosphate binding
|
| Process |
- carboxylic acid metabolic process
- cellular metabolic process
- metabolic process
- organic acid metabolic process
- oxoacid metabolic process
|
| Component |
| — |
|
| Enzyme 108 General Function |
Involved in carboxy-lyase activity |
| Enzyme 108 Specific Function |
Not Available |
| Enzyme 108 Pathways |
Not Available |
| Enzyme 108 Reactions |
Not Available |
| Enzyme 108 Pfam Domain Function |
|
| Enzyme 108 Signals |
|
| Enzyme 108 Transmembrane Regions |
|
| Enzyme 108 Essentiality |
Not Available |
| Enzyme 108 GenBank ID Protein |
4894556  |
| Enzyme 108 UniProtKB/Swiss-Prot ID |
Q9Y602  |
| Enzyme 108 UniProtKB/Swiss-Prot Entry Name |
Q9Y602_HUMAN  |
| Enzyme 108 PDB ID |
Not Available |
| Enzyme 108 Cellular Location |
Not Available |
| Enzyme 108 Gene Sequence |
>804 bp
ATGGCTGACTCAGAAGCACTCCCCTCCCTTGCTGGGGACCCAGTGGCTGTGGAAGCCTTG
CTCCGGGCCGTGTTTGGGGTTGTTGTGGATGAGGCCATTCAGAAAGGAACCAGTGTCTCC
CAGAAGGTCTGTGAGTGGAAGGAGCCTGAGGAGCTGAAGCAGCTGCTGGATTTGGAGCTG
CGGAGCCAGGGCGAGTCACAGAAGCAGATCCTGGAGCGGTGTCGGGCTGTGATTCGCTAC
AGTGTCAAGACTGGTCACCCTCGGTTCTTCAACCAGCTCTTCTCTGGGTTGGATCCCCAT
GCTCTGGCCGGGCGCATTATCACTGAGAGCCTCAACACCAGCCAGTACACATATGAAATC
GCCCCCGTGTTTGTGCTCATGGAAGAGGAGGTGCTGAGGAAACTGCGGGCCCTGGTGGGC
TGGAGCTCTGGGGACGGAATCTTCTGCCCTGGTGGCTCCATCTCCAACATGTATGCTGTA
AATCTGGCCCGCTATCAGCGCTACCCGGATTGCAAGCAGAGGGGCCTCCGCACACTGCCG
CCCCTGGCCCTATTCACATCGAAGGAGGTGGGGAAGAGGCACAGGCCCAACCCTGGGCTC
CTGATTCTAATCTCCAGCCATGTCACTACTCCATCCAGAAGGGAGCTGCGTTTCTGGGAC
TTGGCACCGACAGTGTCCGAGTGGTCAAGGCTGATGAGAGAGGGAAAATGGTCCCCGAGG
ATCTGGAGAGGCAGATTGGTATGGCCGAGGCTGAGGGTGCTGTGCCGTTCCTGGTCAGTG
CCACCTCTGGCACCACTGTGCTAG
|
| Enzyme 108 GenBank Gene ID |
AF116545  |
| Enzyme 108 GeneCard ID |
CSAD  |
| Enzyme 108 GenAtlas ID |
Not Available |
| Enzyme 108 HGNC ID |
Not Available |
| Enzyme 108 Chromosome Location |
1 |
| Enzyme 108 Locus |
12q13.11-q14.3 |
| Enzyme 108 SNPs |
SNPJam Report  |
| Enzyme 108 General References |
Not Available |
| Enzyme 108 Metabolite References |
Not Available |
|
Enzyme 109
[top]
|
| Enzyme 109 ID |
15228 |
| Enzyme 109 Name |
Cysteine conjugate-beta lyase |
| Enzyme 109 Synonyms |
- cytoplasmic (Glutamine transaminase K, kyneurenine aminotransferase), isoform CRA_a
- SubName: cDNA FLJ77833, highly similar to H.sapiens glutamine transaminase K
- SubName: cDNA, FLJ95217, Homo sapiens cysteine conjugate-beta lyase
- cytoplasmic (glutaminetransaminase K, kyneurenine aminotransferase) (CCBL1), mRNA
|
| Enzyme 109 Gene Name |
CCBL1 |
| Enzyme 109 Protein Sequence |
>Cysteine conjugate-beta lyase
MAKQLQARRLDGIDYNPWVEFVKLASEHDVVNLGQGFPDFPPPDFAVEAFQHAVSGDFML
NQYTKTFGYPPLTKILASFFGELLGQEIDPLRNVLVTVGGYGALFTAFQALVDEGDEVII
IEPFFDCYEPMTMMAGGRPVFVSLKPGPIQNGELGSSSNWQLDPMELAGKFTSRTKALVL
NTPNNPLGKVFSREELELVASLCQQHDVVCITDEVYQWMVYDGHQHISIASLPGMWERTL
TIGSAGKTFSATGWKVGWVLGPDHIMKHLRTVHQNSVFHCPTQSQAAVAESFEREQLLFR
QPSSYFVQFPQAMQRCRDHMIRSLQSVGLKPIIPQGSYFLITDISDFKRKMPDLPGAVDE
PYDRRFVKWMIKNKGLVAIPVSIFYSVPHQKHFDHYIRFCFVKDEATLQAMDEKLRKWKV
EL
|
| Enzyme 109 Number of Residues |
422 |
| Enzyme 109 Molecular Weight |
47874.8 |
| Enzyme 109 Theoretical pI |
6.45 |
| Enzyme 109 GO Classification |
| Function |
- 1-aminocyclopropane-1-carboxylate synthase activity
- binding
- carbon-sulfur lyase activity
- catalytic activity
- cofactor binding
- lyase activity
- pyridoxal phosphate binding
- transferase activity
- transferase activity, transferring nitrogenous groups
|
| Process |
- biosynthetic process
- metabolic process
|
| Component |
| — |
|
| Enzyme 109 General Function |
Involved in 1-aminocyclopropane-1-carboxylate synthase activity |
| Enzyme 109 Specific Function |
Not Available |
| Enzyme 109 Pathways |
Not Available |
| Enzyme 109 Reactions |
Not Available |
| Enzyme 109 Pfam Domain Function |
|
| Enzyme 109 Signals |
|
| Enzyme 109 Transmembrane Regions |
|
| Enzyme 109 Essentiality |
Not Available |
| Enzyme 109 GenBank ID Protein |
158255792  |
| Enzyme 109 UniProtKB/Swiss-Prot ID |
A8K563  |
| Enzyme 109 UniProtKB/Swiss-Prot Entry Name |
A8K563_HUMAN  |
| Enzyme 109 PDB ID |
1W7N  |
| Enzyme 109 PDB File |
Show |
| Enzyme 109 3D Structure |
|
| Enzyme 109 Cellular Location |
Not Available |
| Enzyme 109 Gene Sequence |
>1269 bp
ATGGCCAAACAGCTGCAGGCCCGAAGGCTAGACGGGATCGACTACAACCCCTGGGTGGAG
TTTGTGAAACTGGCCAGTGAGCATGACGTCGTGAACTTGGGCCAGGGCTTCCCGGATTTC
CCACCACCAGACTTTGCCGTGGAAGCCTTTCAGCACGCTGTCAGTGGAGACTTTATGCTT
AACCAGTACACCAAGACATTTGGTTACCCACCACTGACGAAGATCCTGGCAAGTTTCTTT
GGGGAGCTGCTGGGTCAGGAGATAGACCCGCTCAGGAATGTGCTGGTGACTGTTGGTGGC
TATGGGGCCCTGTTCACAGCCTTCCAGGCCCTGGTGGACGAAGGAGACGAGGTCATCATC
ATCGAACCCTTTTTTGACTGCTACGAGCCCATGACAATGATGGCAGGGGGTCGTCCTGTG
TTTGTGTCCCTGAAGCCGGGTCCCATCCAGAATGGAGAACTGGGTTCCAGCAGCAACTGG
CAGCTGGACCCCATGGAGCTGGCCGGCAAATTCACATCACGCACCAAAGCCCTGGTCCTC
AACACCCCCAACAACCCCCTGGGCAAGGTGTTCTCCAGGGAAGAGCTGGAGCTGGTGGCC
AGCCTTTGCCAGCAGCATGACGTGGTGTGTATCACTGATGAAGTCTACCAGTGGATGGTC
TACGACGGGCACCAGCACATCAGCATTGCCAGCCTCCCTGGCATGTGGGAACGGACCCTG
ACCATCGGCAGCGCCGGCAAGACCTTCAGCGCCACTGGCTGGAAGGTGGGCTGGGTCCTG
GGTCCAGATCACATCATGAAGCACCTGCGGACCGTGCACCAGAACTCCGTCTTCCACTGC
CCCACGCAGAGCCAGGCTGCAGTAGCCGAGAGCTTTGAACGGGAGCAGCTGCTCTTCCGC
CAACCCAGCAGCTACTTTGTGCAGTTCCCGCAGGCCATGCAGCGCTGCCGTGACCACATG
ATACGTAGCCTACAGTCAGTGGGCCTGAAGCCCATCATCCCTCAGGGCAGCTACTTCCTC
ATCACAGACATCTCAGACTTCAAGAGGAAGATGCCTGACTTGCCTGGAGCTGTGGATGAG
CCCTATGACAGACGCTTCGTCAAGTGGATGATCAAGAACAAGGGCTTGGTGGCCATCCCT
GTCTCCATCTTCTATAGTGTGCCACATCAGAAGCACTTTGACCACTATATCCGCTTCTGT
TTTGTGAAGGATGAAGCCACGCTCCAGGCCATGGACGAGAAGCTGCGGAAGTGGAAGGTG
GAACTCTAG
|
| Enzyme 109 GenBank Gene ID |
AK291178  |
| Enzyme 109 GeneCard ID |
CCBL1  |
| Enzyme 109 GenAtlas ID |
CCBL1  |
| Enzyme 109 HGNC ID |
HGNC:1564  |
| Enzyme 109 Chromosome Location |
9 |
| Enzyme 109 Locus |
9q34.11 |
| Enzyme 109 SNPs |
SNPJam Report  |
| Enzyme 109 General References |
Not Available |
| Enzyme 109 Metabolite References |
Not Available |
|
Enzyme 110
[top]
|
| Enzyme 110 ID |
16424 |
| Enzyme 110 Name |
cDNA, FLJ95372, highly similar to Homo sapiens branched chain aminotransferase 2, mitochondrial(BCAT2), mRNA (Branched chain aminotransferase 2, mitochondrial) |
| Enzyme 110 Synonyms |
Not Available |
| Enzyme 110 Gene Name |
BCAT2 |
| Enzyme 110 Protein Sequence |
>cDNA, FLJ95372, highly similar to Homo sapiens branched chain aminotransferase 2, mitochondrial(BCAT2), mRNA (Branched chain aminotransferase 2, mitochondrial)
MAAAALGQIWARKLLSVPWLLCGPRRYASSSFKAADLQLEMTQKPHKKPGPGEPLVFGKT
FTDHMLMVEWNDKGWGQPRIQPFQNLTLHPASSSLHYSLQLFEGMKAFKGKDQQVRLFRP
WLNMDRMLRSAMRLCLPSFDKLELLECIRRLIEVDKDWVPDAAGTSLYVRPVLIGNEPSL
GVSQPTRALLFVILCPVGAYFPGGSVTPVSLLADPAFIRAWVGGVGNYKLGGNYGPTVLV
QQEALKRGCEQVLWLYGPDHQLTEVGTMNIFVYWTHEDGVLELVTPPLNGVILPGVVRQS
LLDMAQTWGEFRVVERTITMKQLLRALEEGRVREVFGSGTACQVCPVHRILYKDRNLHIP
TMENGPELILRFQKELKEIQYGIRAHEWMFPV
|
| Enzyme 110 Number of Residues |
392 |
| Enzyme 110 Molecular Weight |
44288 |
| Enzyme 110 Theoretical pI |
8.82 |
| Enzyme 110 GO Classification |
| Function |
- branched-chain-amino-acid transaminase activity
- catalytic activity
- transaminase activity
- transferase activity
- transferase activity, transferring nitrogenous groups
|
| Process |
- amino acid and derivative metabolism
- amino acid metabolism
- branched chain family amino acid metabolism
- cellular metabolism
- metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 110 General Function |
Amino acid transport and metabolism |
| Enzyme 110 Specific Function |
Not Available |
| Enzyme 110 Pathways |
Not Available |
| Enzyme 110 Reactions |
Not Available |
| Enzyme 110 Pfam Domain Function |
|
| Enzyme 110 Signals |
|
| Enzyme 110 Transmembrane Regions |
|
| Enzyme 110 Essentiality |
Not Available |
| Enzyme 110 GenBank ID Protein |
Not Available |
| Enzyme 110 UniProtKB/Swiss-Prot ID |
B2RB87  |
| Enzyme 110 UniProtKB/Swiss-Prot Entry Name |
B2RB87_HUMAN  |
| Enzyme 110 PDB ID |
1KTA  |
| Enzyme 110 PDB File |
Show |
| Enzyme 110 3D Structure |
|
| Enzyme 110 Cellular Location |
Not Available |
| Enzyme 110 Gene Sequence |
Not Available |
| Enzyme 110 GenBank Gene ID |
AK314548  |
| Enzyme 110 GeneCard ID |
B2RB87  |
| Enzyme 110 GenAtlas ID |
Not Available |
| Enzyme 110 HGNC ID |
Not Available |
| Enzyme 110 Chromosome Location |
19 |
| Enzyme 110 Locus |
19q13 |
| Enzyme 110 SNPs |
SNPJam Report  |
| Enzyme 110 General References |
Not Available |
| Enzyme 110 Metabolite References |
Not Available |
|
Enzyme 111
[top]
|
| Enzyme 111 ID |
16487 |
| Enzyme 111 Name |
cDNA, FLJ94281, Homo sapiens cystathionine-beta-synthase (CBS), mRNA (Cystathionine-beta-synthase, isoform CRA_b) |
| Enzyme 111 Synonyms |
Not Available |
| Enzyme 111 Gene Name |
CBS |
| Enzyme 111 Protein Sequence |
>cDNA, FLJ94281, Homo sapiens cystathionine-beta-synthase (CBS), mRNA (Cystathionine-beta-synthase, isoform CRA_b)
MPSETPQAEVGPTGCPHRSGPHSAKGSLEKGSPEDKEAKEPLWIRPDAPSRCTWQLGRPA
SESPHHHTAPAKSPKILPDILKKIGDTPMVRINKIGKKFGLKCELLAKCEFFNAGGSVKD
RISLRMIEDAERDGTLKPGDTIIEPTSGNTGIGLALAAAVRGYRCIIVMPEKMSSEKVDV
LRALGAEIVRTPTNARFDSPESHVGVAWRLKNEIPNSHILDQYRNASNPLAHYDTTADEI
LQQCDGKLDMLVASVGTGGTITGIARKLKEKCPGCRIIGVDPEGSILAEPEELNQTEQTT
YEVEGIGYDFIPTVLDRTVVDKWFKSNDEEAFTFARMLIAQEGLLCGGSAGSTVAVAVKA
AQELQEGQRCVVILPDSVRNYMTKFLSDRWMLQKGFLKEEDLTEKKPWWWHLRVQELGLS
APLTVLPTITCGHTIEILREKGFDQAPVVDEAGVILGMVTLGNMLSSLLAGKVQPSDQVG
KVIYKQFKQIRLTDTLGRLSHILEMDHFALVVHEQIQYHSTGKSSQRQMVFGVVTAIDLL
NFVAAQERDQK
|
| Enzyme 111 Number of Residues |
551 |
| Enzyme 111 Molecular Weight |
60587 |
| Enzyme 111 Theoretical pI |
6.63 |
| Enzyme 111 GO Classification |
| Function |
- carbon-oxygen lyase activity
- catalytic activity
- cystathionine beta-synthase activity
- hydro-lyase activity
- lyase activity
|
| Process |
- L-serine metabolism
- amino acid and derivative metabolism
- amino acid metabolism
- cellular metabolism
- cysteine biosynthesis
- cysteine biosynthesis from serine
- cysteine biosynthesis via cystathione
- metabolism
- physiological process
- serine family amino acid metabolism
- sulfur amino acid biosynthesis
- sulfur amino acid metabolism
|
| Component |
- cell
- cytoplasm
- intracellular
|
|
| Enzyme 111 General Function |
Amino acid transport and metabolism |
| Enzyme 111 Specific Function |
Not Available |
| Enzyme 111 Pathways |
Not Available |
| Enzyme 111 Reactions |
Not Available |
| Enzyme 111 Pfam Domain Function |
|
| Enzyme 111 Signals |
|
| Enzyme 111 Transmembrane Regions |
|
| Enzyme 111 Essentiality |
Not Available |
| Enzyme 111 GenBank ID Protein |
Not Available |
| Enzyme 111 UniProtKB/Swiss-Prot ID |
B2R993  |
| Enzyme 111 UniProtKB/Swiss-Prot Entry Name |
B2R993_HUMAN  |
| Enzyme 111 PDB ID |
1JBQ  |
| Enzyme 111 PDB File |
Show |
| Enzyme 111 3D Structure |
|
| Enzyme 111 Cellular Location |
Not Available |
| Enzyme 111 Gene Sequence |
Not Available |
| Enzyme 111 GenBank Gene ID |
AK313691  |
| Enzyme 111 GeneCard ID |
B2R993  |
| Enzyme 111 GenAtlas ID |
Not Available |
| Enzyme 111 HGNC ID |
Not Available |
| Enzyme 111 Chromosome Location |
21 |
| Enzyme 111 Locus |
21q22.3 |
| Enzyme 111 SNPs |
SNPJam Report  |
| Enzyme 111 General References |
Not Available |
| Enzyme 111 Metabolite References |
Not Available |
|
Enzyme 112
[top]
|
| Enzyme 112 ID |
16502 |
| Enzyme 112 Name |
cDNA, FLJ93078, Homo sapiens glutamic-oxaloacetic transaminase 1, soluble(aspartate aminotransferase 1) (GOT1), mRNA (Glutamic-oxaloacetic transaminase 1, soluble (Aspartate aminotransferase 1), isoform CRA_b) |
| Enzyme 112 Synonyms |
Not Available |
| Enzyme 112 Gene Name |
GOT1 |
| Enzyme 112 Protein Sequence |
>cDNA, FLJ93078, Homo sapiens glutamic-oxaloacetic transaminase 1, soluble(aspartate aminotransferase 1) (GOT1), mRNA (Glutamic-oxaloacetic transaminase 1, soluble (Aspartate aminotransferase 1), isoform CRA_b)
MAPPSVFAEVPQAQPVLVFKLTADFREDPDPRKVNLGVGAYRTDDCHPWVLPVVKKVEQK
IANDNSLNHEYLPILGLAEFRSCASRLALGDDSPALKEKRVGGVQSLGGTGALRIGADFL
ARWYNGTNNKNTPVYVSSPTWENHNAVFSAAGFKDIRSYRYWDAEKRGLDLQGFLNDLEN
APEFSIVVLHACAHNPTGIDPTPEQWKQIASVMKHRFLFPFFDSAYQGFASGNLERDAWA
IRYFVSEGFEFFCAQSFSKNFGLYNERVGNLTVVGKEPESILQVLSQMEKIVRITWSNPP
AQGARIVASTLSNPELFEEWTGNVKTMADRILTMRSELRARLEALKTPGTWNHITDQIGM
FSFTGLNPKQVEYLVNEKHIYLLPSGRINVSGLTTKNLDYVATSIHEAVTKIQ
|
| Enzyme 112 Number of Residues |
413 |
| Enzyme 112 Molecular Weight |
46248 |
| Enzyme 112 Theoretical pI |
7.01 |
| Enzyme 112 GO Classification |
| Function |
- catalytic activity
- transaminase activity
- transferase activity
- transferase activity, transferring nitrogenous groups
|
| Process |
- amino acid and derivative metabolism
- amino acid metabolism
- biosynthesis
- cellular metabolism
- metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 112 General Function |
Amino acid transport and metabolism |
| Enzyme 112 Specific Function |
Not Available |
| Enzyme 112 Pathways |
Not Available |
| Enzyme 112 Reactions |
Not Available |
| Enzyme 112 Pfam Domain Function |
|
| Enzyme 112 Signals |
|
| Enzyme 112 Transmembrane Regions |
|
| Enzyme 112 Essentiality |
Not Available |
| Enzyme 112 GenBank ID Protein |
Not Available |
| Enzyme 112 UniProtKB/Swiss-Prot ID |
B2R6R7  |
| Enzyme 112 UniProtKB/Swiss-Prot Entry Name |
B2R6R7_HUMAN  |
| Enzyme 112 PDB ID |
1AJS  |
| Enzyme 112 PDB File |
Show |
| Enzyme 112 3D Structure |
|
| Enzyme 112 Cellular Location |
Not Available |
| Enzyme 112 Gene Sequence |
Not Available |
| Enzyme 112 GenBank Gene ID |
AK312684  |
| Enzyme 112 GeneCard ID |
B2R6R7  |
| Enzyme 112 GenAtlas ID |
Not Available |
| Enzyme 112 HGNC ID |
Not Available |
| Enzyme 112 Chromosome Location |
10 |
| Enzyme 112 Locus |
10q24.1-q25.1 |
| Enzyme 112 SNPs |
SNPJam Report  |
| Enzyme 112 General References |
Not Available |
| Enzyme 112 Metabolite References |
Not Available |
|
Enzyme 113
[top]
|
| Enzyme 113 ID |
16503 |
| Enzyme 113 Name |
cDNA, FLJ93913, Homo sapiens tyrosine aminotransferase (TAT), nuclear gene encodingmitochondrial protein, mRNA (Tyrosine aminotransferase, isoform CRA_a) |
| Enzyme 113 Synonyms |
Not Available |
| Enzyme 113 Gene Name |
TAT |
| Enzyme 113 Protein Sequence |
>cDNA, FLJ93913, Homo sapiens tyrosine aminotransferase (TAT), nuclear gene encodingmitochondrial protein, mRNA (Tyrosine aminotransferase, isoform CRA_a)
MDPYMIQMSSKGNLPSILDVHVNVGGRSSVPGKMKGRKARWSVRPSDMAKKTFNPIRAIV
DNMKVKPNPNKTMISLSIGDPTVFGNLPTDPEVTQAMKDALDSGKYNGYAPSIGFLSSRE
EIASYYHCPEAPLEAKDVILTSGCSQAIDLCLAVLANPGQNILVPRPGFSLYKTLAESMG
IEVKLYNLLPEKSWEIDLKQLEYLIDEKTACLIVNNPSNPCGSVFSKRHLQKILAVAARQ
CVPILADEIYGDMVFSDCKYEPLATLSTDVPILSCGGLAKRWLVPGWRLGWILIHDRRDI
FGNEIRDGLVKLSQRILGPCTIVQGALKSILCRTPGEFYHNTLSFLKSNADLCYGALAAI
PGLRPVRPSGAMYLMVGIEMEHFPEFENDVEFTERLVAEQSVHCLPATCFEYPNFIRVVI
TVPEVMMLEACSRIQEFCEQHYHCAEGSQEECDK
|
| Enzyme 113 Number of Residues |
454 |
| Enzyme 113 Molecular Weight |
50400 |
| Enzyme 113 Theoretical pI |
6.24 |
| Enzyme 113 GO Classification |
| Function |
- 1-aminocyclopropane-1-carboxylate synthase activity
- binding
- carbon-sulfur lyase activity
- catalytic activity
- lyase activity
- pyridoxal phosphate binding
- transaminase activity
- transferase activity
- transferase activity, transferring nitrogenous groups
- tyrosine transaminase activity
- vitamin binding
|
| Process |
- amino acid and derivative metabolism
- amino acid catabolism
- amino acid metabolism
- aromatic amino acid family catabolism
- aromatic amino acid family metabolism
- biosynthesis
- cellular metabolism
- metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 113 General Function |
Amino acid transport and metabolism |
| Enzyme 113 Specific Function |
Not Available |
| Enzyme 113 Pathways |
Not Available |
| Enzyme 113 Reactions |
Not Available |
| Enzyme 113 Pfam Domain Function |
|
| Enzyme 113 Signals |
|
| Enzyme 113 Transmembrane Regions |
|
| Enzyme 113 Essentiality |
Not Available |
| Enzyme 113 GenBank ID Protein |
Not Available |
| Enzyme 113 UniProtKB/Swiss-Prot ID |
B2R8I1  |
| Enzyme 113 UniProtKB/Swiss-Prot Entry Name |
B2R8I1_HUMAN  |
| Enzyme 113 PDB ID |
Not Available |
| Enzyme 113 Cellular Location |
Not Available |
| Enzyme 113 Gene Sequence |
Not Available |
| Enzyme 113 GenBank Gene ID |
AK313380  |
| Enzyme 113 GeneCard ID |
B2R8I1  |
| Enzyme 113 GenAtlas ID |
Not Available |
| Enzyme 113 HGNC ID |
Not Available |
| Enzyme 113 Chromosome Location |
16 |
| Enzyme 113 Locus |
16q22.1 |
| Enzyme 113 SNPs |
SNPJam Report  |
| Enzyme 113 General References |
Not Available |
| Enzyme 113 Metabolite References |
Not Available |