|
Enzyme 1
[top]
|
| Enzyme 1 ID |
5563 |
| Enzyme 1 Name |
6-phosphogluconolactonase |
| Enzyme 1 Synonyms |
- 6PGL
|
| Enzyme 1 Gene Name |
PGLS |
| Enzyme 1 Protein Sequence |
>6-phosphogluconolactonase
MAAPAPGLISVFSSSQELGAALAQLVAQRAACCLAGARARFALGLSGGSLVSMLARELPA
AVAPAGPASLARWTLGFCDERLVPFDHAESTYGLYRTHLLSRLPIPESQVITINPELPVE
EAAEDYAKKLRQAFQGDSIPVFDLLILGVGPDGHTCSLFPDHPLLQEREKIVAPISDSPK
PPPQRVTLTLPVLNAARTVIFVATGEGKAAVLKRILEDQEENPLPAALVQPHTGKLCWFL
DEAAARLLTVPFEKHSTL
|
| Enzyme 1 Number of Residues |
258 |
| Enzyme 1 Molecular Weight |
27546.5 |
| Enzyme 1 Theoretical pI |
5.95 |
| Enzyme 1 GO Classification |
| Function |
- 6-phosphogluconolactonase activity
- carboxylesterase activity
- catalytic activity
- hydrolase activity
- hydrolase activity, acting on ester bonds
|
| Process |
- alcohol metabolic process
- carbohydrate metabolic process
- glucose catabolic process
- glucose metabolic process
- hexose metabolic process
- metabolic process
- monosaccharide metabolic process
- pentose-phosphate shunt
- primary metabolic process
- small molecule metabolic process
|
| Component |
| — |
|
| Enzyme 1 General Function |
Involved in 6-phosphogluconolactonase activity |
| Enzyme 1 Specific Function |
Hydrolysis of 6-phosphogluconolactone to 6- phosphogluconate |
| Enzyme 1 Pathways |
|
| Enzyme 1 Reactions |
- 6-phospho-D-glucono-1,5-lactone + H2O = 6-phospho-D-gluconate [RN:R02035]
|
| Enzyme 1 Pfam Domain Function |
Not Available |
| Enzyme 1 Signals |
|
| Enzyme 1 Transmembrane Regions |
|
| Enzyme 1 Essentiality |
Not Available |
| Enzyme 1 GenBank ID Protein |
6912586  |
| Enzyme 1 UniProtKB/Swiss-Prot ID |
O95336  |
| Enzyme 1 UniProtKB/Swiss-Prot Entry Name |
6PGL_HUMAN  |
| Enzyme 1 PDB ID |
Not Available |
| Enzyme 1 Cellular Location |
Not Available |
| Enzyme 1 Gene Sequence |
>777 bp
ATGGCCGCGCCGGCCCCGGGCCTCATCTCGGTGTTCTCGAGTTCCCAGGAGCTGGGTGCG
GCGCTAGCGCAGCTGGTGGCCCAGCGCGCAGCATGCTGCCTGGCAGGGGCCCGCGCCCGT
TTCGCGCTCGGCCTGTCGGGCGGGAGCCTCGTCTCGATGCTAGCCCGCGAGCTACCCGCC
GCCGTCGCCCCTGCCGGGCCAGCTAGCTTAGCGCGCTGGACGCTGGGCTTCTGCGACGAG
CGCCTCGTGCCCTTCGATCACGCCGAGAGCACGTACGGCCTCTACCGGACGCATCTTCTC
TCCAGACTGCCGATCCCAGAAAGCCAGGTGATCACCATTAACCCCGAGCTGCCTGTGGAG
GAGGCGGCTGAGGACTACGCCAAGAAGCTGAGACAGGCATTCCAAGGGGACTCCATCCCG
GTTTTCGACCTGCTGATCCTGGGGGTGGGCCCCGATGGTCACACCTGCTCACTCTTCCCA
GACCACCCCCTCCTACAGGAGCGGGAGAAGATTGTGGCTCCCATCAGTGACTCCCCGAAG
CCACCGCCACAGCGTGTGACCCTCACACTACCTGTCCTGAATGCAGCACGAACTGTCATC
TTTGTGGCAACTGGAGAAGGCAAGGCAGCTGTTCTGAAGCGCATTTTGGAGGACCAGGAG
GAAAACCCGCTGCCCGCCGCCCTGGTCCAGCCCCACACCGGGAAACTGTGCTGGTTCTTG
GACGAGGCGGCCGCCCGCCTCCTGACCGTGCCCTTCGAGAAGCATTCCACTTTGTAG
|
| Enzyme 1 GenBank Gene ID |
NM_012088.2  |
| Enzyme 1 GeneCard ID |
PGLS  |
| Enzyme 1 GenAtlas ID |
PGLS  |
| Enzyme 1 HGNC ID |
HGNC:8903  |
| Enzyme 1 Chromosome Location |
1 |
| Enzyme 1 Locus |
19p13.2 |
| Enzyme 1 SNPs |
SNPJam Report  |
| Enzyme 1 General References |
- Collard F, Collet JF, Gerin I, Veiga-da-Cunha M, Van Schaftingen E: Identification of the cDNA encoding human 6-phosphogluconolactonase, the enzyme catalyzing the second step of the pentose phosphate pathway(1). FEBS Lett. 1999 Oct 8;459(2):223-6. [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
]
- 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
]
|
| Enzyme 1 Metabolite References |
Not Available |
|
Enzyme 2
[top]
|
| Enzyme 2 ID |
5565 |
| Enzyme 2 Name |
GDH/6PGL endoplasmic bifunctional protein |
| Enzyme 2 Synonyms |
- Glucose 1-dehydrogenase
- Hexose-6-phosphate dehydrogenase
- 6-phosphogluconolactonase
- 6PGL
|
| Enzyme 2 Gene Name |
H6PD |
| Enzyme 2 Protein Sequence |
>GDH/6PGL endoplasmic bifunctional protein
MWNMLIVAMCLALLGCLQAQELQGHVSIILLGATGDLAKKYLWQGLFQLYLDEAGRGHSF
SFHGAALTAPKQGQELMAKALESLSCPKDMAPSHCAEHKDQFLQLSQYRQLKTAEDYQAL
NKDIEAQLQHAGLREAGRIFYFSVPPFAYEDIARNINSSCRPGPGAWLRVVLEKPFGHDH
FSAQQLATELGTFFQEEEMYRVDHYLGKQAVAQILPFRDQNRKALDGLWNRHHVERVEII
MKETVDAEGRTSFYEEYGVIRDVLQNHLTEVLTLVAMELPHNVSSAEAVLRHKLQVFQAL
RGLQRGSAVVGQYQSYSEQVRRELQKPDSFHSLTPTFAAVLVHIDNLRWEGVPFILMSGK
ALDERVGYARILFKNQACCVQSEKHWAAAQSQCLPRQLVFHIGHGDLGSPAVLVSRNLFR
PSLPSSWKEMEGPPGLRLFGSPLSDYYAYSPVRERDAHSVLLSHIFHGRKNFFITTENLL
ASWNFWTPLLESLAHKAPRLYPGGAENGRLLDFEFSSGRLFFSQQQPEQLVPGPGPAPMP
SDFQVLRAKYRESPLVSAWSEELISKLANDIEATAVRAVRRFGQFHLALSGGSSPVALFQ
QLATAHYGFPWAHTHLWLVDERCVPLSDPESNFQGLQAHLLQHVRIPYYNIHPMPVHLQQ
RLCAEEDQGAQIYAREISALVANSSFDLVLLGMGADGHTASLFPQSPTGLDGEQLVVLTT
SPSQPHRRMSLSLPLINRAKKVAVLVMGRMKREITTLVSRVGHEPKKWPISGVLPHSGQL
VWYMDYDAFLG
|
| Enzyme 2 Number of Residues |
791 |
| Enzyme 2 Molecular Weight |
88892.0 |
| Enzyme 2 Theoretical pI |
7.31 |
| Enzyme 2 GO Classification |
| Function |
- 6-phosphogluconolactonase activity
- NADP or NADPH binding
- binding
- carboxylesterase activity
- catalytic activity
- glucose-6-phosphate dehydrogenase activity
- hydrolase activity
- hydrolase activity, acting on ester bonds
- 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
- carbohydrate metabolic process
- glucose catabolic process
- glucose metabolic process
- hexose metabolic process
- metabolic process
- monosaccharide metabolic process
- oxidation reduction
- pentose-phosphate shunt
- primary metabolic process
- small molecule metabolic process
|
| Component |
| — |
|
| Enzyme 2 General Function |
Involved in 6-phosphogluconolactonase activity |
| Enzyme 2 Specific Function |
Oxidizes glucose-6-phosphate and glucose, as well as other hexose-6-phosphates |
| Enzyme 2 Pathways |
|
| Enzyme 2 Reactions |
- 6-phospho-D-glucono-1,5-lactone + H2O = 6-phospho-D-gluconate [RN:R02035]
|
| Enzyme 2 Pfam Domain Function |
|
| Enzyme 2 Signals |
|
| Enzyme 2 Transmembrane Regions |
|
| Enzyme 2 Essentiality |
Not Available |
| Enzyme 2 GenBank ID Protein |
4186038  |
| Enzyme 2 UniProtKB/Swiss-Prot ID |
O95479  |
| Enzyme 2 UniProtKB/Swiss-Prot Entry Name |
G6PE_HUMAN  |
| Enzyme 2 PDB ID |
Not Available |
| Enzyme 2 Cellular Location |
Not Available |
| Enzyme 2 Gene Sequence |
>2376 bp
ATGTGGAATATGCTCATAGTGGCGATGTGCTTGGCCCTTCTGGGCTGCCTGCAAGCCCAG
GAGCTCCAGGGACATGTCTCCATAATCCTGCTGGGAGCAACTGGGGACCTGGCTAAGAAG
TACTTATGGCAGGGACTGTTCCAGCTGTACCTGGATGAAGCGGGGAGGGGTCACAGTTTT
AGCTTCCATGGAGCTGCTCTGACAGCCCCCAAGCAGGGTCAAGAGCTCATGGCCAAGGCC
CTGGAATCCCTCTCCTGCCCCAAGGACATGGCACCCAGTCACTGTGCAGAGCACAAGGAT
CAGTTCCTGCAGCTGAGCCAGTACCGCCAACTGAAGACGGCCGAGGACTATCAGGCCCTG
AACAAGGACATCGAGGCACAGCTCCAGCACGCAGGCCTCCGGGAGGCTGGCAGGATCTTC
TACTTCTCAGTGCCACCCTTCGCCTATGAAGACATTGCCCGCAACATCAACAGTAGCTGC
CGGCCAGGCCCGGGCGCCTGGCTGCGGGTTGTCCTTGAGAAACCCTTTGGCCATGACCAC
TTCTCAGCCCAGCAGCTGGCCACAGAACTCGGGACCTTTTTCCAGGAGGAGGAGATGTAC
CGGGTGGACCATTACTTAGGCAAGCAGGCTGTGGCGCAGATCCTGCCTTTCCGAGACCAG
AACCGCAAGGCTTTGGACGGCCTCTGGAACCGGCACCATGTGGAGCGGGTGGAGATCATC
ATGAAAGAGACCGTGGATGCTGAAGGCCGCACCAGCTTCTATGAGGAGTACGGTGTCATT
CGCGACGTCCTCCAGAACCATCTGACGGAGGTCCTCACCCTCGTGGCCATGGAGCTGCCC
CACAATGTCAGCAGTGCGGAGGCTGTGCTGCGGCACAAGCTTCAGGTCTTCCAGGCGCTG
CGGGGCCTGCAGAGGGGCAGTGCCGTCGTGGGCCAGTACCAGTCTTACAGTGAGCAGGTG
CGCAGAGAGCTGCAGAAGCCAGACAGCTTCCACAGCCTGACGCCGACCTTCGCAGGTGTC
CTAGTGCACATTGACAACCTTCGCTGGGAGGGCGTGCCTTTCATCCTGATGTCTGGCAAA
GCCTTGGACGAGAGAGTGGGCTACGCTCGGATCTTGTTCAAGAACCAGGCCTGCTGTGTG
CAGAGCGAAAAGCACTGGGCCGCGGCGCAGAGCCAGTGCCTGCCCCGGCAGCTCGTCTTC
CACATCGGCCATGGCGACCTGGGCAGCCCTGCCGTGCTGGTCAGCAGGAACCTGTTCAGG
CCCTCCCTGCCCTCCAGCTGGAAGGAAATGGAGGGACCACCTGGGCTCCGCCTTTTCGGC
AGCCCTCTGTCCGATTACTACGCCTACAGCCCTGTGCGGGAGCGGGACGCCCACTCCGTC
CTCTTATCCCATATCTTCCATGGCCGGAAGAATTTCTTCATCACCACAGAGAACTTGCTG
GCCTCCTGGAACTTCTGGACCCCTCTGCTGGAGAGCCTGGCCCATAAGGCCCCACGCCTC
TACCCTGGAGGAGCTGAGAATGGCCGTCTGTTGGACTTTGAGTTCAGTAGCGGCCGGTTG
TTCTTTTCCCAGCAGCAGCCGGAGCAGCTGGTGCCAGGGCCAGGGCCGGCCCCAATGCCC
AGTGACTTCCAGGTCCTCAGGGCCAAGTACCGAGAGAGCCCGCTGGTCTCCGCCTGGTCC
GAGGAGCTGATCTCTAAGCTGGCTAATGACATCGAGGCCACCGCTGTGCGAGCCGTGCGG
CGCTTTGGCCAGTTCCACCTGGCACTGTCGGGGGGCTCGAGCCCCGTGGCCCTGTTCCAG
CAGCTGGCCACGGCGCACTATGGCTTCCCCTGGGCCCACACGCACCTGTGGCTGGTTGAC
GAGCGCTGCGTCCCACTCTCAGACCCGGAGTCCAACTTCCAGGGCCTGCAGGCCCACCTG
CTGCAGCACGTCCGGATCCCCTACTACAACATCCACCCCATGCCTGTGCACCTGCAGCAG
CGGCTCTGCGCCGAGGAGGACCAGGGCGCCCAGATCTATGCCAGGGAGATCTCAGCCCTG
GTGGCCAACAGCAGCTTCGACCTGGTGCTGCTGGGCATGGGTGCCGACGGGCACACAGCC
TCCCTCTTCCCACAGTCACCCACTGGCCTGGATGGCGAGCAGCTGGTCGTGCTGACCACG
AGCCCCTCCCAGCCACACCGCCGCATGAGCCTTAGCCTGCCTCTCATCAACCGCGCCAAG
AAGGTGGCAGTCCTGGTCATGGGCAGGATGAAGCGTGAGATCACCACGCTGGTGAGCCGG
GTGGGCCATGAGCCCAAGAAGTGGCCCATCTCGGGTGTCCTGCCGCACTCCGGCCAGCTG
GTGTGGTACATGGACTACGACGCCTTCCTGGGATGA
|
| Enzyme 2 GenBank Gene ID |
AJ012590  |
| Enzyme 2 GeneCard ID |
H6PD  |
| Enzyme 2 GenAtlas ID |
H6PD  |
| Enzyme 2 HGNC ID |
HGNC:4795  |
| Enzyme 2 Chromosome Location |
1 |
| Enzyme 2 Locus |
1p36 |
| Enzyme 2 SNPs |
SNPJam Report  |
| Enzyme 2 General References |
- Mason PJ, Stevens D, Diez A, Knight SW, Scopes DA, Vulliamy TJ: Human hexose-6-phosphate dehydrogenase (glucose 1-dehydrogenase) encoded at 1p36: coding sequence and expression. Blood Cells Mol Dis. 1999 Feb;25(1):30-7. [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
]
- 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
]
- Wang Y, Du D, Fang L, Yang G, Zhang C, Zeng R, Ullrich A, Lottspeich F, Chen Z: Tyrosine phosphorylated Par3 regulates epithelial tight junction assembly promoted by EGFR signaling. EMBO J. 2006 Nov 1;25(21):5058-70. Epub 2006 Oct 19. [PubMed
]
- Chen R, Jiang X, Sun D, Han G, Wang F, Ye M, Wang L, Zou H: Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry. J Proteome Res. 2009 Feb;8(2):651-61. [PubMed
]
- Draper N, Walker EA, Bujalska IJ, Tomlinson JW, Chalder SM, Arlt W, Lavery GG, Bedendo O, Ray DW, Laing I, Malunowicz E, White PC, Hewison M, Mason PJ, Connell JM, Shackleton CH, Stewart PM: Mutations in the genes encoding 11beta-hydroxysteroid dehydrogenase type 1 and hexose-6-phosphate dehydrogenase interact to cause cortisone reductase deficiency. Nat Genet. 2003 Aug;34(4):434-9. [PubMed
]
|
| Enzyme 2 Metabolite References |
Not Available |
|
Enzyme 3
[top]
|
| Enzyme 3 ID |
13079 |
| Enzyme 3 Name |
Putative uncharacterized protein PGD |
| Enzyme 3 Synonyms |
- SubName: cDNA FLJ51182, highly similar to 6-phosphogluconate dehydrogenase, decarboxylating (EC 1.1.1.44)
|
| Enzyme 3 Gene Name |
PGD |
| Enzyme 3 Protein Sequence |
>Putative uncharacterized protein PGD
MISSRNWYHCWILVTSSLTEEILNIGTPQDGAETSRPREFYLWGAESVVERKGPGMAHRS
CQEGTKKGTGKWTAISALEYGVPVTLIGEAVFARCLSSLKDERIQASKKLKGPQKFQFDG
DKKSFLEDIRKALYASKIISYAQGFMLLRQAATEFGWTLNYGGIALMWRGGCIIRSVFLG
KIKDAFDRNPELQNLLLDDFFKSAVENCQDSWRRAVSTGVQAGIPMPCFTTALSFYDGYR
HEMLPASLIQAQRDYFGAHTYELLAKPGQFIHTNWTGHGGTVSSSSYNA
|
| Enzyme 3 Number of Residues |
289 |
| Enzyme 3 Molecular Weight |
32311.5 |
| Enzyme 3 Theoretical pI |
8.75 |
| Enzyme 3 GO Classification |
| Function |
- NADP or NADPH binding
- binding
- catalytic activity
- coenzyme binding
- cofactor binding
- 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
- phosphogluconate dehydrogenase (decarboxylating) activity
- phosphogluconate dehydrogenase (decarboxylating) activity
|
| Process |
- alcohol metabolic process
- glucose catabolic process
- glucose metabolic process
- hexose metabolic process
- metabolic process
- monosaccharide metabolic process
- oxidation reduction
- pentose-phosphate shunt
- small molecule metabolic process
|
| Component |
| — |
|
| Enzyme 3 General Function |
Involved in oxidoreductase activity |
| Enzyme 3 Specific Function |
Not Available |
| Enzyme 3 Pathways |
Not Available |
| Enzyme 3 Reactions |
Not Available |
| Enzyme 3 Pfam Domain Function |
|
| Enzyme 3 Signals |
|
| Enzyme 3 Transmembrane Regions |
|
| Enzyme 3 Essentiality |
Not Available |
| Enzyme 3 GenBank ID Protein |
194384114  |
| Enzyme 3 UniProtKB/Swiss-Prot ID |
A9Z1X1  |
| Enzyme 3 UniProtKB/Swiss-Prot Entry Name |
A9Z1X1_HUMAN  |
| Enzyme 3 PDB ID |
2PGD  |
| Enzyme 3 PDB File |
Show |
| Enzyme 3 3D Structure |
|
| Enzyme 3 Cellular Location |
Not Available |
| Enzyme 3 Gene Sequence |
>870 bp
ATGATTTCATCGAGAAATTGGTACCATTGTTGGATACTGGTGACATCATCATTGACGGAG
GAAATTCTGAATATAGGGACACCACAAGACGGTGCCGAGACCTCAAGGCCAAGGGAATTT
TATTTGTGGGGAGCGGAGTCAGTGGTGGAGAGGAAGGGGCCCGGTATGGCCCATCGCTCA
TGCCAGGAGGGAACAAAGAAGGGCACAGGGAAGTGGACCGCCATCTCCGCCCTGGAATAC
GGCGTACCCGTCACCCTCATTGGAGAAGCTGTCTTTGCTCGGTGCTTATCATCTCTGAAG
GATGAGAGAATTCAAGCTAGCAAAAAGCTGAAGGGTCCCCAGAAGTTCCAGTTTGATGGT
GATAAGAAATCATTCCTGGAGGACATTCGGAAGGCACTCTACGCTTCCAAGATCATCTCT
TACGCTCAAGGCTTTATGCTGCTAAGGCAGGCAGCCACCGAGTTTGGCTGGACTCTCAAT
TATGGTGGCATCGCCCTGATGTGGAGAGGGGGCTGCATCATTAGAAGTGTATTCCTAGGA
AAGATAAAGGATGCATTTGATCGAAACCCGGAACTTCAGAACCTCCTACTGGACGACTTC
TTTAAGTCAGCTGTTGAAAACTGCCAGGACTCCTGGCGGCGGGCAGTCAGCACTGGGGTC
CAGGCTGGCATTCCCATGCCCTGTTTTACCACTGCCCTCTCCTTCTATGACGGGTACAGA
CATGAGATGCTTCCAGCCAGCCTCATCCAGGCTCAGCGGGATTACTTCGGGGCTCACACC
TATGAACTCTTGGCCAAACCAGGGCAGTTTATCCACACCAACTGGACAGGCCATGGTGGC
ACCGTGTCATCCTCGTCATACAATGCCTGA
|
| Enzyme 3 GenBank Gene ID |
AK303898  |
| Enzyme 3 GeneCard ID |
PGD  |
| Enzyme 3 GenAtlas ID |
PGD  |
| Enzyme 3 HGNC ID |
HGNC:8891  |
| Enzyme 3 Chromosome Location |
1 |
| Enzyme 3 Locus |
1p36.3-p36.13 |
| Enzyme 3 SNPs |
SNPJam Report  |
| Enzyme 3 General References |
- 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
]
|
| Enzyme 3 Metabolite References |
Not Available |