|
Enzyme 1
[top]
|
| Enzyme 1 ID |
5392 |
| Enzyme 1 Name |
Methionine synthase |
| Enzyme 1 Synonyms |
- 5-methyltetrahydrofolate--homocysteine methyltransferase
- Vitamin-B12 dependent methionine synthase
- MS
|
| Enzyme 1 Gene Name |
MTR |
| Enzyme 1 Protein Sequence |
>Methionine synthase
MSPALQDLSQPEGLKKTLRDEINAILQKRIMVLDGGMGTMIQREKLNEEHFRGQEFKDHA
RPLKGNNDILSITQPDVIYQIHKEYLLAGADIIETNTFSSTSIAQADYGLEHLAYRMNMC
SAGVARKAAEEVTLQTGIKRFVAGALGPTNKTLSVSPSVERPDYRNITFDELVEAYQEQA
KGLLDGGVDILLIETIFDTANAKAALFALQNLFEEKYAPRPIFISGTIVDKSGRTLSGQT
GEGFVISVSHGEPLCIGLNCALGAAEMRPFIEIIGKCTTAYVLCYPNAGLPNTFGDYDET
PSMMAKHLKDFAMDGLVNIVGGCCGSTPDHIREIAEAVKNCKPRVPPATAFEGHMLLSGL
EPFRIGPYTNFVNIGERCNVAGSRKFAKLIMAGNYEEALCVAKVQVEMGAQVLDVNMDDG
MLDGPSAMTRFCNLIASEPDIAKVPLCIDSSNFAVIEAGLKCCQGKCIVNSISLKEGEDD
FLEKARKIKKYGAAMVVMAFDEEGQATETDTKIRVCTRAYHLLVKKLGFNPNDIIFDPNI
LTIGTGMEEHNLYAINFIHATKVIKETLPGARISGGLSNLSFSFRGMEAIREAMHGVFLY
HAIKSGMDMGIVNAGNLPVYDDIHKELLQLCEDLIWNKDPEATEKLLRYAQTQGTGGKKV
IQTDEWRNGPVEERLEYALVKGIEKHIIEDTEEARLNQKKYPRPLNIIEGPLMNGMKIVG
DLFGAGKMFLPQVIKSARVMKKAVGHLIPFMEKEREETRVLNGTVEEEDPYQGTIVLATV
KGDVHDIGKNIVGVVLGCNNFRVIDLGVMTPCDKILKAALDHKADIIGLSGLITPSLDEM
IFVAKEMERLAIRIPLLIGGATTSKTHTAVKIAPRYSAPVIHVLDASKSVVVCSQLLDEN
LKDEYFEEIMEEYEDIRQDHYESLKERRYLPLSQARKSGFQMDWLSEPHPVKPTFIGTQV
FEDYDLQKLVDYIDWKPFFDVWQLRGKYPNRGFPKIFNDKTVGGEARKVYDDAHNMLNTL
ISQKKLRARGVVGFWPAQSIQDDIHLYAEAAVPQAAEPIATFYGLRQQAEKDSASTEPYY
CLSDFIAPLHSGIRDYLGLFAVACFGVEELSKAYEDDGDDYSSIMVKALGDRLAEAFAEE
LHERVRRELWAYCGSEQLDVADLRRLRYKGIRPAPGYPSQPDHTEKLTMWRLADIEQSTG
IRLTESLAMAPASAVSGLYFSNLKSKYFAVGKISKDQVEDYALRKNISVAEVEKWLGPIL
GYDTD
|
| Enzyme 1 Number of Residues |
1265 |
| Enzyme 1 Molecular Weight |
140525.9 |
| Enzyme 1 Theoretical pI |
5.27 |
| Enzyme 1 GO Classification |
| Function |
- S-methyltransferase activity
- binding
- catalytic activity
- cation binding
- cobalamin binding
- homocysteine S-methyltransferase activity
- ion binding
- metal ion binding
- methionine synthase activity
- methyltransferase activity
- transferase activity
- transferase activity, transferring one-carbon groups
- transition metal ion binding
- vitamin binding
- zinc ion binding
|
| Process |
- cellular amino acid and derivative metabolic process
- cellular amino acid metabolic process
- cellular aromatic compound metabolic process
- cellular metabolic process
- metabolic process
- methionine biosynthetic process
- pteridine and derivative metabolic process
- sulfur amino acid biosynthetic process
- sulfur amino acid metabolic process
|
| Component |
|
|
| Enzyme 1 General Function |
Involved in cobalamin binding |
| Enzyme 1 Specific Function |
Catalyzes the transfer of a methyl group from methyl- cobalamin to homocysteine, yielding enzyme-bound cob(I)alamin and methionine. Subsequently, remethylates the cofactor using methyltetrahydrofolate |
| Enzyme 1 Pathways |
|
| Enzyme 1 Reactions |
- 5-methyltetrahydrofolate + L-homocysteine = tetrahydrofolate + L-methionine [RN:R00946]
|
| Enzyme 1 Pfam Domain Function |
|
| Enzyme 1 Signals |
|
| Enzyme 1 Transmembrane Regions |
|
| Enzyme 1 Essentiality |
Not Available |
| Enzyme 1 GenBank ID Protein |
Not Available |
| Enzyme 1 UniProtKB/Swiss-Prot ID |
Q99707  |
| Enzyme 1 UniProtKB/Swiss-Prot Entry Name |
METH_HUMAN  |
| Enzyme 1 PDB ID |
Not Available |
| Enzyme 1 Cellular Location |
Not Available |
| Enzyme 1 Gene Sequence |
>3798 bp
ATGTCACCCGCGCTCCAAGACCTGTCGCAACCCGAAGGTCTGAAGAAAACCCTGCGGGAT
GAGATCAATGCCATTCTGCAGAAGAGGATTATGGTGCTGGATGGAGGGATGGGGACCATG
ATCCAGCGGGAGAAGCTAAACGAAGAACACTTCCGAGGTCAGGAATTTAAAGATCATGCC
AGGCCGCTGAAAGGCAACAATGACATTTTAAGTATAACTCAGCCTGATGTCATTTACCAA
ATCCATAAGGAATACTTGCTGGCTGGGGCAGATATCATTGAAACAAATACTTTTAGCAGC
ACTAGTATTGCCCAAGCTGACTATGGCCTTGAACACTTGGCCTACCGGATGAACATGTGC
TCTGCAGGAGTGGCCAGAAAAGCTGCCGAGGAGGTAACTCTCCAGACAGGAATTAAGAGG
TTTGTGGCAGGGGCTCTGGGTCCGACTAATAAGACACTCTCTGTGTCCCCATCTGTGGAA
AGGCCGGATTATAGGAACATCACATTTGATGAGCTTGTTGAAGCATACCAAGAGCAGGCC
AAAGGACTTCTGGATGGCGGGGTTGATATCTTACTCATTGAAACTATTTTTGATACTGCC
AATGCCAAGGCAGCCTTGTTTGCACTCCAAAATCTTTTTGAGGAGAAATATGCTCCCCGG
CCTATCTTTATTTCAGGGACGATCGTTGATAAAAGTGGGCGGACTCTTTCCGGACAGACA
GGAGAGGGATTTGTCATCAGCGTGTCTCATGGAGAACCACTCTGCATTGGATTAAATTGT
GCTTTGGGTGCAGCTGAGATGAGACCTTTTATTGAAATAATTGGAAAATGTACAACAGCC
TATGTCCTCTGTTATCCCAATGCAGGTCTTCCCAACACCTTTGGTGACTATGATGAAACG
CCTTCTATGATGGCCAAGCACCTAAAGGATTTTGCTATGGATGGCTTGGTCAATATAGTT
GGAGGATGCTGTGGGTCAACACCAGATCATATCAGGGAAATTGCTGAAGCTGTGAAAAAT
TGTAAGCCTAGAGTTCCACCTGCCACTGCTTTTGAAGGACATATGTTACTGTCTGGTCTA
GAGCCCTTCAGGATTGGACCGTACACCAACTTTGTTAACATTGGAGAGCGCTGTAATGTT
GCAGGATCAAGGAAGTTTGCTAAACTCATCATGGCAGGAAACTATGAAGAAGCCTTGTGT
GTTGCCAAAGTGCAGGTGGAAATGGGAGCCCAGGTGTTGGATGTCAACATGGATGATGGC
ATGCTAGATGGTCCAAGTGCAATGACCAGATTTTGCAACTTAATTGCTTCCGAGCCAGAC
ATCGCAAAGGTACCTTTGTGCATCGACTCCTCCAATTTTGCTGTGATTGAAGCTGGGTTA
AAGTGCTGCCAAGGGAAGTGCATTGTCAATAGCATTAGTCTGAAGGAAGGAGAGGACGAC
TTCTTGGAGAAGGCCAGGAAGATTAAAAAGTATGGAGCTGCTATGGTGGTCATGGCTTTT
GATGAAGAAGGACAGGCAACAGAAACAGACACAAAAATCAGAGTGTGCACCCGGGCCTAC
CATCTGCTTGTGAAAAAACTGGGCTTTAATCCAAATGACATTATTTTTGACCCTAATATC
CTAACCATTGGGACTGGAATGGAGGAACACAACTTGTATGCCATTAATTTTATCCATGCA
ACAAAAGTCATTAAAGAAACATTACCTGGAGCCAGAATAAGTGGAGGTCTTTCCAACTTG
TCCTTCTCCTTCCGAGGAATGGAAGCCATTCGAGAAGCAATGCATGGGGTTTTCCTTTAC
CATGCAATCAAGTCTGGCATGGACATGGGGATAGTGAATGCTGGAAACCTCCCTGTGTAT
GATGATATCCATAAGGAACTTCTGCAGCTCTGTGAAGATCTCATCTGGAATAAAGACCCT
GAGGCCACTGAGAAGCTCTTACGTTATGCCCAGACTCAAGGCACAGGAGGGAAGAAAGTC
ATTCAGACTGATGAGTGGAGAAATGGCCCTGTCGAAGAACGCCTTGAGTATGCCCTTGTG
AAGGGCATTGAAAAACATATTATTGAGGATACTGAGGAAGCCAGGTTAAACCAAAAAAAA
TATCCCCGACCTCTCAATATAATTGAAGGACCCCTGATGAATGGAATGAAAATTGTTGGT
GATCTTTTTGGAGCTGGAAAAATGTTTCTACCTCAGGTTATAAAGTCAGCCCGGGTTATG
AAGAAGGCTGTTGGCCACCTTATCCCTTTCATGGAAAAAGAAAGAGAAGAAACCAGAGTG
CTTAACGGCACAGTAGAAGAAGAGGACCCTTACCAGGGCACCATCGTGCTGGCCACTGTT
AAAGGCGACGTGCACGACATAGGCAAGAACATAGTTGGAGTAGTCCTTGGCTGCAATAAT
TTCCGAGTTATTGATTTAGGAGTCATGACTCCATGTGATAAGATACTGAAAGCTGCTCTT
GACCACAAAGCAGATATAATTGGCCTGTCAGGACTCATCACTCCTTCCCTGGATGAAATG
ATTTTTGTTGCCAAGGAAATGGAGAGATTAGCTATAAGGATTCCATTGTTGATTGGAGGA
GCAACCACTTCAAAAACCCACACAGCAGTTAAAATAGCTCCGAGATACAGTGCACCTGTA
ATCCATGTCCTGGACGCGTCCAAGAGTGTGGTGGTGTGTTCCCAGCTGTTAGATGAAAAT
CTAAAGGATGAATACTTTGAGGAAATCATGGAAGAATATGAAGATATTAGACAGGACCAT
TATGAGTCTCTCAAGGAGAGGAGATACTTACCCTTAAGTCAAGCCAGAAAAAGTGGTTTC
CAAATGGATTGGCTGTCTGAACCTCACCCAGTGAAGCCCACGTTTATTGGGACCCAGGTC
TTTGAAGACTATGACCTGCAGAAGCTGGTGGACTACATTGACTGGAAGCCTTTCTTTGAT
GTCTGGCAGCTCCGGGGCAAGTACCCGAATCGAGGCTTCCCCAAGATATTTAACGACAAA
ACAGTAGGTGGAGAGGCCAGGAAGGTCTACGATGATGCCCACAATATGCTGAACACACTG
ATTAGTCAAAAGAAACTCCGGGCCCGGGGTGTGGTTGGGTTCTGGCCAGCACAGAGTATC
CAAGACGACATTCACCTGTACGCAGAGGCTGCTGTGCCCCAGGCTGCAGAGCCCATAGCC
ACTTTCTATGGGTTAAGGCAACAGGCTGAGAAGGACTCTGCCAGCACGGAGCCATACTAC
TGCCTCTCAGACTTCATCGCTCCCTTGCATTCTGGCATCCGTGACTACCTGGGCCTGTTT
GCCGTTGCCTGCTTTGGGGTAGAAGAGCTGAGCAAGGCCTATGAGGATGATGGTGACGAC
TACAGCAGCATCATGGTCAAGGCGCTGGGGGACCGGCTGGCAGAGGCCTTTGCAGAAGAG
CTCCATGAAAGAGTTCGCCGAGAACTGTGGGCCTACTGTGGCAGTGAGCAGCTGGACGTC
GCAGACCTGCGAAGGTTGCGGTACAAGGGCATCCGCCCGGCTCCTGGCTACCCCAGCCAG
CCCGACCACACCGAGAAGCTCACCATGTGGAGACTCGCAGACATCGAGCAGTCTACAGGC
ATTAGGTTAACAGAATCATTAGCAATGGCACCTGCTTCAGCAGTCTCAGGCCTCTACTTC
TCCAATTTGAAGTCCAAATATTTTGCTGTGGGGAAGATTTCCAAGGATCAGGTTGAGGAT
TATGCATTGAGGAAGAACATATCTGTGGCTGAGGTTGAGAAATGGCTTGGACCCATTTTG
GGATATGATACAGACTAA
|
| Enzyme 1 GenBank Gene ID |
U71285  |
| Enzyme 1 GeneCard ID |
MTR  |
| Enzyme 1 GenAtlas ID |
MTR  |
| Enzyme 1 HGNC ID |
HGNC:7468  |
| Enzyme 1 Chromosome Location |
1 |
| Enzyme 1 Locus |
1q43 |
| Enzyme 1 SNPs |
SNPJam Report  |
| Enzyme 1 General References |
- Leclerc D, Campeau E, Goyette P, Adjalla CE, Christensen B, Ross M, Eydoux P, Rosenblatt DS, Rozen R, Gravel RA: Human methionine synthase: cDNA cloning and identification of mutations in patients of the cblG complementation group of folate/cobalamin disorders. Hum Mol Genet. 1996 Dec;5(12):1867-74. [PubMed
]
- Li YN, Gulati S, Baker PJ, Brody LC, Banerjee R, Kruger WD: Cloning, mapping and RNA analysis of the human methionine synthase gene. Hum Mol Genet. 1996 Dec;5(12):1851-8. [PubMed
]
- Chen LH, Liu ML, Hwang HY, Chen LS, Korenberg J, Shane B: Human methionine synthase. cDNA cloning, gene localization, and expression. J Biol Chem. 1997 Feb 7;272(6):3628-34. [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
]
- Gulati S, Baker P, Li YN, Fowler B, Kruger W, Brody LC, Banerjee R: Defects in human methionine synthase in cblG patients. Hum Mol Genet. 1996 Dec;5(12):1859-65. [PubMed
]
- Doolin MT, Barbaux S, McDonnell M, Hoess K, Whitehead AS, Mitchell LE: Maternal genetic effects, exerted by genes involved in homocysteine remethylation, influence the risk of spina bifida. Am J Hum Genet. 2002 Nov;71(5):1222-6. Epub 2002 Oct 9. [PubMed
]
- O'Leary VB, Mills JL, Pangilinan F, Kirke PN, Cox C, Conley M, Weiler A, Peng K, Shane B, Scott JM, Parle-McDermott A, Molloy AM, Brody LC: Analysis of methionine synthase reductase polymorphisms for neural tube defects risk association. Mol Genet Metab. 2005 Jul;85(3):220-7. Epub 2005 Mar 17. [PubMed
]
|
| Enzyme 1 Metabolite References |
Not Available |
|
Enzyme 2
[top]
|
| Enzyme 2 ID |
5420 |
| Enzyme 2 Name |
Methylenetetrahydrofolate reductase |
| Enzyme 2 Synonyms |
Not Available |
| Enzyme 2 Gene Name |
MTHFR |
| Enzyme 2 Protein Sequence |
>Methylenetetrahydrofolate reductase
MVNEARGNSSLNPCLEGSASSGSESSKDSSRCSTPGLDPERHERLREKMRRRLESGDKWF
SLEFFPPRTAEGAVNLISRFDRMAAGGPLYIDVTWHPAGDPGSDKETSSMMIASTAVNYC
GLETILHMTCCRQRLEEITGHLHKAKQLGLKNIMALRGDPIGDQWEEEEGGFNYAVDLVK
HIRSEFGDYFDICVAGYPKGHPEAGSFEADLKHLKEKVSAGADFIITQLFFEADTFFRFV
KACTDMGITCPIVPGIFPIQGYHSLRQLVKLSKLEVPQEIKDVIEPIKDNDAAIRNYGIE
LAVSLCQELLASGLVPGLHFYTLNREMATTEVLKRLGMWTEDPRRPLPWALSAHPKRREE
DVRPIFWASRPKSYIYRTQEWDEFPNGRWGNSSSPAFGELKDYYLFYLKSKSPKEELLKM
WGEELTSEESVFEVFVLYLSGEPNRNGHKVTCLPWNDEPLAAETSLLKEELLRVNRQGIL
TINSQPNINGKPSSDPIVGWGPSGGYVFQKAYLEFFTSRETAEALLQVLKKYELRVNYHL
VNVKGENITNAPELQPNAVTWGIFPGREIIQPTVVDPVSFMFWKDEAFALWIERWGKLYE
EESPSRTIIQYIHDNYFLVNLVDNDFPLDNCLWQVVEDTLELLNRPTQNARETEAP
|
| Enzyme 2 Number of Residues |
656 |
| Enzyme 2 Molecular Weight |
74595.9 |
| Enzyme 2 Theoretical pI |
5.00 |
| Enzyme 2 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 2 General Function |
Involved in methylenetetrahydrofolate reductase (NADPH) activity |
| Enzyme 2 Specific Function |
Catalyzes the conversion of 5,10- methylenetetrahydrofolate to 5-methyltetrahydrofolate, a co- substrate for homocysteine remethylation to methionine |
| Enzyme 2 Pathways |
|
| Enzyme 2 Reactions |
- 5-methyltetrahydrofolate + NAD(P)+ = 5,10-methylenetetrahydrofolate + NAD(P)H + H+ [RN:R01224 R07168]
|
| Enzyme 2 Pfam Domain Function |
|
| Enzyme 2 Signals |
|
| Enzyme 2 Transmembrane Regions |
|
| Enzyme 2 Essentiality |
Not Available |
| Enzyme 2 GenBank ID Protein |
6139053  |
| Enzyme 2 UniProtKB/Swiss-Prot ID |
P42898  |
| Enzyme 2 UniProtKB/Swiss-Prot Entry Name |
MTHR_HUMAN  |
| Enzyme 2 PDB ID |
Not Available |
| Enzyme 2 Cellular Location |
Not Available |
| Enzyme 2 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 2 GenBank Gene ID |
U09806  |
| Enzyme 2 GeneCard ID |
MTHFR  |
| Enzyme 2 GenAtlas ID |
MTHFR  |
| Enzyme 2 HGNC ID |
HGNC:7436  |
| Enzyme 2 Chromosome Location |
1 |
| Enzyme 2 Locus |
1p36.3 |
| Enzyme 2 SNPs |
SNPJam Report  |
| Enzyme 2 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
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- 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
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- 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
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- 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
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- 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
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- 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
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- 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 2 Metabolite References |
Not Available |
|
Enzyme 3
[top]
|
| Enzyme 3 ID |
5566 |
| Enzyme 3 Name |
Trifunctional purine biosynthetic protein adenosine-3 |
| Enzyme 3 Synonyms |
- Phosphoribosylamine--glycine ligase
- Glycinamide ribonucleotide synthetase
- GARS
- Phosphoribosylglycinamide synthetase
- Phosphoribosylformylglycinamidine cyclo-ligase
- AIR synthase
- AIRS
- Phosphoribosyl-aminoimidazole synthetase
- Phosphoribosylglycinamide formyltransferase
- 5'-phosphoribosylglycinamide transformylase
- GAR transformylase
- GART
|
| Enzyme 3 Gene Name |
GART |
| Enzyme 3 Protein Sequence |
>Trifunctional purine biosynthetic protein adenosine-3
MAARVLIIGSGGREHTLAWKLAQSHHVKQVLVAPGNAGTACSEKISNTAISISDHTALAQ
FCKEKKIEFVVVGPEAPLAAGIVGNLRSAGVQCFGPTAEAAQLESSKRFAKEFMDRHGIP
TAQWKAFTKPEEACSFILSADFPALVVKASGLAAGKGVIVAKSKEEACKAVQEIMQEKAF
GAAGETIVIEELLDGEEVSCLCFTDGKTVAPMPPAQDHKRLLEGDGGPNTGGMGAYCPAP
QVSNDLLLKIKDTVLQRTVDGMQQEGTPYTGILYAGIMLTKNGPKVLEFNCRFGDPECQV
ILPLLKSDLYEVIQSTLDGLLCTSLPVWLENHTALTVVMASKGYPGDYTKGVEITGFPEA
QALGLEVFHAGTALKNGKVVTHGGRVLAVTAIRENLISALEEAKKGLAAIKFEGAIYRKD
VGFRAIAFLQQPRSLTYKESGVDIAAGNMLVKKIQPLAKATSRSGCKVDLGGFAGLFDLK
AAGFKDPLLASGTDGVGTKLKIAQLCNKHDTIGQDLVAMCVNDILAQGAEPLFFLDYFSC
GKLDLSVTEAVVAGIAKACGKAGCALLGGETAEMPDMYPPGEYDLAGFAVGAMERDQKLP
HLERITEGDVVVGIASSGLHSNGFSLVRKIVAKSSLQYSSPAPDGCGDQTLGDLLLTPTR
IYSHSLLPVLRSGHVKAFAHITGGGLLENIPRVLPEKLGVDLDAQTWRIPRVFSWLQQEG
HLSEEEMARTFNCGVGAVLVVSKEQTEQILRDIQQHKEEAWVIGSVVARAEGSPRVKVKN
LIESMQINGSVLKNGSLTNHFSFEKKKARVAVLISGTGSNLQALIDSTREPNSSAQIDIV
ISNKAAVAGLDKAERAGIPTRVINHKLYKNRVEFDSAIDLVLEEFSIDIVCLAGFMRILS
GPFVQKWNGKMLNIHPSLLPSFKGSNAHEQALETGVTVTGCTVHFVAEDVDAGQIILQEA
VPVKRGDTVATLSERVKLAEHKIFPAALQLVASGTVQLGENGKICWVKEE
|
| Enzyme 3 Number of Residues |
1010 |
| Enzyme 3 Molecular Weight |
107766.3 |
| Enzyme 3 Theoretical pI |
6.68 |
| Enzyme 3 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- adenyl ribonucleotide binding
- binding
- catalytic activity
- cyclo-ligase activity
- glycine hydroxymethyltransferase activity
- hydroxymethyl-, formyl- and related transferase activity
- ligase activity
- ligase activity, forming carbon-nitrogen bonds
- methyltransferase activity
- nucleoside binding
- phosphoribosylamine-glycine ligase activity
- phosphoribosylformylglycinamidine cyclo-ligase activity
- phosphoribosylglycinamide formyltransferase activity
- purine nucleoside binding
- transferase activity
- transferase activity, transferring one-carbon groups
|
| Process |
- 'de novo' IMP biosynthetic process
- IMP biosynthetic process
- biosynthetic process
- cellular aromatic compound metabolic process
- cellular metabolic process
- cellular nitrogen compound metabolic process
- metabolic process
- nitrogen compound metabolic process
- nucleobase metabolic process
- nucleobase, nucleoside and nucleotide metabolic process
- nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
- nucleoside phosphate metabolic process
- nucleotide metabolic process
- purine base biosynthetic process
- purine base metabolic process
- purine nucleoside monophosphate biosynthetic process
- purine nucleotide biosynthetic process
- purine nucleotide metabolic process
- purine ribonucleoside monophosphate biosynthetic process
|
| Component |
- cell part
- cytoplasm
- intracellular part
|
|
| Enzyme 3 General Function |
Involved in catalytic activity |
| Enzyme 3 Specific Function |
ATP + 5-phospho-D-ribosylamine + glycine = ADP + phosphate + N(1)-(5-phospho-D-ribosyl)glycinamide |
| Enzyme 3 Pathways |
|
| Enzyme 3 Reactions |
- ATP + 5-phospho-D-ribosylamine + glycine = ADP + phosphate + N1-(5-phospho-D-ribosyl)glycinamide [RN:R04144]
|
| Enzyme 3 Pfam Domain Function |
|
| Enzyme 3 Signals |
|
| Enzyme 3 Transmembrane Regions |
|
| Enzyme 3 Essentiality |
Not Available |
| Enzyme 3 GenBank ID Protein |
31642  |
| Enzyme 3 UniProtKB/Swiss-Prot ID |
P22102  |
| Enzyme 3 UniProtKB/Swiss-Prot Entry Name |
PUR2_HUMAN  |
| Enzyme 3 PDB ID |
Not Available |
| Enzyme 3 Cellular Location |
Not Available |
| Enzyme 3 Gene Sequence |
>3033 bp
ATGGCAGCCCGAGTACTTATAATTGGCAGTGGAGGAAGGGAACATACGCTGGCCTGGAAA
CTTGCACAGTCTCATCATGTCAAACAAGTGTTGGTTGCCCCAGGAAACGCAGGCACTGCC
TGCTCTGAAAAGATTTCAAATACCGCCATCTCAATCAGTGACCACACTGCCCTTGCTCAA
TTCTGCAAAGAGAAGAAAATTGAATTTGTAGTTGTTGGACCAGAAGCACCTCTGGCTGCT
GGGATTGTTGGGAACCTGAGGTCTGCAGGAGTGCAATGCTTTGGCCCAACAGCAGAAGCG
GCTCAGTTAGAGTCCAGCAAAAGGTTTGCCAAAGAGTTTATGGACAGACATGGAATCCCA
ACCGCACAATGGAAGGCTTTCACCAAACCTGAAGAAGCCTGCAGCTTCATTTTGAGTGCA
GACTTCCCTGCTTTGGTTGTGAAGGCCAGTGGTCTTGCAGCTGGAAAAGGGGTGATTGTT
GCAAAGAGCAAAGAAGAGGCCTGCAAAGCTGTACAAGAGATCATGCAGGAGAAAGCCTTT
GGGGCAGCTGGAGAAACAATTGTCATTGAAGAACTTCTTGACGGAGAAGAGGTGTCGTGT
CTGTGTTTCACTGATGGCAAGACTGTGGCCCCCATGCCCCCAGCACAGGACCATAAGCGA
TTACTGGAGGGAGATGGTGGCCCTAACACAGGGGGAATGGGAGCCTATTGTCCAGCCCCT
CAGGTTTCTAATGATCTATTACTAAAAATTAAAGATACTGTTCTTCAGAGGACAGTGGAT
GGCATGCAGCAAGAGGGTACTCCATATACAGGTATTCTCTATGCTGGAATAATGCTGACC
AAGAATGGCCCAAAAGTTCTAGAGTTTAATTGCCGTTTTGGTGATCCAGAGTGCCAAGTA
ATCCTCCCACTTCTTAAAAGTGATCTTTATGAAGTGATTCAGTCCACCTTAGATGGACTG
CTCTGCACATCTCTGCCTGTTTGGCTAGAAAACCACACCGCCCTAACTGTTGTCATGGCA
AGTAAAGGTTATCCTGGAGACTACACCAAGGGTGTAGAGATAACAGGGTTTCCTGAGGCT
CAAGCTCTAGGACTGGAGGTGTTCCATGCAGGCACTGCCCTCAAAAATGGCAAAGTAGTA
ACTCATGGGGGTAGAGTTCTTGCAGTCACAGCCATCCGGGAAAATCTCATATCAGCCCTT
GAGGAAGCCAAGAAAGGACTAGCTGCTATAAAGTTTGAGGGAGCAATTTATAGGAAAGAC
GTCGGCTTTCGTGCCATAGCTTTCCTCCAGCAGCCCAGGAGTTTGACTTACAAGGAATCT
GGAGTAGATATCGCAGCTGGAAATATGCTGGTCAAGAAAATTCAGCCTTTAGCAAAAGCC
ACTTCCAGATCAGGCTGTAAAGTTGATCTTGGAGGTTTTGCTGGTCTTTTTGATTTAAAA
GCAGCTGGTTTCAAAGATCCCCTTCTGGCCTCTGGAACAGATGGCGTTGGAACTAAACTA
AAGATTGCCCAGCTATGCAATAAACATGATACCATTGGTCAAGATTTGGTAGCAATGTGT
GTTAATGATATTCTGGCACAAGGAGCAGAGCCCCTCTTCTTCCTTGATTACTTTTCCTGT
GGAAAACTTGACCTCAGTGTAACTGAAGCTGTTGTTGCTGGAATTGCTAAAGCTTGTGGA
AAAGCTGGATGTGCTCTCCTTGGAGGTGAAACAGCAGAAATGCCTGACATGTATCCCCCT
GGAGAGTATGACCTAGCTGGGTTTGCCGTTGGTGCCATGGAGCGAGATCAGAAACTCCCT
CACCTGGAAAGAATCACTGAGGGTGATGTTGTTGTTGGAATAGCTTCATCTGGTCTTCAT
AGCAATGGATTTAGCCTTGTGAGGAAAATCGTTGCAAAATCTTCCCTCCAGTACTCCTCT
CCAGCACCTGATGGTTGTGGTGACCAGACTTTAGGGGACTTACTTCTCACGCCTACCAGA
ATCTACAGCCATTCACTGTTACCTGTCCTACGTTCAGGACATGTCAAAGCCTTTGCCCAT
ATTACTGGTGGAGGATTACTAGAGAACATCCCCAGAGTCCTCCCTGAGAAACTTGGGGTA
GATTTAGATGCCCAGACCTGGAGGATCCCCAGGGTTTTCTCATGGTTGCAGCAGGAAGGA
CACCTCTCTGAGGAAGAGATGGCCAGAACATTTAACTGTGGGGTTGGCGCTGTCCTTGTG
GTATCAAAGGAGCAGACAGAGCAGATTCTGAGGGATATCCAGCAGCACAAGGAAGAAGCC
TGGGTGATTGGCAGTGTGGTTGCACGAGCTGAAGGTTCCCCACGTGTGAAAGTCAAGAAT
CTGATTGAAAGCATGCAAATAAATGGGTCAGTGTTGAAGAATGGCTCCCTGACAAATCAT
TTCTCTTTTGAAAAAAAAAAGGCCAGAGTGGCTGTCTTAATATCTGGAACAGGATCGAAC
CTGCAAGCACTTATAGACAGTACTCGGGAACCAAATAGCTCTGCACAAATTGATATTGTT
ATCTCCAACAAAGCCGCAGTAGCTGGGTTAGATAAAGCGGAAAGAGCTGGTATTCCCACT
AGAGTAATTAATCATAAACTGTATAAAAATCGTGTAGAATTTGACAGTGCAATTGACCTA
GTCCTTGAAGAGTTCTCCATAGACATAGTCTGTCTTGCAGGATTCATGAGAATTCTTTCT
GGCCCCTTTGTCCAAAAGTGGAATGGAAAAATGCTCAATATCCACCCATCCTTGCTCCCT
TCTTTTAAGGGTTCAAATGCCCATGAGCAAGCCCTGGAAACCGGAGTCACAGTTACTGGG
TGCACTGTACACTTTGTAGCTGAAGATGTGGATGCTGGACAGATTATTTTGCAAGAAGCT
GTTCCCGTGAAGAGGGGTGATACTGTCGCAACTCTTTCTGAAAGAGTAAAATTAGCAGAA
CATAAAATATTTCCTGCAGCCCTTCAGCTGGTGGCCAGTGGAACTGTACAGCTTGGAGAA
AATGGCAAGATCTGTTGGGTTAAAGAGGAATGA
|
| Enzyme 3 GenBank Gene ID |
X54199  |
| Enzyme 3 GeneCard ID |
GART  |
| Enzyme 3 GenAtlas ID |
GART  |
| Enzyme 3 HGNC ID |
HGNC:4163  |
| Enzyme 3 Chromosome Location |
2 |
| Enzyme 3 Locus |
21q22.1|21q22.11 |
| Enzyme 3 SNPs |
SNPJam Report  |
| Enzyme 3 General References |
- Aimi J, Qiu H, Williams J, Zalkin H, Dixon JE: De novo purine nucleotide biosynthesis: cloning of human and avian cDNAs encoding the trifunctional glycinamide ribonucleotide synthetase-aminoimidazole ribonucleotide synthetase-glycinamide ribonucleotide transformylase by functional complementation in E. coli. Nucleic Acids Res. 1990 Nov 25;18(22):6665-72. [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
]
- Kan JL, Moran RG: Intronic polyadenylation in the human glycinamide ribonucleotide formyltransferase gene. Nucleic Acids Res. 1997 Aug 1;25(15):3118-23. [PubMed
]
- Schild D, Brake AJ, Kiefer MC, Young D, Barr PJ: Cloning of three human multifunctional de novo purine biosynthetic genes by functional complementation of yeast mutations. Proc Natl Acad Sci U S A. 1990 Apr;87(8):2916-20. [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
]
- 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
]
- Zhang Y, Desharnais J, Greasley SE, Beardsley GP, Boger DL, Wilson IA: Crystal structures of human GAR Tfase at low and high pH and with substrate beta-GAR. Biochemistry. 2002 Dec 3;41(48):14206-15. [PubMed
]
- Zhang Y, Desharnais J, Marsilje TH, Li C, Hedrick MP, Gooljarsingh LT, Tavassoli A, Benkovic SJ, Olson AJ, Boger DL, Wilson IA: Rational design, synthesis, evaluation, and crystal structure of a potent inhibitor of human GAR Tfase: 10-(trifluoroacetyl)-5,10-dideazaacyclic-5,6,7,8-tetrahydrofolic acid. Biochemistry. 2003 May 27;42(20):6043-56. [PubMed
]
- Dahms TE, Sainz G, Giroux EL, Caperelli CA, Smith JL: The apo and ternary complex structures of a chemotherapeutic target: human glycinamide ribonucleotide transformylase. Biochemistry. 2005 Jul 26;44(29):9841-50. [PubMed
]
|
| Enzyme 3 Metabolite References |
Not Available |
|
Enzyme 4
[top]
|
| Enzyme 4 ID |
5959 |
| Enzyme 4 Name |
Formimidoyltransferase-cyclodeaminase |
| Enzyme 4 Synonyms |
- Formiminotransferase-cyclodeaminase
- FTCD
- LCHC1
- Glutamate formimidoyltransferase
- Glutamate formiminotransferase
- Glutamate formyltransferase
- Formimidoyltetrahydrofolate cyclodeaminase
- Formiminotetrahydrofolate cyclodeaminase
|
| Enzyme 4 Gene Name |
FTCD |
| Enzyme 4 Protein Sequence |
>Formimidoyltransferase-cyclodeaminase
MSQLVECVPNFSEGKNQEVIDAISGAITQTPGCVLLDVDAGPSTNRTVYTFVGPPECVVE
GALNAARVASRLIDMSRHQGEHPRMGALDVCPFIPVRGVSVDECVLCAQAFGQRLAEELD
VPVYLYGEAARMDSRRTLPAIRAGEYEALPKKLQQADWAPDFGPSSFVPSWGATATGARK
FLIAFNINLLGTKEQAHRIALNLREQGRGKDQPGRLKKVQGIGWYLDEKNLAQVSTNLLD
FEVTALHTVYEETCREAQELSLPVVGSQLVGLVPLKALLDAAAFYCEKENLFILEEEQRI
RLVVSRLGLDSLCPFSPKERIIEYLVPERGPERGLGSKSLRAFVGEVGARSAAPGGGSVA
AAAAAMGAALGSMVGLMTYGRRQFQSLDTTMRRLIPPFREASAKLTTLVDADAEAFTAYL
EAMRLPKNTPEEKDRRTAALQEGLRRAVSVPLTLAETVASLWPALQELARCGNLACRSDL
QVAAKALEMGVFGAYFNVLINLRDITDEAFKDQIHHRVSSLLQEAKTQAALVLDCLETRQ
E
|
| Enzyme 4 Number of Residues |
541 |
| Enzyme 4 Molecular Weight |
58925.9 |
| Enzyme 4 Theoretical pI |
5.45 |
| Enzyme 4 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 4 General Function |
Involved in catalytic activity |
| Enzyme 4 Specific Function |
Binds and promotes bundling of vimentin filaments originating from the Golgi |
| Enzyme 4 Pathways |
|
| Enzyme 4 Reactions |
- 5-formimidoyltetrahydrofolate = 5,10-methenyltetrahydrofolate + NH3 [RN:R02302]
|
| Enzyme 4 Pfam Domain Function |
|
| Enzyme 4 Signals |
|
| Enzyme 4 Transmembrane Regions |
|
| Enzyme 4 Essentiality |
Not Available |
| Enzyme 4 GenBank ID Protein |
6537208  |
| Enzyme 4 UniProtKB/Swiss-Prot ID |
O95954  |
| Enzyme 4 UniProtKB/Swiss-Prot Entry Name |
FTCD_HUMAN  |
| Enzyme 4 PDB ID |
Not Available |
| Enzyme 4 Cellular Location |
Not Available |
| Enzyme 4 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 4 GenBank Gene ID |
AF169017  |
| Enzyme 4 GeneCard ID |
FTCD  |
| Enzyme 4 GenAtlas ID |
FTCD  |
| Enzyme 4 HGNC ID |
HGNC:3974  |
| Enzyme 4 Chromosome Location |
2 |
| Enzyme 4 Locus |
21q22.3 |
| Enzyme 4 SNPs |
SNPJam Report  |
| Enzyme 4 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 4 Metabolite References |
Not Available |
|
Enzyme 5
[top]
|
| Enzyme 5 ID |
5961 |
| Enzyme 5 Name |
Aminomethyltransferase, mitochondrial |
| Enzyme 5 Synonyms |
- Glycine cleavage system T protein
- GCVT
|
| Enzyme 5 Gene Name |
AMT |
| Enzyme 5 Protein Sequence |
>Aminomethyltransferase, mitochondrial
MQRAVSVVARLGFRLQAFPPALCRPLSCAQEVLRRTPLYDFHLAHGGKMVAFAGWSLPVQ
YRDSHTDSHLHTRQHCSLFDVSHMLQTKILGSDRVKLMESLVVGDIAELRPNQGTLSLFT
NEAGGILDDLIVTNTSEGHLYVVSNAGCWEKDLALMQDKVRELQNQGRDVGLEVLDNALL
ALQGPTAAQVLQAGVADDLRKLPFMTSAVMEVFGVSGCRVTRCGYTGEDGVEISVPVAGA
VHLATAILKNPEVKLAGLAARDSLRLEAGLCLYGNDIDEHTTPVEGSLSWTLGKRRRAAM
DFPGAKVIVPQLKGRVQRRRVGLMCEGAPMRAHSPILNMEGTKIGTVTSGCPSPSLKKNV
AMGYVPCEYSRPGTMLLVEVRRKQQMAVVSKMPFVPTNYYTLK
|
| Enzyme 5 Number of Residues |
403 |
| Enzyme 5 Molecular Weight |
43945.7 |
| Enzyme 5 Theoretical pI |
8.69 |
| Enzyme 5 GO Classification |
| Function |
- aminomethyltransferase activity
- catalytic activity
- methyltransferase activity
- transferase activity
- transferase activity, transferring one-carbon groups
|
| Process |
- cellular amino acid and derivative metabolic process
- cellular amino acid metabolic process
- cellular metabolic process
- glycine catabolic process
- glycine metabolic process
- metabolic process
- serine family amino acid metabolic process
|
| Component |
- cell part
- cytoplasm
- intracellular part
|
|
| Enzyme 5 General Function |
Involved in aminomethyltransferase activity |
| Enzyme 5 Specific Function |
The glycine cleavage system catalyzes the degradation of glycine |
| Enzyme 5 Pathways |
- Glycine, Serine and Threonine Metabolism (map00260
)
- Nitrogen Metabolism (map00910
)
- One Carbon Pool By Folate (map00670
)
|
| Enzyme 5 Reactions |
- [protein]-S8-aminomethyldihydrolipoyllysine + tetrahydrofolate = [protein]-dihydrolipoyllysine + 5,10-methylenetetrahydrofolate + NH3 [RN:R04125]
|
| Enzyme 5 Pfam Domain Function |
|
| Enzyme 5 Signals |
|
| Enzyme 5 Transmembrane Regions |
|
| Enzyme 5 Essentiality |
Not Available |
| Enzyme 5 GenBank ID Protein |
158254632  |
| Enzyme 5 UniProtKB/Swiss-Prot ID |
P48728  |
| Enzyme 5 UniProtKB/Swiss-Prot Entry Name |
GCST_HUMAN  |
| Enzyme 5 PDB ID |
Not Available |
| Enzyme 5 Cellular Location |
Not Available |
| Enzyme 5 Gene Sequence |
>1212 bp
ATGCAGAGGGCTGTAAGTGTGGTGGCCCGTCTGGGCTTTCGCCTGCAGGCATTCCCCCCG
GCCTTGTGTCGTCCACTTAGTTGCGCACAGGAGGTGCTCCGCAGGACACCGCTCTATGAC
TTCCACCTGGCCCACGGCGGGAAAATGGTGGCGTTTGCGGGTTGGAGTCTGCCAGTGCAG
TACCGGGACAGTCACACTGACTCGCACCTGCACACACGCCAGCACTGCTCGCTCTTTGAC
GTGTCTCATATGCTGCAGACCAAGATACTTGGTAGTGACCGGGTGAAGCTGATGGAGAGT
CTAGTGGTTGGAGACATTGCAGAGCTAAGACCAAACCAGGGGACACTGTCGCTGTTTACC
AACGAGGCTGGAGGCATCTTAGATGACTTGATTGTAACCAATACTTCTGAGGGCCACCTG
TATGTGGTGTCCAACGCTGGCTGCTGGGAGAAAGATTTGGCCCTCATGCAGGACAAGGTC
AGGGAGCTTCAGAACCAGGGCAGAGATGTGGGCCTGGAGGTGTTGGATAATGCCCTGCTA
GCTCTGCAAGGCCCCACTGCAGCCCAGGTACTACAGGCCGGCGTGGCAGATGACCTGAGG
AAACTGCCCTTCATGACCAGTGCTGTGATGGAGGTGTTTGGCGTGTCTGGCTGCCGCGTG
ACCCGCTGTGGCTACACAGGAGAGGATGGTGTGGAGATCTCGGTGCCGGTAGCGGGGGCA
GTTCACCTGGCAACAGCTATTCTGAAAAACCCAGAGGTGAAGCTGGCAGGGCTGGCAGCC
AGGGACAGCCTGCGCCTGGAGGCAGGCCTCTGCCTGTATGGGAATGACATTGATGAACAC
ACTACACCTGTGGAGGGCAGCCTCAGTTGGACACTGGGGAAGCGCCGCCGAGCTGCTATG
GACTTCCCTGGAGCCAAGGTCATTGTTCCCCAGCTGAAGGGCAGGGTGCAGCGGAGGCGT
GTGGGGTTGATGTGTGAGGGGGCCCCCATGCGGGCACACAGTCCCATCCTGAACATGGAG
GGTACCAAGATTGGTACTGTGACTAGTGGCTGCCCCTCCCCCTCTCTGAAGAAGAATGTG
GCGATGGGTTATGTGCCCTGCGAGTACAGTCGTCCAGGGACAATGCTGCTGGTAGAGGTG
CGGCGGAAGCAGCAGATGGCTGTAGTCAGCAAGATGCCCTTTGTGCCCACAAACTACTAT
ACCCTCAAGTGA
|
| Enzyme 5 GenBank Gene ID |
AK290600  |
| Enzyme 5 GeneCard ID |
AMT  |
| Enzyme 5 GenAtlas ID |
AMT  |
| Enzyme 5 HGNC ID |
HGNC:473  |
| Enzyme 5 Chromosome Location |
3 |
| Enzyme 5 Locus |
3p21.2-p21.1 |
| Enzyme 5 SNPs |
SNPJam Report  |
| Enzyme 5 General References |
- Hayasaka K, Nanao K, Takada G, Okamura-Ikeda K, Motokawa Y: Isolation and sequence determination of cDNA encoding human T-protein of the glycine cleavage system. Biochem Biophys Res Commun. 1993 Apr 30;192(2):766-71. [PubMed
]
- Nanao K, Takada G, Takahashi E, Seki N, Komatsu Y, Okamura-Ikeda K, Motokawa Y, Hayasaka K: Structure and chromosomal localization of the aminomethyltransferase gene (AMT) Genomics. 1994 Jan 1;19(1):27-30. [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
]
- Nanao K, Okamura-Ikeda K, Motokawa Y, Danks DM, Baumgartner ER, Takada G, Hayasaka K: Identification of the mutations in the T-protein gene causing typical and atypical nonketotic hyperglycinemia. Hum Genet. 1994 Jun;93(6):655-8. [PubMed
]
- Kure S, Mandel H, Rolland MO, Sakata Y, Shinka T, Drugan A, Boneh A, Tada K, Matsubara Y, Narisawa K: A missense mutation (His42Arg) in the T-protein gene from a large Israeli-Arab kindred with nonketotic hyperglycinemia. Hum Genet. 1998 Apr;102(4):430-4. [PubMed
]
- Kure S, Shinka T, Sakata Y, Osamu N, Takayanagi M, Tada K, Matsubara Y, Narisawa K: A one-base deletion (183delC) and a missense mutation (D276H) in the T-protein gene from a Japanese family with nonketotic hyperglycinemia. J Hum Genet. 1998;43(2):135-7. [PubMed
]
- Toone JR, Applegarth DA, Coulter-Mackie MB, James ER: Biochemical and molecular investigations of patients with nonketotic hyperglycinemia. Mol Genet Metab. 2000 Jun;70(2):116-21. [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
]
|
| Enzyme 5 Metabolite References |
Not Available |
|
Enzyme 6
[top]
|
| Enzyme 6 ID |
6070 |
| Enzyme 6 Name |
Dihydrofolate reductase |
| Enzyme 6 Synonyms |
Not Available |
| Enzyme 6 Gene Name |
DHFR |
| Enzyme 6 Protein Sequence |
>Dihydrofolate reductase
MVGSLNCIVAVSQNMGIGKNGDLPWPPLRNEFRYFQRMTTTSSVEGKQNLVIMGKKTWFS
IPEKNRPLKGRINLVLSRELKEPPQGAHFLSRSLDDALKLTEQPELANKVDMVWIVGGSS
VYKEAMNHPGHLKLFVTRIMQDFESDTFFPEIDLEKYKLLPEYPGVLSDVQEEKGIKYKF
EVYEKND
|
| Enzyme 6 Number of Residues |
187 |
| Enzyme 6 Molecular Weight |
21452.6 |
| Enzyme 6 Theoretical pI |
7.60 |
| Enzyme 6 GO Classification |
| Function |
- NADP or NADPH binding
- binding
- catalytic activity
- dihydrofolate reductase activity
- nucleotide binding
- 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
- cellular nitrogen compound metabolic process
- glycine biosynthetic process
- glycine metabolic process
- metabolic process
- nitrogen compound metabolic process
- nucleobase, nucleoside and nucleotide metabolic process
- nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
- nucleoside phosphate metabolic process
- nucleotide biosynthetic process
- nucleotide metabolic process
- oxidation reduction
- serine family amino acid metabolic process
|
| Component |
| — |
|
| Enzyme 6 General Function |
Involved in dihydrofolate reductase activity |
| Enzyme 6 Specific Function |
Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis |
| Enzyme 6 Pathways |
- Folate and Pterine Biosynthesis (map00790
)
- One Carbon Pool By Folate (map00670
)
|
| Enzyme 6 Reactions |
- 5,6,7,8-tetrahydrofolate + NADP+ = 7,8-dihydrofolate + NADPH + H+ [RN:R00939]
|
| Enzyme 6 Pfam Domain Function |
|
| Enzyme 6 Signals |
|
| Enzyme 6 Transmembrane Regions |
|
| Enzyme 6 Essentiality |
Not Available |
| Enzyme 6 GenBank ID Protein |
182724  |
| Enzyme 6 UniProtKB/Swiss-Prot ID |
P00374  |
| Enzyme 6 UniProtKB/Swiss-Prot Entry Name |
DYR_HUMAN  |
| Enzyme 6 PDB ID |
1MVT  |
| Enzyme 6 PDB File |
Show |
| Enzyme 6 3D Structure |
|
| Enzyme 6 Cellular Location |
Not Available |
| Enzyme 6 Gene Sequence |
>564 bp
ATGGTTGGTTCGCTAAACTGCATCGTCGCTGTGTCCCAGAACATGGGCATCGGCAAGAAC
GGGGACCTGCCCTGGCCACCGCTCAGGAATGAATTCAGATATTTCCAGAGAATGACCACA
ACCTCTTCAGTAGAAGGTAAACAGAATCTGGTGATTATGGGTAAGAAGACCTGGTTCTCC
ATTCCTGAGAAGAATCGACCTTTAAAGGGTAGAATTAATTTAGTTCTCAGCAGAGAACTC
AAGGAACCTCCACAAGGAGCTCATTTTCTTTCCAGAAGTCTAGATGATGCCTTAAAACTT
ACTGAACAACCAGAATTAGCAAATAAAGTAGACATGGTCTGGATAGTTGGTGGCAGTTCT
GTTTATAAGGAAGCCATGAATCACCCAGGCCATCTTAAACTATTTGTGACAAGGATCATG
CAAGACTTTGAAAGTGACACGTTTTTTCCAGAAATTGATTTGGAGAAATATAAACTTCTG
CCAGAATACCCAGGTGTTCTCTCTGATGTCCAGGAGGAGAAAGGCATTAAGTACAAATTT
GAAGTATATGAGAAGAATGATTAA
|
| Enzyme 6 GenBank Gene ID |
J00140  |
| Enzyme 6 GeneCard ID |
DHFR  |
| Enzyme 6 GenAtlas ID |
DHFR  |
| Enzyme 6 HGNC ID |
HGNC:2861  |
| Enzyme 6 Chromosome Location |
5 |
| Enzyme 6 Locus |
5q11.2-q13.2 |
| Enzyme 6 SNPs |
SNPJam Report  |
| Enzyme 6 General References |
- Chen MJ, Shimada T, Moulton AD, Cline A, Humphries RK, Maizel J, Nienhuis AW: The functional human dihydrofolate reductase gene. J Biol Chem. 1984 Mar 25;259(6):3933-43. [PubMed
]
- Masters JN, Attardi G: The nucleotide sequence of the cDNA coding for the human dihydrofolic acid reductase. Gene. 1983 Jan-Feb;21(1-2):59-63. [PubMed
]
- Yang JK, Masters JN, Attardi G: Human dihydrofolate reductase gene organization. Extensive conservation of the G + C-rich 5' non-coding sequence and strong intron size divergence from homologous mammalian genes. J Mol Biol. 1984 Jun 25;176(2):169-87. [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
]
- Oefner C, D'Arcy A, Winkler FK: Crystal structure of human dihydrofolate reductase complexed with folate. Eur J Biochem. 1988 Jun 1;174(2):377-85. [PubMed
]
- Davies JF 2nd, Delcamp TJ, Prendergast NJ, Ashford VA, Freisheim JH, Kraut J: Crystal structures of recombinant human dihydrofolate reductase complexed with folate and 5-deazafolate. Biochemistry. 1990 Oct 9;29(40):9467-79. [PubMed
]
- Stockman BJ, Nirmala NR, Wagner G, Delcamp TJ, DeYarman MT, Freisheim JH: Sequence-specific 1H and 15N resonance assignments for human dihydrofolate reductase in solution. Biochemistry. 1992 Jan 14;31(1):218-29. [PubMed
]
- Lewis WS, Cody V, Galitsky N, Luft JR, Pangborn W, Chunduru SK, Spencer HT, Appleman JR, Blakley RL: Methotrexate-resistant variants of human dihydrofolate reductase with substitutions of leucine 22. Kinetics, crystallography, and potential as selectable markers. J Biol Chem. 1995 Mar 10;270(10):5057-64. [PubMed
]
- Cody V, Galitsky N, Luft JR, Pangborn W, Rosowsky A, Blakley RL: Comparison of two independent crystal structures of human dihydrofolate reductase ternary complexes reduced with nicotinamide adenine dinucleotide phosphate and the very tight-binding inhibitor PT523. Biochemistry. 1997 Nov 11;36(45):13897-903. [PubMed
]
- Gangjee A, Vidwans AP, Vasudevan A, Queener SF, Kisliuk RL, Cody V, Li R, Galitsky N, Luft JR, Pangborn W: Structure-based design and synthesis of lipophilic 2,4-diamino-6-substituted quinazolines and their evaluation as inhibitors of dihydrofolate reductases and potential antitumor agents. J Med Chem. 1998 Aug 27;41(18):3426-34. [PubMed
]
- Klon AE, Heroux A, Ross LJ, Pathak V, Johnson CA, Piper JR, Borhani DW: Atomic structures of human dihydrofolate reductase complexed with NADPH and two lipophilic antifolates at 1.09 a and 1.05 a resolution. J Mol Biol. 2002 Jul 12;320(3):677-93. [PubMed
]
- Cody V, Galitsky N, Luft JR, Pangborn W, Gangjee A: Analysis of two polymorphic forms of a pyrido[2,3-d]pyrimidine N9-C10 reversed-bridge antifolate binary complex with human dihydrofolate reductase. Acta Crystallogr D Biol Crystallogr. 2003 Apr;59(Pt 4):654-61. Epub 2003 Mar 25. [PubMed
]
- Cody V, Luft JR, Pangborn W, Gangjee A: Analysis of three crystal structure determinations of a 5-methyl-6-N-methylanilino pyridopyrimidine antifolate complex with human dihydrofolate reductase. Acta Crystallogr D Biol Crystallogr. 2003 Sep;59(Pt 9):1603-9. Epub 2003 Aug 19. [PubMed
]
- Cody V, Luft JR, Pangborn W, Gangjee A, Queener SF: Structure determination of tetrahydroquinazoline antifolates in complex with human and Pneumocystis carinii dihydrofolate reductase: correlations between enzyme selectivity and stereochemistry. Acta Crystallogr D Biol Crystallogr. 2004 Apr;60(Pt 4):646-55. Epub 2004 Mar 23. [PubMed
]
- Cody V, Luft JR, Pangborn W: Understanding the role of Leu22 variants in methotrexate resistance: comparison of wild-type and Leu22Arg variant mouse and human dihydrofolate reductase ternary crystal complexes with methotrexate and NADPH. Acta Crystallogr D Biol Crystallogr. 2005 Feb;61(Pt 2):147-55. Epub 2005 Jan 19. [PubMed
]
- Kovalevskaya NV, Smurnyy YD, Polshakov VI, Birdsall B, Bradbury AF, Frenkiel T, Feeney J: Solution structure of human dihydrofolate reductase in its complex with trimethoprim and NADPH. J Biomol NMR. 2005 Sep;33(1):69-72. [PubMed
]
- Reynolds RC, Campbell SR, Fairchild RG, Kisliuk RL, Micca PL, Queener SF, Riordan JM, Sedwick WD, Waud WR, Leung AK, Dixon RW, Suling WJ, Borhani DW: Novel boron-containing, nonclassical antifolates: synthesis and preliminary biological and structural evaluation. J Med Chem. 2007 Jul 12;50(14):3283-9. Epub 2007 Jun 15. [PubMed
]
- Cody V, Pace J, Makin J, Piraino J, Queener SF, Rosowsky A: Correlations of inhibitor kinetics for Pneumocystis jirovecii and human dihydrofolate reductase with structural data for human active site mutant enzyme complexes. Biochemistry. 2009 Mar 3;48(8):1702-11. [PubMed
]
- Volpato JP, Yachnin BJ, Blanchet J, Guerrero V, Poulin L, Fossati E, Berghuis AM, Pelletier JN: Multiple conformers in active site of human dihydrofolate reductase F31R/Q35E double mutant suggest structural basis for methotrexate resistance. J Biol Chem. 2009 Jul 24;284(30):20079-89. Epub 2009 May 28. [PubMed
]
- Gangjee A, Li W, Kisliuk RL, Cody V, Pace J, Piraino J, Makin J: Design, synthesis, and X-ray crystal structure of classical and nonclassical 2-amino-4-oxo-5-substituted-6-ethylthieno[2,3-d]pyrimidines as dual thymidylate synthase and dihydrofolate reductase inhibitors and as potential antitumor agents. J Med Chem. 2009 Aug 13;52(15):4892-902. [PubMed
]
|
| Enzyme 6 Metabolite References |
Not Available |
|
Enzyme 7
[top]
|
| Enzyme 7 ID |
6072 |
| Enzyme 7 Name |
Serine hydroxymethyltransferase, mitochondrial |
| Enzyme 7 Synonyms |
- SHMT
- Glycine hydroxymethyltransferase
- Serine methylase
|
| Enzyme 7 Gene Name |
SHMT2 |
| Enzyme 7 Protein Sequence |
>Serine hydroxymethyltransferase, mitochondrial
MLYFSLFWAARPLQRCGQLVRMAIRAQHSNAAQTQTGEANRGWTGQESLSDSDPEMWELL
QREKDRQCRGLELIASENFCSRAALEALGSCLNNKYSEGYPGKRYYGGAEVVDEIELLCQ
RRALEAFDLDPAQWGVNVQPYSGSPANLAVYTALLQPHDRIMGLDLPDGGHLTHGYMSDV
KRISATSIFFESMPYKLNPKTGLIDYNQLALTARLFRPRLIIAGTSAYARLIDYARMREV
CDEVKAHLLADMAHISGLVAAKVIPSPFKHADIVTTTTHKTLRGARSGLIFYRKGVKAVD
PKTGREIPYTFEDRINFAVFPSLQGGPHNHAIAAVAVALKQACTPMFREYSLQVLKNARA
MADALLERGYSLVSGGTDNHLVLVDLRPKGLDGARAERVLELVSITANKNTCPGDRSAIT
PGGLRLGAPALTSRQFREDDFRRVVDFIDEGVNIGLEVKSKTAKLQDFKSFLLKDSETSQ
RLANLRQRVEQFARAFPMPGFDEH
|
| Enzyme 7 Number of Residues |
504 |
| Enzyme 7 Molecular Weight |
55992.4 |
| Enzyme 7 Theoretical pI |
8.67 |
| Enzyme 7 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 7 General Function |
Involved in catalytic activity |
| Enzyme 7 Specific Function |
Interconversion of serine and glycine |
| Enzyme 7 Pathways |
|
| Enzyme 7 Reactions |
- 5,10-methylenetetrahydrofolate + glycine + H2O = tetrahydrofolate + L-serine [RN:R00945]
|
| Enzyme 7 Pfam Domain Function |
|
| Enzyme 7 Signals |
|
| Enzyme 7 Transmembrane Regions |
|
| Enzyme 7 Essentiality |
Not Available |
| Enzyme 7 GenBank ID Protein |
15080303  |
| Enzyme 7 UniProtKB/Swiss-Prot ID |
P34897  |
| Enzyme 7 UniProtKB/Swiss-Prot Entry Name |
GLYM_HUMAN  |
| Enzyme 7 PDB ID |
Not Available |
| Enzyme 7 Cellular Location |
Not Available |
| Enzyme 7 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 7 GenBank Gene ID |
BC011911  |
| Enzyme 7 GeneCard ID |
SHMT2  |
| Enzyme 7 GenAtlas ID |
SHMT2  |
| Enzyme 7 HGNC ID |
HGNC:10852  |
| Enzyme 7 Chromosome Location |
1 |
| Enzyme 7 Locus |
12q12-q14 |
| Enzyme 7 SNPs |
SNPJam Report  |
| Enzyme 7 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 7 Metabolite References |
Not Available |
|
Enzyme 8
[top]
|
| Enzyme 8 ID |
6074 |
| Enzyme 8 Name |
Serine hydroxymethyltransferase, cytosolic |
| Enzyme 8 Synonyms |
- SHMT
- Glycine hydroxymethyltransferase
- Serine methylase
|
| Enzyme 8 Gene Name |
SHMT1 |
| Enzyme 8 Protein Sequence |
>Serine hydroxymethyltransferase, cytosolic
MTMPVNGAHKDADLWSSHDKMLAQPLKDSDVEVYNIIKKESNRQRVGLELIASENFASRA
VLEALGSCLNNKYSEGYPGQRYYGGTEFIDELETLCQKRALQAYKLDPQCWGVNVQPYSG
SPANFAVYTALVEPHGRIMGLDLPDGGHLTHGFMTDKKKISATSIFFESMPYKVNPDTGY
INYDQLEENARLFHPKLIIAGTSCYSRNLEYARLRKIADENGAYLMADMAHISGLVAAGV
VPSPFEHCHVVTTTTHKTLRGCRAGMIFYRKGVKSVDPKTGKEILYNLESLINSAVFPGL
QGGPHNHAIAGVAVALKQAMTLEFKVYQHQVVANCRALSEALTELGYKIVTGGSDNHLIL
VDLRSKGTDGGRAEKVLEACSIACNKNTCPGDRSALRPSGLRLGTPALTSRGLLEKDFQK
VAHFIHRGIELTLQIQSDTGVRATLKEFKERLAGDKYQAAVQALREEVESFASLFPLPGL
PDF
|
| Enzyme 8 Number of Residues |
483 |
| Enzyme 8 Molecular Weight |
53082.2 |
| Enzyme 8 Theoretical pI |
7.77 |
| Enzyme 8 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 8 General Function |
Involved in catalytic activity |
| Enzyme 8 Specific Function |
Interconversion of serine and glycine |
| Enzyme 8 Pathways |
|
| Enzyme 8 Reactions |
- 5,10-methylenetetrahydrofolate + glycine + H2O = tetrahydrofolate + L-serine [RN:R00945]
|
| Enzyme 8 Pfam Domain Function |
|
| Enzyme 8 Signals |
|
| Enzyme 8 Transmembrane Regions |
|
| Enzyme 8 Essentiality |
Not Available |
| Enzyme 8 GenBank ID Protein |
14124914  |
| Enzyme 8 UniProtKB/Swiss-Prot ID |
P34896  |
| Enzyme 8 UniProtKB/Swiss-Prot Entry Name |
GLYC_HUMAN  |
| Enzyme 8 PDB ID |
1BJ4  |
| Enzyme 8 PDB File |
Show |
| Enzyme 8 3D Structure |
|
| Enzyme 8 Cellular Location |
Not Available |
| Enzyme 8 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 8 GenBank Gene ID |
BC007979  |
| Enzyme 8 GeneCard ID |
SHMT1  |
| Enzyme 8 GenAtlas ID |
SHMT1  |
| Enzyme 8 HGNC ID |
HGNC:10850  |
| Enzyme 8 Chromosome Location |
1 |
| Enzyme 8 Locus |
17p11.2 |
| Enzyme 8 SNPs |
SNPJam Report  |
| Enzyme 8 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 8 Metabolite References |
Not Available |
|
Enzyme 9
[top]
|
| Enzyme 9 ID |
6130 |
| Enzyme 9 Name |
Folylpolyglutamate synthase, mitochondrial |
| Enzyme 9 Synonyms |
- Folylpoly-gamma-glutamate synthetase
- FPGS
- Tetrahydrofolylpolyglutamate synthase
- Tetrahydrofolate synthase
|
| Enzyme 9 Gene Name |
FPGS |
| Enzyme 9 Protein Sequence |
>Folylpolyglutamate synthase, mitochondrial
MSRARSHLRAALFLAAASARGITTQVAARRGLSAWPVPQEPSMEYQDAVRMLNTLQTNAG
YLEQVKRQRGDPQTQLEAMELYLARSGLQVEDLDRLNIIHVTGTKGKGSTCAFTECILRS
YGLKTGFFSSPHLVQVRERIRINGQPISPELFTKYFWRLYHRLEETKDGSCVSMPPYFRF
LTLMAFHVFLQEKVDLAVVEVGIGGAYDCTNIIRKPVVCGVSSLGIDHTSLLGDTVEKIA
WQKGGIFKQGVPAFTVLQPEGPLAVLRDRAQQISCPLYLCPMLEALEEGGPPLTLGLEGE
HQRSNAALALQLAHCWLQRQDRHGAGEPKASRPGLLWQLPLAPVFQPTSHMRLGLRNTEW
PGRTQVLRRGPLTWYLDGAHTASSAQACVRWFRQALQGRERPSGGPEVRVLLFNATGDRD
PAALLKLLQPCQFDYAVFCPNLTEVSSTGNADQQNFTVTLDQVLLRCLEHQQHWNHLDEE
QASPDLWSAPSPEPGGSASLLLAPHPPHTCSASSLVFSCISHALQWISQGRDPIFQPPSP
PKGLLTHPVAHSGASILREAAAIHVLVTGSLHLVGGVLKLLEPALSQ
|
| Enzyme 9 Number of Residues |
587 |
| Enzyme 9 Molecular Weight |
64608.5 |
| Enzyme 9 Theoretical pI |
8.00 |
| Enzyme 9 GO Classification |
| Function |
- ATP binding
- acid-amino acid ligase activity
- adenyl nucleotide binding
- adenyl ribonucleotide binding
- binding
- catalytic activity
- ligase activity
- ligase activity, forming carbon-nitrogen bonds
- nucleoside binding
- purine nucleoside binding
- tetrahydrofolylpolyglutamate synthase activity
|
| Process |
- biosynthetic process
- cellular aromatic compound metabolic process
- cellular metabolic process
- folic acid and derivative biosynthetic process
- folic acid and derivative metabolic process
- metabolic process
|
| Component |
| — |
|
| Enzyme 9 General Function |
Involved in tetrahydrofolylpolyglutamate synthase activity |
| Enzyme 9 Specific Function |
Conversion of folates to polyglutamate derivatives. This allows tissues to concentrate folate at higher levels than in plasma |
| Enzyme 9 Pathways |
- Folate and Pterine Biosynthesis (map00790
)
|
| Enzyme 9 Reactions |
- ATP + tetrahydropteroyl-[gamma-Glu]n + L-glutamate = ADP + phosphate + tetrahydropteroyl-[gamma-Glu]n+1 [RN:R04241]
|
| Enzyme 9 Pfam Domain Function |
Not Available |
| Enzyme 9 Signals |
|
| Enzyme 9 Transmembrane Regions |
|
| Enzyme 9 Essentiality |
Not Available |
| Enzyme 9 GenBank ID Protein |
39992602  |
| Enzyme 9 UniProtKB/Swiss-Prot ID |
Q05932  |
| Enzyme 9 UniProtKB/Swiss-Prot Entry Name |
FOLC_HUMAN  |
| Enzyme 9 PDB ID |
Not Available |
| Enzyme 9 Cellular Location |
Not Available |
| Enzyme 9 Gene Sequence |
>1764 bp
ATGTCGCGGGCGCGGAGCCACCTGCGCGCCGCTCTATTCCTGGCAGCGGCGTCTGCGCGC
GGCGTAACGACCCAGGTCGCGGCGCGGCGGGGCTTGAGCGCGTGGCCGGTGCCGCAGGAG
CCGAGCATGGAGTACCAGGATGCCGTGCGCATGCTCAATACCCTGCAGACCAATGCCGGC
TACCTGGAGCAGGTGAAGCGCCAGCGGGGTGACCCTCAGACACAGTTGGAAGCCATGGAA
CTGTACCTGGCACGGAGTGGGCTGCAGGTGGAGGACTTGGACCGGCTGAACATCATCCAC
GTCACTGGGACGAAGGGGAAGGGCTCCACCTGTGCCTTCACGGAATGTATCCTCCGAAGC
TATGGCCTGAAGACGGGATTCTTTAGCTCTCCCCACCTGGTGCAGGTTCGGGAGCGGATC
CGCATCAATGGGCAGCCCATCAGTCCTGAGCTCTTCACCAAGTACTTCTGGCGCCTCTAC
CACCGGCTGGAGGAGACCAAGGATGGCAGCTGTGTCTCCATGCCCCCCTACTTCCGCTTC
CTGACACTCATGGCCTTCCACGTCTTCCTCCAAGAGAAGGTGGACCTGGCAGTGGTGGAG
GTGGGCATTGGCGGGGCTTATGACTGCACCAACATCATCAGGAAGCCTGTGGTGTGCGGA
GTCTCCTCTCTTGGCATCGACCACACCAGCCTCCTGGGGGATACGGTGGAGAAGATCGCA
TGGCAGAAAGGGGGCATCTTTAAGCAAGGTGTCCCTGCCTTCACTGTGCTCCAACCTGAA
GGTCCCCTGGCAGTGCTGAGGGACCGAGCCCAGCAGATCTCATGTCCTCTATACCTGTGT
CCGATGCTGGAGGCCCTCGAGGAAGGGGGGCCGCCGCTGACCCTGGGCCTGGAGGGGGAG
CACCAGCGGTCCAACGCCGCCTTGGCCTTGCAGCTGGCCCACTGCTGGCTGCAGCGGCAG
GACCGCCATGGTGCTGGGGAGCCAAAGGCATCCAGGCCAGGGCTCCTGTGGCAGCTGCCC
CTGGCACCTGTGTTCCAGCCCACATCCCACATGCGGCTCGGGCTTCGGAACACGGAGTGG
CCGGGCCGGACGCAGGTGCTGCGGCGCGGGCCCCTCACCTGGTACCTGGACGGTGCGCAC
ACCGCCAGCAGCGCGCAGGCCTGCGTGCGCTGGTTCCGCCAGGCGCTGCAGGGCCGCGAG
AGGCCGAGCGGTGGCCCCGAGGTTCGAGTCTTGCTCTTCAATGCTACCGGGGACCGGGAC
CCGGCGGCCCTGCTGAAGCTGCTGCAGCCCTGCCAGTTTGACTATGCCGTCTTCTGCCCT
AACCTGACAGAGGTGTCATCCACAGGCAACGCAGACCAACAGAACTTCACAGTGACACTG
GACCAGGTCCTGCTCCGCTGCCTGGAACACCAGCAGCACTGGAACCACCTGGACGAAGAG
CAGGCCAGCCCGGACCTCTGGAGTGTCCCCAGCCCAGAGCCCGGTGGGTCCGCATCCCTG
CTTCTGGCGCCCCACCCACCCCACACCTGCAGTGCCAGCTCCCTCGTCTTCAGCTGCATT
TCACATGCCTTGCAATGGATCAGCCAAGGCCGAGACCCCATCTTCCAGCCACCTAGTCCC
CCAAAGGGCCTCCTCACCCACCCTGTGGCTCACAGTGGGGCCAGCATACTCCGTGAGGCT
GCTGCCATCCATGTGCTAGTCACTGGCAGCCTGCACCTGGTGGGTGGTGTCCTGAAGCTG
CTGGAGCCCGCACTGTCCCAGTAG
|
| Enzyme 9 GenBank Gene ID |
BC064393  |
| Enzyme 9 GeneCard ID |
FPGS  |
| Enzyme 9 GenAtlas ID |
FPGS  |
| Enzyme 9 HGNC ID |
HGNC:3824  |
| Enzyme 9 Chromosome Location |
9 |
| Enzyme 9 Locus |
9q34.1 |
| Enzyme 9 SNPs |
SNPJam Report  |
| Enzyme 9 General References |
- 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
]
- Garrow TA, Admon A, Shane B: Expression cloning of a human cDNA encoding folylpoly(gamma-glutamate) synthetase and determination of its primary structure. Proc Natl Acad Sci U S A. 1992 Oct 1;89(19):9151-5. [PubMed
]
- Freemantle SJ, Taylor SM, Krystal G, Moran RG: Upstream organization of and multiple transcripts from the human folylpoly-gamma-glutamate synthetase gene. J Biol Chem. 1995 Apr 21;270(16):9579-84. [PubMed
]
- Taylor SM, Freemantle SJ, Moran RG: Structural organization of the human folypoly-gamma-glutamate synthetase gene: evidence for a single genomic locus. Cancer Res. 1995 Dec 15;55(24):6030-4. [PubMed
]
- Cichowicz DJ, Shane B: Mammalian folylpoly-gamma-glutamate synthetase. 1. Purification and general properties of the hog liver enzyme. Biochemistry. 1987 Jan 27;26(2):504-12. [PubMed
]
|
| Enzyme 9 Metabolite References |
Not Available |
|
Enzyme 10
[top]
|
| Enzyme 10 ID |
6164 |
| Enzyme 10 Name |
Bifunctional purine biosynthesis protein PURH |
| Enzyme 10 Synonyms |
- Phosphoribosylaminoimidazolecarboxamide formyltransferase
- 5-aminoimidazole-4-carboxamide ribonucleotide formyltransferase
- AICAR transformylase
- IMP cyclohydrolase
- ATIC
- IMP synthase
- Inosinicase
|
| Enzyme 10 Gene Name |
ATIC |
| Enzyme 10 Protein Sequence |
>Bifunctional purine biosynthesis protein PURH
MAPGQLALFSVSDKTGLVEFARNLTALGLNLVASGGTAKALRDAGLAVRDVSELTGFPEM
LGGRVKTLHPAVHAGILARNIPEDNADMARLDFNLIRVVACNLYPFVKTVASPGVTVEEA
VEQIDIGGVTLLRAAAKNHARVTVVCEPEDYVVVSTEMQSSESKDTSLETRRQLALKAFT
HTAQYDEAISDYFRKQYSKGVSQMPLRYGMNPHQTPAQLYTLQPKLPITVLNGAPGFINL
CDALNAWQLVKELKEALGIPAAASFKHVSPAGAAVGIPLSEDEAKVCMVYDLYKTLTPIS
AAYARARGADRMSSFGDFVALSDVCDVPTAKIISREVSDGIIAPGYEEEALTILSKKKNG
NYCVLQMDQSYKPDENEVRTLFGLHLSQKRNNGVVDKSLFSNVVTKNKDLPESALRDLIV
ATIAVKYTQSNSVCYAKNGQVIGIGAGQQSRIHCTRLAGDKANYWWLRHHPQVLSMKFKT
GVKRAEISNAIDQYVTGTIGEDEDLIKWKALFEEVPELLTEAEKKEWVEKLTEVSISSDA
FFPFRDNVDRAKRSGVAYIAAPSGSAADKVVIEACDELGIILAHTNLRLFHH
|
| Enzyme 10 Number of Residues |
592 |
| Enzyme 10 Molecular Weight |
64615.3 |
| Enzyme 10 Theoretical pI |
6.70 |
| Enzyme 10 GO Classification |
| Function |
- IMP cyclohydrolase activity
- catalytic activity
- cyclohydrolase activity
- glycine hydroxymethyltransferase activity
- hydrolase activity
- hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
- hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amidines
- hydroxymethyl-, formyl- and related transferase activity
- methyltransferase activity
- phosphoribosylaminoimidazolecarboxamide formyltransferase activity
- transferase activity
- transferase activity, transferring one-carbon groups
|
| Process |
- IMP biosynthetic process
- cellular nitrogen compound metabolic process
- metabolic process
- nitrogen compound metabolic process
- nucleobase, nucleoside and nucleotide metabolic process
- nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
- nucleoside phosphate metabolic process
- nucleotide metabolic process
- purine nucleoside monophosphate biosynthetic process
- purine nucleotide biosynthetic process
- purine nucleotide metabolic process
- purine ribonucleoside monophosphate biosynthetic process
|
| Component |
| — |
|
| Enzyme 10 General Function |
Involved in IMP cyclohydrolase activity |
| Enzyme 10 Specific Function |
Bifunctional enzyme that catalyzes 2 steps in purine biosynthesis |
| Enzyme 10 Pathways |
|
| Enzyme 10 Reactions |
- IMP + H2O = 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide [RN:R01127]
|
| Enzyme 10 Pfam Domain Function |
|
| Enzyme 10 Signals |
|
| Enzyme 10 Transmembrane Regions |
|
| Enzyme 10 Essentiality |
Not Available |
| Enzyme 10 GenBank ID Protein |
21104440  |
| Enzyme 10 UniProtKB/Swiss-Prot ID |
P31939  |
| Enzyme 10 UniProtKB/Swiss-Prot Entry Name |
PUR9_HUMAN  |
| Enzyme 10 PDB ID |
1P4R  |
| Enzyme 10 PDB File |
Show |
| Enzyme 10 3D Structure |
|
| Enzyme 10 Cellular Location |
Not Available |
| Enzyme 10 Gene Sequence |
>1779 bp
ATGGCTCCCGGCCAGCTCGCCTTATTTAGTGTCTCTGACAAAACCGGCCTTGTGGAATTT
GCAAGAAACCTGACCGCTCTTGGTTTGAATCTGGTCGCTTCCGGAGGGACTGCAAAAGCT
CTCAGGGATGCTGGTCTGGCAGTCAGAGATGTCTCTGAGTTGACGGGATTTCCTGAAATG
TTGGGGGGACGTGTGAAAACTTTGCATCCTGCAGTCCATGCTGGAATCCTAGCTCGTAAT
ATTCCAGAAGATAATGCTGACATGGCCAGACTTGATTTCAATCTTATAAGAGTTGTTGCC
TGCAATCTCTATCCCTTTGTAAAGACAGTGGCTTCTCCAGGTGTAACTGTTGAGGAGGCT
GTGGAGCAAATTGACATTGGTGGAGTAACCTTACTGAGAGCTGCAGCCAAAAACCACGCT
CGAGTGACAGTGGTGTGTGAACCAGAGGACTATGTGGTGGTGTCCACGGAGATGCAGAGC
TCCGAGAGTAAGGACACCTCCTTGGAGACTAGACGCCAGTTAGCCTTGAAGGCATTCACT
CATACGGCACAATATGATGAAGCAATTTCAGATTATTTCAGGAAACAGTACAGCAAAGGC
GTATCTCAGATGCCCTTGAGATATGGAATGAACCCACATCAGACCCCTGCCCAGCTGTAC
ACACTGCAGCCCAAGCTTCCCATCACAGTTCTAAATGGAGCCCCTGGATTTATAAACTTG
TGCGATGCTTTGAACGCCTGGCAGCTGGTGAAGGAACTCAAGGAGGCTTTAGGTATTCCA
GCCGCTGCCTCTTTCAAACATGTCAGCCCAGCAGGTGCTGCTGTTGGAATTCCACTCAGT
GAAGATGAGGCCAAAGTCTGCATGGTTTATGATCTCTATAAAACCCTCACACCCATCTCA
GCGGCATATGCAAGAGCAAGAGGGGCTGATAGGATGTCTTCATTTGGTGATTTTGTTGCA
TTGTCCGATGTTTGTGATGTACCAACTGCAAAAATTATTTCCAGAGAAGTATCTGATGGT
ATAATTGCCCCAGGATATGAAGAAGAAGCCTTGACAATACTTTCCAAAAAGAAAAATGGA
AACTATTGTGTCCTTCAGATGGACCAATCTTACAAACCAGATGAAAATGAAGTTCGAACT
CTCTTTGGTCTTCATTTAAGCCAGAAGAGAAATAATGGTGTCGTCGACAAGTCATTATTT
AGCAATGTTGTTACCAAAAATAAAGATTTGCCAGAGTCTGCCCTCCGAGACCTCATCGTA
GCCACCATTGCTGTCAAGTACACTCAGTCTAACTCTGTGTGCTACGCCAAGAACGGGCAG
GTTATCGGCATTGGAGCAGGACAGCAGTCTCGTATACACTGCACTCGCCTTGCAGGAGAT
AAGGCAAACTATTGGTGGCTTAGACACCATCCACAAGTGCTTTCGATGAAGTTTAAAACA
GGAGTGAAGAGAGCAGAAATCTCCAATGCCATCGATCAATATGTGACTGGAACCATTGGC
GAGGATGAAGATTTGATAAAGTGGAAGGCACTGTTTGAGGAAGTCCCTGAGTTACTCACT
GAGGCAGAGAAGAAGGAATGGGTTGAGAAACTGACTGAAGTTTCTATCAGCTCTGATGCC
TTCTTCCCTTTCCGAGATAACGTAGACAGAGCTAAAAGGAGTGGTGTGGCGTACATTGCG
GCTCCCTCCGGTTCTGCTGCTGACAAAGTTGTGATTGAGGCCTGCGACGAACTGGGAATC
ATCCTCGCTCATACGAACCTTCGGCTCTTCCACCACTGA
|
| Enzyme 10 GenBank Gene ID |
AB062403  |
| Enzyme 10 GeneCard ID |
ATIC  |
| Enzyme 10 GenAtlas ID |
ATIC  |
| Enzyme 10 HGNC ID |
HGNC:794  |
| Enzyme 10 Chromosome Location |
2 |
| Enzyme 10 Locus |
2q35 |
| Enzyme 10 SNPs |
SNPJam Report  |
| Enzyme 10 General References |
- Rayl EA, Moroson BA, Beardsley GP: The human purH gene product, 5-aminoimidazole-4-carboxamide ribonucleotide formyltransferase/IMP cyclohydrolase. Cloning, sequencing, expression, purification, kinetic analysis, and domain mapping. J Biol Chem. 1996 Jan 26;271(4):2225-33. [PubMed
]
- Yamauchi M, Seki N, Mita K, Saito T, Tsuji S, Hongo E, Morimyo M, Shiomi T, Koyama H, Ayusawa D: Isolation of human purH gene expressed in the rodent transformant cells by subtractive enrichment of 3'-untranslated region of human transcript. DNA Res. 1995 Dec 31;2(6):269-75. [PubMed
]
- Sugita T, Aya H, Ueno M, Ishizuka T, Kawashima K: Characterization of molecularly cloned human 5-aminoimidazole-4-carboxamide ribonucleotide transformylase. J Biochem (Tokyo). 1997 Aug;122(2):309-13. [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
]
- Rasmussen HH, van Damme J, Puype M, Gesser B, Celis JE, Vandekerckhove J: Microsequences of 145 proteins recorded in the two-dimensional gel protein database of normal human epidermal keratinocytes. Electrophoresis. 1992 Dec;13(12):960-9. [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
]
- 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
]
- Wolan DW, Cheong CG, Greasley SE, Wilson IA: Structural insights into the human and avian IMP cyclohydrolase mechanism via crystal structures with the bound XMP inhibitor. Biochemistry. 2004 Feb 10;43(5):1171-83. [PubMed
]
- Cheong CG, Wolan DW, Greasley SE, Horton PA, Beardsley GP, Wilson IA: Crystal structures of human bifunctional enzyme aminoimidazole-4-carboxamide ribonucleotide transformylase/IMP cyclohydrolase in complex with potent sulfonyl-containing antifolates. J Biol Chem. 2004 Apr 23;279(17):18034-45. Epub 2004 Feb 13. [PubMed
]
- Marie S, Heron B, Bitoun P, Timmerman T, Van Den Berghe G, Vincent MF: AICA-ribosiduria: a novel, neurologically devastating inborn error of purine biosynthesis caused by mutation of ATIC. Am J Hum Genet. 2004 Jun;74(6):1276-81. Epub 2004 Apr 26. [PubMed
]
|
| Enzyme 10 Metabolite References |
Not Available |
|
Enzyme 11
[top]
|
| Enzyme 11 ID |
6208 |
| Enzyme 11 Name |
Bifunctional methylenetetrahydrofolate dehydrogenase/cyclohydrolase, mitochondrial |
| Enzyme 11 Synonyms |
- NAD-dependent methylenetetrahydrofolate dehydrogenase
- Methenyltetrahydrofolate cyclohydrolase
|
| Enzyme 11 Gene Name |
MTHFD2 |
| Enzyme 11 Protein Sequence |
>Bifunctional methylenetetrahydrofolate dehydrogenase/cyclohydrolase, mitochondrial
MAATSLMSALAARLLQPAHSCSLRLRPFHLAAVRNEAVVISGRKLAQQIKQEVRQEVEEW
VASGNKRPHLSVILVGENPASHSYVLNKTRAAAVVGINSETIMKPASISEEELLNLINKL
NNDDNVDGLLVQLPLPEHIDERRICNAVSPDKDVDGFHVINVGRMCLDQYSMLPATPWGV
WEIIKRTGIPTLGKNVVVAGRSKNVGMPIAMLLHTDGAHERPGGDATVTISHRYTPKEQL
KKHTILADIVISAAGIPNLITADMIKEGAAVIDVGINRVHDPVTAKPKLVGDVDFEGVRQ
KAGYITPVPGGVGPMTVAMLMKNTIIAAKKVLRLEEREVLKSKELGVATN
|
| Enzyme 11 Number of Residues |
350 |
| Enzyme 11 Molecular Weight |
37894.8 |
| Enzyme 11 Theoretical pI |
9.12 |
| Enzyme 11 GO Classification |
| Function |
- binding
- catalytic activity
|
| Process |
- cellular aromatic compound metabolic process
- cellular metabolic process
- folic acid and derivative biosynthetic process
- folic acid and derivative metabolic process
- metabolic process
|
| Component |
| — |
|
| Enzyme 11 General Function |
Involved in catalytic activity |
| Enzyme 11 Specific Function |
5,10-methylenetetrahydrofolate + NAD(+) = 5,10-methenyltetrahydrofolate + NADH |
| Enzyme 11 Pathways |
- Glyoxylate and Dicarboxylate Metabolism (map00630
)
- One Carbon Pool By Folate (map00670
)
|
| Enzyme 11 Reactions |
- 5,10-methenyltetrahydrofolate + H2O = 10-formyltetrahydrofolate [RN:R01655]
|
| Enzyme 11 Pfam Domain Function |
|
| Enzyme 11 Signals |
|
| Enzyme 11 Transmembrane Regions |
|
| Enzyme 11 Essentiality |
Not Available |
| Enzyme 11 GenBank ID Protein |
94721354  |
| Enzyme 11 UniProtKB/Swiss-Prot ID |
P13995  |
| Enzyme 11 UniProtKB/Swiss-Prot Entry Name |
MTDC_HUMAN  |
| Enzyme 11 PDB ID |
Not Available |
| Enzyme 11 Cellular Location |
Not Available |
| Enzyme 11 Gene Sequence |
>1053 bp
ATGGCTGCGACTTCTCTAATGTCTGCTTTGGCTGCCCGGCTGCTGCAGCCCGCGCACAGC
TGCTCCCTTCGCCTTCGCCCTTTCCACCTCGCGGCAGTTCGAAATGAAGCTGTTGTCATT
TCTGGAAGGAAACTGGCCCAGCAGATCAAGCAGGAAGTGCGGCAGGAGGTAGAAGAGTGG
GTGGCCTCAGGCAACAAACGGCCACACCTGAGTGTGATCCTGGTTGGCGAGAATCCTGCA
AGTCACTCCTATGTCCTCAACAAAACCAGGGCAGCTGCAGTTGTGGGAATCAACAGTGAG
ACAATTATGAAACCAGCTTCAATTTCAGAGGAAGAATTGTTGAATTTAATCAATAAACTG
AATAATGATGATAATGTAGATGGCCTCCTTGTTCAGTTGCCTCTTCCAGAGCATATTGAT
GAGAGAAGGATCTGCAATGCTGTTTCTCCAGACAAGGATGTTGATGGCTTTCATGTAATT
AATGTAGGACGAATGTGTTTGGATCAGTATTCCATGTTACCGGCTACTCCATGGGGTGTG
TGGGAAATAATCAAGCGAACTGGCATTCCAACCCTAGGGAAGAATGTGGTTGTGGCTGGA
AGGTCAAAAAACGTTGGAATGCCCATTGCAATGTTACTGCACACAGATGGGGCGCATGAA
CGTCCCGGAGGTGATGCCACTGTTACAATATCTCATCGATATACTCCCAAAGAGCAGTTG
AAGAAACATACAATTCTTGCAGATATTGTAATATCTGCTGCAGGTATTCCAAATCTGATC
ACAGCAGATATGATCAAGGAAGGAGCAGCAGTCATTGATGTGGGAATAAATAGAGTTCAC
GATCCTGTAACTGCCAAACCCAAGTTGGTTGGAGATGTGGATTTTGAAGGAGTCAGACAA
AAAGCTGGGTATATCACTCCAGTTCCTGGAGGTGTTGGCCCCATGACAGTGGCAATGCTA
ATGAAGAATACCATTATTGCTGCAAAAAAGGTGCTGAGGCTTGAAGAGCGAGAAGTGCTG
AAGTCTAAAGAGCTTGGGGTAGCCACTAATTAA
|
| Enzyme 11 GenBank Gene ID |
NM_006636.3  |
| Enzyme 11 GeneCard ID |
MTHFD2  |
| Enzyme 11 GenAtlas ID |
MTHFD2  |
| Enzyme 11 HGNC ID |
HGNC:7434  |
| Enzyme 11 Chromosome Location |
2 |
| Enzyme 11 Locus |
2p13.1 |
| Enzyme 11 SNPs |
SNPJam Report  |
| Enzyme 11 General References |
- Peri KG, Belanger C, Mackenzie RE: Nucleotide sequence of the human NAD-dependent methylene tetrahydrofolate dehydrogenase-cyclohydrolase. Nucleic Acids Res. 1989 Nov 11;17(21):8853. [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
]
- 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 11 Metabolite References |
Not Available |
|
Enzyme 12
[top]
|
| Enzyme 12 ID |
6211 |
| Enzyme 12 Name |
C-1-tetrahydrofolate synthase, cytoplasmic |
| Enzyme 12 Synonyms |
- C1-THF synthase
- Methylenetetrahydrofolate dehydrogenase
- Methenyltetrahydrofolate cyclohydrolase
- Formyltetrahydrofolate synthetase
|
| Enzyme 12 Gene Name |
MTHFD1 |
| Enzyme 12 Protein Sequence |
>C-1-tetrahydrofolate synthase, cytoplasmic
MAPAEILNGKEISAQIRARLKNQVTQLKEQVPGFTPRLAILQVGNRDDSNLYINVKLKAA
EEIGIKATHIKLPRTTTESEVMKYITSLNEDSTVHGFLVQLPLDSENSINTEEVINAIAP
EKDVDGLTSINAGRLARGDLNDCFIPCTPKGCLELIKETGVPIAGRHAVVVGRSKIVGAP
MHDLLLWNNATVTTCHSKTAHLDEEVNKGDILVVATGQPEMVKGEWIKPGAIVIDCGINY
VPDDKKPNGRKVVGDVAYDEAKERASFITPVPGGVGPMTVAMLMQSTVESAKRFLEKFKP
GKWMIQYNNLNLKTPVPSDIDISRSCKPKPIGKLAREIGLLSEEVELYGETKAKVLLSAL
ERLKHRPDGKYVVVTGITPTPLGEGKSTTTIGLVQALGAHLYQNVFACVRQPSQGPTFGI
KGGAAGGGYSQVIPMEEFNLHLTGDIHAITAANNLVAAAIDARIFHELTQTDKALFNRLV
PSVNGVRRFSDIQIRRLKRLGIEKTDPTTLTDEEINRFARLDIDPETITWQRVLDTNDRF
LRKITIGQAPTEKGHTRTAQFDISVASEIMAVLALTTSLEDMRERLGKMVVASSKKGEPV
SAEDLGVSGALTVLMKDAIKPNLMQTLEGTPVFVHAGPFANIAHGNSSIIADRIALKLVG
PEGFVVTEAGFGADIGMEKFFNIKCRYSGLCPHVVVLVATVRALKMHGGGPTVTAGLPLP
KAYIQENLELVEKGFSNLKKQIENARMFGIPVVVAVNAFKTDTESELDLISRLSREHGAF
DAVKCTHWAEGGKGALALAQAVQRAAQAPSSFQLLYDLKLPVEDKIRIIAQKIYGADDIE
LLPEAQHKAEVYTKQGFGNLPICMAKTHLSLSHNPEQKGVPTGFILPIRDIRASVGAGFL
YPLVGTMSTMPGLPTRPCFYDIDLDPETEQVNGLF
|
| Enzyme 12 Number of Residues |
935 |
| Enzyme 12 Molecular Weight |
101558.4 |
| Enzyme 12 Theoretical pI |
7.32 |
| Enzyme 12 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- adenyl ribonucleotide binding
- binding
- catalytic activity
- formate-tetrahydrofolate ligase activity
- ligase activity
- ligase activity, forming carbon-nitrogen bonds
- nucleoside binding
- purine nucleoside binding
|
| Process |
- cellular aromatic compound metabolic process
- cellular metabolic process
- folic acid and derivative biosynthetic process
- folic acid and derivative metabolic process
- metabolic process
|
| Component |
| — |
|
| Enzyme 12 General Function |
Involved in formate-tetrahydrofolate ligase activity |
| Enzyme 12 Specific Function |
5,10-methylenetetrahydrofolate + NADP(+) = 5,10-methenyltetrahydrofolate + NADPH |
| Enzyme 12 Pathways |
- Glyoxylate and Dicarboxylate Metabolism (map00630
)
- One Carbon Pool By Folate (map00670
)
|
| Enzyme 12 Reactions |
- ATP + formate + tetrahydrofolate = ADP + phosphate + 10-formyltetrahydrofolate [RN:R00943]
|
| Enzyme 12 Pfam Domain Function |
|
| Enzyme 12 Signals |
|
| Enzyme 12 Transmembrane Regions |
|
| Enzyme 12 Essentiality |
Not Available |
| Enzyme 12 GenBank ID Protein |
189065440  |
| Enzyme 12 UniProtKB/Swiss-Prot ID |
P11586  |
| Enzyme 12 UniProtKB/Swiss-Prot Entry Name |
C1TC_HUMAN  |
| Enzyme 12 PDB ID |
1DIA  |
| Enzyme 12 PDB File |
Show |
| Enzyme 12 3D Structure |
|
| Enzyme 12 Cellular Location |
Not Available |
| Enzyme 12 Gene Sequence |
>2808 bp
ATGGCGCCAGCAGAAATCCTGAACGGGAAGGAGATCTCCGCGCAAATAAGGGCGAGACTG
AAAAATCAAGTCACTCAGTTGAAGGAGCAAGTACCTGGTTTCACACCACGCCTGGCAATA
TTACAGGTTGGCAACAGAGATGATTCCAATCTTTATATAAATGTGAAGCTGAAGGCTGCT
GAAGAGATTGGGATCAAAGCCACTCACATTAAGTTACCAAGAACAACCACAGAATCTGAG
GTGATGAAGTACATTACATCTTTGAATGAAGACTCTACTGTACATGGGTTCTTAGTGCAG
CTACCTTTAGATTCAGAGAATTCCATTAACACTGAAGAAGTGATCAATGCTATTGCACCC
GAGAAGGATGTGGATGGATTGACTAGCATCAATGCTGGGAGACTTGCTAGAGGTGACCTC
AATGACTGTTTCATTCCTTGTACGCCTAAGGGATGCTTGGAACTCATCAAAGAGACAGGG
GTGCCGATTGCCGGAAGGCATGCTGTGGTGGTTGGGCGCAGTAAAATAGTTGGGGCCCCG
ATGCATGACTTGCTTCTGTGGAACAATGCCACAGTGACCACCTGCCACTCCAAGACTGCC
CATCTGGATGAGGAGGTAAATAAAGGTGACATCCTGGTGGTTGCAACTGGTCAGCCTGAA
ATGGTTAAAGGGGAGTGGATCAAACCTGGGGCAATAGTCATCGACTGTGGAATCAATTAT
GTCCCAGATGATAAAAAACCAAATGGGAGAAAAGTTGTGGGTGATGTGGCATACGACGAG
GCCAAAGAGAGGGCGAGCTTCATCACTCCTGTTCCTGGCGGCGTAGGGCCCATGACAGTT
GCAATGCTCATGCAGAGCACAGTAGAGAGTGCCAAGCGTTTCCTGGAGAAATTTAAGCCA
GGAAAGTGGATGATTCAGTATAACAACCTTAACCTCAAGACACCTGTTCCAAGTGACATT
GATATATCACGATCTTGTAAACCGAAGCCCATTGGTAAGCTGGCTCGAGAAATTGGTCTG
CTGTCTGAAGAGGTAGAATTATATGGTGAAACAAAGGCCAAAGTTCTGCTGTCAGCACTA
GAACGCCTGAAGCACCGGCCTGATGGGAAATACGTGGTGGTGACTGGAATAACTCCAACA
CCCCTGGGAGAAGGGAAAAGCACAACTACAATCGGGCTAGTGCAAGCCCTTGGTGCCCAT
CTCTACCAGAATGTCTTTGCGTGTGTGCGACAGCCTTCTCAGGGCCCCACCTTTGGAATA
AAAGGTGGCGCTGCAGGAGGCGGCTACTCCCAGGTCATTCCTATGGAAGAGTTTAATCTC
CACCTCACAGGTGACATCCATGCCATCACTGCAGCTAATAACCTCGTTGCTGCGGCCATT
GATGCTCGGATATTTCATGAACTGACCCAGACAGACAAGGCTCTCTTTAATCGTTTGGTG
CCATCAGTAAATGGAGTGAGAAGGTTCTCTGACATCCAAATCCGAAGGTTAAAGAGACTA
GGCATTGAAAAGACTGACCCTACCACACTGACAGATGAAGAGATAAACAGATTTGCAAGA
TTGGACATTGATCCAGAAACCATAACTTGGCAAAGAGTGTTGGATACCAATGATAGATTC
CTGAGGAAGATCACGATTGGACAGGCTCCAACGGAGAAGGGTCACACACGGACGGCCCAG
TTTGATATCTCTGTGGCCAGTGAAATTATGGCTGTCCTGGCTCTCACCACTTCTCTAGAA
GACATGAGAGAGAGACTGGGCAAAATGGTGGTGGCATCCAGTAAGAAAGGAGAGCCCGTC
AGTGCCGAAGATCTGGGGGTGAGTGGTGCACTGACAGTGCTTATGAAGGACGCAATCAAG
CCCAATCTCATGCAGACACTGGAGGGCACTCCAGTGTTTGTCCATGCTGGCCCGTTTGCC
AACATCGCACATGGCAATTCCTCCATCATTGCAGACCAGATCGCACTCAAGCTTGTTGGC
CCAGAAGGGTTTGTAGTGACGGAAGCAGGATTTGGAGCAGACATTGGAATGGAAAAGTTT
TTTAACATCAAATGCCGGTATTCCGGCCTCTGCCCCCACGTGGTGGTGCTTGTTGCCACT
GTCAGGGCTCTCAAGATGCACGGGGGCGGCCCCACGGTCACTGCTGGACTGCCTCTTCCC
AAGGCTTACATACAGGAGAACCTGGAGCTGGTTGAAAAAGGCTTCAGTAACTTGAAGAAA
CAAATTGAAAATGCCAGAATGTTTGGAATTCCAGTAGTAGTGGCCGTGAATGCATTCAAG
ACGGATACAGAGTCTGAGCTGGACCTCATCAGCCGCCTTTCCAGAGAACATGGGGCTTTT
GATGCCGTGAAGTGCACTCACTGGGCAGAAGGGGGCAAGGGTGCCTTAGCCCTGGCTCAG
GCCGTCCAGAGAGCAGCACAAGCACCCAGCAGCTTCCAGCTCCTTTATGACCTCAAGCTC
CCAGTTGAGGATAAAATCAGGATCATTGCACAGAAGATCTATGGAGCAGATGACATTGAA
TTACTTCCCGAAGCTCAACACAAAGCTGAAGTCTACACGAAGCAGGGCTTTGGGAATCTC
CCCATCTGCATGGCTAAAACACACTTGTCTTTGTCTCACAACCCAGAGCAAAAAGGTGTC
CCTACAGGCTTCATTCTGCCCATTCGCGACATCCGCGCCAGCGTTGGGGCTGGTTTTCTG
TACCCCTTAGTAGGAACGATGAGCACAATGCCTGGACTCCCCACCCGGCCCTGTTTTTAT
GATATTGATTTGGACCCTGAAACAGAACAGGTGAATGGATTATTCTAA
|
| Enzyme 12 GenBank Gene ID |
AK312361  |
| Enzyme 12 GeneCard ID |
MTHFD1  |
| Enzyme 12 GenAtlas ID |
MTHFD1  |
| Enzyme 12 HGNC ID |
HGNC:7432  |
| Enzyme 12 Chromosome Location |
1 |
| Enzyme 12 Locus |
14q24 |
| Enzyme 12 SNPs |
SNPJam Report  |
| Enzyme 12 General References |
- Hum DW, Bell AW, Rozen R, MacKenzie RE: Primary structure of a human trifunctional enzyme. Isolation of a cDNA encoding methylenetetrahydrofolate dehydrogenase-methenyltetrahydrofolate cyclohydrolase-formyltetrahydrofolate synthetase. J Biol Chem. 1988 Nov 5;263(31):15946-50. [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
]
- 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
]
- 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
]
- Allaire M, Li Y, MacKenzie RE, Cygler M: The 3-D structure of a folate-dependent dehydrogenase/cyclohydrolase bifunctional enzyme at 1.5 A resolution. Structure. 1998 Feb 15;6(2):173-82. [PubMed
]
- Schmidt A, Wu H, MacKenzie RE, Chen VJ, Bewly JR, Ray JE, Toth JE, Cygler M: Structures of three inhibitor complexes provide insight into the reaction mechanism of the human methylenetetrahydrofolate dehydrogenase/cyclohydrolase. Biochemistry. 2000 May 30;39(21):6325-35. [PubMed
]
- Hol FA, van der Put NM, Geurds MP, Heil SG, Trijbels FJ, Hamel BC, Mariman EC, Blom HJ: Molecular genetic analysis of the gene encoding the trifunctional enzyme MTHFD (methylenetetrahydrofolate-dehydrogenase, methenyltetrahydrofolate-cyclohydrolase, formyltetrahydrofolate synthetase) in patients with neural tube defects. Clin Genet. 1998 Feb;53(2):119-25. [PubMed
]
- Brody LC, Conley M, Cox C, Kirke PN, McKeever MP, Mills JL, Molloy AM, O'Leary VB, Parle-McDermott A, Scott JM, Swanson DA: A polymorphism, R653Q, in the trifunctional enzyme methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase/formyltetrahydrofolate synthetase is a maternal genetic risk factor for neural tube defects: report of the Birth Defects Research Group. Am J Hum Genet. 2002 Nov;71(5):1207-15. Epub 2002 Oct 16. [PubMed
]
- Parle-McDermott A, Kirke PN, Mills JL, Molloy AM, Cox C, O'Leary VB, Pangilinan F, Conley M, Cleary L, Brody LC, Scott JM: Confirmation of the R653Q polymorphism of the trifunctional C1-synthase enzyme as a maternal risk for neural tube defects in the Irish population. Eur J Hum Genet. 2006 Jun;14(6):768-72. [PubMed
]
- Webb EL, Rudd MF, Sellick GS, El Galta R, Bethke L, Wood W, Fletcher O, Penegar S, Withey L, Qureshi M, Johnson N, Tomlinson I, Gray R, Peto J, Houlston RS: Search for low penetrance alleles for colorectal cancer through a scan of 1467 non-synonymous SNPs in 2575 cases and 2707 controls with validation by kin-cohort analysis of 14 704 first-degree relatives. Hum Mol Genet. 2006 Nov 1;15(21):3263-71. Epub 2006 Sep 25. [PubMed
]
- Christensen KE, Rohlicek CV, Andelfinger GU, Michaud J, Bigras JL, Richter A, Mackenzie RE, Rozen R: The MTHFD1 p.Arg653Gln variant alters enzyme function and increases risk for congenital heart defects. Hum Mutat. 2009 Feb;30(2):212-20. [PubMed
]
|
| Enzyme 12 Metabolite References |
Not Available |
|
Enzyme 13
[top]
|
| Enzyme 13 ID |
6225 |
| Enzyme 13 Name |
10-formyltetrahydrofolate dehydrogenase |
| Enzyme 13 Synonyms |
- 10-FTHFDH
- Aldehyde dehydrogenase family 1 member L1
|
| Enzyme 13 Gene Name |
ALDH1L1 |
| Enzyme 13 Protein Sequence |
>10-formyltetrahydrofolate dehydrogenase
MKIAVIGQSLFGQEVYCHLRKEGHEVVGVFTVPDKDGKADPLGLEAEKDGVPVFKYSRWR
AKGQALPDVVAKYQALGAELNVLPFCSQFIPMEIISAPRHGSIIYHPSLLPRHRGASAIN
WTLIHGDKKGGFSIFWADDGLDTGDLLLQKECEVLPDDTVSTLYNRFLFPEGIKGMVQAV
RLIAEGKAPRLPQPEEGATYEGIQKKETAKINWDQPAEAIHNWIRGNDKVPGAWTEACEQ
KLTFFNSTLNTSGLVPEGDALPIPGAHRPGVVTKAGLILFGNDDKMLLVKNIQLEDGKMI
LASNFFKGAASSVLELTEAELVTAEAVRSVWQRILPKVLEVEDSTDFFKSGAASVDVVRL
VEEVKELCDGLELENEDVYMASTFGDFIQLLVRKLRGDDEEGECSIDYVEMAVNKRTVRM
PHQLFIGGEFVDAEGAKTSETINPTDGSVICQVSLAQVTDVDKAVAAAKDAFENGRWGKI
SARDRGRLMYRLADLMEQHQEELATIEALDAGAVYTLALKTHVGMSIQTFRYFAGWCDKI
QGSTIPINQARPNRNLTLTRKEPVGVCGIIIPWNYPLMMLSWKTAACLAAGNTVVIKPAQ
VTPLTALKFAELTLKAGIPKGVVNVLPGSGSLVGQRLSDHPDVRKIGFTGSTEVGKHIMK
SCAISNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIH
DEFVRRVVEEVRKMKVGNPLDRDTDHGPQNHHAHLVKLMEYCQHGVKEGATLVCGGNQVP
RPGFFFEPTVFTDVEDHMFIAKEESFGPVMIISRFADGDLDAVLSRANATEFGLASGVFT
RDINKALYVSDKLQAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEAALNEYLRVKTVTF
EY
|
| Enzyme 13 Number of Residues |
902 |
| Enzyme 13 Molecular Weight |
98828.5 |
| Enzyme 13 Theoretical pI |
5.76 |
| Enzyme 13 GO Classification |
| Function |
- acyl carrier activity
- binding
- catalytic activity
- cofactor binding
- formyltetrahydrofolate dehydrogenase activity
- glycine hydroxymethyltransferase activity
- hydroxymethyl-, formyl- and related transferase activity
- methyltransferase 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
- substrate-specific transporter activity
- transferase activity
- transferase activity, transferring one-carbon groups
- transporter activity
|
| Process |
- 10-formyltetrahydrofolate catabolic process
- 10-formyltetrahydrofolate metabolic process
- biosynthetic process
- cellular aromatic compound metabolic process
- cellular metabolic process
- folic acid and derivative metabolic process
- metabolic process
- one-carbon metabolic process
- oxidation reduction
- tetrahydrofolate metabolic process
|
| Component |
- cell part
- cytoplasm
- intracellular part
|
|
| Enzyme 13 General Function |
Involved in formyltetrahydrofolate dehydrogenase activity |
| Enzyme 13 Specific Function |
10-formyltetrahydrofolate + NADP(+) + H(2)O = tetrahydrofolate + CO(2) + NADPH |
| Enzyme 13 Pathways |
|
| Enzyme 13 Reactions |
- 10-formyltetrahydrofolate + NADP+ + H2O = tetrahydrofolate + CO2 + NADPH + H+ [RN:R00941]
|
| Enzyme 13 Pfam Domain Function |
|
| Enzyme 13 Signals |
|
| Enzyme 13 Transmembrane Regions |
|
| Enzyme 13 Essentiality |
Not Available |
| Enzyme 13 GenBank ID Protein |
3560541  |
| Enzyme 13 UniProtKB/Swiss-Prot ID |
O75891  |
| Enzyme 13 UniProtKB/Swiss-Prot Entry Name |
FTHFD_HUMAN  |
| Enzyme 13 PDB ID |
1S3I  |
| Enzyme 13 PDB File |
Show |
| Enzyme 13 3D Structure |
|
| Enzyme 13 Cellular Location |
Not Available |
| Enzyme 13 Gene Sequence |
>2709 bp
ATGAAGATTGCAGTGATTGGACAGAGCCTGTTTGGCCAGGAAGTTTACTGCCACCTGAGG
AAGGAGGGCCACGAAGTGGTGGGTGTGTTCACTGTTCCAGACAAGGATGGAAAGGCCGAC
CCCCTGGGTCTGGAAGCTGAGAAGGATGGAGTGCCGGTATTCAAGTACTCCCGGTGGCGT
GCAAAAGCGCAAGCTTTGCCTGATGTGGTGGCAAAATACCAGGCTTTGGGGGCCGAACTC
AACGTCCTGCCCTCCTGCAGCCAATTCATCCCCATGGAGATAATCAGTGCCCCCCGGCAT
GGCTCCATCATCTATCACCCGTCACTGCTCCCTAGGCACCGAGGGGCCTCGGCCATCAAC
TGGACCCTCATTCACGGAGATAAGAAAGGGGGGTTTTCCATCTTCTGGGCGGATGATGGT
CTGGACACCGGAGACCTGCTGCTGCAGAAGGAGTGTGAGGTGCTCCCGGACGACACCGTG
AGCACGCTGTACAACCGCTTCCTCTTCCCTGAAGGCATCAAAGGGGTGGTGCAGGCCGTG
AGGCTGATCGCTGAGGGCAAAGCCCCCAGACTCCCTCAGCCTAAGGAAGGAGCCACCTAT
GAGGGGATTCAGAAGAAGGAGACAGCCAAGATCAACTGGGACCAGCCGGCAGAGGCCATT
CACAACTGGATCCGCGGGAACGACAAGGTGCCGGGAGCCTGGACAGAGGCCTGTGAACAG
AAACTGACATTTTTCAACTCAACGCTGAACACTTCAGGCCTGGTGCCCGAGGGAGACGCT
TTGCCCATCCCAGGAGCCCATCGGCCAGGGGTGGTCACCAAAGCAGGACTCATCCTCTTT
GGGAATGATGACAAAATGCTGCTGGTGAAGAATATTCAGCTGGAGGATGGCAAAATGATC
CTGGCCTCGAACTTCTTTAAGGGGGCAGCCAGCAGTGTCCTTGAGCTGACAGAGGCAGAG
CTGGTTACTGCGGAGGCTGTGCGGAGTGTTTGGCAGCGGATCCTCCCCAAAGTACTGGAG
GTTGAAGACTCCACTGATTTCTTCAAGTCAGGGGCCGCGTCTGTGGACGTTGTGAGGCTG
GTGGAGGAAGTGAAGGAGCTGTGTGATGGCCTGGAGTTAGAAAATGAAGATGTGTACATG
GCATCCACCTTTGGGGACTTCATCCAGCTGTTAGTGAGGAAGCTGCGAGGGGACGATGAG
GAGGGCGAGTGCAGCATTGACTACGTGGAAATGGCAGTGAACAAGCGCACTGTCCGCATG
CCCCACCAGCTCTTCATTGGGGGGGAGTTCGTGGATGCCGAGGGCGCCAAGACCTCTGAG
ACCATCAATCCCACCGATGGAAGTGTCATCTGCCAGGTATCCCTGGCCCAAGTCACCGAC
GTCGACAAGGCAGTGGCCGCNGCCAAGGGTGCCTTTGAGAATGGACGGTGGGGGAAGATC
AGTGCGCGGGACCGGGGCCGGCTGATGTACAGGTTGGCAGATCTCATGGAGCAGCACCAG
GAGGAGCTGGCCACCATTGAGGCCCTGGATGCGGGTGCCGTCTACACGCTGGCCCTGAAG
ACCCACGTGGGCATGTCCATCCAGACCTTCCGATACTTTGCTGGCTGGTGTGACAAGATC
CAGGGCTCCACCATCCCCATCAACCAGGCCAGACCCAACCGCAACCTGACCTTGACCAGG
AAGGAGCCTGTTGGGGTTTGTGGCATCATCATCCCCTGGAACTATCCCCTGATGATGCTG
TCCTGGAAGACAGCTGCCTGCCTGGCTGCCGGGAACACAGTGGTGATCAAGCCTGCTCAG
GTGACCCCACTCACAGCCTTGAAGTTTGCAGAGCTGACATTAAAGGCCGGGATTCCCAAA
GGTGTGGTCAACGTCCTCCCAGGATCTGGCTCCCTGGTCGGCCAGAGACTCTCAGACCAT
CCTGATGTGAGGAAAATCGGGTTCACAGGCTCCACAGAGGTGGGCAAGCACATCATGAAA
AGCTGTGCCATAAGTAACGTGAAGAAGGTGTCCCTGGAACTGGGCGGGGAGTCACCCTTC
ATCATCTTTGCTGACTGTGACCTCAACAAGGCTGTGCAGATGGGGATGAGTTCTGTTTTC
TTCAGCAAAGGAGAGAATTGCATTGCAGCAGGCCGACTCTTTGTGGAGGACTCCATTCAT
GATGAGTTCGTGCGGAGAGTGGTAGAAGAGGTGCGGAAGATGAAGGTGGGCAACCCGCTG
GACAGGGACACCGACCACGGGCCGCAGAATCACCATGCCCACCTTGTGAAGCTGATGGAG
TACTGCCAGCATGGCGTGAAGGAAGGGGCCACACTGGTCTGCGGCGGGAATCAGGTCCCT
CGGCCAGGGTTCTTCTTTGAGCCAACTGTTTTCACAGACGTGGAAGACCACATGTTCATA
GCCAAGGAGGAGTCCTTCGGGCCTGTCATGATCATCTCTCGGTTTGCTGATGGGGACTTG
GATGCCGTGCTGTCTCGGGCCAATGCCACGGAATTTGGCCTGGCTTCTGGTGTCTTCACC
AGGGACATCAACAAGGCCCTGTATGTCAGTGACAAGCTCCAGGCAGGCACTGTGTTTGTC
AACACGTACAACAAGACCGACGTGGCCGCTCCCTTCGGAGGATTCAAACAGTCTGGATTT
GGCAAAGATCTAGGAGAGGCGGCTCTGAACGAGTACCTGCGGGTCAAGACAGTGACCTTC
GAATACTGA
|
| Enzyme 13 GenBank Gene ID |
AF052732  |
| Enzyme 13 GeneCard ID |
ALDH1L1  |
| Enzyme 13 GenAtlas ID |
ALDH1L1  |
| Enzyme 13 HGNC ID |
HGNC:3978  |
| Enzyme 13 Chromosome Location |
3 |
| Enzyme 13 Locus |
3q21.3 |
| Enzyme 13 SNPs |
SNPJam Report  |
| Enzyme 13 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
]
- 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
]
- 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 13 Metabolite References |
Not Available |
|
Enzyme 14
[top]
|
| Enzyme 14 ID |
8804 |
| Enzyme 14 Name |
Gamma-glutamyl hydrolase |
| Enzyme 14 Synonyms |
- Conjugase
- GH
- Gamma-Glu-X carboxypeptidase
|
| Enzyme 14 Gene Name |
GGH |
| Enzyme 14 Protein Sequence |
>Gamma-glutamyl hydrolase
MASPGCLLCVLGLLLCGAASLELSRPHGDTAKKPIIGILMQKCRNKVMKNYGRYYIAASY
VKYLESAGARVVPVRLDLTEKDYEILFKSINGILFPGGSVDLRRSDYAKVAKIFYNLSIQ
SFDDGDYFPVWGTCLGFEELSLLISGECLLTATDTVDVAMPLNFTGGQLHSRMFQNFPTE
LLLSLAVEPLTANFHKWSLSVKNFTMNEKLKKFFNVLTTNTDGKIEFISTMEGYKYPVYG
VQWHPEKAPYEWKNLDGISHAPNAVKTAFYLAEFFVNEARKNNHHFKSESEEEKALIYQF
SPIYTGNISSFQQCYIFD
|
| Enzyme 14 Number of Residues |
318 |
| Enzyme 14 Molecular Weight |
35964.0 |
| Enzyme 14 Theoretical pI |
7.14 |
| Enzyme 14 GO Classification |
| Function |
- catalytic activity
- exopeptidase activity
- hydrolase activity
- omega peptidase activity
- peptidase activity
- peptidase activity, acting on L-amino acid peptides
|
| Process |
- cellular amino acid and derivative metabolic process
- cellular amino acid metabolic process
- cellular metabolic process
- glutamine family amino acid metabolic process
- glutamine metabolic process
- metabolic process
|
| Component |
| — |
|
| Enzyme 14 General Function |
Involved in catalytic activity |
| Enzyme 14 Specific Function |
Hydrolyzes the polyglutamate sidechains of pteroylpolyglutamates. Progressively removes gamma-glutamyl residues from pteroylpoly-gamma-glutamate to yield pteroyl-alpha- glutamate (folic acid) and free glutamate. May play an important role in the bioavailability of dietary pteroylpolyglutamates and in the metabolism of pteroylpolyglutamates and antifolates |
| Enzyme 14 Pathways |
- Folate and Pterine Biosynthesis (map00790
)
|
| Enzyme 14 Reactions |
- Hydrolysis of a gamma-glutamyl bond ALL_REAC (other) R04242
|
| Enzyme 14 Pfam Domain Function |
|
| Enzyme 14 Signals |
|
| Enzyme 14 Transmembrane Regions |
|
| Enzyme 14 Essentiality |
Not Available |
| Enzyme 14 GenBank ID Protein |
Not Available |
| Enzyme 14 UniProtKB/Swiss-Prot ID |
Q92820  |
| Enzyme 14 UniProtKB/Swiss-Prot Entry Name |
GGH_HUMAN  |
| Enzyme 14 PDB ID |
1L9X  |
| Enzyme 14 PDB File |
Show |
| Enzyme 14 3D Structure |
|
| Enzyme 14 Cellular Location |
Not Available |
| Enzyme 14 Gene Sequence |
>957 bp
ATGGCCAGTCCGGGCTGCCTGCTGTGCGTGCTGGGCCTGCTACTCTGCGGGGCGGCGAGC
CTCGAGCTGTCTAGACCCCACGGCGACACCGCCAAGAAGCCCATCATCGGAATATTAATG
CAAAAATGCCGTAATAAAGTCATGAAAAACTATGGAAGATACTATATTGCTGCGTCCTAT
GTAAAGTACTTGGAGTCTGCAGGTGCGAGAGTTGTACCAGTAAGGCTGGATCTTACAGAG
AAAGACTATGAAATACTTTTCAAATCTATTAATGGAATCCTTTTCCCTGGAGGAAGTGTT
GACCTCAGACGCTCAGATTATGCTAAAGTGGCCAAAATATTTTATAACTTGTCCATACAG
AGTTTTGATGATGGAGACTATTTTCCTGTGTGGGGCACATGCCTTGGATTTGAAGAGCTT
TCACTGCTGATTAGTGGAGAGTGCTTATTAACTGCCACAGATACTGTTGACGTGGCAATG
CCGCTGAACTTCACTGGAGGTCAATTGCACAGCAGAATGTTCCAGAATTTTCCTACTGAG
TTGTTGCTGTCATTAGCAGTAGAACCTCTGACTGCCAATTTCCATAAGTGGAGCCTCTCC
GTGAAGAATTTTACAATGAATGAAAAGTTAAAGAAGTTTTTCAATGTCTTAACTACAAAT
ACAGATGGCAAGATTGAGTTTATTTCAACAATGGAAGGATATAAGTATCCAGTATATGGT
GTCCAGTGGCATCCAGAGAAAGCACCTTATGAGTGGAAGAATTTGGATGGCATTTCCCAT
GCACCTAATGCTGTGAAAACCGCATTTTATTTAGCAGAGTTTTTTGTTAATGAAGCTCGG
AAAAACAACCATCATTTTAAATCTGAATCTGAAGAGGAGAAAGCATTGATTTATCAGTTC
AGTCCAATTTATACTGGAAATATTTCTTCATTTCAGCAATGTTACATATTTGATTGA
|
| Enzyme 14 GenBank Gene ID |
U55206  |
| Enzyme 14 GeneCard ID |
GGH  |
| Enzyme 14 GenAtlas ID |
GGH  |
| Enzyme 14 HGNC ID |
HGNC:4248  |
| Enzyme 14 Chromosome Location |
8 |
| Enzyme 14 Locus |
8q12.3 |
| Enzyme 14 SNPs |
SNPJam Report  |
| Enzyme 14 General References |
- Yao R, Schneider E, Ryan TJ, Galivan J: Human gamma-glutamyl hydrolase: cloning and characterization of the enzyme expressed in vitro. Proc Natl Acad Sci U S A. 1996 Sep 17;93(19):10134-8. [PubMed
]
- Yin D, Chave KJ, Macaluso CR, Galivan J, Yao R: Structural organization of the human gamma-glutamyl hydrolase gene. Gene. 1999 Oct 1;238(2):463-70. [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
]
- Chave KJ, Galivan J, Ryan TJ: Site-directed mutagenesis establishes cysteine-110 as essential for enzyme activity in human gamma-glutamyl hydrolase. Biochem J. 1999 Nov 1;343 Pt 3:551-5. [PubMed
]
- Chave KJ, Auger IE, Galivan J, Ryan TJ: Molecular modeling and site-directed mutagenesis define the catalytic motif in human gamma -glutamyl hydrolase. J Biol Chem. 2000 Dec 22;275(51):40365-70. [PubMed
]
- Basrur V, Yang F, Kushimoto T, Higashimoto Y, Yasumoto K, Valencia J, Muller J, Vieira WD, Watabe H, Shabanowitz J, Hearing VJ, Hunt DF, Appella E: Proteomic analysis of early melanosomes: identification of novel melanosomal proteins. J Proteome Res. 2003 Jan-Feb;2(1):69-79. [PubMed
]
- Chi A, Valencia JC, Hu ZZ, Watabe H, Yamaguchi H, Mangini NJ, Huang H, Canfield VA, Cheng KC, Yang F, Abe R, Yamagishi S, Shabanowitz J, Hearing VJ, Wu C, Appella E, Hunt DF: Proteomic and bioinformatic characterization of the biogenesis and function of melanosomes. J Proteome Res. 2006 Nov;5(11):3135-44. [PubMed
]
- Li H, Ryan TJ, Chave KJ, Van Roey P: Three-dimensional structure of human gamma -glutamyl hydrolase. A class I glatamine amidotransferase adapted for a complex substate. J Biol Chem. 2002 Jul 5;277(27):24522-9. Epub 2002 Apr 12. [PubMed
]
|
| Enzyme 14 Metabolite References |
Not Available |
|
Enzyme 15
[top]
|
| Enzyme 15 ID |
13028 |
| Enzyme 15 Name |
Folylpolyglutamate synthase |
| Enzyme 15 Synonyms |
Not Available |
| Enzyme 15 Gene Name |
FPGS |
| Enzyme 15 Protein Sequence |
>Folylpolyglutamate synthase
MLNTLQTNAGYLEQVKRQRGDPQTQLEAMELYLARSGLQVEDLDRLNIIHVTGTKGKGST
CAFTECILRSYGLKTGFFSSPHLVQVRERIRINGQPISPELFTKYFWRLYHRLEETKDGS
CVSMPPYFRFLTLMAFHVFLQEKVDLAVVEVGIGGAYDCTNIIRKPVVCGVSSLGIDHTS
LLGDTVEKIAWQKGGIFKQGVPAFTVLQPEGPLAVLRDRAQQISCPLYLCPMLEALEEGG
PPLTLGLEGEHQRSNAALALQLAHCWLQRQDRHGAGEPKASRPGLLWQLPLAPVFQPTSH
MRLGLRNTEWPGRTQVLRRGPLTWYLDGAHTASSAQACVRWFRQALQGRERPSGGPEVRV
LLFNATGDRDPAALLKLLQPCQFDYAVFCPNLTEVSSTGNADQQNFTVTLDQVLLRCLEH
QQHWNHLDEEQASPDLWSAPSPEPGGSASLLLAPHPPHTCSASSLVFSCISHALQWISQG
RDPIFQPPSPPKGLLTHPVAHSGASILREAAAIHVLVTGSLHLVGGVLKLLEPALSQ
|
| Enzyme 15 Number of Residues |
537 |
| Enzyme 15 Molecular Weight |
59173.4 |
| Enzyme 15 Theoretical pI |
7.42 |
| Enzyme 15 GO Classification |
| Function |
- ATP binding
- acid-amino acid ligase activity
- adenyl nucleotide binding
- adenyl ribonucleotide binding
- binding
- catalytic activity
- ligase activity
- ligase activity, forming carbon-nitrogen bonds
- nucleoside binding
- purine nucleoside binding
- tetrahydrofolylpolyglutamate synthase activity
|
| Process |
- biosynthetic process
- cellular aromatic compound metabolic process
- cellular metabolic process
- folic acid and derivative biosynthetic process
- folic acid and derivative metabolic process
- metabolic process
|
| Component |
| — |
|
| Enzyme 15 General Function |
Involved in tetrahydrofolylpolyglutamate synthase activity |
| Enzyme 15 Specific Function |
Not Available |
| Enzyme 15 Pathways |
Not Available |
| Enzyme 15 Reactions |
Not Available |
| Enzyme 15 Pfam Domain Function |
Not Available |
| Enzyme 15 Signals |
|
| Enzyme 15 Transmembrane Regions |
|
| Enzyme 15 Essentiality |
Not Available |
| Enzyme 15 GenBank ID Protein |
57162270  |
| Enzyme 15 UniProtKB/Swiss-Prot ID |
Q5JU19  |
| Enzyme 15 UniProtKB/Swiss-Prot Entry Name |
Q5JU19_HUMAN  |
| Enzyme 15 PDB ID |
Not Available |
| Enzyme 15 Cellular Location |
Not Available |
| Enzyme 15 Gene Sequence |
>1614 bp
ATGCTCAATACCCTGCAGACCAATGCCGGCTACCTGGAGCAGGTGAAGCGCCAGCGGGGT
GACCCTCAGACACAGTTGGAAGCCATGGAACTGTACCTGGCACGGAGTGGGCTGCAGGTG
GAGGACTTGGACCGGCTGAACATCATCCACGTCACTGGGACGAAGGGGAAGGGCTCCACC
TGTGCCTTCACGGAATGTATCCTCCGAAGCTATGGCCTGAAGACGGGATTCTTTAGCTCT
CCCCACCTGGTGCAGGTTCGGGAGCGGATCCGCATCAATGGGCAGCCCATCAGTCCTGAG
CTCTTCACCAAGTACTTCTGGCGCCTCTACCACCGGCTGGAGGAGACCAAGGATGGCAGC
TGTGTCTCCATGCCCCCCTACTTCCGCTTCCTGACACTCATGGCCTTCCACGTCTTCCTC
CAAGAGAAGGTGGACCTGGCAGTGGTGGAGGTGGGCATTGGCGGGGCTTATGACTGCACC
AACATCATCAGGAAGCCTGTGGTGTGCGGAGTCTCCTCTCTTGGCATCGACCACACCAGC
CTCCTGGGGGATACGGTGGAGAAGATCGCATGGCAGAAAGGGGGCATCTTTAAGCAAGGT
GTCCCTGCCTTCACTGTGCTCCAACCTGAAGGTCCCCTGGCAGTGCTGAGGGACCGAGCC
CAGCAGATCTCATGTCCTCTATACCTGTGTCCGATGCTGGAGGCCCTCGAGGAAGGGGGG
CCGCCGCTGACCCTGGGCCTGGAGGGGGAGCACCAGCGGTCCAACGCCGCCTTGGCCTTG
CAGCTGGCCCACTGCTGGCTGCAGCGGCAGGACCGCCATGGTGCTGGGGAGCCAAAGGCA
TCCAGGCCAGGGCTCCTGTGGCAGCTGCCCCTGGCACCTGTGTTCCAGCCCACATCCCAC
ATGCGGCTCGGGCTTCGGAACACGGAGTGGCCGGGCCGGACGCAGGTGCTGCGGCGCGGG
CCCCTCACCTGGTACCTGGACGGTGCGCACACCGCCAGCAGCGCGCAGGCCTGCGTGCGC
TGGTTCCGCCAGGCGCTGCAGGGCCGCGAGAGGCCGAGCGGTGGCCCCGAGGTTCGAGTC
TTGCTCTTCAATGCTACCGGGGACCGGGACCCGGCGGCCCTGCTGAAGCTGCTGCAGCCC
TGCCAGTTTGACTATGCCGTCTTCTGCCCTAACCTGACAGAGGTGTCATCCACAGGCAAC
GCAGACCAACAGAACTTCACAGTGACACTGGACCAGGTCCTGCTCCGCTGCCTGGAACAC
CAGCAGCACTGGAACCACCTGGACGAAGAGCAGGCCAGCCCGGACCTCTGGAGTGCCCCC
AGCCCAGAGCCCGGTGGGTCCGCATCCCTGCTTCTGGCGCCCCACCCACCCCACACCTGC
AGTGCCAGCTCCCTCGTCTTCAGCTGCATTTCACATGCCTTGCAATGGATCAGCCAAGGC
CGAGACCCCATCTTCCAGCCACCTAGTCCCCCAAAGGGCCTCCTCACCCACCCTGTGGCT
CACAGTGGGGCCAGCATACTCCGTGAGGCTGCTGCCATCCATGTGCTAGTCACTGGCAGC
CTGCACCTGGTGGGTGGTGTCCTGAAGCTGCTGGAGCCCGCACTGTCCCAGTAG
|
| Enzyme 15 GenBank Gene ID |
AL162586  |
| Enzyme 15 GeneCard ID |
FPGS  |
| Enzyme 15 GenAtlas ID |
FPGS  |
| Enzyme 15 HGNC ID |
HGNC:3824  |
| Enzyme 15 Chromosome Location |
9 |
| Enzyme 15 Locus |
9q34.1 |
| Enzyme 15 SNPs |
SNPJam Report  |
| Enzyme 15 General References |
Not Available |
| Enzyme 15 Metabolite References |
Not Available |
|
Enzyme 16
[top]
|
| Enzyme 16 ID |
13030 |
| Enzyme 16 Name |
Dihydrofolate reductase |
| Enzyme 16 Synonyms |
- SubName: cDNA, FLJ93028, Homo sapiens dihydrofolate reductase (DHFR), mRNA
|
| Enzyme 16 Gene Name |
DYR |
| Enzyme 16 Protein Sequence |
>Dihydrofolate reductase
MVGSLNCIVAVSQNMGIGKNGDLPWPPLRNEFRYFQRMTTTSSVEGKQNLVIMGKKTWFS
IPEKNRPLKGRINLVLSRELKEPPQGAHFLSRSLDDALKLTEQPELANKVDMVWIVGGSS
VYKEAMNHPGHLKLFVTRIMQDFESDTFFPEIDLEKYKLLPEYPGVLSDVQEEKGIKYKF
EVYEKND
|
| Enzyme 16 Number of Residues |
187 |
| Enzyme 16 Molecular Weight |
21452.6 |
| Enzyme 16 Theoretical pI |
7.60 |
| Enzyme 16 GO Classification |
| Function |
- NADP or NADPH binding
- binding
- catalytic activity
- dihydrofolate reductase activity
- nucleotide binding
- 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
- cellular nitrogen compound metabolic process
- glycine biosynthetic process
- glycine metabolic process
- metabolic process
- nitrogen compound metabolic process
- nucleobase, nucleoside and nucleotide metabolic process
- nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
- nucleoside phosphate metabolic process
- nucleotide biosynthetic process
- nucleotide metabolic process
- oxidation reduction
- serine family amino acid metabolic process
|
| Component |
| — |
|
| Enzyme 16 General Function |
Involved in dihydrofolate reductase activity |
| Enzyme 16 Specific Function |
Not Available |
| Enzyme 16 Pathways |
Not Available |
| Enzyme 16 Reactions |
Not Available |
| Enzyme 16 Pfam Domain Function |
|
| Enzyme 16 Signals |
|
| Enzyme 16 Transmembrane Regions |
|
| Enzyme 16 Essentiality |
Not Available |
| Enzyme 16 GenBank ID Protein |
189069188  |
| Enzyme 16 UniProtKB/Swiss-Prot ID |
B0YJ76  |
| Enzyme 16 UniProtKB/Swiss-Prot Entry Name |
B0YJ76_HUMAN  |
| Enzyme 16 PDB ID |
1MVT  |
| Enzyme 16 PDB File |
Show |
| Enzyme 16 3D Structure |
|
| Enzyme 16 Cellular Location |
Not Available |
| Enzyme 16 Gene Sequence |
>564 bp
ATGGTTGGTTCGCTAAACTGCATCGTCGCTGTGTCCCAGAACATGGGCATCGGCAAGAAC
GGGGACCTGCCCTGGCCACCGCTCAGGAATGAATTCAGATATTTCCAGAGAATGACCACA
ACCTCTTCAGTAGAAGGTAAACAGAATCTGGTGATTATGGGTAAGAAGACCTGGTTCTCC
ATTCCTGAGAAGAATCGACCTTTAAAGGGTAGAATTAATTTAGTTCTCAGCAGAGAACTC
AAGGAACCTCCACAAGGAGCTCATTTTCTTTCCAGAAGTCTAGATGATGCCTTAAAACTT
ACTGAACAACCAGAATTAGCAAATAAAGTAGACATGGTCTGGATAGTTGGTGGCAGTTCT
GTTTATAAGGAAGCCATGAATCACCCAGGCCATCTTAAACTATTTGTGACAAGGATCATG
CAAGACTTTGAAAGTGACACGTTTTTTCCAGAAATTGATTTGGAGAAATATAAACTTCTG
CCAGAATACCCAGGTGTTCTCTCTGATGTCCAGGAGGAGAAAGGCATTAAGTACAAATTT
GAAGTATATGAGAAGAATGATTAA
|
| Enzyme 16 GenBank Gene ID |
AK312642  |
| Enzyme 16 GeneCard ID |
DYR  |
| Enzyme 16 GenAtlas ID |
DYR  |
| Enzyme 16 HGNC ID |
HGNC:2861  |
| Enzyme 16 Chromosome Location |
Not Available |
| Enzyme 16 Locus |
Not Available |
| Enzyme 16 SNPs |
SNPJam Report  |
| Enzyme 16 General References |
- Kao TT, Wang KC, Chang WN, Lin CY, Chen BH, Wu HL, Shi GY, Tsai JN, Fu TF: Characterization and comparative studies of zebrafish and human recombinant dihydrofolate reductases--inhibition by folic acid and polyphenols. Drug Metab Dispos. 2008 Mar;36(3):508-16. Epub 2007 Dec 3. [PubMed
]
|
| Enzyme 16 Metabolite References |
Not Available |
|
Enzyme 17
[top]
|
| Enzyme 17 ID |
13031 |
| Enzyme 17 Name |
cDNA FLJ76259, highly similar to Homo sapiens aminomethyltransferase |
| Enzyme 17 Synonyms |
- glycine cleavage system protein T
- AMT, mRNA
- HCG2001997, isoform CRA_a
|
| Enzyme 17 Gene Name |
Not Available |
| Enzyme 17 Protein Sequence |
>cDNA FLJ76259, highly similar to Homo sapiens aminomethyltransferase
MQRAVSVVARLGFRLQAFPPALCRPLSCAQEVLRRTPLYDFHLAHGGKMVAFAGWSLPVQ
YRDSHTDSHLHTRQHCSLFDVSHMLQTKILGSDRVKLMESLVVGDIAELRPNQGTLSLFT
NEAGGILDDLIVTNTSEGHLYVVSNAGCWEKDLALMQDKVRELQNQGRDVGLEVLDNALL
ALQGPTAAQVLQAGVADDLRKLPFMTSAVMEVFGVSGCRVTRCGYTGEDGVEISVPVAGA
VHLATAILKNPEVKLAGLAARDSLRLEAGLCLYGNDIDEHTTPVEGSLSWTLGKRRRAAM
DFPGAKVIVPQLKGRVQRRRVGLMCEGAPMRAHSPILNMEGTKIGTVTSGCPSPSLKKNV
AMGYVPCEYSRPGTMLLVEVRRKQQMAVVSKMPFVPTNYYTLK
|
| Enzyme 17 Number of Residues |
403 |
| Enzyme 17 Molecular Weight |
43947 |
| Enzyme 17 Theoretical pI |
8.69 |
| Enzyme 17 GO Classification |
Not Available |
| Enzyme 17 General Function |
Amino acid transport and metabolism |
| Enzyme 17 Specific Function |
Not Available |
| Enzyme 17 Pathways |
Not Available |
| Enzyme 17 Reactions |
Not Available |
| Enzyme 17 Pfam Domain Function |
Not Available |
| Enzyme 17 Signals |
|
| Enzyme 17 Transmembrane Regions |
|
| Enzyme 17 Essentiality |
Not Available |
| Enzyme 17 GenBank ID Protein |
158254632  |
| Enzyme 17 UniProtKB/Swiss-Prot ID |
A8K3I5  |
| Enzyme 17 UniProtKB/Swiss-Prot Entry Name |
A8K3I5_HUMAN  |
| Enzyme 17 PDB ID |
Not Available |
| Enzyme 17 Cellular Location |
Not Available |
| Enzyme 17 Gene Sequence |
Not Available |
| Enzyme 17 GenBank Gene ID |
AK290600  |
| Enzyme 17 GeneCard ID |
A8K3I5  |
| Enzyme 17 GenAtlas ID |
Not Available |
| Enzyme 17 HGNC ID |
Not Available |
| Enzyme 17 Chromosome Location |
Not Available |
| Enzyme 17 Locus |
Not Available |
| Enzyme 17 SNPs |
Not Available |
| Enzyme 17 General References |
Not Available |
| Enzyme 17 Metabolite References |
Not Available |
|
Enzyme 18
[top]
|
| Enzyme 18 ID |
13032 |
| Enzyme 18 Name |
cDNA FLJ78616, highly similar to Homo sapiens phosphoribosylglycinamide formyltransferase, phosphoribosylglycinamide synthetase, phosphoribosylaminoimidazole synthetase |
| Enzyme 18 Synonyms |
- GART, transcript variant 1, mRNA
- Phosphoribosylglycinamide formyltransferase, phosphoribosylglycinamide synthetase, phosphoribosylaminoimidazole synthetase, isoform CRA_b
|
| Enzyme 18 Gene Name |
GART |
| Enzyme 18 Protein Sequence |
>cDNA FLJ78616, highly similar to Homo sapiens phosphoribosylglycinamide formyltransferase, phosphoribosylglycinamide synthetase, phosphoribosylaminoimidazole synthetase
MAARVLIIGSGGREHTLAWKLAQSHHVKQVLVAPGNAGTACSEKISNTAISISDHTALAQ
FCKEKKIEFVVVGPEAPLAAGIVGNLRSAGVQCFGPTAEAAQLESSKRFAKEFMDRHGIP
TAQWKAFTKPEEACSFILSADFPALVVKASGLAAGKGVIVAKSKEEACKAVQEIMQEKAF
GAAGETIVIEELLDGEEVSCLCFTDGKTVAPMPPAQDHKRLLEGDGGPNTGGMGAYCPAP
QVSNDLLLKIKDTVLQRTVDGMQQEGTPYTGILYAGIMLTKNGPKVLEFNCRFGDPECQV
ILPLLKSDLYEVIQSTLDGLLCTSLPVWLENHTALTVVMASKGYPGDYTKGVEITGFPEA
QALGLEVFHAGTALKNGKVVTHGGRVLAVTAIRENLISALEEAKKGLAAIKFEGAIYRKD
VGFRAIAFLQQPRSLTYKESGVDIAAGNMLVKKIQPLAKATSRSGCKVDLGGFAGLFDLK
AAGFKDPLLASGTDGVGTKLKIAQLCNKHDTIGQDLVAMCVNDILAQGAEPLFFLDYFSC
GKLDLSVTEAVVAGIAKACGKAGCALLGGETAEMPDMYPPGEYDLAGFAVGAMERDQKLP
HLERITEGDVVVGIASSGLHSNGFSLVRKIVAKSSLQYSSPAPDGCGDQTLGDLLLTPTR
IYSHSLLPVLRSGHVKAFAHITGGGLLENIPRVLPEKLGVDLDAQTWRIPRVFSWLQQEG
HLSEEEMARTFNCGVGAVLVVSKEQTEQILRDIQQHKEEAWVIGSVVARAEGSPRVKVKN
LIESMQINGSVLKNGSLTNHFSFEKKKARVAVLISGTGSNLQALIDSTREPNSSAQIDIV
ISNKAAVAGLDKAERAGIPTRVINHKLYKNRVEFDSAIDLVLEEFSIDIVCLAGFMRILS
GPFVQKWNGKMLNIHPSLLPSFKGSNAHEQALETGVTVTGCTVHFVAEDVDAGQIILQEA
VPVKRGDTVATLSERVKLAEHKIFPAALQLVASGTVQLGENGKICWVKEE
|
| Enzyme 18 Number of Residues |
1010 |
| Enzyme 18 Molecular Weight |
107768 |
| Enzyme 18 Theoretical pI |
6.68 |
| Enzyme 18 GO Classification |
Not Available |
| Enzyme 18 General Function |
Nucleotide transport and metabolism |
| Enzyme 18 Specific Function |
Not Available |
| Enzyme 18 Pathways |
Not Available |
| Enzyme 18 Reactions |
Not Available |
| Enzyme 18 Pfam Domain Function |
Not Available |
| Enzyme 18 Signals |
|
| Enzyme 18 Transmembrane Regions |
|
| Enzyme 18 Essentiality |
Not Available |
| Enzyme 18 GenBank ID Protein |
158259255  |
| Enzyme 18 UniProtKB/Swiss-Prot ID |
A8KA32  |
| Enzyme 18 UniProtKB/Swiss-Prot Entry Name |
A8KA32_HUMAN  |
| Enzyme 18 PDB ID |
Not Available |
| Enzyme 18 Cellular Location |
Not Available |
| Enzyme 18 Gene Sequence |
Not Available |
| Enzyme 18 GenBank Gene ID |
AK292897  |
| Enzyme 18 GeneCard ID |
A8KA32  |
| Enzyme 18 GenAtlas ID |
Not Available |
| Enzyme 18 HGNC ID |
Not Available |
| Enzyme 18 Chromosome Location |
Not Available |
| Enzyme 18 Locus |
Not Available |
| Enzyme 18 SNPs |
SNPJam Report  |
| Enzyme 18 General References |
Not Available |
| Enzyme 18 Metabolite References |
Not Available |
|
Enzyme 19
[top]
|
| Enzyme 19 ID |
13033 |
| Enzyme 19 Name |
Methionyl-tRNA formyltransferase, mitochondrial |
| Enzyme 19 Synonyms |
- MtFMT
|
| Enzyme 19 Gene Name |
MTFMT |
| Enzyme 19 Protein Sequence |
>Methionyl-tRNA formyltransferase, mitochondrial
MRVLVRRCWGPPLAHGARRGRPSPQWRALARLGWEDCRDSRVREKPPWRVLFFGTDQFAR
EALRALHAARENKEEELIDKLEVVTMPSPSPKGLPVKQYAVQSQLPVYEWPDVGSGEYDV
GVVASFGRLLNEALILKFPYGILNVHPSCLPRWRGPAPVIHTVLHGDTVTGVTIMQIRPK
RFDVGPILKQETVPVPPKSTAKELEAVLSRLGANMLISVLKNLPESLSNGRQQPMEGATY
APKISAGTSCIKWEEQTSEQIFRLYRAIGNIIPLQTLWMANTIKLLDLVEVNSSVLADPK
LTGQALIPGSVIYHKQSQILLVYCKDGWIGVRSVMLKKSLTATDFYNGYLHPWYQKNSQA
QPSQCRFQTLRLPTKKKQKKTVAMQQCIE
|
| Enzyme 19 Number of Residues |
389 |
| Enzyme 19 Molecular Weight |
43831.7 |
| Enzyme 19 Theoretical pI |
10.19 |
| Enzyme 19 GO Classification |
| Function |
- catalytic activity
- glycine hydroxymethyltransferase activity
- hydroxymethyl-, formyl- and related transferase activity
- methionyl-tRNA formyltransferase activity
- methyltransferase activity
- transferase activity
- transferase activity, transferring one-carbon groups
|
| Process |
- biosynthetic process
- cellular macromolecule biosynthetic process
- macromolecule biosynthetic process
- metabolic process
- translation
|
| Component |
| — |
|
| Enzyme 19 General Function |
Involved in methionyl-tRNA formyltransferase activity |
| Enzyme 19 Specific Function |
Formylates methionyl-tRNA in mitochondria. A single tRNA(Met) gene gives rise to both an initiator and an elongator species via an unknown mechanism |
| Enzyme 19 Pathways |
|
| Enzyme 19 Reactions |
- 10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O = tetrahydrofolate + N-formylmethionyl-tRNAfMet [RN:R03940]
|
| Enzyme 19 Pfam Domain Function |
|
| Enzyme 19 Signals |
|
| Enzyme 19 Transmembrane Regions |
|
| Enzyme 19 Essentiality |
Not Available |
| Enzyme 19 GenBank ID Protein |
164663775  |
| Enzyme 19 UniProtKB/Swiss-Prot ID |
Q96DP5  |
| Enzyme 19 UniProtKB/Swiss-Prot Entry Name |
FMT_HUMAN  |
| Enzyme 19 PDB ID |
Not Available |
| Enzyme 19 Cellular Location |
Not Available |
| Enzyme 19 Gene Sequence |
>1170 bp
ATGAGGGTGTTGGTGCGGCGCTGTTGGGGTCCTCCGCTGGCTCATGGCGCCAGGCGTGGG
AGGCCGAGTCCCCAGTGGCGAGCACTGGCCCGACTCGGCTGGGAGGACTGCCGGGACTCC
AGAGTCCGCGAGAAGCCTCCCTGGCGGGTGCTCTTCTTCGGCACGGACCAGTTCGCCCGC
GAGGCGCTGCGGGCGCTGCACGCCGCCAGGGAAAACAAAGAAGAAGAGTTAATCGACAAA
CTGGAGGTGGTCACAATGCCTTCCCCATCACCAAAAGGACTGCCAGTGAAGCAATATGCT
GTGCAGTCTCAGCTTCCCGTATATGAGTGGCCGGATGTGGGATCTGGAGAATATGATGTT
GGAGTAGTGGCTTCGTTTGGCCGACTTTTGAATGAGGCTCTTATTCTTAAATTTCCCTAT
GGCATATTGAATGTTCATCCCAGTTGCCTCCCGAGATGGCGTGGCCCAGCCCCTGTAATC
CATACAGTGCTTCACGGAGACACAGTTACTGGAGTAACAATTATGCAAATTAGACCTAAA
AGGTTTGATGTAGGCCCAATTCTCAAACAAGAAACTGTTCCTGTGCCACCCAAGAGCACT
GCAAAGGAATTGGAAGCAGTGTTGTCAAGACTGGGTGCCAACATGCTCATTTCAGTTTTG
AAAAATTTGCCTGAAAGTCTGAGCAATGGAAGGCAGCAGCCAATGGAGGGGGCGACTTAC
GCCCCTAAGATTTCTGCTGGTACCAGTTGTATAAAATGGGAGGAACAAACTTCAGAACAA
ATATTCAGACTTTACCGTGCCATTGGAAATATAATTCCGTTGCAGACGCTCTGGATGGCG
AATACCATTAAACTTCTGGATTTGGTAGAAGTTAACAGTTCAGTCCTTGCTGATCCAAAA
TTAACGGGACAGGCTCTTATTCCAGGATCAGTAATATACCACAAACAGTCACAAATACTA
TTGGTTTATTGCAAGGATGGTTGGATTGGTGTTCGATCAGTGATGCTCAAGAAATCACTA
ACAGCTACTGACTTCTACAATGGATATTTGCACCCCTGGTACCAGAAAAATTCCCAAGCT
CAACCAAGCCAATGCAGATTTCAGACTCTCAGACTTCCAACAAAGAAGAAGCAGAAAAAA
ACTGTTGCTATGCAACAATGCATTGAGTAG
|
| Enzyme 19 GenBank Gene ID |
NM_139242.3  |
| Enzyme 19 GeneCard ID |
MTFMT  |
| Enzyme 19 GenAtlas ID |
MTFMT  |
| Enzyme 19 HGNC ID |
HGNC:29666  |
| Enzyme 19 Chromosome Location |
1 |
| Enzyme 19 Locus |
15q22.31 |
| Enzyme 19 SNPs |
SNPJam Report  |
| Enzyme 19 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
]
- 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 19 Metabolite References |
Not Available |
|
Enzyme 20
[top]
|
| Enzyme 20 ID |
13034 |
| Enzyme 20 Name |
Monofunctional C1-tetrahydrofolate synthase, mitochondrial |
| Enzyme 20 Synonyms |
- Formyltetrahydrofolate synthetase
|
| Enzyme 20 Gene Name |
MTHFD1L |
| Enzyme 20 Protein Sequence |
>Monofunctional C1-tetrahydrofolate synthase, mitochondrial
MGTRLPLVLRQLRRPPQPPGPPRRLRVPCRASSGGGGGGGGGREGLLGQRRPQDGQARSS
CSPGGRTPAARDSIVREVIQNSKEVLSLLQEKNPAFKPVLAIIQAGDDNLMQEINQNLAE
EAGLNITHICLPPDSSEAEIIDEILKINEDTRVHGLALQISENLFSNKVLNALKPEKDVD
GVTDINLGKLVRGDAHECFVSPVAKAVIELLEKSGVNLDGKKILVVGAHGSLEAALQCLF
QRKGSMTMSIQWKTRQLQSKLHEADIVVLGSPKPEEIPLTWIQPGTTVLNCSHDFLSGKV
GCGSPRIHFGGLIEEDDVILLAAALRIQNMVSSGRRWLREQQHRRWRLHCLKLQPLSPVP
SDIEISRGQTPKAVDVLAKEIGLLADEIEIYGKSKAKVRLSVLERLKDQADGKYVLVAGI
TPTPLGEGKSTVTIGLVQALTAHLNVNSFACLRQPSQGPTFGVKGGAAGGGYAQVIPMEE
FNLHLTGDIHAITAANNLLAAAIDTRILHENTQTDKALYNRLVPLVNGVREFSEIQLARL
KKLGINKTDPSTLTEEEVSKFARLDIDPSTITWQRVLDTNDRFLRKITIGQGNTEKGHYR
QAQFDIAVASEIMAVLALTDSLADMKARLGRMVVASDKSGQPVTADDLGVTGALTVLMKD
AIKPNLMQTLEGTPVFVHAGPFANIAHGNSSVLADKIALKLVGEEGFVVTEAGFGADIGM
EKFFNIKCRASGLVPNVVVLVATVRALKMHGGGPSVTAGVPLKKEYTEENIQLVADGCCN
LQKQIQITQLFGVPVVVALNVFKTDTRAEIDLVCELAKRAGAFDAVPCYHWSVGGKGSVD
LARAVREAASKRSRFQFLYDVQVPIVDKIRTIAQAVYGAKDIELSPEAQAKIDRYTQQGF
GNLPICMAKTHLSLSHQPDKKGVPRDFILPISDVRASIGAGFIYPLVGTMSTMPGLPTRP
CFYDIDLDTETEQVKGLF
|
| Enzyme 20 Number of Residues |
978 |
| Enzyme 20 Molecular Weight |
105789.1 |
| Enzyme 20 Theoretical pI |
8.15 |
| Enzyme 20 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- adenyl ribonucleotide binding
- binding
- catalytic activity
- formate-tetrahydrofolate ligase activity
- ligase activity
- ligase activity, forming carbon-nitrogen bonds
- nucleoside binding
- purine nucleoside binding
|
| Process |
- cellular aromatic compound metabolic process
- cellular metabolic process
- folic acid and derivative biosynthetic process
- folic acid and derivative metabolic process
- metabolic process
|
| Component |
| — |
|
| Enzyme 20 General Function |
Involved in formate-tetrahydrofolate ligase activity |
| Enzyme 20 Specific Function |
May provide the missing metabolic reaction required to link the mitochondria and the cytoplasm in the mammalian model of one-carbon folate metabolism in embryonic an transformed cells complementing thus the enzymatic activities of MTHFD2 |
| Enzyme 20 Pathways |
- Glyoxylate and Dicarboxylate Metabolism (map00630
)
- One Carbon Pool By Folate (map00670
)
|
| Enzyme 20 Reactions |
- ATP + formate + tetrahydrofolate = ADP + phosphate + 10-formyltetrahydrofolate [RN:R00943]
|
| Enzyme 20 Pfam Domain Function |
|
| Enzyme 20 Signals |
|
| Enzyme 20 Transmembrane Regions |
|
| Enzyme 20 Essentiality |
Not Available |
| Enzyme 20 GenBank ID Protein |
Not Available |
| Enzyme 20 UniProtKB/Swiss-Prot ID |
Q6UB35  |
| Enzyme 20 UniProtKB/Swiss-Prot Entry Name |
C1TM_HUMAN  |
| Enzyme 20 PDB ID |
Not Available |
| Enzyme 20 Cellular Location |
Not Available |
| Enzyme 20 Gene Sequence |
>2937 bp
ATGGGCACGCGTCTGCCGCTCGTCCTGCGCCAGCTCCGCCGCCCGCCCCAGCCCCCGGGC
CCTCCGCGCCGCCTCCGTGTGCCCTGTCGCGCTAGCAGCGGCGGCGGCGGAGGCGGCGGC
GGTGGCCGGGAGGGCCTGCTTGGACAGCGGCGGCCGCAGGATGGCCAGGCCCGGAGCAGC
TGCAGCCCCGGCGGCCGAACGCCCGCGGCGCGGGACTCCATCGTCAGAGAAGTCATTCAG
AATTCAAAAGAAGTTCTAAGTTTATTGCAAGAAAAAAACCCTGCCTTCAAGCCGGTTCTT
GCAATTATCCAGGCAGGTGACGACAACTTGATGCAGGAAATCAACCAGAATTTGGCTGAG
GAGGCTGGTCTGAACATCACTCACATTTGCCTCCCTCCAGATAGCAGTGAAGCCGAGATT
ATAGATGAAATCTTAAAGATCAATGAAGATACCAGAGTACATGGCCTTGCCCTTCAGATC
TCTGAGAACTTGTTTAGCAACAAAGTCCTCAATGCCTTGAAACCAGAAAAAGATGTGGAT
GGAGTAACAGACATAAACCTGGGGAAGCTGGTGCGAGGGGATGCCCATGAATGTTTTGTT
TCACCTGTTGCCAAAGCTGTAATTGAACTTCTTGAAAAATCAGGTGTCAACCTAGATGGA
AAGAAGATTTTGGTAGTGGGGGCCCATGGGTCTTTGGAAGCTGCTCTACAATGCCTGTTC
CAGAGAAAAGGGTCCATGACAATGAGCATCCAGTGGAAAACACGCCAGCTTCAAAGCAAG
CTTCACGAGGCTGACATTGTGGTCCTAGGCTCACCTAAGCCAGAAGAGATTCCCCTTACT
TGGATACAACCAGGAACTACTGTTCTCAACTGCTCCCATGACTTCCTGTCAGGGAAGGTT
GGGTGTGGCTCTCCAAGAATACATTTTGGTGGACTCATTGAGGAAGATGATGTGATTCTC
CTTGCTGCAGCTCTGCGAATTCAGAACATGGTCAGTAGTGGAAGGAGATGGCTTCGTGAA
CAGCAGCACAGGCGGTGGAGACTTCACTGCTTGAAACTTCAGCCTCTCTCCCCTGTGCCA
AGTGACATTGAGATTTCAAGAGGACAAACTCCAAAAGCTGTGGATGTCCTTGCCAAGGAG
ATTGGATTGCTTGCAGATGAAATTGAAATCTATGGCAAAAGCAAAGCCAAAGTACGTTTG
TCCGTGCTAGAAAGGTTAAAGGATCAAGCAGATGGAAAATACGTCTTAGTTGCTGGGATC
ACACCCACCCCTCTTGGAGAAGGGAAGAGCACAGTCACCATCGGGCTTGTGCAGGCTCTG
ACCGCACACCTGAATGTCAACTCCTTTGCCTGCTTGAGGCAGCCTTCCCAAGGACCGACG
TTTGGAGTGAAAGGAGGAGCCGCGGGTGGTGGATATGCCCAGGTCATCCCCATGGAGGAG
TTCAACCTTCACTTGACTGGAGACATCCACGCCATCACCGCTGCCAATAACTTGCTGGCT
GCCGCCATCGACACGAGGATTCTTCATGAAAACACGCAAACAGATAAGGCTCTGTATAAT
CGGCTGGTTCCTTTAGTGAATGGTGTCAGAGAATTTTCAGAAATTCAGCTTGCTCGGCTA
AAAAAACTGGGAATAAATAAGACTGATCCGAGCACACTGACAGAAGAGGAAGTGAGTAAA
TTTGCCCGTCTCGACATCGACCCATCTACCATCACGTGGCAGAGAGTATTGGATACAAAT
GACCGATTTCTACGAAAAATAACCATCGGGCAGGGAAACACAGAGAAGGGCCATTACCGG
CAGGCGCAGTTTGACATCGCAGTGGCCAGCGAGATCATGGCGGTGCTGGCCCTGACGGAC
AGCCTCGCAGACATGAAGGCACGGCTGGGAAGGATGGTGGTGGCCAGTGACAAAAGCGGG
CAGCCTGTGACAGCAGATGATTTGGGGGTGACAGGTGCTTTGACAGTTTTGATGAAAGAT
GCAATAAAACCAAACCTGATGCAGACCCTGGAAGGGACACCTGTGTTCGTGCATGCGGGC
CCTTTTGCTAACATTGCTCACGGCAACTCTTCAGTGTTGGCTGATAAAATTGCCCTGAAA
CTGGTTGGTGAAGAAGGATTTGTAGTGACCGAAGCTGGCTTTGGTGCTGACATCGGAATG
GAGAAATTCTTCAACATCAAGTGCCGAGCTTCCGGCTTGGTGCCCAACGTGGTTGTGTTA
GTGGCAACGGTGCGAGCTCTGAAGATGCATGGAGGCGGGCCAAGTGTAACGGCTGGTGTT
CCTCTTAAGAAAGAATATACAGAGGAGAACATCCAGCTGGTGGCAGACGGCTGCTGTAAC
CTCCAGAAGCAAATTCAGATCACTCAGCTCTTTGGGGTTCCCGTTGTGGTGGCTCTGAAT
GTCTTCAAGACCGACACCCGCGCTGAGATTGACTTGGTGTGTGAGCTTGCAAAGCGGGCT
GGTGCCTTTGATGCAGTCCCCTGCTATCACTGGTCCGTTGGTGGAAAAGGATCGGTGGAC
TTGGCTCGGGCTGTGAGAGAGGCTGCGAGTAAAAGAAGCCGATTCCAGTTCCTGTATGAT
GTTCAGGTTCCAATTGTGGACAAGATAAGGACCATTGCTCAGGCTGTCTATGGAGCCAAA
GATATTGAACTCTCTCCTGAGGCACAAGCCAAAATAGATCGTTACACTCAACAGGGTTTT
GGAAATTTGCCCATCTGCATGGCAAAGACCCACCTTTCTCTATCTCACCAACCTGACAAA
AAAGGTGTGCCAAGGGACTTCATCTTACCTATCAGTGACGTCCGGGCCAGCATAGGCGCT
GGGTTCATTTACCCTTTGGTCGGAACGATGAGCACCATGCCAGGACTGCCCACCCGGCCC
TGCTTTTATGACATAGATCTTGATACCGAAACAGAACAAGTTAAAGGCTTGTTCTAA
|
| Enzyme 20 GenBank Gene ID |
AY374130  |
| Enzyme 20 GeneCard ID |
MTHFD1L  |
| Enzyme 20 GenAtlas ID |
MTHFD1L  |
| Enzyme 20 HGNC ID |
HGNC:21055  |
| Enzyme 20 Chromosome Location |
6 |
| Enzyme 20 Locus |
6q25.1 |
| Enzyme 20 SNPs |
SNPJam Report  |
| Enzyme 20 General References |
- Prasannan P, Pike S, Peng K, Shane B, Appling DR: Human mitochondrial C1-tetrahydrofolate synthase: gene structure, tissue distribution of the mRNA, and immunolocalization in Chinese hamster ovary calls. J Biol Chem. 2003 Oct 31;278(44):43178-87. Epub 2003 Aug 22. [PubMed
]
- Sugiura T, Nagano Y, Inoue T, Hirotani K: A novel mitochondrial C1-tetrahydrofolate synthetase is upregulated in human colon adenocarcinoma. Biochem Biophys Res Commun. 2004 Feb 27;315(1):204-11. [PubMed
]
- Mungall AJ, Palmer SA, Sims SK, Edwards CA, Ashurst JL, Wilming L, Jones MC, Horton R, Hunt SE, Scott CE, Gilbert JG, Clamp ME, Bethel G, Milne S, Ainscough R, Almeida JP, Ambrose KD, Andrews TD, Ashwell RI, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beare DM, Beasley H, Beasley O, Bird CP, Blakey S, Bray-Allen S, Brook J, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Clark SY, Clark G, Clee CM, Clegg S, Cobley V, Collier RE, Collins JE, Colman LK, Corby NR, Coville GJ, Culley KM, Dhami P, Davies J, Dunn M, Earthrowl ME, Ellington AE, Evans KA, Faulkner L, Francis MD, Frankish A, Frankland J, French L, Garner P, Garnett J, Ghori MJ, Gilby LM, Gillson CJ, Glithero RJ, Grafham DV, Grant M, Gribble S, Griffiths C, Griffiths M, Hall R, Halls KS, Hammond S, Harley JL, Hart EA, Heath PD, Heathcott R, Holmes SJ, Howden PJ, Howe KL, Howell GR, Huckle E, Humphray SJ, Humphries MD, Hunt AR, Johnson CM, Joy AA, Kay M, Keenan SJ, Kimberley AM, King A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd CR, Lloyd DM, Loveland JE, Lovell J, Martin S, Mashreghi-Mohammadi M, Maslen GL, Matthews L, McCann OT, McLaren SJ, McLay K, McMurray A, Moore MJ, Mullikin JC, Niblett D, Nickerson T, Novik KL, Oliver K, Overton-Larty EK, Parker A, Patel R, Pearce AV, Peck AI, Phillimore B, Phillips S, Plumb RW, Porter KM, Ramsey Y, Ranby SA, Rice CM, Ross MT, Searle SM, Sehra HK, Sheridan E, Skuce CD, Smith S, Smith M, Spraggon L, Squares SL, Steward CA, Sycamore N, Tamlyn-Hall G, Tester J, Theaker AJ, Thomas DW, Thorpe A, Tracey A, Tromans A, Tubby B, Wall M, Wallis JM, West AP, White SS, Whitehead SL, Whittaker H, Wild A, Willey DJ, Wilmer TE, Wood JM, Wray PW, Wyatt JC, Young L, Younger RM, Bentley DR, Coulson A, Durbin R, Hubbard T, Sulston JE, Dunham I, Rogers J, Beck S: The DNA sequence and analysis of human chromosome 6. Nature. 2003 Oct 23;425(6960):805-11. [PubMed
]
- Walkup AS, Appling DR: Enzymatic characterization of human mitochondrial C1-tetrahydrofolate synthase. Arch Biochem Biophys. 2005 Oct 15;442(2):196-205. Epub 2005 Aug 30. [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
]
- 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
]
- 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
]
- 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 20 Metabolite References |
Not Available |
|
Enzyme 21
[top]
|
| Enzyme 21 ID |
13035 |
| Enzyme 21 Name |
Methylenetetrahydrofolate dehydrogenase (NADP+ dependent) 2, methenyltetrahydrofolate cyclohydrolase |
| Enzyme 21 Synonyms |
- SubName: Methylenetetrahydrofolate dehydrogenase (NADP+ dependent) 2, methenyltetrahydrofolate cyclohydrolase, isoform CRA_b
- SubName: cDNA FLJ52745, highly similar to Bifunctional methylenetetrahydrofolatedehydrogenase/cyclohydrolase, mitochondrial
|
| Enzyme 21 Gene Name |
MTHFD2 |
| Enzyme 21 Protein Sequence |
>Methylenetetrahydrofolate dehydrogenase (NADP+ dependent) 2, methenyltetrahydrofolate cyclohydrolase
MKPASISEEELLNLINKLNNDDNVDGLLVQLPLPEHIDERRICNAVSPDKDVDGFHVINV
GRMCLDQYSMLPATPWGVWEIIKRTGIPTLGKNVVVAGRSKNVGMPIAMLLHTDGAHERP
GGDATVTISHRYTPKEQLKKHTILADIVISAAGIPNLITADMIKEGAAVIDVGINRVHDP
VTAKPKLVGDVDFEGVRQKAGYITPVPGGVGPMTVAMLMKNTIIAAKKVLRLEEREVLKS
KELGVATN
|
| Enzyme 21 Number of Residues |
248 |
| Enzyme 21 Molecular Weight |
26849.1 |
| Enzyme 21 Theoretical pI |
7.22 |
| Enzyme 21 GO Classification |
| Function |
- binding
- catalytic activity
|
| Process |
- cellular aromatic compound metabolic process
- cellular metabolic process
- folic acid and derivative biosynthetic process
- folic acid and derivative metabolic process
- metabolic process
|
| Component |
| — |
|
| Enzyme 21 General Function |
Involved in catalytic activity |
| Enzyme 21 Specific Function |
Not Available |
| Enzyme 21 Pathways |
Not Available |
| Enzyme 21 Reactions |
Not Available |
| Enzyme 21 Pfam Domain Function |
|
| Enzyme 21 Signals |
|
| Enzyme 21 Transmembrane Regions |
|
| Enzyme 21 Essentiality |
Not Available |
| Enzyme 21 GenBank ID Protein |
194390168  |
| Enzyme 21 UniProtKB/Swiss-Prot ID |
Q7Z650  |
| Enzyme 21 UniProtKB/Swiss-Prot Entry Name |
Q7Z650_HUMAN  |
| Enzyme 21 PDB ID |
Not Available |
| Enzyme 21 Cellular Location |
Not Available |
| Enzyme 21 Gene Sequence |
>747 bp
ATGAAACCAGCTTCAATTTCAGAGGAAGAATTGTTGAATTTAATCAATAAACTGAATAAT
GATGATAATGTAGATGGCCTCCTTGTTCAGTTGCCTCTTCCAGAGCATATTGATGAGAGA
AGGATCTGCAATGCTGTTTCTCCAGACAAGGATGTTGATGGCTTTCATGTAATTAATGTA
GGACGAATGTGTTTGGATCAGTATTCCATGTTACCGGCTACTCCATGGGGTGTGTGGGAA
ATAATCAAGCGAACTGGCATTCCAACCCTAGGGAAGAATGTGGTTGTGGCTGGAAGGTCA
AAAAACGTTGGAATGCCCATTGCAATGTTACTGCACACAGATGGGGCGCATGAACGTCCC
GGAGGTGATGCCACTGTTACAATATCTCATCGATATACTCCCAAAGAGCAGTTGAAGAAA
CATACAATTCTTGCAGATATTGTAATATCTGCTGCAGGTATTCCAAATCTGATCACAGCA
GATATGATCAAGGAAGGAGCAGCAGTCATTGATGTGGGAATAAATAGAGTTCACGATCCT
GTAACTGCCAAACCCAAGTTGGTTGGAGATGTGGATTTTGAAGGAGTCAGACAAAAAGCT
GGGTATATCACTCCAGTTCCTGGAGGTGTTGGCCCCATGACAGTGGCAATGCTAATGAAG
AATACCATTATTGCTGCAAAAAAGGTGCTGAGGCTTGAAGAGCGAGAAGTGCTGAAGTCT
AAAGAGCTTGGGGTAGCCACTAATTAA
|
| Enzyme 21 GenBank Gene ID |
AK300035  |
| Enzyme 21 GeneCard ID |
MTHFD2  |
| Enzyme 21 GenAtlas ID |
MTHFD2  |
| Enzyme 21 HGNC ID |
HGNC:7434  |
| Enzyme 21 Chromosome Location |
2 |
| Enzyme 21 Locus |
2p13.1 |
| Enzyme 21 SNPs |
SNPJam Report  |
| Enzyme 21 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 21 Metabolite References |
Not Available |
|
Enzyme 22
[top]
|
| Enzyme 22 ID |
16499 |
| Enzyme 22 Name |
Putative uncharacterized protein |
| Enzyme 22 Synonyms |
Not Available |
| Enzyme 22 Gene Name |
MTHFD1 |
| Enzyme 22 Protein Sequence |
>Putative uncharacterized protein
MAPAEILNGKEISAQIRARLKNQVTQLKEQVPGFTPRLAILQVGNRDDSNLYINVKLKAA
EEIGIKATHIKLPRTTTESEVMKYITSLNEDSTVHGFLVQLPLDSENSINTEEVINAIAP
EKDVDGLTSINAGRLARGDLNDCFIPCTPKGCLELIKETGVPIAGRHAVVVGRSKIVGAP
MHDLLLWNNATVTTCHSKTAHLDEEVNKGDILVVATGQPEMVKGEWIKPGAIVIDCGINY
VPDDKKPNGRKVVGDVAYDEAKERASFITPVPGGVGPMTVAMLMQSTVESAKRFLEKFKP
GKWMIQYNNLNLKTPVPSDIDISRSCKPKPIGKLAREIGLLSEEVELYGETKAKVLLSAL
ERLKHRPDGKYVVVTGITPTPLGEGKSTTTIGLVQALGAHLYQNVFACVRQPSQGPTFGI
KGGAAGGGYSQVIPMEEFNLHLTGDIHAITAANNLVAAAIDARIFHELTQTDKALFNRLV
PSVNGVRRFSDIQIRRLKRLGIEKTDPTTLTDEEINRFARLDIDPETITWQRVLDTNDRF
LRKITIGQAPTEKGHTRTAQFDISVASEIMAVLALTTSLEDMRERLGKMVVASSKKGEPV
SAEDLGVSGALTVLMKDAIKPNLMQTLEGTPVFVHAGPFANIAHGNSSIIADQIALKLVG
PEGFVVTEAGFGADIGMEKFFNIKCRYSGLCPHVVVLVATVRALKMHGGGPTVTAGLPLP
KAYIQENLELVEKGFSNLKKQIENARMFGIPVVVAVNAFKTDTESELDLISRLSREHGAF
DAVKCTHWAEGGKGALALAQAVQRAAQAPSSFQLLYDLKLPVEDKIRIIAQKIYGADDIE
LLPEAQHKAEVYTKQGFGNLPICMAKTHLSLSHNPEQKGVPTGFILPIRDIRASVGAGFL
YPLVGTMSTMPGLPTRPCFYDIDLDPETEQVNGLF
|
| Enzyme 22 Number of Residues |
935 |
| Enzyme 22 Molecular Weight |
101532 |
| Enzyme 22 Theoretical pI |
7.19 |
| Enzyme 22 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- binding
- catalytic activity
- formate-tetrahydrofolate ligase activity
- ligase activity
- ligase activity, forming carbon-nitrogen bonds
- nucleotide binding
- purine nucleotide binding
|
| Process |
- aromatic compound metabolism
- cellular metabolism
- folic acid and derivative biosynthesis
- folic acid and derivative metabolism
- metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 22 General Function |
Nucleotide transport and metabolism |
| Enzyme 22 Specific Function |
Not Available |
| Enzyme 22 Pathways |
Not Available |
| Enzyme 22 Reactions |
Not Available |
| Enzyme 22 Pfam Domain Function |
|
| Enzyme 22 Signals |
|
| Enzyme 22 Transmembrane Regions |
|
| Enzyme 22 Essentiality |
Not Available |
| Enzyme 22 GenBank ID Protein |
Not Available |
| Enzyme 22 UniProtKB/Swiss-Prot ID |
B2R5Y2  |
| Enzyme 22 UniProtKB/Swiss-Prot Entry Name |
B2R5Y2_HUMAN  |
| Enzyme 22 PDB ID |
1DIA  |
| Enzyme 22 PDB File |
Show |
| Enzyme 22 3D Structure |
|
| Enzyme 22 Cellular Location |
Not Available |
| Enzyme 22 Gene Sequence |
Not Available |
| Enzyme 22 GenBank Gene ID |
AK312361  |
| Enzyme 22 GeneCard ID |
B2R5Y2  |
| Enzyme 22 GenAtlas ID |
Not Available |
| Enzyme 22 HGNC ID |
Not Available |
| Enzyme 22 Chromosome Location |
14 |
| Enzyme 22 Locus |
14q24 |
| Enzyme 22 SNPs |
SNPJam Report  |
| Enzyme 22 General References |
Not Available |
| Enzyme 22 Metabolite References |
Not Available |