|
Enzyme 1
[top]
|
| Enzyme 1 ID |
5392 |
| Enzyme 1 Name |
Methionine synthase |
| Enzyme 1 Synonyms |
- 5-methyltetrahydrofolate-- homocysteine methyltransferase
- Methionine synthase, vitamin-B12 dependent
- 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 |
140529 |
| Enzyme 1 Theoretical pI |
5.27 |
| Enzyme 1 GO Classification |
| Function |
- S-methyltransferase activity
- binding
- catalytic activity
- cation binding
- cobalamin binding
- cobalt ion binding
- dihydropteroate synthase activity
- homocysteine S-methyltransferase activity
- ion binding
- methionine synthase activity
- methyltransferase activity
- transferase activity
- transferase activity, transferring alkyl or aryl (other than methyl) groups
- transferase activity, transferring one-carbon groups
- transition metal ion binding
- vitamin binding
|
| Process |
- amino acid and derivative metabolism
- amino acid metabolism
- aromatic compound metabolism
- cellular metabolism
- folic acid and derivative biosynthesis
- folic acid and derivative metabolism
- metabolism
- methionine biosynthesis
- physiological process
- sulfur amino acid biosynthesis
- sulfur amino acid metabolism
|
| Component |
|
|
| Enzyme 1 General Function |
Amino acid transport and metabolism |
| 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
|
| Enzyme 1 Pfam Domain Function |
|
| Enzyme 1 Signals |
|
| Enzyme 1 Transmembrane Regions |
|
| Enzyme 1 Essentiality |
Not Available |
| Enzyme 1 GenBank ID Protein |
1923221  |
| 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
]
- 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
]
|
| 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 |
74597 |
| 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 |
- amino acid and derivative metabolism
- amino acid metabolism
- cellular metabolism
- metabolism
- methionine metabolism
- physiological process
- sulfur amino acid metabolism
|
| Component |
| — |
|
| Enzyme 2 General Function |
Amino acid transport and metabolism |
| 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 + NADP+ = 5,10-methylenetetrahydrofolate + NADPH + H+
|
| 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, 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, 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
]
- 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
]
- 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
]
- 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
]
- Schneider JA, Rees DC, Liu YT, Clegg JB: Worldwide distribution of a common methylenetetrahydrofolate reductase mutation. Am J Hum Genet. 1998 May;62(5):1258-60. [PubMed
]
- van der Put NM, Gabreels F, Stevens EM, Smeitink JA, Trijbels FJ, Eskes TK, van den Heuvel LP, Blom HJ: A second common mutation in the methylenetetrahydrofolate reductase gene: an additional risk factor for neural-tube defects? Am J Hum Genet. 1998 May;62(5):1044-51. [PubMed
]
- Kluijtmans LA, Wendel U, Stevens EM, van den Heuvel LP, Trijbels FJ, Blom HJ: Identification of four novel mutations in severe methylenetetrahydrofolate reductase deficiency. Eur J Hum Genet. 1998 May-Jun;6(3):257-65. [PubMed
]
- Weisberg I, Tran P, Christensen B, Sibani S, Rozen R: A second genetic polymorphism in methylenetetrahydrofolate reductase (MTHFR) associated with decreased enzyme activity. Mol Genet Metab. 1998 Jul;64(3):169-72. [PubMed
]
- 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
]
|
| Enzyme 2 Metabolite References |
Not Available |
|
Enzyme 3
[top]
|
| Enzyme 3 ID |
5566 |
| Enzyme 3 Name |
Trifunctional purine biosynthetic protein adenosine-3 [Includes: Phosphoribosylamine--glycine ligase |
| Enzyme 3 Synonyms |
- GARS
- Glycinamide ribonucleotide synthetase
- Phosphoribosylglycinamide synthetase
- Phosphoribosylformylglycinamidine cyclo-ligase
- AIRS
- Phosphoribosyl-aminoimidazole synthetase
- AIR synthase
- Phosphoribosylglycinamide formyltransferase
- GART
- GAR transformylase
- 5'-phosphoribosylglycinamide transformylase]
|
| Enzyme 3 Gene Name |
GART |
| Enzyme 3 Protein Sequence |
>Trifunctional purine biosynthetic protein adenosine-3 [Includes: Phosphoribosylamine--glycine ligase
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 |
107768 |
| Enzyme 3 Theoretical pI |
6.68 |
| Enzyme 3 GO Classification |
| Function |
- catalytic activity
- cyclo-ligase activity
- glycine hydroxymethyltransferase activity
- hydroxymethyl-, formyl- and related transferase activity
- ligase activity
- ligase activity, forming carbon-nitrogen bonds
- methyltransferase activity
- phosphoribosylamine-glycine ligase activity
- phosphoribosylformylglycinamidine cyclo-ligase activity
- phosphoribosylglycinamide formyltransferase activity
- transferase activity
- transferase activity, transferring one-carbon groups
|
| Process |
- 'de novo' IMP biosynthesis
- IMP biosynthesis
- biosynthesis
- cellular metabolism
- metabolism
- nucleobase metabolism
- nucleobase, nucleoside, nucleotide and nucleic acid metabolism
- nucleotide metabolism
- physiological process
- purine base biosynthesis
- purine base metabolism
- purine nucleoside monophosphate biosynthesis
- purine nucleotide biosynthesis
- purine nucleotide metabolism
- purine ribonucleoside monophosphate biosynthesis
|
| Component |
- cell
- cytoplasm
- intracellular
|
|
| Enzyme 3 General Function |
Nucleotide transport and metabolism |
| Enzyme 3 Specific Function |
ATP + 5-phospho-D-ribosylamine + glycine = ADP + phosphate + 1-N-(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
|
| 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 |
Not Available |
| Enzyme 3 Locus |
Not Available |
| 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
]
- 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
]
|
| 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[Includes: 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 |
58927 |
| Enzyme 4 Theoretical pI |
5.45 |
| Enzyme 4 GO Classification |
| Function |
- binding
- catalytic activity
- folic acid binding
- transferase activity
- vitamin binding
|
| Process |
- metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 4 General Function |
Amino acid transport and metabolism |
| Enzyme 4 Specific Function |
Folate-dependent enzyme, that displays both transferase and deaminase activity. Serves to channel one-carbon units from formiminoglutamate to the folate pool |
| Enzyme 4 Pathways |
|
| Enzyme 4 Reactions |
- 5-formimidoyltetrahydrofolate = 5,10-methenyltetrahydrofolate + NH3
|
| 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 |
Not Available |
| Enzyme 4 Locus |
Not Available |
| 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
]
- 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
]
- 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 precursor |
| Enzyme 5 Synonyms |
- Glycine cleavage system T protein
- GCVT
|
| Enzyme 5 Gene Name |
AMT |
| Enzyme 5 Protein Sequence |
>Aminomethyltransferase, mitochondrial precursor
MQRAVSVVARLGFRLQAFPPALCRPLSCAQEVLRRTPLYDFHLAHGGKMVAFAGWSLPVQ
YRDSHTDSHLHTRQHCSLFDVSHMLQTKILGSDRVKLMESLVVGDIAELRPNQGTLSLFT
NEAGGILDDLIVTNTSEGHLYVVSNAGCWEKDLALMQDKVRELQNQGRDVGLEVLDNALL
ALQGPTAAQVLQAGVADDLRKLPFMTSAVMEVFGVSGCRVTRCGYTGEDGVEISVPVAGA
VHLATAILKNPEVKLAGLAARDSLRLEAGLCLYGNDIDEHTTPVEGSLSWTLGKRRRAAM
DFPGAKVIVPQLKGRVQRRRVGLMCEGAPMRAHSPILNMEGTKIGTVTSGCPSPSLKKNV
AMGYVPCEYSRPGTMLLVEVRRKQQMAVVSKMPFVPTNYYTLK
|
| Enzyme 5 Number of Residues |
403 |
| Enzyme 5 Molecular Weight |
43947 |
| 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 |
- amino acid and derivative metabolism
- amino acid metabolism
- cellular metabolism
- glycine catabolism
- glycine metabolism
- metabolism
- physiological process
- serine family amino acid metabolism
|
| Component |
- cell
- cytoplasm
- intracellular
|
|
| Enzyme 5 General Function |
Amino acid transport and metabolism |
| 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-S-aminomethyldihydrolipoyllysine + tetrahydrofolate = protein-dihydrolipoyllysine + 5,10-methylenetetrahydrofolate + NH3
|
| Enzyme 5 Pfam Domain Function |
|
| Enzyme 5 Signals |
|
| Enzyme 5 Transmembrane Regions |
Not Available |
| Enzyme 5 Essentiality |
Not Available |
| Enzyme 5 GenBank ID Protein |
391721  |
| 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 |
D13811  |
| 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
]
- 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 |
21453 |
| Enzyme 6 Theoretical pI |
7.60 |
| Enzyme 6 GO Classification |
| Function |
- NADP binding
- binding
- catalytic activity
- coenzyme binding
- cofactor binding
- dihydrofolate reductase 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 |
- amino acid and derivative metabolism
- amino acid metabolism
- cellular metabolism
- glycine biosynthesis
- glycine metabolism
- metabolism
- nucleobase, nucleoside, nucleotide and nucleic acid metabolism
- nucleotide biosynthesis
- nucleotide metabolism
- physiological process
- serine family amino acid metabolism
|
| Component |
| — |
|
| Enzyme 6 General Function |
Coenzyme transport and metabolism |
| Enzyme 6 Specific Function |
5,6,7,8-tetrahydrofolate + NADP(+) = 7,8- dihydrofolate + NADPH |
| 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+
|
| 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
]
- 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
]
- 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
]
- 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
]
|
| Enzyme 6 Metabolite References |
Not Available |
|
Enzyme 7
[top]
|
| Enzyme 7 ID |
6072 |
| Enzyme 7 Name |
Serine hydroxymethyltransferase, mitochondrial precursor |
| Enzyme 7 Synonyms |
- Serine methylase
- Glycine hydroxymethyltransferase
- SHMT
|
| Enzyme 7 Gene Name |
SHMT2 |
| Enzyme 7 Protein Sequence |
>Serine hydroxymethyltransferase, mitochondrial precursor
MLYFSLFWAARPLQRCGQLVRMAIRAQHSNAAQTQTGEANRGWTGQESLSDSDPEMWELL
QREKDRQCRGLELIASENFCSRAALEALGSCLNNKYSEGYPGKRYYGGAEVVDEIELLCQ
RRALEAFDLDPAQWGVNVQPYSGSPANLAVYTALLQPHDRIMGLDLPDGGHLTHGYMSDV
KRISATSIFFESMPYKLNPKTGLIDYNQLALTARLFRPRLIIAGTSAYARLIDYARMREV
CDEVKAHLLADMAHISGLVAAKVIPSPFKHADIVTTTTHKTLRGARSGLIFYRKGVKAVD
PKTGREIPYTFEDRINFAVFPSLQGGPHNHAIAAVAVALKQACTPMFREYSLQVLKNARA
MADALLERGYSLVSGGTDNHLVLVDLRPKGLDGARAERVLELVSITANKNTCPGDRSAIT
PGGLRLGAPALTSRQFREDDFRRVVDFIDEGVNIGLEVKSKTAKLQDFKSFLLKDSETSQ
RLANLRQRVEQFARAFPMPGFDEH
|
| Enzyme 7 Number of Residues |
504 |
| Enzyme 7 Molecular Weight |
55994 |
| Enzyme 7 Theoretical pI |
8.67 |
| Enzyme 7 GO Classification |
| Function |
- catalytic activity
- glycine hydroxymethyltransferase activity
- methyltransferase activity
- transferase activity
- transferase activity, transferring one-carbon groups
|
| Process |
- L-serine metabolism
- amino acid and derivative metabolism
- amino acid metabolism
- cellular metabolism
- glycine metabolism
- metabolism
- physiological process
- serine family amino acid metabolism
|
| Component |
| — |
|
| Enzyme 7 General Function |
Amino acid transport and metabolism |
| Enzyme 7 Specific Function |
Interconversion of serine and glycine |
| Enzyme 7 Pathways |
|
| Enzyme 7 Reactions |
- 5,10-methylenetetrahydrofolate + glycine + H2O = tetrahydrofolate + L-serine
|
| Enzyme 7 Pfam Domain Function |
|
| Enzyme 7 Signals |
|
| Enzyme 7 Transmembrane Regions |
Not Available |
| Enzyme 7 Essentiality |
Not Available |
| Enzyme 7 GenBank ID Protein |
746436  |
| 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 |
>1452 bp
ATGGCCATTCGGGCTCAGCACAGCAACGCAGCCCAGACTCAGACTGGGGAAGCAAACAGG
GGCTGGACAGGCCAGGAGAGCCTGTCGGACAGTGATCCTGAGATGTGGGAGTTGCTGCAG
AGGGAGAAGGACAGGCAGTGTCGTGGCCTGGAGCTCATTGCCTCAGAGAACTTCTGCAGC
CGAGCTGCGCTGGAGGCCCTGGGGTCCTGTCTGAACAACAAGTACTCGGAGGGTTATCCT
GGCAAGAGATACTATGGGGGAGCAGAGGTGGTGGATGAAATTGAGCTGCTGTGCCAGCGC
CGGGCCTTGGAAGCCTTTGACCTGGATCCTGCACAGTGGGGAGTCAATGTCCAGCCCTAC
TCCGGGTCCCCAGCCAACCTGGCCGTCTACACAGCCCTTCTGCAACCTCACGACCGGATC
ATGGGGCTGGACCTGCCCGATGGGGGCCATCTCACCCACGGCTACATGTCTGACGTCAAG
CGGATATCAGCCACGTCCATCTTCTTCGAGTCTATGCCCTATAAGCTCAACCCCAAAACT
GGCCTCATTGACTACAACCAGCTGGCACTGACTGCTCGACTTTTCCGGCCACGGCTCATC
ATAGCTGGCACCAGCGCCTATGCTCGCCTCATTGACTACGCCCGCATGAGAGAGGTGTGT
GATGAAGTCAAAGCACACCTGCTGGCAGACATGGCCCACATCAGTGGCCTGGTGGCTGCC
AAGGTGATTCCCTCGCCTTTCAAGCACGCGGACATCGTCACCACCACTACTCACAAGACT
CTTCGAGGGGCCAGGTCAGGGCTCATCTTCTACCGGAAAGGGGTGAAGGCTGTGGACCCC
AAGACTGGCCGGGAGATCCCTTACACATTTGAGGACCGAATCAACTTTGCCGTGTTCCCA
TCCCTGCAGGGGGGCCCCCACAATCATGCCATTGCTGCAGTAGCTGTGGCCCTAAAGCAG
GCCTGCACCCCCATGTTCCGGGAGTACTCCCTGCAGGTTCTGAAGAATGCTCGGGCCATG
GCAGATGCCCTGCTAGAGCGAGGCTACTCACTGGTATCAGGTGGTACTGACAACCACCTG
GTGCTGGTGGACCTGCGGCCCAAGGGCCTGGATGGAGCTCGGGCTGAGCGGGTGCTAGAG
CTTGTATCCATCACTGCCAACAAGAACACCTGTCCTGGAGACCGAAGTGCCATCACACCG
GGCGGCCTGCGGCTTGGGGCCCCAGCCTTAACTTCTCGACAGTTCCGTGAGGATGACTTC
CGGAGAGTTGTGGACTTTATAGATGAAGGGGTCAACATTGGCTTAGAGGTGAAGAGCAAG
ACTGCCAAGCTCCAGGATTTCAAATCCTTCCTGCTTAAGGACTCAGAAACAAGTCAGCGT
CTGGCCAACCTCAGGCAACGGGTGGAGCAGTTTGCCAGGGCCTTCCCCATGCCTGGTTTT
GATGAGCATTGA
|
| Enzyme 7 GenBank Gene ID |
U23143  |
| Enzyme 7 GeneCard ID |
SHMT2  |
| Enzyme 7 GenAtlas ID |
SHMT2  |
| Enzyme 7 HGNC ID |
HGNC:10852  |
| Enzyme 7 Chromosome Location |
12 |
| 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
]
- 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
]
|
| Enzyme 7 Metabolite References |
Not Available |
|
Enzyme 8
[top]
|
| Enzyme 8 ID |
6074 |
| Enzyme 8 Name |
Serine hydroxymethyltransferase, cytosolic |
| Enzyme 8 Synonyms |
- Serine methylase
- Glycine hydroxymethyltransferase
- SHMT
|
| 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 |
53083 |
| Enzyme 8 Theoretical pI |
7.77 |
| Enzyme 8 GO Classification |
| Function |
- catalytic activity
- glycine hydroxymethyltransferase activity
- methyltransferase activity
- transferase activity
- transferase activity, transferring one-carbon groups
|
| Process |
- L-serine metabolism
- amino acid and derivative metabolism
- amino acid metabolism
- cellular metabolism
- glycine metabolism
- metabolism
- physiological process
- serine family amino acid metabolism
|
| Component |
| — |
|
| Enzyme 8 General Function |
Amino acid transport and metabolism |
| Enzyme 8 Specific Function |
Interconversion of serine and glycine |
| Enzyme 8 Pathways |
|
| Enzyme 8 Reactions |
- 5,10-methylenetetrahydrofolate + glycine + H2O = tetrahydrofolate + L-serine
|
| Enzyme 8 Pfam Domain Function |
|
| Enzyme 8 Signals |
|
| Enzyme 8 Transmembrane Regions |
|
| Enzyme 8 Essentiality |
Not Available |
| Enzyme 8 GenBank ID Protein |
307422  |
| 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
GTGCAGGCTCTCCGGGAGGAGGTTGAGAGCTTCGCCTCTCTCTTCCCTCTGCCTGGCCTG
CCTGACTTCTAA
|
| Enzyme 8 GenBank Gene ID |
L11931  |
| Enzyme 8 GeneCard ID |
SHMT1  |
| Enzyme 8 GenAtlas ID |
SHMT1  |
| Enzyme 8 HGNC ID |
HGNC:10850  |
| Enzyme 8 Chromosome Location |
17 |
| 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
]
- 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 precursor |
| Enzyme 9 Synonyms |
- Folylpoly-gamma-glutamate synthetase
- FPGS
- Tetrahydrofolate synthase
- Tetrahydrofolylpolyglutamate synthase
|
| Enzyme 9 Gene Name |
FPGS |
| Enzyme 9 Protein Sequence |
>Folylpolyglutamate synthase, mitochondrial precursor
MSRARSHLRAALFLAAASARGITTQVAARRGLSAWPVPQEPSMEYQDAVRMLNTLQTNAG
YLEQVKRQRGDPQTQLEAMELYLARSGLQVEDLDRLNIIHVTGTKGKGSTCAFTECILRS
YGLKTGFFSSPHLVQVRERIRINGQPISPELFTKYFWRLYHRLEETKDGSCVSMPPYFRF
LTLMAFHVFLQEKVDLAVVEVGIGGAYDCTNIIRKPVVCGVSSLGIDHTSLLGDTVEKIA
WQKGGIFKQGVPAFTVLQPEGPLAVLRDRAQQISCPLYLCPMLEALEEGGPPLTLGLEGE
HQRSNAALALQLAHCWLQRQDRHGAGEPKASRPGLLWQLPLAPVFQPTSHMRLGLRNTEW
PGRTQVLRRGPLTWYLDGAHTASSAQACVRWFRQALQGRERPSGGPEVRVLLFNATGDRD
PAALLKLLQPCQFDYAVFCPNLTEVSSTGNADQQNFTVTLDQVLLRCLEHQQHWNHLDEE
QASPDLWSAPSPEPGGSASLLLAPHPPHTCSASSLVFSCISHALQWISQGRDPIFQPPSP
PKGLLTHPVAHSGASILREAAAIHVLVTGSLHLVGGVLKLLEPALSQ
|
| Enzyme 9 Number of Residues |
587 |
| Enzyme 9 Molecular Weight |
64610 |
| Enzyme 9 Theoretical pI |
8.00 |
| Enzyme 9 GO Classification |
| Function |
- ATP binding
- acid-amino acid ligase activity
- adenyl nucleotide binding
- binding
- catalytic activity
- ligase activity
- ligase activity, forming carbon-nitrogen bonds
- nucleotide binding
- purine nucleotide binding
- tetrahydrofolylpolyglutamate synthase activity
|
| Process |
- aromatic compound metabolism
- biosynthesis
- cellular metabolism
- folic acid and derivative biosynthesis
- folic acid and derivative metabolism
- metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 9 General Function |
Coenzyme transport and metabolism |
| 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 + tetrahydrofolyl-[Glu]n + L-glutamate = ADP + phosphate + tetrahydrofolyl-[Glu]n+1
|
| Enzyme 9 Pfam Domain Function |
|
| Enzyme 9 Signals |
|
| Enzyme 9 Transmembrane Regions |
Not Available |
| Enzyme 9 Essentiality |
Not Available |
| Enzyme 9 GenBank ID Protein |
292029  |
| 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 |
>1638 bp
ATGGAGTACCAGGATGCCGTGCGCATGCTCAATACCCTGCAGACCAATGCCGGCTACCTG
GAGCAGGTGAAGCGCCAGCGGGGTGACCCTCAGACACAGTTGGAAGCCATGGAACTGTAC
CTGGCACGGAGTGGGCTGCAGGTGGAGGACTTGGACCGGCTGAACATCATCCACGTCACT
GGGACGAAGGGGAAGGGCTCCACCTGTGCCTTCACGGAATGTATCCTCCGAAGCTATGGC
CTGAAGACGGGATTCTTTAGCTCTCCCCACCTGGTGCAGGTTCGGGAGCGGATCCGCATC
AATGGGCAGCCCATCAGTCCTGAGCTCTTCACCAAGTACTTCTGGCGCCTCTACCACCGG
CTGGAGGAGACCAAGGATGGCAGCTGTGTCTCCATGCCCCCCTACTTCCGCTTCCTGACA
CTCATGGCCTTCCACGTCTTCCTCCAAGAGAAGGTGGACCTGGCAGTGGTGGAGGTGGGC
ATTGGCGGGGCTTATGACTGCACCAACATCATCAGGAAGCCTGTGGTGTGCGGAGTCTCC
TCTCTTGGCATCGACCACACCAGCCTCCTGGGGGATACGGTGGAGAAGATCGCATGGCAG
AAAGGGGGCATCTTTAAGCAAGGTGTCCCTGCCTTCACTGTGCTCCAACCTGAAGGTCCC
CTGGCAGTGCTGAGGGACCGAGCCCAGCAGATCTCATGTCCTCTATACCTGTGTCCGATG
CTGGAGGCCCTCGAGGAAGGGGGGCCGCCGCTGACCCTGGGCCTGGAGGGGGAGCACCAG
CGGTCCAACGCCGCCTTGGCCTTGCAGCTGGCCCACTGCTGGCTGCAGCGGCAGGACCGC
CATGGTGCTGGGGAGCCAAAGGCATCCAGGCCAGGGCTCCTGTGGCAGCTGCCCCTGGCA
CCTGTGTTCCAGCCCACATCCCACATGCGGCTCGGGCTTCGGAACACGGAGTGGCCGGGC
CGGACGCAGGTGCTGCGGCGCGGGCCCCTCACCTGGTACCTGGACGGTGCGCACACCGCC
AGCAGCGCGCAGGCCTGCGTGCGCTGGTTCCGCCAGGCGCTGCAGGGCCGCGAGAGGCCG
AGCGGTGGCCCCGAGGTTCGAGTCTTGCTCTTCAATGCTACCGGGGACCGGGACCCGGCG
GCCCTGCTGAAGCTGCTGCAGCCCTGCCAGTTTGACTATGCCGTCTTCTGCCCTAACCTG
ACAGAGGTGTCATCCACAGGCAACGCAGACCAACAGAACTTCACAGTGACACTGGACCAG
GTCCTGCTCCGCTGCCTGGAACACCAGCAGCACTGGAACCACCTGGACGAAGAGCAGGCC
AGCCCGGACCTCTGGAGTGCCCCCAGCCCAGAGCCCGGTGGGTCCGCATCCCTGCTTCTG
GCGCCCCACCCACCCCACACCTGCAGTGCCAGCTCCCTCGTCTTCAGCTGCATTTCACAT
GCCTTGCAATGGATCAGCCAAGGCCGAGACCCCATCTTCCAGCCACCTAGTCCCCCAAAG
GGCCTCCTCACCCACCCTGTGGCTCACAGTGGGGCCAGCATACTCCGTGAGGCTGCTGCC
ATCCATGTGCTAGTCACTGGCAGCCTGCACCTGGTGGGTGGTGTCCTGAAGCTGCTGGAG
CCCGCACTGTCCCAGTAG
|
| Enzyme 9 GenBank Gene ID |
M98045  |
| 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 |
- 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 [Includes: Phosphoribosylaminoimidazolecarboxamide formyltransferase |
| Enzyme 10 Synonyms |
- 5-aminoimidazole-4-carboxamide ribonucleotide formyltransferase
- AICAR transformylase
- IMP cyclohydrolase
- Inosinicase
- IMP synthetase
- ATIC]
|
| Enzyme 10 Gene Name |
ATIC |
| Enzyme 10 Protein Sequence |
>Bifunctional purine biosynthesis protein PURH [Includes: Phosphoribosylaminoimidazolecarboxamide formyltransferase
MAPGQLALFSVSDKTGLVEFARNLTALGLNLVASGGTAKALRDAGLAVRDVSELTGFPEM
LGGRVKTLHPAVHAGILARNIPEDNADMARLDFNLIRVVACNLYPFVKTVASPGVTVEEA
VEQIDIGGVTLLRAAAKNHARVTVVCEPEDYVVVSTEMQSSESKDTSLETRRQLALKAFT
HTAQYDEAISDYFRKQYSKGVSQMPLRYGMNPHQTPAQLYTLQPKLPITVLNGAPGFINL
CDALNAWQLVKELKEALGIPAAASFKHVSPAGAAVGIPLSEDEAKVCMVYDLYKTLTPIS
AAYARARGADRMSSFGDFVALSDVCDVPTAKIISREVSDGIIAPGYEEEALTILSKKKNG
NYCVLQMDQSYKPDENEVRTLFGLHLSQKRNNGVVDKSLFSNVVTKNKDLPESALRDLIV
ATIAVKYTQSNSVCYAKNGQVIGIGAGQQSRIHCTRLAGDKANYWWLRHHPQVLSMKFKT
GVKRAEISNAIDQYVTGTIGEDEDLIKWKALFEEVPELLTEAEKKEWVEKLTEVSISSDA
FFPFRDNVDRAKRSGVAYIAAPSGSAADKVVIEACDELGIILAHTNLRLFHH
|
| Enzyme 10 Number of Residues |
592 |
| Enzyme 10 Molecular Weight |
64616 |
| 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 |
- cellular metabolism
- metabolism
- nucleobase, nucleoside, nucleotide and nucleic acid metabolism
- nucleotide metabolism
- physiological process
- purine nucleotide biosynthesis
- purine nucleotide metabolism
|
| Component |
| — |
|
| Enzyme 10 General Function |
Nucleotide transport and metabolism |
| Enzyme 10 Specific Function |
10-formyltetrahydrofolate + 5-amino-1-(5- phospho-D-ribosyl)imidazole-4-carboxamide = tetrahydrofolate + 5- formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide |
| Enzyme 10 Pathways |
|
| Enzyme 10 Reactions |
- IMP + H2O = 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
|
| Enzyme 10 Pfam Domain Function |
|
| Enzyme 10 Signals |
|
| Enzyme 10 Transmembrane Regions |
|
| Enzyme 10 Essentiality |
Not Available |
| Enzyme 10 GenBank ID Protein |
1263196  |
| 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 |
>1776 bp
ATGTCTTCTCTCTCAGCCTTATTTAGTGTCTCTGACAAAACCGGCCTTGTGGAATTTGCA
AGAAACCTGACCGCTCTTGGTTTGAACCTGGTCGCTTCCGGAGGGACTGCAAAAGCTCTC
AGGGATGCTGGTCTGGCAGTCAGAGATGTCTCTGAGTTGACGGGATTTCCTGAAATGTTG
GGGGGACGTGTGAAAACTTTGCATCCTGCAGTCCATGCTGGAATCCTAGCTCGTAATATT
CCAGAAGATAATGCTGACATGGCCAGACTTGATTTCAATCTTATAAGAGTTGTCGCCTGC
AATCTCTATCCCTTTGTAAAGACAGTGGCTTCTCCAGGTGTAACTGTTGAGGAGGCTGTG
GAGCAAATTGACATTGGTGGAGTAACCTTACTGAGAGCTGCAGCCAAAAACCACGCTCGA
GTGACAGTGGTGTGTGAACCAGAGGACTATGTGGTGGTGTCCACGGAGATGCAGAGCTCC
GAGAGTAAGGGCACCTCCTTGGAGACTAGACGCCAGTTAGCCTTGAAGGCATTCACTCAT
ACGGCACAATATGATGAAGCAATTTCAGATTATTTCAGGAAACAGTACAGCAAAGGCGTA
TCTCAGATGCCCTTGAGATATGGAATGAACCCACATCAGACCCCTGCCCAGCTGTACACA
CTGCAGCCCAAGCTTCCCATCACAGTTCTAAATGGAGCCCCTGGATTTATAAACTTGTGC
GATGCTTTGAACGCCTGGCAGCTGGTGAAGGAACTCAAGGAGGCTTTAGGTATTCCAGCC
GCTGCCTCTTTCAAACATGTCAGCCCAGCAGGTGCTGCTGTTGGAATTCCACTCAGTGAA
GATGAGGCCAAAGTCTGCATGGTTTATGATCTCTATAAAACCCTCACACCCATCTCAGCG
GCATATGCAAGAGCAAGAGGGGCTGATAGGATGTCTTCATTTGGTGATTTTGTTGCATTG
TCTGATGTTTGTGATGTACCAACTGCAAAAATTATTTCCAGAGAAGTATCTGATGGTATA
ATTGCCCCAGGATATGAAGAAGAAGCCTTGACAATACTTTCCAAAAAGAAAAATGGAAAC
TATTGTGTCCTTCAGATGGACCAATCTTACAAACCAGATGAAAATGAAGTTCGAACTCTC
TTTGGTCTTCATTTAAGCCAGAAGAGAAATAATGGTGTCGTCGACAAGTCATTATTTAGC
AATGTTGTTACCAAAAATAAAGATTTGCCAGAGTCTGCCCTCCGAGACCTCATCGTAGCC
ACCATTGCTGTCAAGTACACTCAGTCTAACTCTGTGTGCTACGCCAAGAACGGGCAGGTT
ATCGGCATTGGAGCAGGACAGCAGTCTCGTATACACTGCACTCGCCTTGCAGGAGATAAG
GCAAACTATTGGTGGCTTAGACACCATCCACAAGTGCTTTCGATGAAGTTTAAAACAGGA
GTGAAGAGAGCAGAAATCTCCAATGCCATCGATCAATATGTGACTGGAACCATTGGCGAG
GATGAAGATTTGATAAAGTGGAAGGCACTGTTTGAGGAAGTCCCTGAGTTACTCACTGAG
GCAGAGAAGAAGGAATGGGTTGAGAAACTGACTGAAGTTTCTATCAGCTCTGATGCCTTC
TTCCCTTTCCGAGATAACGTAGACAGAGCTAAAAGGAGTGGTGTGGCGTACATTGCGGCT
CCCTCCGGTTCTGCTGCTGACAAAGTTGTGATTGAGGCCTGCGACGAACTGGGAATCATC
CTCGCTCATACGAACCTTCGGCTCTTCCACCACTGA
|
| Enzyme 10 GenBank Gene ID |
U37436  |
| 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
]
- 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
]
|
| Enzyme 10 Metabolite References |
Not Available |
|
Enzyme 11
[top]
|
| Enzyme 11 ID |
6208 |
| Enzyme 11 Name |
Bifunctional methylenetetrahydrofolate dehydrogenase/cyclohydrolase, mitochondrial precursor [Includes: NAD-dependent methylenetetrahydrofolate dehydrogenase |
| Enzyme 11 Synonyms |
Not Available |
| Enzyme 11 Gene Name |
MTHFD2 |
| Enzyme 11 Protein Sequence |
>Bifunctional methylenetetrahydrofolate dehydrogenase/cyclohydrolase, mitochondrial precursor [Includes: NAD-dependent methylenetetrahydrofolate dehydrogenase
MAATSLMSALAARLLQPAHSCSLRLRPFHLAAVRNEAVVISGRKLAQQIKQEVRQEVEEW
VASGNKRPHLSVILVGENPASHSYVLNKTRAAAVVGINSETIMKPASISEEELLNLINKL
NNDDNVDGLLVQLPLPEHIDERRICNAVSPDKDVDGFHVINVGRMCLDQYSMLPATPWGV
WEIIKRTGIPTLGKNVVVAGRSKNVGMPIAMLLHTDGAHERPGGDATVTISHRYTPKEQL
KKHTILADIVISAAGIPNLITADMIKEGAAVIDVGINRVHDPVTAKPKLVGDVDFEGVRQ
KAGYITPVPGGVGPMTVAMLMKNTIIAAKKVLRLEEREVLKSKELGVATN
|
| Enzyme 11 Number of Residues |
350 |
| Enzyme 11 Molecular Weight |
37896 |
| Enzyme 11 Theoretical pI |
9.12 |
| Enzyme 11 GO Classification |
| Function |
|
| Process |
- aromatic compound metabolism
- cellular metabolism
- folic acid and derivative biosynthesis
- folic acid and derivative metabolism
- metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 11 General Function |
Coenzyme transport and metabolism |
| 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
|
| Enzyme 11 Pfam Domain Function |
|
| Enzyme 11 Signals |
|
| Enzyme 11 Transmembrane Regions |
Not Available |
| Enzyme 11 Essentiality |
Not Available |
| Enzyme 11 GenBank ID Protein |
35071  |
| 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 |
>1035 bp
ATGTCTGCTTTGGCTGCCCGGCTGCTGCAGCCCGCGCACAGCTGCTCCCTTCGCCTTCGC
CCTTTCCACCTCGCGGCAGTTCGAAATGAAGCTGTTGTCATTTCTGGAAGGAAACTGGCC
CAGCAGATCAAGCAGGAAGTGCGGCAGGAGGTAGAAGAGTGGGTGGCCTCAGGCAACAAA
CGGCCACACCTGAGTGTGATCCTGGTTGGCGAGAATCCTGCAAGTCACTCCTATGTCCTC
AACAAAACCAGGGCAGCTGCAGTTGTGGGAATCAACAGTGAGACAATTATGAAACCAGCT
TCAATTTCAGAGGAAGAATTGTTGAATTTAATCAATAAACTGAATAATGATGATAATGTA
GATGGCCTCCTTGTTCAGTTGCCTCTTCCAGAGCATATTGATGAGAGAAGGATCTGCAAT
GCTGTTTCTCCAGACAAGGATGTTGATGGCTTTCATGTAATTAATGTAGGACGAATGTGT
TTGGATCAGTATTCCATGTTACCGGCTACTCCATGGGGTGTGTGGGAAATAATCAAGCGA
ACTGGCATTCCAACCCTAGGGAAGAATGTGGTTGTGGCTGGAAGGTCAAAAAACGTTGGA
ATGCCCATTGCAATGTTACTGCACACAGATGGGGCGCATGAACGTCCCGGAGGTGATGCC
ACTGTTACAATATCTCATCGATATACTCCCAAAGAGCAGTTGAAGAAACATACAATTCTT
GCAGATATTGTAATATCTGCTGCAGGTATTCCAAATCTGATCACAGCAGATATGATCAAG
GAAGGAGCAGCAGTCATTGATGTGGGAATAAATAGAGTTCACGATCCTGTAACTGCCAAA
CCCAAGTTGGTTGGAGATGTGGATTTTGAAGGAGTCAGACAAAAAGCTGGGTATATCACT
CCAGTTCCTGGAGGTGTTGGCCCCATGACAGTGGCAATGCTAATGAAGAATACCATTATT
GCTGCAAAAAAGGTGCTGAGGCTTGAAGAGCGAGAAGTGCTGAAGTCTAAAGAGCTTGGG
GTAGCCACTAATTAA
|
| Enzyme 11 GenBank Gene ID |
X16396  |
| 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
]
|
| 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[Includes: Methylenetetrahydrofolate dehydrogenase
|
| 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 |
101561 |
| Enzyme 12 Theoretical pI |
7.32 |
| Enzyme 12 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 12 General Function |
Nucleotide transport and metabolism |
| 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
|
| Enzyme 12 Pfam Domain Function |
|
| Enzyme 12 Signals |
|
| Enzyme 12 Transmembrane Regions |
|
| Enzyme 12 Essentiality |
Not Available |
| Enzyme 12 GenBank ID Protein |
307178  |
| Enzyme 12 UniProtKB/Swiss-Prot ID |
P11586  |
| Enzyme 12 UniProtKB/Swiss-Prot Entry Name |
C1TC_HUMAN  |
| Enzyme 12 PDB ID |
Not Available |
| 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
AACATCGCACATGGCAATTCCTCCATCATTGCAGACCGGATCGCACTCAAGCTTGTTGGC
CCAGAAGGGTTTGTAGTGACGGAAGCAGGATTTGGAGCAGACATTGGAATGGAAAAGTTT
TTTAACATCAAATGCCGGTATTCCGGCCTCTGCCCCCACGTGGTGGTGCTTGTTGCCACT
GTCAGGGCTCTCAAGATGCACGGGGGCGGCCCCACGGTCACTGCTGGACTGCCTCTTCCC
AAGGCTTACATACAGGAGAACCTGGAGCTGGTTGAAAAAGGCTTCAGTAACTTGAAGAAA
CAAATTGAAAATGCCAGAATGTTTGGAATTCCAGTAGTAGTGGCCGTGAATGCATTCAAG
ACGGATACAGAGTCTGAGCTGGACCTCATCAGCCGCCTTTCCAGAGAACATGGGGCTTTT
GATGCCGTGAAGTGCACTCACTGGGCAGAAGGGGGCAAGGGTGCCTTAGCCCTGGCTCAG
GCCGTCCAGAGAGCAGCACAAGCACCCAGCAGCTTCCAGCTCCTTTATGACCTCAAGCTC
CCAGTTGAGGATAAAATCAGGATCATTGCACAGAAGATCTATGGAGCAGATGACATTGAA
TTACTTCCCGAAGCTCAACACAAAGCTGAAGTCTACACGAAGCAGGGCTTTGGGAATCTC
CCCATCTGCATGGCTAAAACACACTTGTCTTTGTCTCACAACCCAGAGCAAAAAGGTGTC
CCTACAGGCTTCATTCTGCCCATTCGCGACATCCGCGCCAGCGTTGGGGCTGGTTTTCTG
TACCCCTTAGTAGGAACGATGAGCACAATGCCTGGACTCCCCACCCGGCCCTGTTTTTAT
GATATTGATTTGGACCCTGAAACAGAACAGGTGAATGGATTATTCTAA
|
| Enzyme 12 GenBank Gene ID |
J04031  |
| Enzyme 12 GeneCard ID |
MTHFD1  |
| Enzyme 12 GenAtlas ID |
MTHFD1  |
| Enzyme 12 HGNC ID |
HGNC:7432  |
| Enzyme 12 Chromosome Location |
14 |
| 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
]
- 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
]
- 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
]
- 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
]
|
| 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 1 family 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 |
98830 |
| Enzyme 13 Theoretical pI |
5.76 |
| Enzyme 13 GO Classification |
| Function |
- 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
- transferase activity
- transferase activity, transferring one-carbon groups
|
| Process |
- 10-formyltetrahydrofolate catabolism
- 10-formyltetrahydrofolate metabolism
- aromatic compound metabolism
- biosynthesis
- cellular metabolism
- folic acid and derivative metabolism
- metabolism
- one-carbon compound metabolism
- physiological process
|
| Component |
- cell
- cytoplasm
- intracellular
|
|
| Enzyme 13 General Function |
Energy production and conversion |
| 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+
|
| 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 |
Not Available |
| 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 |
3q21.2 |
| Enzyme 13 SNPs |
SNPJam Report  |
| Enzyme 13 General References |
Not Available |
| Enzyme 13 Metabolite References |
Not Available |
|
Enzyme 14
[top]
|
| Enzyme 14 ID |
8804 |
| Enzyme 14 Name |
Gamma-glutamyl hydrolase precursor |
| Enzyme 14 Synonyms |
- Gamma-Glu-X carboxypeptidase
- Conjugase
- GH
|
| Enzyme 14 Gene Name |
GGH |
| Enzyme 14 Protein Sequence |
>Gamma-glutamyl hydrolase precursor
MASPGCLLCVLGLLLCGAASLELSRPHGDTAKKPIIGILMQKCRNKVMKNYGRYYIAASY
VKYLESAGARVVPVRLDLTEKDYEILFKSINGILFPGGSVDLRRSDYAKVAKIFYNLSIQ
SFDDGDYFPVWGTCLGFEELSLLISGECLLTATDTVDVAMPLNFTGGQLHSRMFQNFPTE
LLLSLAVEPLTANFHKWSLSVKNFTMNEKLKKFFNVLTTNTDGKIEFISTMEGYKYPVYG
VQWHPEKAPYEWKNLDGISHAPNAVKTAFYLAEFFVNEARKNNHHFKSESEEEKALIYQF
SPIYTGNISSFQQCYIFD
|
| Enzyme 14 Number of Residues |
318 |
| Enzyme 14 Molecular Weight |
35965 |
| Enzyme 14 Theoretical pI |
7.14 |
| Enzyme 14 GO Classification |
| Function |
|
| Process |
- amino acid and derivative metabolism
- amino acid metabolism
- cellular metabolism
- glutamine family amino acid metabolism
- glutamine metabolism
- metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 14 General Function |
Not Available |
| 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
|
| Enzyme 14 Pfam Domain Function |
|
| Enzyme 14 Signals |
|
| Enzyme 14 Transmembrane Regions |
Not Available |
| Enzyme 14 Essentiality |
Not Available |
| Enzyme 14 GenBank ID Protein |
2951931  |
| 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
]
|
| 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 |
59175 |
| Enzyme 15 Theoretical pI |
7.42 |
| Enzyme 15 GO Classification |
| Function |
- ATP binding
- acid-amino acid ligase activity
- adenyl nucleotide binding
- binding
- catalytic activity
- ligase activity
- ligase activity, forming carbon-nitrogen bonds
- nucleotide binding
- purine nucleotide binding
- tetrahydrofolylpolyglutamate synthase activity
|
| Process |
- aromatic compound metabolism
- biosynthesis
- cellular metabolism
- folic acid and derivative biosynthesis
- folic acid and derivative metabolism
- metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 15 General Function |
Coenzyme transport and metabolism |
| Enzyme 15 Specific Function |
Not Available |
| Enzyme 15 Pathways |
Not Available |
| Enzyme 15 Reactions |
Not Available |
| Enzyme 15 Pfam Domain Function |
|
| Enzyme 15 Signals |
|
| Enzyme 15 Transmembrane Regions |
|
| Enzyme 15 Essentiality |
Not Available |
| Enzyme 15 GenBank ID Protein |
Not Available |
| 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 |
Not Available |
| Enzyme 15 GenBank Gene ID |
AL162586  |
| Enzyme 15 GeneCard ID |
Q5JU19  |
| Enzyme 15 GenAtlas ID |
FPGS  |
| Enzyme 15 HGNC ID |
HGNC:3824  |
| Enzyme 15 Chromosome Location |
Not Available |
| Enzyme 15 Locus |
Not Available |
| 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 (cDNA, FLJ93028, Homo sapiens dihydrofolate reductase (DHFR), mRNA) |
| Enzyme 16 Synonyms |
Not Available |
| Enzyme 16 Gene Name |
DYR |
| Enzyme 16 Protein Sequence |
>Dihydrofolate reductase (cDNA, FLJ93028, Homo sapiens dihydrofolate reductase (DHFR), mRNA)
MVGSLNCIVAVSQNMGIGKNGDLPWPPLRNEFRYFQRMTTTSSVEGKQNLVIMGKKTWFS
IPEKNRPLKGRINLVLSRELKEPPQGAHFLSRSLDDALKLTEQPELANKVDMVWIVGGSS
VYKEAMNHPGHLKLFVTRIMQDFESDTFFPEIDLEKYKLLPEYPGVLSDVQEEKGIKYKF
EVYEKND
|
| Enzyme 16 Number of Residues |
187 |
| Enzyme 16 Molecular Weight |
21453 |
| Enzyme 16 Theoretical pI |
Not Available |
| Enzyme 16 GO Classification |
Not Available |
| Enzyme 16 General Function |
Not Available |
| 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 |
Not Available |
| Enzyme 16 UniProtKB/Swiss-Prot ID |
B0YJ76  |
| Enzyme 16 UniProtKB/Swiss-Prot Entry Name |
B0YJ76_HUMAN  |
| Enzyme 16 PDB ID |
Not Available |
| Enzyme 16 Cellular Location |
Not Available |
| Enzyme 16 Gene Sequence |
Not Available |
| Enzyme 16 GenBank Gene ID |
Not Available |
| Enzyme 16 GeneCard ID |
B0YJ76  |
| Enzyme 16 GenAtlas ID |
Not Available |
| Enzyme 16 HGNC ID |
Not Available |
| Enzyme 16 Chromosome Location |
Not Available |
| Enzyme 16 Locus |
Not Available |
| Enzyme 16 SNPs |
SNPJam Report  |
| Enzyme 16 General References |
Not Available |
| 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 precursor |
| Enzyme 19 Synonyms |
- MtFMT
|
| Enzyme 19 Gene Name |
MTFMT |
| Enzyme 19 Protein Sequence |
>Methionyl-tRNA formyltransferase, mitochondrial precursor
MRVLVRRCWGPPLAHGARRGRPSPQWRALARLGWEDCRDSRVREKPPWRVLFFGTDQFAR
EALRALHAARENKEEELIDKLEVVTMPSPSPKGLPVKQYAVQSQLPVYEWPDVGSGEYDV
GVVASFGRLLNEALILKFPYGILNVHPSCLPRWRGPAPVIHTVLHGDTVTGVTIMQIRPK
RFDVGPILKQETVPVPPKSTAKELEAVLSRLGANMLISVLKNLPESLSNGRQQPMEGATY
APKISAGTSCIKWEEQTSEQIFRLYRAIGNIIPLQTLWMANTIKLLDLVEVNSSVLADPK
LTGQALIPGSVIYHKQSQILLVYCKDGWIGVRSVMLKKSLTATDFYNGYLHPWYQKNSQA
QPSQCRFQTLRLPTKKKQKKTVAMQQCIE
|
| Enzyme 19 Number of Residues |
389 |
| Enzyme 19 Molecular Weight |
43833 |
| 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 |
- biosynthesis
- macromolecule biosynthesis
- macromolecule metabolism
- metabolism
- physiological process
- protein biosynthesis
|
| Component |
| — |
|
| Enzyme 19 General Function |
Translation, ribosomal structure and biogenesis |
| 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] ALL_REAC R03940
|
| Enzyme 19 Pfam Domain Function |
|
| Enzyme 19 Signals |
|
| Enzyme 19 Transmembrane Regions |
|
| Enzyme 19 Essentiality |
Not Available |
| Enzyme 19 GenBank ID Protein |
133777035  |
| 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 |
Not Available |
| Enzyme 19 GenBank Gene ID |
BC016630  |
| Enzyme 19 GeneCard ID |
Q96DP5  |
| Enzyme 19 GenAtlas ID |
MTFMT  |
| Enzyme 19 HGNC ID |
HGNC:29666  |
| Enzyme 19 Chromosome Location |
Not Available |
| Enzyme 19 Locus |
Not Available |
| Enzyme 19 SNPs |
SNPJam Report  |
| Enzyme 19 General References |
Not Available |
| Enzyme 19 Metabolite References |
Not Available |
|
Enzyme 20
[top]
|
| Enzyme 20 ID |
13034 |
| Enzyme 20 Name |
C1-tetrahydrofolate synthase |
| Enzyme 20 Synonyms |
- Methylenetetrahydrofolate dehydrogenase
- NADP+ dependent1-like
- Mitochondrial C1-tetrahydrofolate synthetase
|
| Enzyme 20 Gene Name |
MTHFD1L |
| Enzyme 20 Protein Sequence |
>C1-tetrahydrofolate synthase
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 |
105791 |
| Enzyme 20 Theoretical pI |
8.15 |
| Enzyme 20 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 20 General Function |
Nucleotide transport and metabolism |
| Enzyme 20 Specific Function |
Not Available |
| 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] ALL_REAC R00943
- (other) R01655
|
| Enzyme 20 Pfam Domain Function |
|
| Enzyme 20 Signals |
|
| Enzyme 20 Transmembrane Regions |
|
| Enzyme 20 Essentiality |
Not Available |
| Enzyme 20 GenBank ID Protein |
34811726  |
| Enzyme 20 UniProtKB/Swiss-Prot ID |
Q6UB35  |
| Enzyme 20 UniProtKB/Swiss-Prot Entry Name |
Q6UB35_HUMAN  |
| Enzyme 20 PDB ID |
Not Available |
| Enzyme 20 Cellular Location |
Not Available |
| Enzyme 20 Gene Sequence |
Not Available |
| Enzyme 20 GenBank Gene ID |
AY374130  |
| Enzyme 20 GeneCard ID |
Q6UB35  |
| Enzyme 20 GenAtlas ID |
MTHFD1L  |
| Enzyme 20 HGNC ID |
HGNC:21055  |
| Enzyme 20 Chromosome Location |
Not Available |
| Enzyme 20 Locus |
Not Available |
| 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
]
|
| Enzyme 20 Metabolite References |
Not Available |
|
Enzyme 21
[top]
|
| Enzyme 21 ID |
13035 |
| Enzyme 21 Name |
Methylenetetrahydrofolate dehydrogenase |
| Enzyme 21 Synonyms |
- NADP+ dependent2, methenyltetrahydrofolate cyclohydrolase
- Methylenetetrahydrofolate dehydrogenase
- NADP+ dependent2, methenyltetrahydrofolate cyclohydrolase, isoform CRA_b
|
| Enzyme 21 Gene Name |
MTHFD2 |
| Enzyme 21 Protein Sequence |
>Methylenetetrahydrofolate dehydrogenase
MKPASISEEELLNLINKLNNDDNVDGLLVQLPLPEHIDERRICNAVSPDKDVDGFHVINV
GRMCLDQYSMLPATPWGVWEIIKRTGIPTLGKNVVVAGRSKNVGMPIAMLLHTDGAHERP
GGDATVTISHRYTPKEQLKKHTILADIVISAAGIPNLITADMIKEGAAVIDVGINRVHDP
VTAKPKLVGDVDFEGVRQKAGYITPVPGGVGPMTVAMLMKNTIIAAKKVLRLEEREVLKS
KELGVATN
|
| Enzyme 21 Number of Residues |
248 |
| Enzyme 21 Molecular Weight |
26850 |
| Enzyme 21 Theoretical pI |
7.22 |
| Enzyme 21 GO Classification |
| Function |
|
| Process |
- aromatic compound metabolism
- cellular metabolism
- folic acid and derivative biosynthesis
- folic acid and derivative metabolism
- metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 21 General Function |
Coenzyme transport and metabolism |
| 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 |
31418096  |
| 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 |
Not Available |
| Enzyme 21 GenBank Gene ID |
BC015062  |
| Enzyme 21 GeneCard ID |
Q7Z650  |
| Enzyme 21 GenAtlas ID |
MTHFD2  |
| Enzyme 21 HGNC ID |
HGNC:7434  |
| Enzyme 21 Chromosome Location |
Not Available |
| Enzyme 21 Locus |
Not Available |
| Enzyme 21 SNPs |
SNPJam Report  |
| Enzyme 21 General References |
- Strausberg RL, Feingold EA, Grouse LH, Derge JG, Klausner RD, Collins FS, Wagner L, Shenmen CM, Schuler GD, Altschul SF, Zeeberg B, Buetow KH, Schaefer CF, Bhat NK, Hopkins RF, Jordan H, Moore T, Max SI, Wang J, Hsieh F, Diatchenko L, Marusina K, Farmer AA, Rubin GM, Hong L, Stapleton M, Soares MB, Bonaldo MF, Casavant TL, Scheetz TE, Brownstein MJ, Usdin TB, Toshiyuki S, Carninci P, Prange C, Raha SS, Loquellano NA, Peters GJ, Abramson RD, Mullahy SJ, Bosak SA, McEwan PJ, McKernan KJ, Malek JA, Gunaratne PH, Richards S, Worley KC, Hale S, Garcia AM, Gay LJ, Hulyk SW, Villalon DK, Muzny DM, Sodergren EJ, Lu X, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madan A, Young AC, Shevchenko Y, Bouffard GG, Blakesley RW, Touchman JW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Krzywinski MI, Skalska U, Smailus DE, Schnerch A, Schein JE, Jones SJ, Marra MA: Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. Proc Natl Acad Sci U S A. 2002 Dec 24;99(26):16899-903. Epub 2002 Dec 11. [PubMed
]
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| Enzyme 21 Metabolite References |
Not Available |
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Enzyme 22
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| 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
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| 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
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| Process |
- aromatic compound metabolism
- cellular metabolism
- folic acid and derivative biosynthesis
- folic acid and derivative metabolism
- metabolism
- physiological process
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| Component |
| — |
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| 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 |
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| Enzyme 22 Signals |
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| Enzyme 22 Transmembrane Regions |
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| 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 |