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Human Metabolome Database Version 2.5

 

Showing metabocard for 5,10-Methylene-THF (HMDB01533)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2005-11-16 15:48:42
Update Date 2009-05-05 20:58:50
Accession Number HMDB01533
Secondary Accession Numbers HMDB02365
Common Name 5,10-Methylene-THF
Description 5,10-Methylene-THF is an intermediate in the metabolism of Methane and the metabolism of Nitrogen. It is a substrate for Bifunctional methylenetetrahydrofolate dehydrogenase/cyclohydrolase (mitochondrial), Aminomethyltransferase (mitochondrial), Serine hydroxymethyltransferase (mitochondrial), Methylenetetrahydrofolate reductase, C-1-tetrahydrofolate synthase (cytoplasmic), Serine hydroxymethyltransferase (cytosolic) and Thymidylate synthase.
Synonyms
  1. 5,10-methylene-THF
  2. N5>,N10-methylenetetrahydrofolate
  3. (6R)-5,10-methylenetetrahydrofolate
  4. 5,10-Methenyltetrahydropteroylglutamate
  5. 5,10-Methylene-6-Hydrofolate
  6. 5,10-Methylene-6-Hydrofolic acid
  7. 5,10-Methylenetetrahydrofolate
  8. 5,10-Methylenetetrahydrofolic acid
Chemical IUPAC Name N-{4-[(6aR)-3-amino-1-oxo-1,2,5,6,6a,7-hexahydroimidazo[1,5-f]pteridin-8(9H)-yl]benzoyl}-L-glutamate
Chemical Formula C20H23N7O6
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Heterocyclic molecules
Class
  • Pterins
Sub Class
  • Tetrahydro-pterins
Family
  • Mammalian Metabolite
Species
  • aminal
  • primary amine
  • primary aromatic amine
  • secondary amine
  • secondary aliphatic/aromatic amine (alkylarylamine)
  • carboxylic acid
  • secondary carboxylic acid amide
  • oxo(het)arene
  • aromatic compound
  • heterocyclic compound
Biofunction
  • DNA component
  • Component of Cyanoamino acid metabolism
  • Component of Glycine, serine and threonine metabolism
  • Component of Methane metabolism
  • Component of Nitrogen metabolism
  • Component of Pyrimidine metabolism
Application
Source
  • Endogenous
Average Molecular Weight 457.440
Monoisotopic Molecular Weight 457.170990
Isomeric SMILES NC1=NC2=C(N3CN(C[C@H]3CN2)C2=CC=C(C=C2)C(=O)NC(CCC(O)=O)C(O)=O)C(=O)N1
Canonical SMILES NC1=NC2=C(N3CN(CC3CN2)C2=CC=C(C=C2)C(=O)NC(CCC(O)=O)C(O)=O)C(=O)N1
KEGG Compound ID C00143 Link Image
BioCyc ID METHYLENE-THF Link Image
BiGG ID 34022 Link Image
Wikipedia Link 5,10-methylenetetrahydrofolate Link Image
NuGOwiki Link HMDB01533 Link Image
Metagene Link HMDB01533 Link Image
METLIN ID 6304 Link Image
PubChem Compound Not Available
PubChem Substance Not Available
ChEBI ID 15636 Link Image
CAS Registry Number 31690-11-6
InChI Identifier InChI=1/C20H23N7O6/c21-20-24-16-15(18(31)25-20)27-9-26(8-12(27)7-22-16)11-3-1-10(2-4-11)17(30)23-13(19(32)33)5-6-14(28)29/h1-4,12-13H,5-9H2,(H,23,30)(H,28,29)(H,32,33)(H4,21,22,24,25,31)/t12-,13?/m1/s1
Synthesis Reference Agrawal, Nitish; Mihai, Cornelia; Kohen, Amnon. Microscale synthesis of isotopically labeled R-[6-xH]N5,N10-methylene-5,6,7,8-tetrahydrofolate as a cofactor for thymidylate synthase. Analytical Biochemistry (2004), 328(1), 44-50.
Melting Point (Experimental) Not Available
Experimental Water Solubility Not Available Source: PhysProp
Predicted Water Solubility 0.82299995 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge -2
State Solid
Experimental LogP/Hydrophobicity Not Available Source: PhysProp
Predicted LogP/Hydrophobicity -0.94 [Predicted by ALOGPS]; -1.7 [Predicted by PubChem via XLOGP] Calculated using ALOGPS
Material Safety Data Sheet (MSDS) Not Available
MOL File Show Link Image
SDF File Show Link Image
PDB File Show Link Image
2D Structure
3D Structure
Experimental PDB ID Not Available
Experimental 1H NMR Spectrum Not Available
Experimental 13C NMR Spectrum Not Available
Experimental 13C HSQC Spectrum Not Available
Predicted 1H NMR Spectrum Show Image
Show Peaklist
Predicted 13C NMR Spectrum Show Image
Show Peaklist
Mass Spectrum Not Available
Simplified TOCSY Spectrum Not Available
BMRB Spectrum Not Available
Cellular Location
  • Cytoplasm (Predicted from LogP)
  • mitochondria
Biofluid Location
  • Blood
Tissue Location Not Available
Concentrations (Normal)
Biofluid Blood
Value 0.01 (0.0-0.21) uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Fazili Z, Pfeiffer CM, Zhang M, Jain RB, Koontz D: Influence of 5,10-methylenetetrahydrofolate reductase polymorphism on whole-blood folate concentrations measured by LC-MS/MS, microbiologic assay, and bio-rad radioassay. Clin Chem. 2008 Jan;54(1):197-201. [PubMed Link Image]
Concentrations (Abnormal) Not Available
Associated Disorders Not Available
OMIM ID Not Available
Pathways
Name SMPDB Link KEGG Link
Ammonia Recycling SMP00009 Link Image map00910 Link Image
Folate Metabolism SMP00053 Link Image map00670 Link Image
Glycine and Serine Metabolism SMP00004 Link Image map00260 Link Image
General References
  1. Wikipedia Link Image
Metabolic Enzymes
  1. Thymidylate synthase
  2. Methylenetetrahydrofolate reductase
  3. Aminomethyltransferase, mitochondrial
  4. Serine hydroxymethyltransferase, mitochondrial
  5. Serine hydroxymethyltransferase, cytosolic
  6. C-1-tetrahydrofolate synthase, cytoplasmic
  7. cDNA FLJ76259, highly similar to Homo sapiens aminomethyltransferase
  8. Monofunctional C1-tetrahydrofolate synthase, mitochondrial
  9. Methylenetetrahydrofolate dehydrogenase (NADP+ dependent) 2, methenyltetrahydrofolate cyclohydrolase
  10. Putative uncharacterized protein
Enzyme 1 [top]
Enzyme 1 ID 5316
Enzyme 1 Name Thymidylate synthase
Enzyme 1 Synonyms
  1. TS
  2. TSase
Enzyme 1 Gene Name TYMS
Enzyme 1 Protein Sequence >Thymidylate synthase
MPVAGSELPRRPLPPAAQERDAEPRPPHGELQYLGQIQHILRCGVRKDDRTGTGTLSVFG
MQARYSLRDEFPLLTTKRVFWKGVLEELLWFIKGSTNAKELSSKGVKIWDANGSRDFLDS
LGFSTREEGDLGPVYGFQWRHFGAEYRDMESDYSGQGVDQLQRVIDTIKTNPDDRRIIMC
AWNPRDLPLMALPPCHALCQFYVVNSELSCQLYQRSGDMGLGVPFNIASYALLTYMIAHI
TGLKPGDFIHTLGDAHIYLNHIEPLKIQLQREPRPFPKLRILRKVEKIDDFKAEDFQIEG
YNPHPTIKMEMAV
Enzyme 1 Number of Residues 313
Enzyme 1 Molecular Weight 35715.7
Enzyme 1 Theoretical pI 7.00
Enzyme 1 GO Classification
Function
  • 5,10-methylenetetrahydrofolate-dependent methyltransferase activity
  • catalytic activity
  • methyltransferase activity
  • thymidylate synthase activity
  • transferase activity
  • transferase activity, transferring one-carbon groups
Process
  • cellular nitrogen compound metabolic process
  • dTMP biosynthetic process
  • metabolic process
  • nitrogen compound metabolic process
  • nucleobase, nucleoside and nucleotide metabolic process
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
  • nucleoside phosphate metabolic process
  • nucleotide metabolic process
  • pyrimidine deoxyribonucleoside monophosphate biosynthetic process
  • pyrimidine nucleoside monophosphate biosynthetic process
  • pyrimidine nucleotide biosynthetic process
  • pyrimidine nucleotide metabolic process
Component
Enzyme 1 General Function Involved in thymidylate synthase activity
Enzyme 1 Specific Function 5,10-methylenetetrahydrofolate + dUMP = dihydrofolate + dTMP
Enzyme 1 Pathways
Enzyme 1 Reactions
  • 5,10-methylenetetrahydrofolate + dUMP = dihydrofolate + dTMP [RN:R02101]
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • None
Enzyme 1 Transmembrane Regions
  • None
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 37479 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID P04818 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name TYSY_HUMAN Link Image
Enzyme 1 PDB ID 1JUJ Link Image
Enzyme 1 PDB File Show
Enzyme 1 3D Structure
Enzyme 1 Cellular Location Not Available
Enzyme 1 Gene Sequence >942 bp
ATGCCTGTGGCCGGCTCGGAGCTGCCGCGCCGGCCCTTGCCCCCCGCCGCACAGGAGCGG
GACGCCGAGCCGCGTCCGCCGCACGGGGAGCTGCAGTACCTGGGGCAGATCCAACACATC
CTCCGCTGCGGCGTCAGGAAGGACGACCGCACGGGCACCGGCACCCTGTCGGTATTCGGC
ATGCAGGCGCGCTACAGCCTGAGAGATGAATTCCCTCTGCTGACAACCAAACGTGTGTTC
TGGAAGGGTGTTTTGGAGGAGTTGCTGTGGTTTATCAAGGGATCCACAAATGCTAAAGAG
CTGTCTTCCAAGGGAGTGAAAATCTGGGATGCCAATGGATCCCGAGACTTTTTGGACAGC
CTGGGATTCTCCACCAGAGAAGAAGGGGACTTGGGCCCAGTTTATGGCTTCCAGTGGAGG
CATTTTGGGGCAGAATACAGAGATATGGAATCAGATTATTCAGGACAGGGAGTTGACCAA
CTGCAAAGAGTGATTGACACCATCAAAACCAACCCTGACGACAGAAGAATCATCATGTGC
GCTTGGAATCCAAGAGATCTTCCTCTGATGGCGCTGCCTCCATGCCATGCCCTCTGCCAG
TTCTATGTGGTGAACAGTGAGCTGTCCTGCCAGCTGTACCAGAGATCGGGAGACATGGGC
CTCGGTGTGCCTTTCAACATCGCCAGCTACGCCCTGCTCACGTACATGATTGCGCACATC
ACGGGCCTGAAGCCAGGTGACTTTATACACACTTTGGGAGATGCACATATTTACCTGAAT
CACATCGAGCCACTGAAAATTCAGCTTCAGCGAGAACCCAGACCTTTCCCAAAGCTCAGG
ATTCTTCGAAAAGTTGAGAAAATTGATGACTTCAAAGCTGAAGACTTTCAGATTGAAGGG
TACAATCCGCATCCAACTATTAAAATGGAAATGGCTGTTTAG
Enzyme 1 GenBank Gene ID X02308 Link Image
Enzyme 1 GeneCard ID TYMS Link Image
Enzyme 1 GenAtlas ID TYMS Link Image
Enzyme 1 HGNC ID HGNC:12441 Link Image
Enzyme 1 Chromosome Location 1
Enzyme 1 Locus 18p11.32
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 General References
  1. Takeishi K, Kaneda S, Ayusawa D, Shimizu K, Gotoh O, Seno T: Nucleotide sequence of a functional cDNA for human thymidylate synthase. Nucleic Acids Res. 1985 Mar 25;13(6):2035-43. [PubMed Link Image]
  2. Kaneda S, Nalbantoglu J, Takeishi K, Shimizu K, Gotoh O, Seno T, Ayusawa D: Structural and functional analysis of the human thymidylate synthase gene. J Biol Chem. 1990 Nov 25;265(33):20277-84. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Takeishi K, Kaneda S, Ayusawa D, Shimizu K, Gotoh O, Seno T: Human thymidylate synthase gene: isolation of phage clones which cover a functionally active gene and structural analysis of the region upstream from the translation initiation codon. J Biochem (Tokyo). 1989 Oct;106(4):575-83. [PubMed Link Image]
  5. Shimizu K, Ayusawa D, Takeishi K, Seno T: Purification and NH2-terminal amino acid sequence of human thymidylate synthase in an overproducing transformant of mouse FM3A cells. J Biochem (Tokyo). 1985 Mar;97(3):845-50. [PubMed Link Image]
  6. Davisson VJ, Sirawaraporn W, Santi DV: Expression of human thymidylate synthase in Escherichia coli. J Biol Chem. 1989 Jun 5;264(16):9145-8. [PubMed Link Image]
  7. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed Link Image]
  8. Schiffer CA, Clifton IJ, Davisson VJ, Santi DV, Stroud RM: Crystal structure of human thymidylate synthase: a structural mechanism for guiding substrates into the active site. Biochemistry. 1995 Dec 19;34(50):16279-87. [PubMed Link Image]
  9. Phan J, Koli S, Minor W, Dunlap RB, Berger SH, Lebioda L: Human thymidylate synthase is in the closed conformation when complexed with dUMP and raltitrexed, an antifolate drug. Biochemistry. 2001 Feb 20;40(7):1897-902. [PubMed Link Image]
  10. Phan J, Steadman DJ, Koli S, Ding WC, Minor W, Dunlap RB, Berger SH, Lebioda L: Structure of human thymidylate synthase suggests advantages of chemotherapy with noncompetitive inhibitors. J Biol Chem. 2001 Apr 27;276(17):14170-7. Epub 2001 Jan 24. [PubMed Link Image]
Enzyme 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 5420
Enzyme 2 Name Methylenetetrahydrofolate reductase
Enzyme 2 Synonyms Not Available
Enzyme 2 Gene Name MTHFR
Enzyme 2 Protein Sequence >Methylenetetrahydrofolate reductase
MVNEARGNSSLNPCLEGSASSGSESSKDSSRCSTPGLDPERHERLREKMRRRLESGDKWF
SLEFFPPRTAEGAVNLISRFDRMAAGGPLYIDVTWHPAGDPGSDKETSSMMIASTAVNYC
GLETILHMTCCRQRLEEITGHLHKAKQLGLKNIMALRGDPIGDQWEEEEGGFNYAVDLVK
HIRSEFGDYFDICVAGYPKGHPEAGSFEADLKHLKEKVSAGADFIITQLFFEADTFFRFV
KACTDMGITCPIVPGIFPIQGYHSLRQLVKLSKLEVPQEIKDVIEPIKDNDAAIRNYGIE
LAVSLCQELLASGLVPGLHFYTLNREMATTEVLKRLGMWTEDPRRPLPWALSAHPKRREE
DVRPIFWASRPKSYIYRTQEWDEFPNGRWGNSSSPAFGELKDYYLFYLKSKSPKEELLKM
WGEELTSEESVFEVFVLYLSGEPNRNGHKVTCLPWNDEPLAAETSLLKEELLRVNRQGIL
TINSQPNINGKPSSDPIVGWGPSGGYVFQKAYLEFFTSRETAEALLQVLKKYELRVNYHL
VNVKGENITNAPELQPNAVTWGIFPGREIIQPTVVDPVSFMFWKDEAFALWIERWGKLYE
EESPSRTIIQYIHDNYFLVNLVDNDFPLDNCLWQVVEDTLELLNRPTQNARETEAP
Enzyme 2 Number of Residues 656
Enzyme 2 Molecular Weight 74595.9
Enzyme 2 Theoretical pI 5.00
Enzyme 2 GO Classification
Function
  • catalytic activity
  • methylenetetrahydrofolate reductase (NADPH) activity
  • methylenetetrahydrofolate reductase (NADPH) activity
  • oxidoreductase activity
  • oxidoreductase activity, acting on the CH-NH group of donors
  • oxidoreductase activity, acting on the CH-NH group of donors, NAD or NADP as acceptor
Process
  • cellular amino acid and derivative metabolic process
  • cellular amino acid metabolic process
  • cellular metabolic process
  • metabolic process
  • methionine metabolic process
  • oxidation reduction
  • sulfur amino acid metabolic process
Component
Enzyme 2 General Function Involved in methylenetetrahydrofolate reductase (NADPH) activity
Enzyme 2 Specific Function Catalyzes the conversion of 5,10- methylenetetrahydrofolate to 5-methyltetrahydrofolate, a co- substrate for homocysteine remethylation to methionine
Enzyme 2 Pathways
Enzyme 2 Reactions
  • 5-methyltetrahydrofolate + NAD(P)+ = 5,10-methylenetetrahydrofolate + NAD(P)H + H+ [RN:R01224 R07168]
Enzyme 2 Pfam Domain Function
Enzyme 2 Signals
  • None
Enzyme 2 Transmembrane Regions
  • None
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein 6139053 Link Image
Enzyme 2 UniProtKB/Swiss-Prot ID P42898 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name MTHR_HUMAN Link Image
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 Link Image
Enzyme 2 GeneCard ID MTHFR Link Image
Enzyme 2 GenAtlas ID MTHFR Link Image
Enzyme 2 HGNC ID HGNC:7436 Link Image
Enzyme 2 Chromosome Location 1
Enzyme 2 Locus 1p36.3
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 General References
  1. 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 Link Image]
  2. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  3. Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. 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 Link Image]
  6. 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 Link Image]
  7. 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 Link Image]
  8. van der Put NM, Steegers-Theunissen RP, Frosst P, Trijbels FJ, Eskes TK, van den Heuvel LP, Mariman EC, den Heyer M, Rozen R, Blom HJ: Mutated methylenetetrahydrofolate reductase as a risk factor for spina bifida. Lancet. 1995 Oct 21;346(8982):1070-1. [PubMed Link Image]
  9. 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 Link Image]
  10. Ou CY, Stevenson RE, Brown VK, Schwartz CE, Allen WP, Khoury MJ, Rozen R, Oakley GP Jr, Adams MJ Jr: 5,10 Methylenetetrahydrofolate reductase genetic polymorphism as a risk factor for neural tube defects. Am J Med Genet. 1996 Jun 28;63(4):610-4. [PubMed Link Image]
  11. 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 Link Image]
  12. Chen J, Giovannucci E, Kelsey K, Rimm EB, Stampfer MJ, Colditz GA, Spiegelman D, Willett WC, Hunter DJ: A methylenetetrahydrofolate reductase polymorphism and the risk of colorectal cancer. Cancer Res. 1996 Nov 1;56(21):4862-4. [PubMed Link Image]
  13. 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 Link Image]
  14. 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 Link Image]
  15. 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 Link Image]
  16. 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 Link Image]
  17. Christensen B, Arbour L, Tran P, Leclerc D, Sabbaghian N, Platt R, Gilfix BM, Rosenblatt DS, Gravel RA, Forbes P, Rozen R: Genetic polymorphisms in methylenetetrahydrofolate reductase and methionine synthase, folate levels in red blood cells, and risk of neural tube defects. Am J Med Genet. 1999 May 21;84(2):151-7. [PubMed Link Image]
  18. Skibola CF, Smith MT, Kane E, Roman E, Rollinson S, Cartwright RA, Morgan G: Polymorphisms in the methylenetetrahydrofolate reductase gene are associated with susceptibility to acute leukemia in adults. Proc Natl Acad Sci U S A. 1999 Oct 26;96(22):12810-5. [PubMed Link Image]
  19. 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 Link Image]
  20. Casas JP, Hingorani AD, Bautista LE, Sharma P: Meta-analysis of genetic studies in ischemic stroke: thirty-two genes involving approximately 18,000 cases and 58,000 controls. Arch Neurol. 2004 Nov;61(11):1652-61. [PubMed Link Image]
  21. Ley TJ, Mardis ER, Ding L, Fulton B, McLellan MD, Chen K, Dooling D, Dunford-Shore BH, McGrath S, Hickenbotham M, Cook L, Abbott R, Larson DE, Koboldt DC, Pohl C, Smith S, Hawkins A, Abbott S, Locke D, Hillier LW, Miner T, Fulton L, Magrini V, Wylie T, Glasscock J, Conyers J, Sander N, Shi X, Osborne JR, Minx P, Gordon D, Chinwalla A, Zhao Y, Ries RE, Payton JE, Westervelt P, Tomasson MH, Watson M, Baty J, Ivanovich J, Heath S, Shannon WD, Nagarajan R, Walter MJ, Link DC, Graubert TA, DiPersio JF, Wilson RK: DNA sequencing of a cytogenetically normal acute myeloid leukaemia genome. Nature. 2008 Nov 6;456(7218):66-72. [PubMed Link Image]
Enzyme 2 Metabolite References Not Available
Enzyme 3 [top]
Enzyme 3 ID 5961
Enzyme 3 Name Aminomethyltransferase, mitochondrial
Enzyme 3 Synonyms
  1. Glycine cleavage system T protein
  2. GCVT
Enzyme 3 Gene Name AMT
Enzyme 3 Protein Sequence >Aminomethyltransferase, mitochondrial
MQRAVSVVARLGFRLQAFPPALCRPLSCAQEVLRRTPLYDFHLAHGGKMVAFAGWSLPVQ
YRDSHTDSHLHTRQHCSLFDVSHMLQTKILGSDRVKLMESLVVGDIAELRPNQGTLSLFT
NEAGGILDDLIVTNTSEGHLYVVSNAGCWEKDLALMQDKVRELQNQGRDVGLEVLDNALL
ALQGPTAAQVLQAGVADDLRKLPFMTSAVMEVFGVSGCRVTRCGYTGEDGVEISVPVAGA
VHLATAILKNPEVKLAGLAARDSLRLEAGLCLYGNDIDEHTTPVEGSLSWTLGKRRRAAM
DFPGAKVIVPQLKGRVQRRRVGLMCEGAPMRAHSPILNMEGTKIGTVTSGCPSPSLKKNV
AMGYVPCEYSRPGTMLLVEVRRKQQMAVVSKMPFVPTNYYTLK
Enzyme 3 Number of Residues 403
Enzyme 3 Molecular Weight 43945.7
Enzyme 3 Theoretical pI 8.69
Enzyme 3 GO Classification
Function
  • aminomethyltransferase activity
  • catalytic activity
  • methyltransferase activity
  • transferase activity
  • transferase activity, transferring one-carbon groups
Process
  • cellular amino acid and derivative metabolic process
  • cellular amino acid metabolic process
  • cellular metabolic process
  • glycine catabolic process
  • glycine metabolic process
  • metabolic process
  • serine family amino acid metabolic process
Component
  • cell part
  • cytoplasm
  • intracellular part
Enzyme 3 General Function Involved in aminomethyltransferase activity
Enzyme 3 Specific Function The glycine cleavage system catalyzes the degradation of glycine
Enzyme 3 Pathways
Enzyme 3 Reactions
  • [protein]-S8-aminomethyldihydrolipoyllysine + tetrahydrofolate = [protein]-dihydrolipoyllysine + 5,10-methylenetetrahydrofolate + NH3 [RN:R04125]
Enzyme 3 Pfam Domain Function
Enzyme 3 Signals
  • None
Enzyme 3 Transmembrane Regions
  • None
Enzyme 3 Essentiality Not Available
Enzyme 3 GenBank ID Protein 158254632 Link Image
Enzyme 3 UniProtKB/Swiss-Prot ID P48728 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name GCST_HUMAN Link Image
Enzyme 3 PDB ID Not Available
Enzyme 3 Cellular Location Not Available
Enzyme 3 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 3 GenBank Gene ID AK290600 Link Image
Enzyme 3 GeneCard ID AMT Link Image
Enzyme 3 GenAtlas ID AMT Link Image
Enzyme 3 HGNC ID HGNC:473 Link Image
Enzyme 3 Chromosome Location 3
Enzyme 3 Locus 3p21.2-p21.1
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 General References
  1. 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 Link Image]
  2. 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 Link Image]
  3. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  4. 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 Link Image]
  5. 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 Link Image]
  6. 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 Link Image]
  7. 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 Link Image]
  8. 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 Link Image]
Enzyme 3 Metabolite References Not Available
Enzyme 4 [top]
Enzyme 4 ID 6072
Enzyme 4 Name Serine hydroxymethyltransferase, mitochondrial
Enzyme 4 Synonyms
  1. SHMT
  2. Glycine hydroxymethyltransferase
  3. Serine methylase
Enzyme 4 Gene Name SHMT2
Enzyme 4 Protein Sequence >Serine hydroxymethyltransferase, mitochondrial
MLYFSLFWAARPLQRCGQLVRMAIRAQHSNAAQTQTGEANRGWTGQESLSDSDPEMWELL
QREKDRQCRGLELIASENFCSRAALEALGSCLNNKYSEGYPGKRYYGGAEVVDEIELLCQ
RRALEAFDLDPAQWGVNVQPYSGSPANLAVYTALLQPHDRIMGLDLPDGGHLTHGYMSDV
KRISATSIFFESMPYKLNPKTGLIDYNQLALTARLFRPRLIIAGTSAYARLIDYARMREV
CDEVKAHLLADMAHISGLVAAKVIPSPFKHADIVTTTTHKTLRGARSGLIFYRKGVKAVD
PKTGREIPYTFEDRINFAVFPSLQGGPHNHAIAAVAVALKQACTPMFREYSLQVLKNARA
MADALLERGYSLVSGGTDNHLVLVDLRPKGLDGARAERVLELVSITANKNTCPGDRSAIT
PGGLRLGAPALTSRQFREDDFRRVVDFIDEGVNIGLEVKSKTAKLQDFKSFLLKDSETSQ
RLANLRQRVEQFARAFPMPGFDEH
Enzyme 4 Number of Residues 504
Enzyme 4 Molecular Weight 55992.4
Enzyme 4 Theoretical pI 8.67
Enzyme 4 GO Classification
Function
  • binding
  • catalytic activity
  • cofactor binding
  • glycine hydroxymethyltransferase activity
  • methyltransferase activity
  • pyridoxal phosphate binding
  • transferase activity
  • transferase activity, transferring one-carbon groups
Process
  • L-serine metabolic process
  • cellular amino acid and derivative metabolic process
  • cellular amino acid metabolic process
  • cellular metabolic process
  • glycine metabolic process
  • metabolic process
  • serine family amino acid metabolic process
Component
Enzyme 4 General Function Involved in catalytic activity
Enzyme 4 Specific Function Interconversion of serine and glycine
Enzyme 4 Pathways
Enzyme 4 Reactions
  • 5,10-methylenetetrahydrofolate + glycine + H2O = tetrahydrofolate + L-serine [RN:R00945]
Enzyme 4 Pfam Domain Function
Enzyme 4 Signals
  • None
Enzyme 4 Transmembrane Regions
  • None
Enzyme 4 Essentiality Not Available
Enzyme 4 GenBank ID Protein 15080303 Link Image
Enzyme 4 UniProtKB/Swiss-Prot ID P34897 Link Image
Enzyme 4 UniProtKB/Swiss-Prot Entry Name GLYM_HUMAN Link Image
Enzyme 4 PDB ID Not Available
Enzyme 4 Cellular Location Not Available
Enzyme 4 Gene Sequence >1515 bp
ATGCTGTACTTCTCTTTGTTTTGGGCGGCTCGGCCTCTGCAGAGATGTGGGCAGCTGGTC
AGGATGGCCATTCGGGCTCAGCACAGCAACGCAGCCCAGACTCAGACTGGGGAAGCAAAC
AGGGGCTGGACAGGCCAGGAGAGCCTGTCGGACAGTGATCCTGAGATGTGGGAGTTGCTG
CAGAGGGAGAAGGACAGGCAGTGTCGTGGCCTGGAGCTCATTGCCTCAGAGAACTTCTGC
AGCCGAGCTGCGCTGGAGGCCCTGGGGTCCTGTCTGAACAACAAGTACTCGGAGGGTTAT
CCTGGCAAGAGATACTATGGGGGAGCAGAGGTGGTGGATGAAATTGAGCTGCTGTGCCAG
CGCCGGGCCTTGGAAGCCTTTGACCTGGATCCTGCACAGTGGGGAGTCAATGTCCAGCCC
TACTCCGGGTCCCCAGCCAACCTGGCCGTCTACACAGCCCTTCTGCAACCTCACGACCGG
ATCATGGGGCTGGACCTGCCCGATGGGGGCCATCTCACCCACGGCTACATGTCTGACGTC
AAGCGGATATCAGCCACGTCCATCTTCTTCGAGTCTATGCCCTATAAGCTCAACCCCAAA
ACTGGCCTCATTGACTACAACCAGCTGGCACTGACTGCTCGACTTTTCCGGCCACGGCTC
ATCATAGCTGGCACCAGCGCCTATGCTCGCCTCATTGACTACGCCCGCATGAGAGAGGTG
TGTGATGAAGTCAAAGCACACCTGCTGGCAGACATGGCCCACATCAGTGGCCTGGTGGCT
GCCAAGGTGATTCCCTCGCCTTTCAAGCACGCGGACATCGTCACCACCACTACTCACAAG
ACTCTTCGAGGGGCCAGGTCAGGGCTCATCTTCTACCGGAAAGGGGTGAAGGCTGTGGAC
CCCAAGACTGGCCGGGAGATCCCTTACACATTTGAGGACCGAATCAACTTTGCCGTGTTC
CCATCCCTGCAGGGGGGCCCCCACAATCATGCCATTGCTGCAGTAGCTGTGGCCCTAAAG
CAGGCCTGCACCCCCATGTTCCGGGAGTACTCCCTGCAGGTTCTGAAGAATGCTCGGGCC
ATGGCAGATGCCCTGCTAGAGCGAGGCTACTCACTGGTATCAGGTGGTACTGACAACCAC
CTGGTGCTGGTGGACCTGCGGCCCAAGGGCCTGGATGGAGCTCGGGCTGAGCGGGTGCTA
GAGCTTGTATCCATCACTGCCAACAAGAACACCTGTCCTGGAGACCGAAGTGCCATCACA
CCGGGCGGCCTGCGGCTTGGGGCCCCAGCCTTAACTTCTCGACAGTTCCGTGAGGATGAC
TTCCGGAGAGTTGTGGACTTTATAGATGAAGGGGTCAACATTGGCTTAGAGGTGAAGAGC
AAGACTGCCAAGCTCCAGGATTTCAAATCCTTCCTGCTTAAGGACTCAGAAACAAGTCAG
CGTCTGGCCAACCTCAGGCAACGGGTGGAGCAGTTTGCCAGGGCCTTCCCCATGCCTGGT
TTTGATGAGCATTGA
Enzyme 4 GenBank Gene ID BC011911 Link Image
Enzyme 4 GeneCard ID SHMT2 Link Image
Enzyme 4 GenAtlas ID SHMT2 Link Image
Enzyme 4 HGNC ID HGNC:10852 Link Image
Enzyme 4 Chromosome Location 1
Enzyme 4 Locus 12q12-q14
Enzyme 4 SNPs SNPJam Report Link Image
Enzyme 4 General References
  1. 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 Link Image]
  2. 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 Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. 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 Link Image]
  5. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
Enzyme 4 Metabolite References Not Available
Enzyme 5 [top]
Enzyme 5 ID 6074
Enzyme 5 Name Serine hydroxymethyltransferase, cytosolic
Enzyme 5 Synonyms
  1. SHMT
  2. Glycine hydroxymethyltransferase
  3. Serine methylase
Enzyme 5 Gene Name SHMT1
Enzyme 5 Protein Sequence >Serine hydroxymethyltransferase, cytosolic
MTMPVNGAHKDADLWSSHDKMLAQPLKDSDVEVYNIIKKESNRQRVGLELIASENFASRA
VLEALGSCLNNKYSEGYPGQRYYGGTEFIDELETLCQKRALQAYKLDPQCWGVNVQPYSG
SPANFAVYTALVEPHGRIMGLDLPDGGHLTHGFMTDKKKISATSIFFESMPYKVNPDTGY
INYDQLEENARLFHPKLIIAGTSCYSRNLEYARLRKIADENGAYLMADMAHISGLVAAGV
VPSPFEHCHVVTTTTHKTLRGCRAGMIFYRKGVKSVDPKTGKEILYNLESLINSAVFPGL
QGGPHNHAIAGVAVALKQAMTLEFKVYQHQVVANCRALSEALTELGYKIVTGGSDNHLIL
VDLRSKGTDGGRAEKVLEACSIACNKNTCPGDRSALRPSGLRLGTPALTSRGLLEKDFQK
VAHFIHRGIELTLQIQSDTGVRATLKEFKERLAGDKYQAAVQALREEVESFASLFPLPGL
PDF
Enzyme 5 Number of Residues 483
Enzyme 5 Molecular Weight 53082.2
Enzyme 5 Theoretical pI 7.77
Enzyme 5 GO Classification
Function
  • binding
  • catalytic activity
  • cofactor binding
  • glycine hydroxymethyltransferase activity
  • methyltransferase activity
  • pyridoxal phosphate binding
  • transferase activity
  • transferase activity, transferring one-carbon groups
Process
  • L-serine metabolic process
  • cellular amino acid and derivative metabolic process
  • cellular amino acid metabolic process
  • cellular metabolic process
  • glycine metabolic process
  • metabolic process
  • serine family amino acid metabolic process
Component
Enzyme 5 General Function Involved in catalytic activity
Enzyme 5 Specific Function Interconversion of serine and glycine
Enzyme 5 Pathways
Enzyme 5 Reactions
  • 5,10-methylenetetrahydrofolate + glycine + H2O = tetrahydrofolate + L-serine [RN:R00945]
Enzyme 5 Pfam Domain Function
Enzyme 5 Signals
  • None
Enzyme 5 Transmembrane Regions
  • None
Enzyme 5 Essentiality Not Available
Enzyme 5 GenBank ID Protein 14124914 Link Image
Enzyme 5 UniProtKB/Swiss-Prot ID P34896 Link Image
Enzyme 5 UniProtKB/Swiss-Prot Entry Name GLYC_HUMAN Link Image
Enzyme 5 PDB ID 1BJ4 Link Image
Enzyme 5 PDB File Show
Enzyme 5 3D Structure
Enzyme 5 Cellular Location Not Available
Enzyme 5 Gene Sequence >1452 bp
ATGACGATGCCAGTCAACGGGGCCCACAAGGATGCTGACCTGTGGTCCTCACATGACAAG
ATGCTGGCACAACCCCTCAAAGACAGTGATGTTGAGGTTTACAACATCATTAAGAAGGAG
AGTAACCGGCAGAGGGTTGGATTGGAGCTGATTGCCTCGGAGAATTTCGCCAGCCGAGCA
GTTTTGGAGGCCCTAGGCTCTTGCTTAAATAACAAATACTCTGAGGGGTACCCGGGCCAG
AGATACTATGGCGGGACTGAGTTTATTGATGAACTGGAGACCCTCTGTCAGAAGCGAGCC
CTGCAGGCCTATAAGCTGGACCCACAGTGCTGGGGGGTCAACGTCCAGCCCTACTCAGGC
TCCCCTGCAAACTTTGCTGTGTACACTGCCCTGGTGGAACCCCATGGGCGCATCATGGGC
CTGGACCTTCCGGATGGGGGCCACCTGACCCATGGGTTCATGACAGACAAGAAGAAAATC
TCTGCCACGTCCATCTTCTTTGAATCTATGCCCTACAAGGTGAACCCAGATACTGGCTAC
ATCAACTATGACCAGCTGGAGGAGAACGCACGCCTCTTCCACCCGAAGCTGATCATCGCA
GGAACCAGCTGCTACTCCCGAAACCTGGAATATGCCCGGCTACGGAAGATTGCAGATGAG
AACGGGGCGTATCTCATGGCGGACATGGCTCACATCAGCGGGCTGGTGGCGGCTGGCGTG
GTGCCCTCCCCATTTGAACACTGCCATGTGGTGACCACCACCACTCACAAGACCCTGCGA
GGCTGCCGAGCTGGCATGATCTTCTACAGGAAAGGAGTGAAAAGTGTGGATCCCAAGACT
GGCAAAGAGATTCTGTACAACCTGGAGTCTCTTATCAATTCTGCTGTGTTCCCTGGCCTG
CAGGGAGGTCCCCACAACCACGCCATTGCTGGGGTTGCTGTGGCACTGAAGCAAGCTATG
ACTCTGGAATTTAAAGTTTATCAACACCAGGTGGTGGCCAACTGCAGGGCTCTGTCTGAG
GCCCTGACGGAGCTGGGCTACAAAATAGTCACAGGTGGTTCTGACAACCATTTGATCCTT
GTGGATCTCCGTTCCAAAGGCACAGATGGTGGAAGGGCTGAGAAGGTGCTAGAAGCCTGT
TCTATTGCCTGCAACAAGAACACCTGTCCAGGTGACAGAAGCGCTCTGCGGCCCAGTGGA
CTGCGGCTGGGGACCCCAGCACTGACGTCCCGTGGACTTTTGGAAAAAGACTTCCAAAAA
GTAGCCCACTTTATTCACAGAGGGATAGAGCTGACCCTGCAGATCCAGAGCGACACTGGT
GTCAGAGCCACCCTGAAAGAGTTCAAGGAGAGACTGGCAGGGGATAAGTACCAGGCGGCC
GTGCAGGCTCTCCGGGAGGAGGTTGAGAGCTTCGCCTCTTTCTTCCCTCTGCCTGGCCTG
CCTGACTTCTAA
Enzyme 5 GenBank Gene ID BC007979 Link Image
Enzyme 5 GeneCard ID SHMT1 Link Image
Enzyme 5 GenAtlas ID SHMT1 Link Image
Enzyme 5 HGNC ID HGNC:10850 Link Image
Enzyme 5 Chromosome Location 1
Enzyme 5 Locus 17p11.2
Enzyme 5 SNPs SNPJam Report Link Image
Enzyme 5 General References
  1. 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 Link Image]
  2. 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 Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed Link Image]
  5. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
  6. 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 Link Image]
Enzyme 5 Metabolite References Not Available
Enzyme 6 [top]
Enzyme 6 ID 6211
Enzyme 6 Name C-1-tetrahydrofolate synthase, cytoplasmic
Enzyme 6 Synonyms
  1. C1-THF synthase
  2. Methylenetetrahydrofolate dehydrogenase
  3. Methenyltetrahydrofolate cyclohydrolase
  4. Formyltetrahydrofolate synthetase
Enzyme 6 Gene Name MTHFD1
Enzyme 6 Protein Sequence >C-1-tetrahydrofolate synthase, cytoplasmic
MAPAEILNGKEISAQIRARLKNQVTQLKEQVPGFTPRLAILQVGNRDDSNLYINVKLKAA
EEIGIKATHIKLPRTTTESEVMKYITSLNEDSTVHGFLVQLPLDSENSINTEEVINAIAP
EKDVDGLTSINAGRLARGDLNDCFIPCTPKGCLELIKETGVPIAGRHAVVVGRSKIVGAP
MHDLLLWNNATVTTCHSKTAHLDEEVNKGDILVVATGQPEMVKGEWIKPGAIVIDCGINY
VPDDKKPNGRKVVGDVAYDEAKERASFITPVPGGVGPMTVAMLMQSTVESAKRFLEKFKP
GKWMIQYNNLNLKTPVPSDIDISRSCKPKPIGKLAREIGLLSEEVELYGETKAKVLLSAL
ERLKHRPDGKYVVVTGITPTPLGEGKSTTTIGLVQALGAHLYQNVFACVRQPSQGPTFGI
KGGAAGGGYSQVIPMEEFNLHLTGDIHAITAANNLVAAAIDARIFHELTQTDKALFNRLV
PSVNGVRRFSDIQIRRLKRLGIEKTDPTTLTDEEINRFARLDIDPETITWQRVLDTNDRF
LRKITIGQAPTEKGHTRTAQFDISVASEIMAVLALTTSLEDMRERLGKMVVASSKKGEPV
SAEDLGVSGALTVLMKDAIKPNLMQTLEGTPVFVHAGPFANIAHGNSSIIADRIALKLVG
PEGFVVTEAGFGADIGMEKFFNIKCRYSGLCPHVVVLVATVRALKMHGGGPTVTAGLPLP
KAYIQENLELVEKGFSNLKKQIENARMFGIPVVVAVNAFKTDTESELDLISRLSREHGAF
DAVKCTHWAEGGKGALALAQAVQRAAQAPSSFQLLYDLKLPVEDKIRIIAQKIYGADDIE
LLPEAQHKAEVYTKQGFGNLPICMAKTHLSLSHNPEQKGVPTGFILPIRDIRASVGAGFL
YPLVGTMSTMPGLPTRPCFYDIDLDPETEQVNGLF
Enzyme 6 Number of Residues 935
Enzyme 6 Molecular Weight 101558.4
Enzyme 6 Theoretical pI 7.32
Enzyme 6 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • adenyl ribonucleotide binding
  • binding
  • catalytic activity
  • formate-tetrahydrofolate ligase activity
  • ligase activity
  • ligase activity, forming carbon-nitrogen bonds
  • nucleoside binding
  • purine nucleoside binding
Process
  • cellular aromatic compound metabolic process
  • cellular metabolic process
  • folic acid and derivative biosynthetic process
  • folic acid and derivative metabolic process
  • metabolic process
Component
Enzyme 6 General Function Involved in formate-tetrahydrofolate ligase activity
Enzyme 6 Specific Function 5,10-methylenetetrahydrofolate + NADP(+) = 5,10-methenyltetrahydrofolate + NADPH
Enzyme 6 Pathways
  • Glyoxylate and Dicarboxylate Metabolism (map00630 Link Image)
  • One Carbon Pool By Folate (map00670 Link Image)
Enzyme 6 Reactions
  • ATP + formate + tetrahydrofolate = ADP + phosphate + 10-formyltetrahydrofolate [RN:R00943]
Enzyme 6 Pfam Domain Function
Enzyme 6 Signals
  • None
Enzyme 6 Transmembrane Regions
  • None
Enzyme 6 Essentiality Not Available
Enzyme 6 GenBank ID Protein 189065440 Link Image
Enzyme 6 UniProtKB/Swiss-Prot ID P11586 Link Image
Enzyme 6 UniProtKB/Swiss-Prot Entry Name C1TC_HUMAN Link Image
Enzyme 6 PDB ID 1DIA Link Image
Enzyme 6 PDB File Show
Enzyme 6 3D Structure
Enzyme 6 Cellular Location Not Available
Enzyme 6 Gene Sequence >2808 bp
ATGGCGCCAGCAGAAATCCTGAACGGGAAGGAGATCTCCGCGCAAATAAGGGCGAGACTG
AAAAATCAAGTCACTCAGTTGAAGGAGCAAGTACCTGGTTTCACACCACGCCTGGCAATA
TTACAGGTTGGCAACAGAGATGATTCCAATCTTTATATAAATGTGAAGCTGAAGGCTGCT
GAAGAGATTGGGATCAAAGCCACTCACATTAAGTTACCAAGAACAACCACAGAATCTGAG
GTGATGAAGTACATTACATCTTTGAATGAAGACTCTACTGTACATGGGTTCTTAGTGCAG
CTACCTTTAGATTCAGAGAATTCCATTAACACTGAAGAAGTGATCAATGCTATTGCACCC
GAGAAGGATGTGGATGGATTGACTAGCATCAATGCTGGGAGACTTGCTAGAGGTGACCTC
AATGACTGTTTCATTCCTTGTACGCCTAAGGGATGCTTGGAACTCATCAAAGAGACAGGG
GTGCCGATTGCCGGAAGGCATGCTGTGGTGGTTGGGCGCAGTAAAATAGTTGGGGCCCCG
ATGCATGACTTGCTTCTGTGGAACAATGCCACAGTGACCACCTGCCACTCCAAGACTGCC
CATCTGGATGAGGAGGTAAATAAAGGTGACATCCTGGTGGTTGCAACTGGTCAGCCTGAA
ATGGTTAAAGGGGAGTGGATCAAACCTGGGGCAATAGTCATCGACTGTGGAATCAATTAT
GTCCCAGATGATAAAAAACCAAATGGGAGAAAAGTTGTGGGTGATGTGGCATACGACGAG
GCCAAAGAGAGGGCGAGCTTCATCACTCCTGTTCCTGGCGGCGTAGGGCCCATGACAGTT
GCAATGCTCATGCAGAGCACAGTAGAGAGTGCCAAGCGTTTCCTGGAGAAATTTAAGCCA
GGAAAGTGGATGATTCAGTATAACAACCTTAACCTCAAGACACCTGTTCCAAGTGACATT
GATATATCACGATCTTGTAAACCGAAGCCCATTGGTAAGCTGGCTCGAGAAATTGGTCTG
CTGTCTGAAGAGGTAGAATTATATGGTGAAACAAAGGCCAAAGTTCTGCTGTCAGCACTA
GAACGCCTGAAGCACCGGCCTGATGGGAAATACGTGGTGGTGACTGGAATAACTCCAACA
CCCCTGGGAGAAGGGAAAAGCACAACTACAATCGGGCTAGTGCAAGCCCTTGGTGCCCAT
CTCTACCAGAATGTCTTTGCGTGTGTGCGACAGCCTTCTCAGGGCCCCACCTTTGGAATA
AAAGGTGGCGCTGCAGGAGGCGGCTACTCCCAGGTCATTCCTATGGAAGAGTTTAATCTC
CACCTCACAGGTGACATCCATGCCATCACTGCAGCTAATAACCTCGTTGCTGCGGCCATT
GATGCTCGGATATTTCATGAACTGACCCAGACAGACAAGGCTCTCTTTAATCGTTTGGTG
CCATCAGTAAATGGAGTGAGAAGGTTCTCTGACATCCAAATCCGAAGGTTAAAGAGACTA
GGCATTGAAAAGACTGACCCTACCACACTGACAGATGAAGAGATAAACAGATTTGCAAGA
TTGGACATTGATCCAGAAACCATAACTTGGCAAAGAGTGTTGGATACCAATGATAGATTC
CTGAGGAAGATCACGATTGGACAGGCTCCAACGGAGAAGGGTCACACACGGACGGCCCAG
TTTGATATCTCTGTGGCCAGTGAAATTATGGCTGTCCTGGCTCTCACCACTTCTCTAGAA
GACATGAGAGAGAGACTGGGCAAAATGGTGGTGGCATCCAGTAAGAAAGGAGAGCCCGTC
AGTGCCGAAGATCTGGGGGTGAGTGGTGCACTGACAGTGCTTATGAAGGACGCAATCAAG
CCCAATCTCATGCAGACACTGGAGGGCACTCCAGTGTTTGTCCATGCTGGCCCGTTTGCC
AACATCGCACATGGCAATTCCTCCATCATTGCAGACCAGATCGCACTCAAGCTTGTTGGC
CCAGAAGGGTTTGTAGTGACGGAAGCAGGATTTGGAGCAGACATTGGAATGGAAAAGTTT
TTTAACATCAAATGCCGGTATTCCGGCCTCTGCCCCCACGTGGTGGTGCTTGTTGCCACT
GTCAGGGCTCTCAAGATGCACGGGGGCGGCCCCACGGTCACTGCTGGACTGCCTCTTCCC
AAGGCTTACATACAGGAGAACCTGGAGCTGGTTGAAAAAGGCTTCAGTAACTTGAAGAAA
CAAATTGAAAATGCCAGAATGTTTGGAATTCCAGTAGTAGTGGCCGTGAATGCATTCAAG
ACGGATACAGAGTCTGAGCTGGACCTCATCAGCCGCCTTTCCAGAGAACATGGGGCTTTT
GATGCCGTGAAGTGCACTCACTGGGCAGAAGGGGGCAAGGGTGCCTTAGCCCTGGCTCAG
GCCGTCCAGAGAGCAGCACAAGCACCCAGCAGCTTCCAGCTCCTTTATGACCTCAAGCTC
CCAGTTGAGGATAAAATCAGGATCATTGCACAGAAGATCTATGGAGCAGATGACATTGAA
TTACTTCCCGAAGCTCAACACAAAGCTGAAGTCTACACGAAGCAGGGCTTTGGGAATCTC
CCCATCTGCATGGCTAAAACACACTTGTCTTTGTCTCACAACCCAGAGCAAAAAGGTGTC
CCTACAGGCTTCATTCTGCCCATTCGCGACATCCGCGCCAGCGTTGGGGCTGGTTTTCTG
TACCCCTTAGTAGGAACGATGAGCACAATGCCTGGACTCCCCACCCGGCCCTGTTTTTAT
GATATTGATTTGGACCCTGAAACAGAACAGGTGAATGGATTATTCTAA
Enzyme 6 GenBank Gene ID AK312361 Link Image
Enzyme 6 GeneCard ID MTHFD1 Link Image
Enzyme 6 GenAtlas ID MTHFD1 Link Image
Enzyme 6 HGNC ID HGNC:7432 Link Image
Enzyme 6 Chromosome Location 1
Enzyme 6 Locus 14q24
Enzyme 6 SNPs SNPJam Report Link Image
Enzyme 6 General References
  1. 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 Link Image]
  2. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. 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 Link Image]
  5. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
  6. 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 Link Image]
  7. Schmidt A, Wu H, MacKenzie RE, Chen VJ, Bewly JR, Ray JE, Toth JE, Cygler M: Structures of three inhibitor complexes provide insight into the reaction mechanism of the human methylenetetrahydrofolate dehydrogenase/cyclohydrolase. Biochemistry. 2000 May 30;39(21):6325-35. [PubMed Link Image]
  8. 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 Link Image]
  9. Brody LC, Conley M, Cox C, Kirke PN, McKeever MP, Mills JL, Molloy AM, O'Leary VB, Parle-McDermott A, Scott JM, Swanson DA: A polymorphism, R653Q, in the trifunctional enzyme methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase/formyltetrahydrofolate synthetase is a maternal genetic risk factor for neural tube defects: report of the Birth Defects Research Group. Am J Hum Genet. 2002 Nov;71(5):1207-15. Epub 2002 Oct 16. [PubMed Link Image]
  10. Parle-McDermott A, Kirke PN, Mills JL, Molloy AM, Cox C, O'Leary VB, Pangilinan F, Conley M, Cleary L, Brody LC, Scott JM: Confirmation of the R653Q polymorphism of the trifunctional C1-synthase enzyme as a maternal risk for neural tube defects in the Irish population. Eur J Hum Genet. 2006 Jun;14(6):768-72. [PubMed Link Image]
  11. Webb EL, Rudd MF, Sellick GS, El Galta R, Bethke L, Wood W, Fletcher O, Penegar S, Withey L, Qureshi M, Johnson N, Tomlinson I, Gray R, Peto J, Houlston RS: Search for low penetrance alleles for colorectal cancer through a scan of 1467 non-synonymous SNPs in 2575 cases and 2707 controls with validation by kin-cohort analysis of 14 704 first-degree relatives. Hum Mol Genet. 2006 Nov 1;15(21):3263-71. Epub 2006 Sep 25. [PubMed Link Image]
  12. Christensen KE, Rohlicek CV, Andelfinger GU, Michaud J, Bigras JL, Richter A, Mackenzie RE, Rozen R: The MTHFD1 p.Arg653Gln variant alters enzyme function and increases risk for congenital heart defects. Hum Mutat. 2009 Feb;30(2):212-20. [PubMed Link Image]
Enzyme 6 Metabolite References Not Available
Enzyme 7 [top]
Enzyme 7 ID 13031
Enzyme 7 Name cDNA FLJ76259, highly similar to Homo sapiens aminomethyltransferase
Enzyme 7 Synonyms
  1. glycine cleavage system protein T
  2. AMT, mRNA
  3. HCG2001997, isoform CRA_a
Enzyme 7 Gene Name Not Available
Enzyme 7 Protein Sequence >cDNA FLJ76259, highly similar to Homo sapiens aminomethyltransferase
MQRAVSVVARLGFRLQAFPPALCRPLSCAQEVLRRTPLYDFHLAHGGKMVAFAGWSLPVQ
YRDSHTDSHLHTRQHCSLFDVSHMLQTKILGSDRVKLMESLVVGDIAELRPNQGTLSLFT
NEAGGILDDLIVTNTSEGHLYVVSNAGCWEKDLALMQDKVRELQNQGRDVGLEVLDNALL
ALQGPTAAQVLQAGVADDLRKLPFMTSAVMEVFGVSGCRVTRCGYTGEDGVEISVPVAGA
VHLATAILKNPEVKLAGLAARDSLRLEAGLCLYGNDIDEHTTPVEGSLSWTLGKRRRAAM
DFPGAKVIVPQLKGRVQRRRVGLMCEGAPMRAHSPILNMEGTKIGTVTSGCPSPSLKKNV
AMGYVPCEYSRPGTMLLVEVRRKQQMAVVSKMPFVPTNYYTLK
Enzyme 7 Number of Residues 403
Enzyme 7 Molecular Weight 43947
Enzyme 7 Theoretical pI 8.69
Enzyme 7 GO Classification Not Available
Enzyme 7 General Function Amino acid transport and metabolism
Enzyme 7 Specific Function Not Available
Enzyme 7 Pathways Not Available
Enzyme 7 Reactions Not Available
Enzyme 7 Pfam Domain Function Not Available
Enzyme 7 Signals
  • None
Enzyme 7 Transmembrane Regions
  • None
Enzyme 7 Essentiality Not Available
Enzyme 7 GenBank ID Protein 158254632 Link Image
Enzyme 7 UniProtKB/Swiss-Prot ID A8K3I5 Link Image
Enzyme 7 UniProtKB/Swiss-Prot Entry Name A8K3I5_HUMAN Link Image
Enzyme 7 PDB ID Not Available
Enzyme 7 Cellular Location Not Available
Enzyme 7 Gene Sequence Not Available
Enzyme 7 GenBank Gene ID AK290600 Link Image
Enzyme 7 GeneCard ID A8K3I5 Link Image
Enzyme 7 GenAtlas ID Not Available
Enzyme 7 HGNC ID Not Available
Enzyme 7 Chromosome Location Not Available
Enzyme 7 Locus Not Available
Enzyme 7 SNPs Not Available
Enzyme 7 General References Not Available
Enzyme 7 Metabolite References Not Available
Enzyme 8 [top]
Enzyme 8 ID 13034
Enzyme 8 Name Monofunctional C1-tetrahydrofolate synthase, mitochondrial
Enzyme 8 Synonyms
  1. Formyltetrahydrofolate synthetase
Enzyme 8 Gene Name MTHFD1L
Enzyme 8 Protein Sequence >Monofunctional C1-tetrahydrofolate synthase, mitochondrial
MGTRLPLVLRQLRRPPQPPGPPRRLRVPCRASSGGGGGGGGGREGLLGQRRPQDGQARSS
CSPGGRTPAARDSIVREVIQNSKEVLSLLQEKNPAFKPVLAIIQAGDDNLMQEINQNLAE
EAGLNITHICLPPDSSEAEIIDEILKINEDTRVHGLALQISENLFSNKVLNALKPEKDVD
GVTDINLGKLVRGDAHECFVSPVAKAVIELLEKSGVNLDGKKILVVGAHGSLEAALQCLF
QRKGSMTMSIQWKTRQLQSKLHEADIVVLGSPKPEEIPLTWIQPGTTVLNCSHDFLSGKV
GCGSPRIHFGGLIEEDDVILLAAALRIQNMVSSGRRWLREQQHRRWRLHCLKLQPLSPVP
SDIEISRGQTPKAVDVLAKEIGLLADEIEIYGKSKAKVRLSVLERLKDQADGKYVLVAGI
TPTPLGEGKSTVTIGLVQALTAHLNVNSFACLRQPSQGPTFGVKGGAAGGGYAQVIPMEE
FNLHLTGDIHAITAANNLLAAAIDTRILHENTQTDKALYNRLVPLVNGVREFSEIQLARL
KKLGINKTDPSTLTEEEVSKFARLDIDPSTITWQRVLDTNDRFLRKITIGQGNTEKGHYR
QAQFDIAVASEIMAVLALTDSLADMKARLGRMVVASDKSGQPVTADDLGVTGALTVLMKD
AIKPNLMQTLEGTPVFVHAGPFANIAHGNSSVLADKIALKLVGEEGFVVTEAGFGADIGM
EKFFNIKCRASGLVPNVVVLVATVRALKMHGGGPSVTAGVPLKKEYTEENIQLVADGCCN
LQKQIQITQLFGVPVVVALNVFKTDTRAEIDLVCELAKRAGAFDAVPCYHWSVGGKGSVD
LARAVREAASKRSRFQFLYDVQVPIVDKIRTIAQAVYGAKDIELSPEAQAKIDRYTQQGF
GNLPICMAKTHLSLSHQPDKKGVPRDFILPISDVRASIGAGFIYPLVGTMSTMPGLPTRP
CFYDIDLDTETEQVKGLF
Enzyme 8 Number of Residues 978
Enzyme 8 Molecular Weight 105789.1
Enzyme 8 Theoretical pI 8.15
Enzyme 8 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • adenyl ribonucleotide binding
  • binding
  • catalytic activity
  • formate-tetrahydrofolate ligase activity
  • ligase activity
  • ligase activity, forming carbon-nitrogen bonds
  • nucleoside binding
  • purine nucleoside binding
Process
  • cellular aromatic compound metabolic process
  • cellular metabolic process
  • folic acid and derivative biosynthetic process
  • folic acid and derivative metabolic process
  • metabolic process
Component
Enzyme 8 General Function Involved in formate-tetrahydrofolate ligase activity
Enzyme 8 Specific Function May provide the missing metabolic reaction required to link the mitochondria and the cytoplasm in the mammalian model of one-carbon folate metabolism in embryonic an transformed cells complementing thus the enzymatic activities of MTHFD2
Enzyme 8 Pathways
  • Glyoxylate and Dicarboxylate Metabolism (map00630 Link Image)
  • One Carbon Pool By Folate (map00670 Link Image)
Enzyme 8 Reactions
  • ATP + formate + tetrahydrofolate = ADP + phosphate + 10-formyltetrahydrofolate [RN:R00943]
Enzyme 8 Pfam Domain Function
Enzyme 8 Signals
  • None
Enzyme 8 Transmembrane Regions
  • None
Enzyme 8 Essentiality Not Available
Enzyme 8 GenBank ID Protein Not Available
Enzyme 8 UniProtKB/Swiss-Prot ID Q6UB35 Link Image
Enzyme 8 UniProtKB/Swiss-Prot Entry Name C1TM_HUMAN Link Image
Enzyme 8 PDB ID Not Available
Enzyme 8 Cellular Location Not Available
Enzyme 8 Gene Sequence >2937 bp
ATGGGCACGCGTCTGCCGCTCGTCCTGCGCCAGCTCCGCCGCCCGCCCCAGCCCCCGGGC
CCTCCGCGCCGCCTCCGTGTGCCCTGTCGCGCTAGCAGCGGCGGCGGCGGAGGCGGCGGC
GGTGGCCGGGAGGGCCTGCTTGGACAGCGGCGGCCGCAGGATGGCCAGGCCCGGAGCAGC
TGCAGCCCCGGCGGCCGAACGCCCGCGGCGCGGGACTCCATCGTCAGAGAAGTCATTCAG
AATTCAAAAGAAGTTCTAAGTTTATTGCAAGAAAAAAACCCTGCCTTCAAGCCGGTTCTT
GCAATTATCCAGGCAGGTGACGACAACTTGATGCAGGAAATCAACCAGAATTTGGCTGAG
GAGGCTGGTCTGAACATCACTCACATTTGCCTCCCTCCAGATAGCAGTGAAGCCGAGATT
ATAGATGAAATCTTAAAGATCAATGAAGATACCAGAGTACATGGCCTTGCCCTTCAGATC
TCTGAGAACTTGTTTAGCAACAAAGTCCTCAATGCCTTGAAACCAGAAAAAGATGTGGAT
GGAGTAACAGACATAAACCTGGGGAAGCTGGTGCGAGGGGATGCCCATGAATGTTTTGTT
TCACCTGTTGCCAAAGCTGTAATTGAACTTCTTGAAAAATCAGGTGTCAACCTAGATGGA
AAGAAGATTTTGGTAGTGGGGGCCCATGGGTCTTTGGAAGCTGCTCTACAATGCCTGTTC
CAGAGAAAAGGGTCCATGACAATGAGCATCCAGTGGAAAACACGCCAGCTTCAAAGCAAG
CTTCACGAGGCTGACATTGTGGTCCTAGGCTCACCTAAGCCAGAAGAGATTCCCCTTACT
TGGATACAACCAGGAACTACTGTTCTCAACTGCTCCCATGACTTCCTGTCAGGGAAGGTT
GGGTGTGGCTCTCCAAGAATACATTTTGGTGGACTCATTGAGGAAGATGATGTGATTCTC
CTTGCTGCAGCTCTGCGAATTCAGAACATGGTCAGTAGTGGAAGGAGATGGCTTCGTGAA
CAGCAGCACAGGCGGTGGAGACTTCACTGCTTGAAACTTCAGCCTCTCTCCCCTGTGCCA
AGTGACATTGAGATTTCAAGAGGACAAACTCCAAAAGCTGTGGATGTCCTTGCCAAGGAG
ATTGGATTGCTTGCAGATGAAATTGAAATCTATGGCAAAAGCAAAGCCAAAGTACGTTTG
TCCGTGCTAGAAAGGTTAAAGGATCAAGCAGATGGAAAATACGTCTTAGTTGCTGGGATC
ACACCCACCCCTCTTGGAGAAGGGAAGAGCACAGTCACCATCGGGCTTGTGCAGGCTCTG
ACCGCACACCTGAATGTCAACTCCTTTGCCTGCTTGAGGCAGCCTTCCCAAGGACCGACG
TTTGGAGTGAAAGGAGGAGCCGCGGGTGGTGGATATGCCCAGGTCATCCCCATGGAGGAG
TTCAACCTTCACTTGACTGGAGACATCCACGCCATCACCGCTGCCAATAACTTGCTGGCT
GCCGCCATCGACACGAGGATTCTTCATGAAAACACGCAAACAGATAAGGCTCTGTATAAT
CGGCTGGTTCCTTTAGTGAATGGTGTCAGAGAATTTTCAGAAATTCAGCTTGCTCGGCTA
AAAAAACTGGGAATAAATAAGACTGATCCGAGCACACTGACAGAAGAGGAAGTGAGTAAA
TTTGCCCGTCTCGACATCGACCCATCTACCATCACGTGGCAGAGAGTATTGGATACAAAT
GACCGATTTCTACGAAAAATAACCATCGGGCAGGGAAACACAGAGAAGGGCCATTACCGG
CAGGCGCAGTTTGACATCGCAGTGGCCAGCGAGATCATGGCGGTGCTGGCCCTGACGGAC
AGCCTCGCAGACATGAAGGCACGGCTGGGAAGGATGGTGGTGGCCAGTGACAAAAGCGGG
CAGCCTGTGACAGCAGATGATTTGGGGGTGACAGGTGCTTTGACAGTTTTGATGAAAGAT
GCAATAAAACCAAACCTGATGCAGACCCTGGAAGGGACACCTGTGTTCGTGCATGCGGGC
CCTTTTGCTAACATTGCTCACGGCAACTCTTCAGTGTTGGCTGATAAAATTGCCCTGAAA
CTGGTTGGTGAAGAAGGATTTGTAGTGACCGAAGCTGGCTTTGGTGCTGACATCGGAATG
GAGAAATTCTTCAACATCAAGTGCCGAGCTTCCGGCTTGGTGCCCAACGTGGTTGTGTTA
GTGGCAACGGTGCGAGCTCTGAAGATGCATGGAGGCGGGCCAAGTGTAACGGCTGGTGTT
CCTCTTAAGAAAGAATATACAGAGGAGAACATCCAGCTGGTGGCAGACGGCTGCTGTAAC
CTCCAGAAGCAAATTCAGATCACTCAGCTCTTTGGGGTTCCCGTTGTGGTGGCTCTGAAT
GTCTTCAAGACCGACACCCGCGCTGAGATTGACTTGGTGTGTGAGCTTGCAAAGCGGGCT
GGTGCCTTTGATGCAGTCCCCTGCTATCACTGGTCCGTTGGTGGAAAAGGATCGGTGGAC
TTGGCTCGGGCTGTGAGAGAGGCTGCGAGTAAAAGAAGCCGATTCCAGTTCCTGTATGAT
GTTCAGGTTCCAATTGTGGACAAGATAAGGACCATTGCTCAGGCTGTCTATGGAGCCAAA
GATATTGAACTCTCTCCTGAGGCACAAGCCAAAATAGATCGTTACACTCAACAGGGTTTT
GGAAATTTGCCCATCTGCATGGCAAAGACCCACCTTTCTCTATCTCACCAACCTGACAAA
AAAGGTGTGCCAAGGGACTTCATCTTACCTATCAGTGACGTCCGGGCCAGCATAGGCGCT
GGGTTCATTTACCCTTTGGTCGGAACGATGAGCACCATGCCAGGACTGCCCACCCGGCCC
TGCTTTTATGACATAGATCTTGATACCGAAACAGAACAAGTTAAAGGCTTGTTCTAA
Enzyme 8 GenBank Gene ID AY374130 Link Image
Enzyme 8 GeneCard ID MTHFD1L Link Image
Enzyme 8 GenAtlas ID MTHFD1L Link Image
Enzyme 8 HGNC ID HGNC:21055 Link Image
Enzyme 8 Chromosome Location 6
Enzyme 8 Locus 6q25.1
Enzyme 8 SNPs SNPJam Report Link Image
Enzyme 8 General References
  1. 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 Link Image]
  2. Sugiura T, Nagano Y, Inoue T, Hirotani K: A novel mitochondrial C1-tetrahydrofolate synthetase is upregulated in human colon adenocarcinoma. Biochem Biophys Res Commun. 2004 Feb 27;315(1):204-11. [PubMed Link Image]
  3. Mungall AJ, Palmer SA, Sims SK, Edwards CA, Ashurst JL, Wilming L, Jones MC, Horton R, Hunt SE, Scott CE, Gilbert JG, Clamp ME, Bethel G, Milne S, Ainscough R, Almeida JP, Ambrose KD, Andrews TD, Ashwell RI, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beare DM, Beasley H, Beasley O, Bird CP, Blakey S, Bray-Allen S, Brook J, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Clark SY, Clark G, Clee CM, Clegg S, Cobley V, Collier RE, Collins JE, Colman LK, Corby NR, Coville GJ, Culley KM, Dhami P, Davies J, Dunn M, Earthrowl ME, Ellington AE, Evans KA, Faulkner L, Francis MD, Frankish A, Frankland J, French L, Garner P, Garnett J, Ghori MJ, Gilby LM, Gillson CJ, Glithero RJ, Grafham DV, Grant M, Gribble S, Griffiths C, Griffiths M, Hall R, Halls KS, Hammond S, Harley JL, Hart EA, Heath PD, Heathcott R, Holmes SJ, Howden PJ, Howe KL, Howell GR, Huckle E, Humphray SJ, Humphries MD, Hunt AR, Johnson CM, Joy AA, Kay M, Keenan SJ, Kimberley AM, King A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd CR, Lloyd DM, Loveland JE, Lovell J, Martin S, Mashreghi-Mohammadi M, Maslen GL, Matthews L, McCann OT, McLaren SJ, McLay K, McMurray A, Moore MJ, Mullikin JC, Niblett D, Nickerson T, Novik KL, Oliver K, Overton-Larty EK, Parker A, Patel R, Pearce AV, Peck AI, Phillimore B, Phillips S, Plumb RW, Porter KM, Ramsey Y, Ranby SA, Rice CM, Ross MT, Searle SM, Sehra HK, Sheridan E, Skuce CD, Smith S, Smith M, Spraggon L, Squares SL, Steward CA, Sycamore N, Tamlyn-Hall G, Tester J, Theaker AJ, Thomas DW, Thorpe A, Tracey A, Tromans A, Tubby B, Wall M, Wallis JM, West AP, White SS, Whitehead SL, Whittaker H, Wild A, Willey DJ, Wilmer TE, Wood JM, Wray PW, Wyatt JC, Young L, Younger RM, Bentley DR, Coulson A, Durbin R, Hubbard T, Sulston JE, Dunham I, Rogers J, Beck S: The DNA sequence and analysis of human chromosome 6. Nature. 2003 Oct 23;425(6960):805-11. [PubMed Link Image]
  4. Walkup AS, Appling DR: Enzymatic characterization of human mitochondrial C1-tetrahydrofolate synthase. Arch Biochem Biophys. 2005 Oct 15;442(2):196-205. Epub 2005 Aug 30. [PubMed Link Image]
  5. Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed Link Image]
  6. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  7. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  8. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
  9. Sjoblom T, Jones S, Wood LD, Parsons DW, Lin J, Barber TD, Mandelker D, Leary RJ, Ptak J, Silliman N, Szabo S, Buckhaults P, Farrell C, Meeh P, Markowitz SD, Willis J, Dawson D, Willson JK, Gazdar AF, Hartigan J, Wu L, Liu C, Parmigiani G, Park BH, Bachman KE, Papadopoulos N, Vogelstein B, Kinzler KW, Velculescu VE: The consensus coding sequences of human breast and colorectal cancers. Science. 2006 Oct 13;314(5797):268-74. Epub 2006 Sep 7. [PubMed Link Image]
Enzyme 8 Metabolite References Not Available
Enzyme 9 [top]
Enzyme 9 ID 13035
Enzyme 9 Name Methylenetetrahydrofolate dehydrogenase (NADP+ dependent) 2, methenyltetrahydrofolate cyclohydrolase
Enzyme 9 Synonyms
  1. SubName: Methylenetetrahydrofolate dehydrogenase (NADP+ dependent) 2, methenyltetrahydrofolate cyclohydrolase, isoform CRA_b
  2. SubName: cDNA FLJ52745, highly similar to Bifunctional methylenetetrahydrofolatedehydrogenase/cyclohydrolase, mitochondrial
Enzyme 9 Gene Name MTHFD2
Enzyme 9 Protein Sequence >Methylenetetrahydrofolate dehydrogenase (NADP+ dependent) 2, methenyltetrahydrofolate cyclohydrolase
MKPASISEEELLNLINKLNNDDNVDGLLVQLPLPEHIDERRICNAVSPDKDVDGFHVINV
GRMCLDQYSMLPATPWGVWEIIKRTGIPTLGKNVVVAGRSKNVGMPIAMLLHTDGAHERP
GGDATVTISHRYTPKEQLKKHTILADIVISAAGIPNLITADMIKEGAAVIDVGINRVHDP
VTAKPKLVGDVDFEGVRQKAGYITPVPGGVGPMTVAMLMKNTIIAAKKVLRLEEREVLKS
KELGVATN
Enzyme 9 Number of Residues 248
Enzyme 9 Molecular Weight 26849.1
Enzyme 9 Theoretical pI 7.22
Enzyme 9 GO Classification
Function
  • binding
  • catalytic activity
Process
  • cellular aromatic compound metabolic process
  • cellular metabolic process
  • folic acid and derivative biosynthetic process
  • folic acid and derivative metabolic process
  • metabolic process
Component
Enzyme 9 General Function Involved in catalytic activity
Enzyme 9 Specific Function Not Available
Enzyme 9 Pathways Not Available
Enzyme 9 Reactions Not Available
Enzyme 9 Pfam Domain Function
Enzyme 9 Signals
  • None
Enzyme 9 Transmembrane Regions
  • None
Enzyme 9 Essentiality Not Available
Enzyme 9 GenBank ID Protein 194390168 Link Image
Enzyme 9 UniProtKB/Swiss-Prot ID Q7Z650 Link Image
Enzyme 9 UniProtKB/Swiss-Prot Entry Name Q7Z650_HUMAN Link Image
Enzyme 9 PDB ID Not Available
Enzyme 9 Cellular Location Not Available
Enzyme 9 Gene Sequence >747 bp
ATGAAACCAGCTTCAATTTCAGAGGAAGAATTGTTGAATTTAATCAATAAACTGAATAAT
GATGATAATGTAGATGGCCTCCTTGTTCAGTTGCCTCTTCCAGAGCATATTGATGAGAGA
AGGATCTGCAATGCTGTTTCTCCAGACAAGGATGTTGATGGCTTTCATGTAATTAATGTA
GGACGAATGTGTTTGGATCAGTATTCCATGTTACCGGCTACTCCATGGGGTGTGTGGGAA
ATAATCAAGCGAACTGGCATTCCAACCCTAGGGAAGAATGTGGTTGTGGCTGGAAGGTCA
AAAAACGTTGGAATGCCCATTGCAATGTTACTGCACACAGATGGGGCGCATGAACGTCCC
GGAGGTGATGCCACTGTTACAATATCTCATCGATATACTCCCAAAGAGCAGTTGAAGAAA
CATACAATTCTTGCAGATATTGTAATATCTGCTGCAGGTATTCCAAATCTGATCACAGCA
GATATGATCAAGGAAGGAGCAGCAGTCATTGATGTGGGAATAAATAGAGTTCACGATCCT
GTAACTGCCAAACCCAAGTTGGTTGGAGATGTGGATTTTGAAGGAGTCAGACAAAAAGCT
GGGTATATCACTCCAGTTCCTGGAGGTGTTGGCCCCATGACAGTGGCAATGCTAATGAAG
AATACCATTATTGCTGCAAAAAAGGTGCTGAGGCTTGAAGAGCGAGAAGTGCTGAAGTCT
AAAGAGCTTGGGGTAGCCACTAATTAA
Enzyme 9 GenBank Gene ID AK300035 Link Image
Enzyme 9 GeneCard ID MTHFD2 Link Image
Enzyme 9 GenAtlas ID MTHFD2 Link Image
Enzyme 9 HGNC ID HGNC:7434 Link Image
Enzyme 9 Chromosome Location 2
Enzyme 9 Locus 2p13.1
Enzyme 9 SNPs SNPJam Report Link Image
Enzyme 9 General References
  1. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  2. Venter JC, Adams MD, Myers EW, Li PW, Mural RJ, Sutton GG, Smith HO, Yandell M, Evans CA, Holt RA, Gocayne JD, Amanatides P, Ballew RM, Huson DH, Wortman JR, Zhang Q, Kodira CD, Zheng XH, Chen L, Skupski M, Subramanian G, Thomas PD, Zhang J, Gabor Miklos GL, Nelson C, Broder S, Clark AG, Nadeau J, McKusick VA, Zinder N, Levine AJ, Roberts RJ, Simon M, Slayman C, Hunkapiller M, Bolanos R, Delcher A, Dew I, Fasulo D, Flanigan M, Florea L, Halpern A, Hannenhalli S, Kravitz S, Levy S, Mobarry C, Reinert K, Remington K, Abu-Threideh J, Beasley E, Biddick K, Bonazzi V, Brandon R, Cargill M, Chandramouliswaran I, Charlab R, Chaturvedi K, Deng Z, Di Francesco V, Dunn P, Eilbeck K, Evangelista C, Gabrielian AE, Gan W, Ge W, Gong F, Gu Z, Guan P, Heiman TJ, Higgins ME, Ji RR, Ke Z, Ketchum KA, Lai Z, Lei Y, Li Z, Li J, Liang Y, Lin X, Lu F, Merkulov GV, Milshina N, Moore HM, Naik AK, Narayan VA, Neelam B, Nusskern D, Rusch DB, Salzberg S, Shao W, Shue B, Sun J, Wang Z, Wang A, Wang X, Wang J, Wei M, Wides R, Xiao C, Yan C, Yao A, Ye J, Zhan M, Zhang W, Zhang H, Zhao Q, Zheng L, Zhong F, Zhong W, Zhu S, Zhao S, Gilbert D, Baumhueter S, Spier G, Carter C, Cravchik A, Woodage T, Ali F, An H, Awe A, Baldwin D, Baden H, Barnstead M, Barrow I, Beeson K, Busam D, Carver A, Center A, Cheng ML, Curry L, Danaher S, Davenport L, Desilets R, Dietz S, Dodson K, Doup L, Ferriera S, Garg N, Gluecksmann A, Hart B, Haynes J, Haynes C, Heiner C, Hladun S, Hostin D, Houck J, Howland T, Ibegwam C, Johnson J, Kalush F, Kline L, Koduru S, Love A, Mann F, May D, McCawley S, McIntosh T, McMullen I, Moy M, Moy L, Murphy B, Nelson K, Pfannkoch C, Pratts E, Puri V, Qureshi H, Reardon M, Rodriguez R, Rogers YH, Romblad D, Ruhfel B, Scott R, Sitter C, Smallwood M, Stewart E, Strong R, Suh E, Thomas R, Tint NN, Tse S, Vech C, Wang G, Wetter J, Williams S, Williams M, Windsor S, Winn-Deen E, Wolfe K, Zaveri J, Zaveri K, Abril JF, Guigo R, Campbell MJ, Sjolander KV, Karlak B, Kejariwal A, Mi H, Lazareva B, Hatton T, Narechania A, Diemer K, Muruganujan A, Guo N, Sato S, Bafna V, Istrail S, Lippert R, Schwartz R, Walenz B, Yooseph S, Allen D, Basu A, Baxendale J, Blick L, Caminha M, Carnes-Stine J, Caulk P, Chiang YH, Coyne M, Dahlke C, Mays A, Dombroski M, Donnelly M, Ely D, Esparham S, Fosler C, Gire H, Glanowski S, Glasser K, Glodek A, Gorokhov M, Graham K, Gropman B, Harris M, Heil J, Henderson S, Hoover J, Jennings D, Jordan C, Jordan J, Kasha J, Kagan L, Kraft C, Levitsky A, Lewis M, Liu X, Lopez J, Ma D, Majoros W, McDaniel J, Murphy S, Newman M, Nguyen T, Nguyen N, Nodell M, Pan S, Peck J, Peterson M, Rowe W, Sanders R, Scott J, Simpson M, Smith T, Sprague A, Stockwell T, Turner R, Venter E, Wang M, Wen M, Wu D, Wu M, Xia A, Zandieh A, Zhu X: The sequence of the human genome. Science. 2001 Feb 16;291(5507):1304-51. [PubMed Link Image]
Enzyme 9 Metabolite References Not Available
Enzyme 10 [top]
Enzyme 10 ID 16499
Enzyme 10 Name Putative uncharacterized protein
Enzyme 10 Synonyms Not Available
Enzyme 10 Gene Name MTHFD1
Enzyme 10 Protein Sequence >Putative uncharacterized protein
MAPAEILNGKEISAQIRARLKNQVTQLKEQVPGFTPRLAILQVGNRDDSNLYINVKLKAA
EEIGIKATHIKLPRTTTESEVMKYITSLNEDSTVHGFLVQLPLDSENSINTEEVINAIAP
EKDVDGLTSINAGRLARGDLNDCFIPCTPKGCLELIKETGVPIAGRHAVVVGRSKIVGAP
MHDLLLWNNATVTTCHSKTAHLDEEVNKGDILVVATGQPEMVKGEWIKPGAIVIDCGINY
VPDDKKPNGRKVVGDVAYDEAKERASFITPVPGGVGPMTVAMLMQSTVESAKRFLEKFKP
GKWMIQYNNLNLKTPVPSDIDISRSCKPKPIGKLAREIGLLSEEVELYGETKAKVLLSAL
ERLKHRPDGKYVVVTGITPTPLGEGKSTTTIGLVQALGAHLYQNVFACVRQPSQGPTFGI
KGGAAGGGYSQVIPMEEFNLHLTGDIHAITAANNLVAAAIDARIFHELTQTDKALFNRLV
PSVNGVRRFSDIQIRRLKRLGIEKTDPTTLTDEEINRFARLDIDPETITWQRVLDTNDRF
LRKITIGQAPTEKGHTRTAQFDISVASEIMAVLALTTSLEDMRERLGKMVVASSKKGEPV
SAEDLGVSGALTVLMKDAIKPNLMQTLEGTPVFVHAGPFANIAHGNSSIIADQIALKLVG
PEGFVVTEAGFGADIGMEKFFNIKCRYSGLCPHVVVLVATVRALKMHGGGPTVTAGLPLP
KAYIQENLELVEKGFSNLKKQIENARMFGIPVVVAVNAFKTDTESELDLISRLSREHGAF
DAVKCTHWAEGGKGALALAQAVQRAAQAPSSFQLLYDLKLPVEDKIRIIAQKIYGADDIE
LLPEAQHKAEVYTKQGFGNLPICMAKTHLSLSHNPEQKGVPTGFILPIRDIRASVGAGFL
YPLVGTMSTMPGLPTRPCFYDIDLDPETEQVNGLF
Enzyme 10 Number of Residues 935
Enzyme 10 Molecular Weight 101532
Enzyme 10 Theoretical pI 7.19
Enzyme 10 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 10 General Function Nucleotide transport and metabolism
Enzyme 10 Specific Function Not Available
Enzyme 10 Pathways Not Available
Enzyme 10 Reactions Not Available
Enzyme 10 Pfam Domain Function
Enzyme 10 Signals
  • None
Enzyme 10 Transmembrane Regions
  • None
Enzyme 10 Essentiality Not Available
Enzyme 10 GenBank ID Protein Not Available
Enzyme 10 UniProtKB/Swiss-Prot ID B2R5Y2 Link Image
Enzyme 10 UniProtKB/Swiss-Prot Entry Name B2R5Y2_HUMAN Link Image
Enzyme 10 PDB ID 1DIA Link Image
Enzyme 10 PDB File Show
Enzyme 10 3D Structure
Enzyme 10 Cellular Location Not Available
Enzyme 10 Gene Sequence Not Available
Enzyme 10 GenBank Gene ID AK312361 Link Image
Enzyme 10 GeneCard ID B2R5Y2 Link Image
Enzyme 10 GenAtlas ID Not Available
Enzyme 10 HGNC ID Not Available
Enzyme 10 Chromosome Location 14
Enzyme 10 Locus 14q24
Enzyme 10 SNPs SNPJam Report Link Image
Enzyme 10 General References Not Available
Enzyme 10 Metabolite References Not Available