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Human Metabolome Database Version 2.5

 

Showing metabocard for Tetrahydrofolic acid (HMDB01846)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2006-02-08 11:18:35
Update Date 2009-05-05 20:58:57
Accession Number HMDB01846
Secondary Accession Numbers Not Available
Common Name Tetrahydrofolic acid
Description Tetrahydrofolate is a soluble coenzyme (vitamin B9) that is synthesized de novo by plants and microorganisms, and absorbed from the diet by animals. It is composed of three distinct parts: a pterin ring, a p-ABA (p-aminobenzoic acid) and a polyglutamate chain with a number of residues varying between 1 and 8. Only the tetra-reduced form of the molecule serves as a coenzyme for C1 transfer reactions. In biological systems, the C1-units exist under various oxidation states and the different tetrahydrofolate derivatives constitute a family of related molecules named indistinctly under the generic term folate. (PMID 16042593) Folate is important for cells and tissues that rapidly divide. Cancer cells divide rapidly, and drugs that interfere with folate metabolism are used to treat cancer. Methotrexate is a drug often used to treat cancer because it inhibits the production of the active form, tetrahydrofolate. Unfortunately, methotrexate can be toxic, producing side effects such as inflammation in the digestive tract that make it difficult to eat normally. -- Wikipedia; Signs of folic acid deficiency are often subtle. Diarrhea, loss of appetite, and weight loss can occur. Additional signs are weakness, sore tongue, headaches, heart palpitations, irritability, and behavioral disorders. Women with folate deficiency who become pregnant are more likely to give birth to low birth weight and premature infants, and infants with neural tube defects. In adults, anemia is a sign of advanced folate deficiency. In infants and children, folate deficiency can slow growth rate. Some of these symptoms can also result from a variety of medical conditions other than folate deficiency. It is important to have a physician evaluate these symptoms so that appropriate medical care can be given. -- Wikipedia; Folinic acid is a form of folate that can help 'rescue' or reverse the toxic effects of methotrexate. Folinic acid is not the same as folic acid. Folic acid supplements have little established role in cancer chemotherapy. There have been cases of severe adverse effects of accidental substitution of folic acid for folinic acid in patients receiving methotrexate cancer chemotherapy. It is important for anyone receiving methotrexate to follow medical advice on the use of folic or folinic acid supplements. -- Wikipedia Low concentrations of folate, vitamin B12, or vitamin B6 may increase the level of homocysteine, an amino acid normally found in blood. There is evidence that an elevated homocysteine level is an independent risk factor for heart disease and stroke. The evidence suggests that high levels of homocysteine may damage coronary arteries or make it easier for blood clotting cells called platelets to clump together and form a clot. However, there is currently no evidence available to suggest that lowering homocysteine with vitamins will reduce your risk of heart disease. Clinical intervention trials are needed to determine whether supplementation with folic acid, vitamin B12 or vitamin B6 can lower your risk of developing coronary heart disease. -- Wikipedia
Synonyms
  1. (6S)-Tetrahydrofolate
  2. (6S)-Tetrahydrofolic acid
  3. 5,6,7,8-Tetrahydrofolate
  4. 5,6,7,8-tetrahydrofolic acid
  5. tetra-H-folate
  6. tetrahydrafolate
  7. Tetrahydrofolate
  8. tetrahydrofolic acid
  9. tetrahydropteroyl mono-L-glutamate
  10. tetrahydropteroylglutamate
Chemical IUPAC Name 2-[[4-[(2-amino-4-oxo-5,6,7,8-tetrahydro-1H-pteridin-6-yl)methylamino]benzoyl]amino]pentanedioic acid
Chemical Formula C19H23N7O6
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Heterocyclic molecules
Class
  • Pterins
Sub Class
  • Tetrahydro-pterins
Family
  • Mammalian Metabolite
Species
  • secondary amine
  • secondary aliphatic/aromatic amine (alkylarylamine)
  • carboxylic acid
  • secondary carboxylic acid amide
  • oxo(het)arene
  • imino(het)arene
  • aromatic compound
  • heterocyclic compound
Biofunction
  • DNA component
  • Enzyme co-factor
  • Component of Cyanoamino acid metabolism
  • Component of Folate biosynthesis
  • Component of Glycine, serine and threonine metabolism
  • Component of Glyoxylate and dicarboxylate metabolism
  • Component of Methane metabolism
  • Component of Pyrimidine metabolism
Application
Source
  • Endogenous
Average Molecular Weight 445.429
Monoisotopic Molecular Weight 445.170990
Isomeric SMILES OC(=O)CCC(NC(=O)C1=CC=C(NCC2CNC3=C(N2)C(=O)NC(=N)N3)C=C1)C(O)=O
Canonical SMILES OC(=O)CCC(NC(=O)C1=CC=C(NCC2CNC3=C(N2)C(=O)NC(=N)N3)C=C1)C(O)=O
KEGG Compound ID C00101 Link Image
BioCyc ID THF Link Image
BiGG ID 33856 Link Image
Wikipedia Link Tetrahydrofolic acid Link Image
NuGOwiki Link HMDB01846 Link Image
Metagene Link HMDB01846 Link Image
METLIN ID 714 Link Image
PubChem Compound 1129 Link Image
PubChem Substance 5642917 Link Image
ChEBI ID 15635 Link Image
CAS Registry Number 135-16-0
InChI Identifier InChI=1/C19H23N7O6/c20-19-25-15-14(17(30)26-19)23-11(8-22-15)7-21-10-3-1-9(2-4-10)16(29)24-12(18(31)32)5-6-13(27)28/h1-4,11-12,21,23H,5-8H2,(H,24,29)(H,27,28)(H,31,32)(H4,20,22,25,26,30)
Synthesis Reference Not Available
Melting Point (Experimental) 250 oC (523 K), decomp.
Experimental Water Solubility Not Available Source: PhysProp
Predicted Water Solubility 0.29500002 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge -2
State Solid
Experimental LogP/Hydrophobicity Not Available Source: PhysProp
Predicted LogP/Hydrophobicity -1.45 [Predicted by ALOGPS]; -2.7 [Predicted by PubChem via XLOGP] Calculated using ALOGPS
Material Safety Data Sheet (MSDS)
MOL File Show
SDF File Show
PDB File Show
2D Structure
3D Structure
Experimental PDB ID Not Available
Experimental 1H NMR Spectrum Download Spectrum
Download FID (Bruker)
Show Experimental Conditions Link Image
Experimental 13C NMR Spectrum Not Available
Experimental 13C HSQC Spectrum Download Spectrum
Download FID (Bruker)
Show Experimental Conditions Link Image
Predicted 1H NMR Spectrum Show Image
Show Peaklist
Predicted 13C NMR Spectrum Show Image
Show Peaklist
Mass Spectrum
Low Energy
Download File
Show Experimental Conditions Link Image
Medium Energy
Download File
Show Experimental Conditions Link Image
High Energy
Download File
Show Experimental Conditions Link Image
Simplified TOCSY Spectrum Show Image
Show Peaklist
BMRB Spectrum Show Image
Show Peaklist
Cellular Location
  • Cytoplasm (Predicted from LogP)
  • Extracellular
  • lysosome
  • mitochondria
Biofluid Location
  • Blood
Tissue Location
Tissue References
Brain
Erythrocyte
Fibroblasts
Intestine
Kidney
Liver
Myelin
Neuron
Pancreas
Placenta
Platelet
Prostate
Stratum Corneum
Testes
Concentrations (Normal)
Biofluid Blood
Value 0.0025 +/- 0.0044 uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Fazili Z, Pfeiffer CM, Zhang M: Comparison of serum folate species analyzed by LC-MS/MS with total folate measured by microbiologic assay and Bio-Rad radioassay. Clin Chem. 2007 Apr;53(4):781-4. Epub 2007 Feb 1. [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
Betaine Metabolism SMP00123 Link Image map00260 Link Image
Folate Metabolism SMP00053 Link Image map00670 Link Image
Glycine and Serine Metabolism SMP00004 Link Image map00260 Link Image
Histidine Metabolism SMP00044 Link Image map00340 Link Image
Methionine Metabolism SMP00033 Link Image map00270 Link Image
Pterine Biosynthesis SMP00005 Link Image map00790 Link Image
General References
  1. Garbis SD, Melse-Boonstra A, West CE, van Breemen RB: Determination of folates in human plasma using hydrophilic interaction chromatography-tandem mass spectrometry. Anal Chem. 2001 Nov 15;73(22):5358-64. [PubMed Link Image]
  2. Pemetrexed: new drug. Pleural mesothelioma: a first encouraging trial. Prescrire Int. 2005 Dec;14(80):212-4. [PubMed Link Image]
  3. Asrar FM, O'Connor DL: Bacterially synthesized folate and supplemental folic acid are absorbed across the large intestine of piglets. J Nutr Biochem. 2005 Oct;16(10):587-93. [PubMed Link Image]
  4. Ahmed F, Khan MR, Akhtaruzzaman M, Karim R, Marks GC, Banu CP, Nahar B, Williams G: Efficacy of twice-weekly multiple micronutrient supplementation for improving the hemoglobin and micronutrient status of anemic adolescent schoolgirls in Bangladesh. Am J Clin Nutr. 2005 Oct;82(4):829-35. [PubMed Link Image]
  5. Pieniazek D, Kubalska J, Pronicka E, Stecko E: Disturbances in histidine metabolism in children with speech abnormalities. Acta Anthropogenet. 1985;9(1-3):117-21. [PubMed Link Image]
  6. Ozer B, Serin E, Gumurdulu Y, Kayaselcuk F, Anarat R, Gur G, Kul K, Guclu M, Boyacioglu S: Helicobacter pylori eradication lowers serum homocysteine level in patients without gastric atrophy. World J Gastroenterol. 2005 May 14;11(18):2764-7. [PubMed Link Image]
  7. Greenwald P, Milner JA, Anderson DE, McDonald SS: Micronutrients in cancer chemoprevention. Cancer Metastasis Rev. 2002;21(3-4):217-30. [PubMed Link Image]
  8. Siega-Riz AM, Savitz DA, Zeisel SH, Thorp JM, Herring A: Second trimester folate status and preterm birth. Am J Obstet Gynecol. 2004 Dec;191(6):1851-7. [PubMed Link Image]
  9. Taber LD, O'Brien P, Bowsher RR, Sportsman JR: Competitive particle concentration fluorescence immunoassay for measuring 5,10-dideaza-5,6,7,8-tetrahydrofolic acid (lometrexol) in serum. Clin Chem. 1991 Feb;37(2):254-60. [PubMed Link Image]
  10. Mattson MP: Gene-diet interactions in brain aging and neurodegenerative disorders. Ann Intern Med. 2003 Sep 2;139(5 Pt 2):441-4. [PubMed Link Image]
  11. Dietrich M, Brown CJ, Block G: The effect of folate fortification of cereal-grain products on blood folate status, dietary folate intake, and dietary folate sources among adult non-supplement users in the United States. J Am Coll Nutr. 2005 Aug;24(4):266-74. [PubMed Link Image]
  12. Kamen BA, Smith AK: A review of folate receptor alpha cycling and 5-methyltetrahydrofolate accumulation with an emphasis on cell models in vitro. Adv Drug Deliv Rev. 2004 Apr 29;56(8):1085-97. [PubMed Link Image]
  13. Baggott JE, Johanning GL, Branham KE, Prince CW, Morgan SL, Eto I, Vaughn WH: Cofactor role for 10-formyldihydrofolic acid. Biochem J. 1995 Jun 15;308 ( Pt 3):1031-6. [PubMed Link Image]
  14. Makino Y, Nagano M, Tamura K, Kawarabayashi T: Pregnancy complicated with pure red cell aplasia: a case report. J Perinat Med. 2003;31(6):530-4. [PubMed Link Image]
  15. Pljesa S: [Possible complications of erythropoietin therapy in patients with chronic renal failure] Med Pregl. 2004 May-Jun;57(5-6):254-7. [PubMed Link Image]
  16. Pufulete M, Al-Ghnaniem R, Khushal A, Appleby P, Harris N, Gout S, Emery PW, Sanders TA: Effect of folic acid supplementation on genomic DNA methylation in patients with colorectal adenoma. Gut. 2005 May;54(5):648-53. [PubMed Link Image]
  17. Wang S, Low PS: Folate-mediated targeting of antineoplastic drugs, imaging agents, and nucleic acids to cancer cells. J Control Release. 1998 Apr 30;53(1-3):39-48. [PubMed Link Image]
  18. Hankey GJ, Eikelboom JW, Loh K, Tang M, Pizzi J, Thom J, Yi Q: Sustained homocysteine-lowering effect over time of folic acid-based multivitamin therapy in stroke patients despite increasing folate status in the population. Cerebrovasc Dis. 2005;19(2):110-6. Epub 2004 Dec 17. [PubMed Link Image]
  19. Ramaekers VT, Rothenberg SP, Sequeira JM, Opladen T, Blau N, Quadros EV, Selhub J: Autoantibodies to folate receptors in the cerebral folate deficiency syndrome. N Engl J Med. 2005 May 12;352(19):1985-91. [PubMed Link Image]
  20. Verwei M, Arkbage K, Mocking H, Havenaar R, Groten J: The binding of folic acid and 5-methyltetrahydrofolate to folate-binding proteins during gastric passage differs in a dynamic in vitro gastrointestinal model. J Nutr. 2004 Jan;134(1):31-7. [PubMed Link Image]
  21. Mattson MP: Will caloric restriction and folate protect against AD and PD? Neurology. 2003 Feb 25;60(4):690-5. [PubMed Link Image]
  22. Omura Y: Excessive use of Steroid Hormone & beneficial effects of True St. 36 acupuncture on malignant brain tumors--part I; how to estimate non-invasively presence of excess dose of Steroid Hormone in patients, baseball players & other professional athletes from its toxic effects on heart & pancreas, as well as persistent or recurrent infection--part II. Acupunct Electrother Res. 2005;30(1-2):57-102. [PubMed Link Image]
  23. Paulionis L, Kane SL, Meckling KA: Vitamin status and cognitive function in a long-term care population. BMC Geriatr. 2005 Dec 13;5:16. [PubMed Link Image]
  24. Zhu WY, Alliegro MA, Melera PW: The rate of folate receptor alpha (FR alpha) synthesis in folate depleted CHL cells is regulated by a translational mechanism sensitive to media folate levels, while stable overexpression of its mRNA is mediated by gene amplification and an increase in transcript half-life. J Cell Biochem. 2001 Mar 26;81(2):205-19. [PubMed Link Image]
  25. Tchantchou F: Homocysteine increase folate oxidative brain homocysteine metabolism and various consequences of folate deficiency. J Alzheimers Dis. 2006 Aug;9(4):421-7. [PubMed Link Image]
  26. Lu S, Chen GL, Ren C, Kwabi-Addo B, Epner DE: Methionine restriction selectively targets thymidylate synthase in prostate cancer cells. Biochem Pharmacol. 2003 Sep 1;66(5):791-800. [PubMed Link Image]
  27. Durga J, van Boxtel MP, Schouten EG, Bots ML, Kok FJ, Verhoef P: Folate and the methylenetetrahydrofolate reductase 677C-->T mutation correlate with cognitive performance. Neurobiol Aging. 2006 Feb;27(2):334-43. Epub 2005 Feb 24. [PubMed Link Image]
  28. Stuerenburg HJ, Ganzer S, Arlt S, Muller-Thomsen T: The influence of smoking on plasma folate and lipoproteins in Alzheimer disease, mild cognitive impairment and depression. Neuro Endocrinol Lett. 2005 Jun;26(3):261-3. [PubMed Link Image]
  29. Smith DE, Kok RM, Teerlink T, Jakobs C, Smulders YM: Quantitative determination of erythrocyte folate vitamer distribution by liquid chromatography-tandem mass spectrometry. Clin Chem Lab Med. 2006;44(4):450-9. [PubMed Link Image]
  30. Wolters M, Strohle A, Hahn A: [Age-associated changes in the metabolism of vitamin B(12) and folic acid: prevalence, aetiopathogenesis and pathophysiological consequences] Z Gerontol Geriatr. 2004 Apr;37(2):109-35. [PubMed Link Image]
  31. Wikipedia Link Image
Metabolic Enzymes
  1. Methionine synthase
  2. Methylenetetrahydrofolate reductase
  3. Trifunctional purine biosynthetic protein adenosine-3 [Includes: Phosphoribosylamine--glycine ligase
  4. Formimidoyltransferase-cyclodeaminase
  5. Aminomethyltransferase, mitochondrial precursor
  6. Dihydrofolate reductase
  7. Serine hydroxymethyltransferase, mitochondrial precursor
  8. Serine hydroxymethyltransferase, cytosolic
  9. Folylpolyglutamate synthase, mitochondrial precursor
  10. Bifunctional purine biosynthesis protein PURH [Includes: Phosphoribosylaminoimidazolecarboxamide formyltransferase
  11. Bifunctional methylenetetrahydrofolate dehydrogenase/cyclohydrolase, mitochondrial precursor [Includes: NAD-dependent methylenetetrahydrofolate dehydrogenase
  12. C-1-tetrahydrofolate synthase, cytoplasmic
  13. 10-formyltetrahydrofolate dehydrogenase
  14. Gamma-glutamyl hydrolase precursor
  15. Folylpolyglutamate synthase
  16. Dihydrofolate reductase (cDNA, FLJ93028, Homo sapiens dihydrofolate reductase (DHFR), mRNA)
  17. cDNA FLJ76259, highly similar to Homo sapiens aminomethyltransferase
  18. cDNA FLJ78616, highly similar to Homo sapiens phosphoribosylglycinamide formyltransferase, phosphoribosylglycinamide synthetase, phosphoribosylaminoimidazole synthetase
  19. Methionyl-tRNA formyltransferase, mitochondrial precursor
  20. C1-tetrahydrofolate synthase
  21. Methylenetetrahydrofolate dehydrogenase
  22. Putative uncharacterized protein
Enzyme 1 [top]
Enzyme 1 ID 5392
Enzyme 1 Name Methionine synthase
Enzyme 1 Synonyms
  1. 5-methyltetrahydrofolate-- homocysteine methyltransferase
  2. Methionine synthase, vitamin-B12 dependent
  3. 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
  • cell
  • intracellular
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
  • None
Enzyme 1 Transmembrane Regions
  • None
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 1923221 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID Q99707 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name METH_HUMAN Link Image
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 Link Image
Enzyme 1 GeneCard ID MTR Link Image
Enzyme 1 GenAtlas ID MTR Link Image
Enzyme 1 HGNC ID HGNC:7468 Link Image
Enzyme 1 Chromosome Location 1
Enzyme 1 Locus 1q43
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 General References
  1. 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 Link Image]
  2. 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 Link Image]
  3. 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 Link Image]
  4. 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 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 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
  • 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, 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]
  2. 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]
  3. 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]
  4. 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]
  5. 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]
  6. 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]
  7. 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]
  8. 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]
  9. 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]
  10. 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]
  11. 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]
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
  1. GARS
  2. Glycinamide ribonucleotide synthetase
  3. Phosphoribosylglycinamide synthetase
  4. Phosphoribosylformylglycinamidine cyclo-ligase
  5. AIRS
  6. Phosphoribosyl-aminoimidazole synthetase
  7. AIR synthase
  8. Phosphoribosylglycinamide formyltransferase
  9. GART
  10. GAR transformylase
  11. 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
  • None
Enzyme 3 Transmembrane Regions
  • None
Enzyme 3 Essentiality Not Available
Enzyme 3 GenBank ID Protein 31642 Link Image
Enzyme 3 UniProtKB/Swiss-Prot ID P22102 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name PUR2_HUMAN Link Image
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 Link Image
Enzyme 3 GeneCard ID GART Link Image
Enzyme 3 GenAtlas ID GART Link Image
Enzyme 3 HGNC ID HGNC:4163 Link Image
Enzyme 3 Chromosome Location Not Available
Enzyme 3 Locus Not Available
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 General References
  1. 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 Link Image]
  2. Kan JL, Moran RG: Intronic polyadenylation in the human glycinamide ribonucleotide formyltransferase gene. Nucleic Acids Res. 1997 Aug 1;25(15):3118-23. [PubMed Link Image]
  3. 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 Link Image]
Enzyme 3 Metabolite References Not Available
Enzyme 4 [top]
Enzyme 4 ID 5959
Enzyme 4 Name Formimidoyltransferase-cyclodeaminase
Enzyme 4 Synonyms
  1. Formiminotransferase- cyclodeaminase
  2. FTCD
  3. LCHC1[Includes: Glutamate formimidoyltransferase
  4. Glutamate formiminotransferase
  5. Glutamate formyltransferase
  6. Formimidoyltetrahydrofolate cyclodeaminase
  7. 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
  • None
Enzyme 4 Transmembrane Regions
  • None
Enzyme 4 Essentiality Not Available
Enzyme 4 GenBank ID Protein 6537208 Link Image
Enzyme 4 UniProtKB/Swiss-Prot ID O95954 Link Image
Enzyme 4 UniProtKB/Swiss-Prot Entry Name FTCD_HUMAN Link Image
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 Link Image
Enzyme 4 GeneCard ID FTCD Link Image
Enzyme 4 GenAtlas ID FTCD Link Image
Enzyme 4 HGNC ID HGNC:3974 Link Image
Enzyme 4 Chromosome Location Not Available
Enzyme 4 Locus Not Available
Enzyme 4 SNPs SNPJam Report Link Image
Enzyme 4 General References
  1. 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 Link Image]
  2. 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 Link Image]
  3. 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 Link Image]
Enzyme 4 Metabolite References Not Available
Enzyme 5 [top]
Enzyme 5 ID 5961
Enzyme 5 Name Aminomethyltransferase, mitochondrial precursor
Enzyme 5 Synonyms
  1. Glycine cleavage system T protein
  2. 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
Enzyme 5 Reactions
  • protein-S-aminomethyldihydrolipoyllysine + tetrahydrofolate = protein-dihydrolipoyllysine + 5,10-methylenetetrahydrofolate + NH3
Enzyme 5 Pfam Domain Function
Enzyme 5 Signals
  • 1-23
Enzyme 5 Transmembrane Regions Not Available
Enzyme 5 Essentiality Not Available
Enzyme 5 GenBank ID Protein 391721 Link Image
Enzyme 5 UniProtKB/Swiss-Prot ID P48728 Link Image
Enzyme 5 UniProtKB/Swiss-Prot Entry Name GCST_HUMAN Link Image
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 Link Image
Enzyme 5 GeneCard ID AMT Link Image
Enzyme 5 GenAtlas ID AMT Link Image
Enzyme 5 HGNC ID HGNC:473 Link Image
Enzyme 5 Chromosome Location 3
Enzyme 5 Locus 3p21.2-p21.1
Enzyme 5 SNPs SNPJam Report Link Image
Enzyme 5 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. 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]
  4. 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]
  5. 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]
  6. 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]
  7. 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 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
Enzyme 6 Reactions
  • 5,6,7,8-tetrahydrofolate + NADP+ = 7,8-dihydrofolate + NADPH + H+
Enzyme 6 Pfam Domain Function
Enzyme 6 Signals
  • None
Enzyme 6 Transmembrane Regions
  • None
Enzyme 6 Essentiality Not Available
Enzyme 6 GenBank ID Protein 182724 Link Image
Enzyme 6 UniProtKB/Swiss-Prot ID P00374 Link Image
Enzyme 6 UniProtKB/Swiss-Prot Entry Name DYR_HUMAN Link Image
Enzyme 6 PDB ID 1MVT Link Image
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 Link Image
Enzyme 6 GeneCard ID DHFR Link Image
Enzyme 6 GenAtlas ID DHFR Link Image
Enzyme 6 HGNC ID HGNC:2861 Link Image
Enzyme 6 Chromosome Location 5
Enzyme 6 Locus 5q11.2-q13.2
Enzyme 6 SNPs SNPJam Report Link Image
Enzyme 6 General References
  1. 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 Link Image]
  2. 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 Link Image]
  3. 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 Link Image]
  4. 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 Link Image]
  5. 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 Link Image]
  6. 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 Link Image]
  7. 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 Link Image]
Enzyme 6 Metabolite References Not Available
Enzyme 7 [top]
Enzyme 7 ID 6072
Enzyme 7 Name Serine hydroxymethyltransferase, mitochondrial precursor
Enzyme 7 Synonyms
  1. Serine methylase
  2. Glycine hydroxymethyltransferase
  3. 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
  • 1-18
Enzyme 7 Transmembrane Regions Not Available
Enzyme 7 Essentiality Not Available
Enzyme 7 GenBank ID Protein 746436 Link Image
Enzyme 7 UniProtKB/Swiss-Prot ID P34897 Link Image
Enzyme 7 UniProtKB/Swiss-Prot Entry Name GLYM_HUMAN Link Image
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 Link Image
Enzyme 7 GeneCard ID SHMT2 Link Image
Enzyme 7 GenAtlas ID SHMT2 Link Image
Enzyme 7 HGNC ID HGNC:10852 Link Image
Enzyme 7 Chromosome Location 12
Enzyme 7 Locus 12q12-q14
Enzyme 7 SNPs SNPJam Report Link Image
Enzyme 7 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. 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]
Enzyme 7 Metabolite References Not Available
Enzyme 8 [top]
Enzyme 8 ID 6074
Enzyme 8 Name Serine hydroxymethyltransferase, cytosolic
Enzyme 8 Synonyms
  1. Serine methylase
  2. Glycine hydroxymethyltransferase
  3. 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
  • None
Enzyme 8 Transmembrane Regions
  • None
Enzyme 8 Essentiality Not Available
Enzyme 8 GenBank ID Protein 307422 Link Image
Enzyme 8 UniProtKB/Swiss-Prot ID P34896 Link Image
Enzyme 8 UniProtKB/Swiss-Prot Entry Name GLYC_HUMAN Link Image
Enzyme 8 PDB ID 1BJ4 Link Image
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 Link Image
Enzyme 8 GeneCard ID SHMT1 Link Image
Enzyme 8 GenAtlas ID SHMT1 Link Image
Enzyme 8 HGNC ID HGNC:10850 Link Image
Enzyme 8 Chromosome Location 17
Enzyme 8 Locus 17p11.2
Enzyme 8 SNPs SNPJam Report Link Image
Enzyme 8 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. 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 8 Metabolite References Not Available
Enzyme 9 [top]
Enzyme 9 ID 6130
Enzyme 9 Name Folylpolyglutamate synthase, mitochondrial precursor
Enzyme 9 Synonyms
  1. Folylpoly-gamma-glutamate synthetase
  2. FPGS
  3. Tetrahydrofolate synthase
  4. 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
Enzyme 9 Reactions
  • ATP + tetrahydrofolyl-[Glu]n + L-glutamate = ADP + phosphate + tetrahydrofolyl-[Glu]n+1
Enzyme 9 Pfam Domain Function
Enzyme 9 Signals
  • 1-19
Enzyme 9 Transmembrane Regions Not Available
Enzyme 9 Essentiality Not Available
Enzyme 9 GenBank ID Protein 292029 Link Image
Enzyme 9 UniProtKB/Swiss-Prot ID Q05932 Link Image
Enzyme 9 UniProtKB/Swiss-Prot Entry Name FOLC_HUMAN Link Image
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 Link Image
Enzyme 9 GeneCard ID FPGS Link Image
Enzyme 9 GenAtlas ID FPGS Link Image
Enzyme 9 HGNC ID HGNC:3824 Link Image
Enzyme 9 Chromosome Location 9
Enzyme 9 Locus 9q34.1
Enzyme 9 SNPs SNPJam Report Link Image
Enzyme 9 General References
  1. 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 Link Image]
  2. 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 Link Image]
  3. 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 Link Image]
  4. 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 Link Image]
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
  1. 5-aminoimidazole-4-carboxamide ribonucleotide formyltransferase
  2. AICAR transformylase
  3. IMP cyclohydrolase
  4. Inosinicase
  5. IMP synthetase
  6. 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
  • None
Enzyme 10 Transmembrane Regions
  • None
Enzyme 10 Essentiality Not Available
Enzyme 10 GenBank ID Protein 1263196 Link Image
Enzyme 10 UniProtKB/Swiss-Prot ID P31939 Link Image
Enzyme 10 UniProtKB/Swiss-Prot Entry Name PUR9_HUMAN Link Image
Enzyme 10 PDB ID 1P4R Link Image
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 Link Image
Enzyme 10 GeneCard ID ATIC Link Image
Enzyme 10 GenAtlas ID ATIC Link Image
Enzyme 10 HGNC ID HGNC:794 Link Image
Enzyme 10 Chromosome Location 2
Enzyme 10 Locus 2q35
Enzyme 10 SNPs SNPJam Report Link Image
Enzyme 10 General References
  1. 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 Link Image]
  2. 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 Link Image]
  3. 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 Link Image]
  4. 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 Link Image]
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
  • catalytic activity
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 Link Image)
  • One Carbon Pool By Folate (map00670 Link Image)
Enzyme 11 Reactions
  • 5,10-methenyltetrahydrofolate + H2O = 10-formyltetrahydrofolate
Enzyme 11 Pfam Domain Function
Enzyme 11 Signals
  • 1-20
Enzyme 11 Transmembrane Regions Not Available
Enzyme 11 Essentiality Not Available
Enzyme 11 GenBank ID Protein 35071 Link Image
Enzyme 11 UniProtKB/Swiss-Prot ID P13995 Link Image
Enzyme 11 UniProtKB/Swiss-Prot Entry Name MTDC_HUMAN Link Image
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 Link Image
Enzyme 11 GeneCard ID MTHFD2 Link Image
Enzyme 11 GenAtlas ID MTHFD2 Link Image
Enzyme 11 HGNC ID HGNC:7434 Link Image
Enzyme 11 Chromosome Location 2
Enzyme 11 Locus 2p13.1
Enzyme 11 SNPs SNPJam Report Link Image
Enzyme 11 General References
  1. 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 Link Image]
Enzyme 11 Metabolite References Not Available
Enzyme 12 [top]
Enzyme 12 ID 6211
Enzyme 12 Name C-1-tetrahydrofolate synthase, cytoplasmic
Enzyme 12 Synonyms
  1. 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 Link Image)
  • One Carbon Pool By Folate (map00670 Link Image)
Enzyme 12 Reactions
  • ATP + formate + tetrahydrofolate = ADP + phosphate + 10-formyltetrahydrofolate
Enzyme 12 Pfam Domain Function
Enzyme 12 Signals
  • None
Enzyme 12 Transmembrane Regions
  • None
Enzyme 12 Essentiality Not Available
Enzyme 12 GenBank ID Protein 307178 Link Image
Enzyme 12 UniProtKB/Swiss-Prot ID P11586 Link Image
Enzyme 12 UniProtKB/Swiss-Prot Entry Name C1TC_HUMAN Link Image
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 Link Image
Enzyme 12 GeneCard ID MTHFD1 Link Image
Enzyme 12 GenAtlas ID MTHFD1 Link Image
Enzyme 12 HGNC ID HGNC:7432 Link Image
Enzyme 12 Chromosome Location 14
Enzyme 12 Locus 14q24
Enzyme 12 SNPs SNPJam Report Link Image
Enzyme 12 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. 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]
  3. 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]
  4. 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]
Enzyme 12 Metabolite References Not Available
Enzyme 13 [top]
Enzyme 13 ID 6225
Enzyme 13 Name 10-formyltetrahydrofolate dehydrogenase
Enzyme 13 Synonyms
  1. 10-FTHFDH
  2. 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
  • None
Enzyme 13 Transmembrane Regions
  • None
Enzyme 13 Essentiality Not Available
Enzyme 13 GenBank ID Protein 3560541 Link Image
Enzyme 13 UniProtKB/Swiss-Prot ID O75891 Link Image
Enzyme 13 UniProtKB/Swiss-Prot Entry Name FTHFD_HUMAN Link Image
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 Link Image
Enzyme 13 GeneCard ID ALDH1L1 Link Image
Enzyme 13 GenAtlas ID ALDH1L1 Link Image
Enzyme 13 HGNC ID HGNC:3978 Link Image
Enzyme 13 Chromosome Location 3
Enzyme 13 Locus 3q21.2
Enzyme 13 SNPs SNPJam Report Link Image
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
  1. Gamma-Glu-X carboxypeptidase
  2. Conjugase
  3. 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
  • catalytic activity
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
Enzyme 14 Reactions
  • Hydrolysis of a gamma-glutamyl bond
Enzyme 14 Pfam Domain Function
Enzyme 14 Signals
  • 1-24
Enzyme 14 Transmembrane Regions Not Available
Enzyme 14 Essentiality Not Available
Enzyme 14 GenBank ID Protein 2951931 Link Image
Enzyme 14 UniProtKB/Swiss-Prot ID Q92820 Link Image
Enzyme 14 UniProtKB/Swiss-Prot Entry Name GGH_HUMAN Link Image
Enzyme 14 PDB ID 1L9X Link Image
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 Link Image
Enzyme 14 GeneCard ID GGH Link Image
Enzyme 14 GenAtlas ID GGH Link Image
Enzyme 14 HGNC ID HGNC:4248 Link Image
Enzyme 14 Chromosome Location 8
Enzyme 14 Locus 8q12.3
Enzyme 14 SNPs SNPJam Report Link Image
Enzyme 14 General References
  1. 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 Link Image]
  2. 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 Link Image]
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
  • None
Enzyme 15 Transmembrane Regions
  • None
Enzyme 15 Essentiality Not Available
Enzyme 15 GenBank ID Protein Not Available
Enzyme 15 UniProtKB/Swiss-Prot ID Q5JU19 Link Image
Enzyme 15 UniProtKB/Swiss-Prot Entry Name Q5JU19_HUMAN Link Image
Enzyme 15 PDB ID Not Available
Enzyme 15 Cellular Location Not Available
Enzyme 15 Gene Sequence Not Available
Enzyme 15 GenBank Gene ID AL162586 Link Image
Enzyme 15 GeneCard ID Q5JU19 Link Image
Enzyme 15 GenAtlas ID FPGS Link Image
Enzyme 15 HGNC ID HGNC:3824 Link Image
Enzyme 15 Chromosome Location Not Available
Enzyme 15 Locus Not Available
Enzyme 15 SNPs SNPJam Report Link Image
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
  • None
Enzyme 16 Transmembrane Regions
  • None
Enzyme 16 Essentiality Not Available
Enzyme 16 GenBank ID Protein Not Available
Enzyme 16 UniProtKB/Swiss-Prot ID B0YJ76 Link Image
Enzyme 16 UniProtKB/Swiss-Prot Entry Name B0YJ76_HUMAN Link Image
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 Link Image
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 Link Image
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
  1. glycine cleavage system protein T
  2. AMT, mRNA
  3. 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
  • None
Enzyme 17 Transmembrane Regions
  • None
Enzyme 17 Essentiality Not Available
Enzyme 17 GenBank ID Protein 158254632 Link Image
Enzyme 17 UniProtKB/Swiss-Prot ID A8K3I5 Link Image
Enzyme 17 UniProtKB/Swiss-Prot Entry Name A8K3I5_HUMAN Link Image
Enzyme 17 PDB ID Not Available
Enzyme 17 Cellular Location Not Available
Enzyme 17 Gene Sequence Not Available
Enzyme 17 GenBank Gene ID AK290600 Link Image
Enzyme 17 GeneCard ID A8K3I5 Link Image
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
  1. GART, transcript variant 1, mRNA
  2. 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
  • None
Enzyme 18 Transmembrane Regions
  • None
Enzyme 18 Essentiality Not Available
Enzyme 18 GenBank ID Protein 158259255 Link Image
Enzyme 18 UniProtKB/Swiss-Prot ID A8KA32 Link Image
Enzyme 18 UniProtKB/Swiss-Prot Entry Name A8KA32_HUMAN Link Image
Enzyme 18 PDB ID Not Available
Enzyme 18 Cellular Location Not Available
Enzyme 18 Gene Sequence Not Available
Enzyme 18 GenBank Gene ID AK292897 Link Image
Enzyme 18 GeneCard ID A8KA32 Link Image
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 Link Image
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
  1. 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
  • None
Enzyme 19 Transmembrane Regions
  • None
Enzyme 19 Essentiality Not Available
Enzyme 19 GenBank ID Protein 133777035 Link Image
Enzyme 19 UniProtKB/Swiss-Prot ID Q96DP5 Link Image
Enzyme 19 UniProtKB/Swiss-Prot Entry Name FMT_HUMAN Link Image
Enzyme 19 PDB ID Not Available
Enzyme 19 Cellular Location Not Available
Enzyme 19 Gene Sequence Not Available
Enzyme 19 GenBank Gene ID BC016630 Link Image
Enzyme 19 GeneCard ID Q96DP5 Link Image
Enzyme 19 GenAtlas ID MTFMT Link Image
Enzyme 19 HGNC ID HGNC:29666 Link Image
Enzyme 19 Chromosome Location Not Available
Enzyme 19 Locus Not Available
Enzyme 19 SNPs SNPJam Report Link Image
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
  1. Methylenetetrahydrofolate dehydrogenase
  2. NADP+ dependent1-like
  3. 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 Link Image)
  • One Carbon Pool By Folate (map00670 Link Image)
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
  • None
Enzyme 20 Transmembrane Regions
  • None
Enzyme 20 Essentiality Not Available
Enzyme 20 GenBank ID Protein 34811726 Link Image
Enzyme 20 UniProtKB/Swiss-Prot ID Q6UB35 Link Image
Enzyme 20 UniProtKB/Swiss-Prot Entry Name Q6UB35_HUMAN Link Image
Enzyme 20 PDB ID Not Available
Enzyme 20 Cellular Location Not Available
Enzyme 20 Gene Sequence Not Available
Enzyme 20 GenBank Gene ID AY374130 Link Image
Enzyme 20 GeneCard ID Q6UB35 Link Image
Enzyme 20 GenAtlas ID MTHFD1L Link Image
Enzyme 20 HGNC ID HGNC:21055 Link Image
Enzyme 20 Chromosome Location Not Available
Enzyme 20 Locus Not Available
Enzyme 20 SNPs SNPJam Report Link Image
Enzyme 20 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]
Enzyme 20 Metabolite References Not Available
Enzyme 21 [top]
Enzyme 21 ID 13035
Enzyme 21 Name Methylenetetrahydrofolate dehydrogenase
Enzyme 21 Synonyms
  1. NADP+ dependent2, methenyltetrahydrofolate cyclohydrolase
  2. Methylenetetrahydrofolate dehydrogenase
  3. 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
  • catalytic activity
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
  • None
Enzyme 21 Transmembrane Regions
  • None
Enzyme 21 Essentiality Not Available
Enzyme 21 GenBank ID Protein 31418096 Link Image
Enzyme 21 UniProtKB/Swiss-Prot ID Q7Z650 Link Image
Enzyme 21 UniProtKB/Swiss-Prot Entry Name Q7Z650_HUMAN Link Image
Enzyme 21 PDB ID Not Available
Enzyme 21 Cellular Location Not Available
Enzyme 21 Gene Sequence Not Available
Enzyme 21 GenBank Gene ID BC015062 Link Image
Enzyme 21 GeneCard ID Q7Z650 Link Image
Enzyme 21 GenAtlas ID MTHFD2 Link Image
Enzyme 21 HGNC ID HGNC:7434 Link Image
Enzyme 21 Chromosome Location Not Available
Enzyme 21 Locus Not Available
Enzyme 21 SNPs SNPJam Report Link Image
Enzyme 21 General References
  1. 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 Link Image]
Enzyme 21 Metabolite References Not Available
Enzyme 22 [top]
Enzyme 22 ID 16499
Enzyme 22 Name Putative uncharacterized protein
Enzyme 22 Synonyms Not Available
Enzyme 22 Gene Name MTHFD1
Enzyme 22 Protein Sequence >Putative uncharacterized protein
MAPAEILNGKEISAQIRARLKNQVTQLKEQVPGFTPRLAILQVGNRDDSNLYINVKLKAA
EEIGIKATHIKLPRTTTESEVMKYITSLNEDSTVHGFLVQLPLDSENSINTEEVINAIAP
EKDVDGLTSINAGRLARGDLNDCFIPCTPKGCLELIKETGVPIAGRHAVVVGRSKIVGAP
MHDLLLWNNATVTTCHSKTAHLDEEVNKGDILVVATGQPEMVKGEWIKPGAIVIDCGINY
VPDDKKPNGRKVVGDVAYDEAKERASFITPVPGGVGPMTVAMLMQSTVESAKRFLEKFKP
GKWMIQYNNLNLKTPVPSDIDISRSCKPKPIGKLAREIGLLSEEVELYGETKAKVLLSAL
ERLKHRPDGKYVVVTGITPTPLGEGKSTTTIGLVQALGAHLYQNVFACVRQPSQGPTFGI
KGGAAGGGYSQVIPMEEFNLHLTGDIHAITAANNLVAAAIDARIFHELTQTDKALFNRLV
PSVNGVRRFSDIQIRRLKRLGIEKTDPTTLTDEEINRFARLDIDPETITWQRVLDTNDRF
LRKITIGQAPTEKGHTRTAQFDISVASEIMAVLALTTSLEDMRERLGKMVVASSKKGEPV
SAEDLGVSGALTVLMKDAIKPNLMQTLEGTPVFVHAGPFANIAHGNSSIIADQIALKLVG
PEGFVVTEAGFGADIGMEKFFNIKCRYSGLCPHVVVLVATVRALKMHGGGPTVTAGLPLP
KAYIQENLELVEKGFSNLKKQIENARMFGIPVVVAVNAFKTDTESELDLISRLSREHGAF
DAVKCTHWAEGGKGALALAQAVQRAAQAPSSFQLLYDLKLPVEDKIRIIAQKIYGADDIE
LLPEAQHKAEVYTKQGFGNLPICMAKTHLSLSHNPEQKGVPTGFILPIRDIRASVGAGFL
YPLVGTMSTMPGLPTRPCFYDIDLDPETEQVNGLF
Enzyme 22 Number of Residues 935
Enzyme 22 Molecular Weight 101532
Enzyme 22 Theoretical pI 7.19
Enzyme 22 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • binding
  • catalytic activity
  • formate-tetrahydrofolate ligase activity
  • ligase activity
  • ligase activity, forming carbon-nitrogen bonds
  • nucleotide binding
  • purine nucleotide binding
Process
  • aromatic compound metabolism
  • cellular metabolism
  • folic acid and derivative biosynthesis
  • folic acid and derivative metabolism
  • metabolism
  • physiological process
Component
Enzyme 22 General Function Nucleotide transport and metabolism
Enzyme 22 Specific Function Not Available
Enzyme 22 Pathways Not Available
Enzyme 22 Reactions Not Available
Enzyme 22 Pfam Domain Function
Enzyme 22 Signals
  • None
Enzyme 22 Transmembrane Regions
  • None
Enzyme 22 Essentiality Not Available
Enzyme 22 GenBank ID Protein Not Available
Enzyme 22 UniProtKB/Swiss-Prot ID B2R5Y2 Link Image
Enzyme 22 UniProtKB/Swiss-Prot Entry Name B2R5Y2_HUMAN Link Image
Enzyme 22 PDB ID 1DIA Link Image
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 Link Image
Enzyme 22 GeneCard ID B2R5Y2 Link Image
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 Link Image
Enzyme 22 General References Not Available
Enzyme 22 Metabolite References Not Available