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Human Metabolome Database Version 2.5

 

Showing metabocard for Dihydrofolic acid (HMDB01056)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2005-11-16 15:48:42
Update Date 2009-06-19 23:10:41
Accession Number HMDB01056
Secondary Accession Numbers Not Available
Common Name Dihydrofolic acid
Description Dihydrofolic acid is a folic acid derivative acted upon by dihydrofolate reductase to produce tetrahydrofolic acid. It interacts with bacteria during cell division. It can be targeted with drug analogs to prevent nucleic acid synthesis. Dihydrofolic acid is also known by the name Dihydrofolate - more commonly Vitamin B9.
Synonyms
  1. 7,8-Dihydro-L-folic acid
  2. 7,8-dihydrofolate
  3. 7,8-Dihydrofolic acid
  4. 7,8-Dihydropteroylglutamate
  5. dihydrofolate
  6. H2PteGlu
  7. H2PteGlu1
  8. L-N-[p-[[(2-amino-7,8-dihydro-4-hydroxy-6-pteridinyl)methyl]amino]benzoyl]-Glutamic acid
  9. N-(4-(((2-amino-1,4,7,8-tetrahydro-4-oxo-6-pteridinyl)methyl)amino)benzoyl)-L-Glutamic acid
  10. N-(4-{[(2-amino-4-oxo-3,4,7,8-tetrahydropteridin-6-yl)methyl]amino}benzoyl)-L-glutamic acid
  11. N-(7,8-dihydropteroyl)-L-glutamic acid
  12. N-[4-[[(2-amino-1,4,7,8-tetrahydro-4-oxo-6-pteridinyl)methyl]amino]benzoyl]-L-Glutamic acid
  13. N-[4-[[(2-amino-3,4,7,8-tetrahydro-4-oxo-6-pteridinyl)methyl]amino]benzoyl]-L-Glutamic acid
Chemical IUPAC Name (2S)-2-[[4-[(2-amino-4-oxo-7,8-dihydro-1H-pteridin-6-yl)methylamino]benzoyl]amino]pentanedioic acid
Chemical Formula C19H21N7O6
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Heterocyclic molecules
Class
  • Pterins
Sub Class
  • Dihydro-pterins
Family
  • Mammalian Metabolite
Species
  • imine
  • primary amine
  • primary aromatic amine
  • secondary amine
  • secondary aliphatic/aromatic amine (alkylarylamine)
  • carboxylic acid
  • secondary carboxylic acid amide
  • oxo(het)arene
  • aromatic compound
  • heterocyclic compound
Biofunction
  • Component of Folate biosynthesis
  • Component of Pyrimidine metabolism
Application
—
Source
  • Endogenous
Average Molecular Weight 443.413
Monoisotopic Molecular Weight 443.155334
Isomeric SMILES NC1=NC2=C(N=C(CNC3=CC=C(C=C3)C(=O)N[C@@H](CCC(O)=O)C(O)=O)CN2)C(=O)N1
Canonical SMILES NC1=NC2=C(N=C(CNC3=CC=C(C=C3)C(=O)NC(CCC(O)=O)C(O)=O)CN2)C(=O)N1
KEGG Compound ID C00415 Link Image
BioCyc ID DIHYDROFOLATE Link Image
BiGG ID 34911 Link Image
Wikipedia Link Dihydrofolate Link Image
NuGOwiki Link HMDB01056 Link Image
Metagene Link HMDB01056 Link Image
METLIN ID 5970 Link Image
PubChem Compound 98792 Link Image
PubChem Substance 3705 Link Image
ChEBI ID 15633 Link Image
CAS Registry Number 4033-27-6
InChI Identifier InChI=1/C19H21N7O6/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/h1-4,12,21H,5-8H2,(H,24,29)(H,27,28)(H,31,32)(H4,20,22,25,26,30)/t12-/m0/s1
Synthesis Reference Smith, Karin; Scrimgeour, K. G.; Huennekens, F. M. Folic acid coenzymes and one-carbon metabolism. XV. Synthesis of a new form of dihydrofolate. Biochemical and Biophysical Research Communications (1963), 11(5), 388-92.
Melting Point (Experimental) Not Available
Experimental Water Solubility Not Available Source: PhysProp
Predicted Water Solubility 0.125 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge -2
State Solid
Experimental LogP/Hydrophobicity Not Available Source: PhysProp
Predicted LogP/Hydrophobicity -3.2 [Predicted by PubChem via XLOGP]; -1.61 [Predicted by ALOGPS] 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 Not Available
Experimental 13C NMR Spectrum Not Available
Experimental 13C HSQC Spectrum Not Available
Predicted 1H NMR Spectrum Show Image
Show Peaklist
Predicted 13C NMR Spectrum Show Image
Show Peaklist
Mass Spectrum Not Available
Simplified TOCSY Spectrum Not Available
BMRB Spectrum Not Available
Cellular Location
  • Cytoplasm (Predicted from LogP)
  • Extracellular
  • lysosome
  • mitochondria
Biofluid Location
  • Blood
Tissue Location
Tissue References
Liver —
Concentrations (Normal)
Biofluid Blood
Value 0.005 +/- 0.001 uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Hendel J: Radioimmunoassay for pteroylglutamic acid. Clin Chem. 1981 May;27(5):701-3. [PubMed Link Image]
Concentrations (Abnormal) Not Available
Associated Disorders Not Available
OMIM ID Not Available
Pathways
Name SMPDB Link KEGG Link
Folate Metabolism SMP00053 Link Image map00670 Link Image
Pterine Biosynthesis SMP00005 Link Image map00790 Link Image
General References
  1. Navarro-Peran E, Cabezas-Herrera J, Garcia-Canovas F, Durrant MC, Thorneley RN, Rodriguez-Lopez JN: The antifolate activity of tea catechins. Cancer Res. 2005 Mar 15;65(6):2059-64. [PubMed Link Image]
  2. Wikipedia Link Image
Metabolic Enzymes
  1. Thymidylate synthase
  2. Dihydrofolate reductase
  3. Folylpolyglutamate synthase, mitochondrial precursor
  4. Folylpolyglutamate synthase
  5. Dihydrofolate reductase (cDNA, FLJ93028, Homo sapiens dihydrofolate reductase (DHFR), mRNA)
Enzyme 1 [top]
Enzyme 1 ID 5316
Enzyme 1 Name Thymidylate synthase
Enzyme 1 Synonyms
  1. TS
  2. TSase
Enzyme 1 Gene Name TYMS
Enzyme 1 Protein Sequence >Thymidylate synthase 
MPVAGSELPRRPLPPAAQERDAEPRPPHGELQYLGQIQHILRCGVRKDDRTGTGTLSVFG
MQARYSLRDEFPLLTTKRVFWKGVLEELLWFIKGSTNAKELSSKGVKIWDANGSRDFLDS
LGFSTREEGDLGPVYGFQWRHFGAEYRDMESDYSGQGVDQLQRVIDTIKTNPDDRRIIMC
AWNPRDLPLMALPPCHALCQFYVVNSELSCQLYQRSGDMGLGVPFNIASYALLTYMIAHI
TGLKPGDFIHTLGDAHIYLNHIEPLKIQLQREPRPFPKLRILRKVEKIDDFKAEDFQIEG
YNPHPTIKMEMAV
Enzyme 1 Number of Residues 313
Enzyme 1 Molecular Weight 35716
Enzyme 1 Theoretical pI 7.00
Enzyme 1 GO Classification
Function
  • 5,10-methylenetetrahydrofolate-dependent methyltransferase activity
  • catalytic activity
  • methyltransferase activity
  • thymidylate synthase activity
  • transferase activity
  • transferase activity, transferring one-carbon groups
Process
  • cellular metabolism
  • dTMP biosynthesis
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • nucleotide metabolism
  • physiological process
  • pyrimidine deoxyribonucleoside monophosphate biosynthesis
  • pyrimidine nucleoside monophosphate biosynthesis
  • pyrimidine nucleotide biosynthesis
  • pyrimidine nucleotide metabolism
Component
—
Enzyme 1 General Function Nucleotide transport and metabolism
Enzyme 1 Specific Function 5,10-methylenetetrahydrofolate + dUMP = dihydrofolate + dTMP
Enzyme 1 Pathways
Enzyme 1 Reactions
  • 5,10-methylenetetrahydrofolate + dUMP = dihydrofolate + dTMP
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • None
Enzyme 1 Transmembrane Regions
  • None
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 37479 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID P04818 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name TYSY_HUMAN Link Image
Enzyme 1 PDB ID 1JUJ Link Image
Enzyme 1 PDB File Show
Enzyme 1 3D Structure
Enzyme 1 Cellular Location Not Available
Enzyme 1 Gene Sequence >942 bp 
ATGCCTGTGGCCGGCTCGGAGCTGCCGCGCCGGCCCTTGCCCCCCGCCGCACAGGAGCGG
GACGCCGAGCCGCGTCCGCCGCACGGGGAGCTGCAGTACCTGGGGCAGATCCAACACATC
CTCCGCTGCGGCGTCAGGAAGGACGACCGCACGGGCACCGGCACCCTGTCGGTATTCGGC
ATGCAGGCGCGCTACAGCCTGAGAGATGAATTCCCTCTGCTGACAACCAAACGTGTGTTC
TGGAAGGGTGTTTTGGAGGAGTTGCTGTGGTTTATCAAGGGATCCACAAATGCTAAAGAG
CTGTCTTCCAAGGGAGTGAAAATCTGGGATGCCAATGGATCCCGAGACTTTTTGGACAGC
CTGGGATTCTCCACCAGAGAAGAAGGGGACTTGGGCCCAGTTTATGGCTTCCAGTGGAGG
CATTTTGGGGCAGAATACAGAGATATGGAATCAGATTATTCAGGACAGGGAGTTGACCAA
CTGCAAAGAGTGATTGACACCATCAAAACCAACCCTGACGACAGAAGAATCATCATGTGC
GCTTGGAATCCAAGAGATCTTCCTCTGATGGCGCTGCCTCCATGCCATGCCCTCTGCCAG
TTCTATGTGGTGAACAGTGAGCTGTCCTGCCAGCTGTACCAGAGATCGGGAGACATGGGC
CTCGGTGTGCCTTTCAACATCGCCAGCTACGCCCTGCTCACGTACATGATTGCGCACATC
ACGGGCCTGAAGCCAGGTGACTTTATACACACTTTGGGAGATGCACATATTTACCTGAAT
CACATCGAGCCACTGAAAATTCAGCTTCAGCGAGAACCCAGACCTTTCCCAAAGCTCAGG
ATTCTTCGAAAAGTTGAGAAAATTGATGACTTCAAAGCTGAAGACTTTCAGATTGAAGGG
TACAATCCGCATCCAACTATTAAAATGGAAATGGCTGTTTAG
Enzyme 1 GenBank Gene ID X02308 Link Image
Enzyme 1 GeneCard ID TYMS Link Image
Enzyme 1 GenAtlas ID TYMS Link Image
Enzyme 1 HGNC ID HGNC:12441 Link Image
Enzyme 1 Chromosome Location 18
Enzyme 1 Locus 18p11.32
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 General References
  1. Takeishi K, Kaneda S, Ayusawa D, Shimizu K, Gotoh O, Seno T: Nucleotide sequence of a functional cDNA for human thymidylate synthase. Nucleic Acids Res. 1985 Mar 25;13(6):2035-43. [PubMed Link Image]
  2. Kaneda S, Nalbantoglu J, Takeishi K, Shimizu K, Gotoh O, Seno T, Ayusawa D: Structural and functional analysis of the human thymidylate synthase gene. J Biol Chem. 1990 Nov 25;265(33):20277-84. [PubMed Link Image]
  3. Takeishi K, Kaneda S, Ayusawa D, Shimizu K, Gotoh O, Seno T: Human thymidylate synthase gene: isolation of phage clones which cover a functionally active gene and structural analysis of the region upstream from the translation initiation codon. J Biochem (Tokyo). 1989 Oct;106(4):575-83. [PubMed Link Image]
  4. Shimizu K, Ayusawa D, Takeishi K, Seno T: Purification and NH2-terminal amino acid sequence of human thymidylate synthase in an overproducing transformant of mouse FM3A cells. J Biochem (Tokyo). 1985 Mar;97(3):845-50. [PubMed Link Image]
  5. Davisson VJ, Sirawaraporn W, Santi DV: Expression of human thymidylate synthase in Escherichia coli. J Biol Chem. 1989 Jun 5;264(16):9145-8. [PubMed Link Image]
  6. Schiffer CA, Clifton IJ, Davisson VJ, Santi DV, Stroud RM: Crystal structure of human thymidylate synthase: a structural mechanism for guiding substrates into the active site. Biochemistry. 1995 Dec 19;34(50):16279-87. [PubMed Link Image]
  7. Phan J, Koli S, Minor W, Dunlap RB, Berger SH, Lebioda L: Human thymidylate synthase is in the closed conformation when complexed with dUMP and raltitrexed, an antifolate drug. Biochemistry. 2001 Feb 20;40(7):1897-902. [PubMed Link Image]
  8. Phan J, Steadman DJ, Koli S, Ding WC, Minor W, Dunlap RB, Berger SH, Lebioda L: Structure of human thymidylate synthase suggests advantages of chemotherapy with noncompetitive inhibitors. J Biol Chem. 2001 Apr 27;276(17):14170-7. Epub 2001 Jan 24. [PubMed Link Image]
Enzyme 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 6070
Enzyme 2 Name Dihydrofolate reductase
Enzyme 2 Synonyms Not Available
Enzyme 2 Gene Name DHFR
Enzyme 2 Protein Sequence >Dihydrofolate reductase 
MVGSLNCIVAVSQNMGIGKNGDLPWPPLRNEFRYFQRMTTTSSVEGKQNLVIMGKKTWFS
IPEKNRPLKGRINLVLSRELKEPPQGAHFLSRSLDDALKLTEQPELANKVDMVWIVGGSS
VYKEAMNHPGHLKLFVTRIMQDFESDTFFPEIDLEKYKLLPEYPGVLSDVQEEKGIKYKF
EVYEKND
Enzyme 2 Number of Residues 187
Enzyme 2 Molecular Weight 21453
Enzyme 2 Theoretical pI 7.60
Enzyme 2 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 2 General Function Coenzyme transport and metabolism
Enzyme 2 Specific Function 5,6,7,8-tetrahydrofolate + NADP(+) = 7,8- dihydrofolate + NADPH
Enzyme 2 Pathways
Enzyme 2 Reactions
  • 5,6,7,8-tetrahydrofolate + NADP+ = 7,8-dihydrofolate + 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 182724 Link Image
Enzyme 2 UniProtKB/Swiss-Prot ID P00374 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name DYR_HUMAN Link Image
Enzyme 2 PDB ID 1MVT Link Image
Enzyme 2 PDB File Show
Enzyme 2 3D Structure
Enzyme 2 Cellular Location Not Available
Enzyme 2 Gene Sequence >564 bp 
ATGGTTGGTTCGCTAAACTGCATCGTCGCTGTGTCCCAGAACATGGGCATCGGCAAGAAC
GGGGACCTGCCCTGGCCACCGCTCAGGAATGAATTCAGATATTTCCAGAGAATGACCACA
ACCTCTTCAGTAGAAGGTAAACAGAATCTGGTGATTATGGGTAAGAAGACCTGGTTCTCC
ATTCCTGAGAAGAATCGACCTTTAAAGGGTAGAATTAATTTAGTTCTCAGCAGAGAACTC
AAGGAACCTCCACAAGGAGCTCATTTTCTTTCCAGAAGTCTAGATGATGCCTTAAAACTT
ACTGAACAACCAGAATTAGCAAATAAAGTAGACATGGTCTGGATAGTTGGTGGCAGTTCT
GTTTATAAGGAAGCCATGAATCACCCAGGCCATCTTAAACTATTTGTGACAAGGATCATG
CAAGACTTTGAAAGTGACACGTTTTTTCCAGAAATTGATTTGGAGAAATATAAACTTCTG
CCAGAATACCCAGGTGTTCTCTCTGATGTCCAGGAGGAGAAAGGCATTAAGTACAAATTT
GAAGTATATGAGAAGAATGATTAA
Enzyme 2 GenBank Gene ID J00140 Link Image
Enzyme 2 GeneCard ID DHFR Link Image
Enzyme 2 GenAtlas ID DHFR Link Image
Enzyme 2 HGNC ID HGNC:2861 Link Image
Enzyme 2 Chromosome Location 5
Enzyme 2 Locus 5q11.2-q13.2
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 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 2 Metabolite References Not Available
Enzyme 3 [top]
Enzyme 3 ID 6130
Enzyme 3 Name Folylpolyglutamate synthase, mitochondrial precursor
Enzyme 3 Synonyms
  1. Folylpoly-gamma-glutamate synthetase
  2. FPGS
  3. Tetrahydrofolate synthase
  4. Tetrahydrofolylpolyglutamate synthase
Enzyme 3 Gene Name FPGS
Enzyme 3 Protein Sequence >Folylpolyglutamate synthase, mitochondrial precursor 
MSRARSHLRAALFLAAASARGITTQVAARRGLSAWPVPQEPSMEYQDAVRMLNTLQTNAG
YLEQVKRQRGDPQTQLEAMELYLARSGLQVEDLDRLNIIHVTGTKGKGSTCAFTECILRS
YGLKTGFFSSPHLVQVRERIRINGQPISPELFTKYFWRLYHRLEETKDGSCVSMPPYFRF
LTLMAFHVFLQEKVDLAVVEVGIGGAYDCTNIIRKPVVCGVSSLGIDHTSLLGDTVEKIA
WQKGGIFKQGVPAFTVLQPEGPLAVLRDRAQQISCPLYLCPMLEALEEGGPPLTLGLEGE
HQRSNAALALQLAHCWLQRQDRHGAGEPKASRPGLLWQLPLAPVFQPTSHMRLGLRNTEW
PGRTQVLRRGPLTWYLDGAHTASSAQACVRWFRQALQGRERPSGGPEVRVLLFNATGDRD
PAALLKLLQPCQFDYAVFCPNLTEVSSTGNADQQNFTVTLDQVLLRCLEHQQHWNHLDEE
QASPDLWSAPSPEPGGSASLLLAPHPPHTCSASSLVFSCISHALQWISQGRDPIFQPPSP
PKGLLTHPVAHSGASILREAAAIHVLVTGSLHLVGGVLKLLEPALSQ
Enzyme 3 Number of Residues 587
Enzyme 3 Molecular Weight 64610
Enzyme 3 Theoretical pI 8.00
Enzyme 3 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 3 General Function Coenzyme transport and metabolism
Enzyme 3 Specific Function Conversion of folates to polyglutamate derivatives. This allows tissues to concentrate folate at higher levels than in plasma
Enzyme 3 Pathways
Enzyme 3 Reactions
  • ATP + tetrahydrofolyl-[Glu]n + L-glutamate = ADP + phosphate + tetrahydrofolyl-[Glu]n+1
Enzyme 3 Pfam Domain Function
Enzyme 3 Signals
  • 1-19
Enzyme 3 Transmembrane Regions Not Available
Enzyme 3 Essentiality Not Available
Enzyme 3 GenBank ID Protein 292029 Link Image
Enzyme 3 UniProtKB/Swiss-Prot ID Q05932 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name FOLC_HUMAN Link Image
Enzyme 3 PDB ID Not Available
Enzyme 3 Cellular Location Not Available
Enzyme 3 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 3 GenBank Gene ID M98045 Link Image
Enzyme 3 GeneCard ID FPGS Link Image
Enzyme 3 GenAtlas ID FPGS Link Image
Enzyme 3 HGNC ID HGNC:3824 Link Image
Enzyme 3 Chromosome Location 9
Enzyme 3 Locus 9q34.1
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 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 3 Metabolite References Not Available
Enzyme 4 [top]
Enzyme 4 ID 13028
Enzyme 4 Name Folylpolyglutamate synthase
Enzyme 4 Synonyms Not Available
Enzyme 4 Gene Name FPGS
Enzyme 4 Protein Sequence >Folylpolyglutamate synthase 
MLNTLQTNAGYLEQVKRQRGDPQTQLEAMELYLARSGLQVEDLDRLNIIHVTGTKGKGST
CAFTECILRSYGLKTGFFSSPHLVQVRERIRINGQPISPELFTKYFWRLYHRLEETKDGS
CVSMPPYFRFLTLMAFHVFLQEKVDLAVVEVGIGGAYDCTNIIRKPVVCGVSSLGIDHTS
LLGDTVEKIAWQKGGIFKQGVPAFTVLQPEGPLAVLRDRAQQISCPLYLCPMLEALEEGG
PPLTLGLEGEHQRSNAALALQLAHCWLQRQDRHGAGEPKASRPGLLWQLPLAPVFQPTSH
MRLGLRNTEWPGRTQVLRRGPLTWYLDGAHTASSAQACVRWFRQALQGRERPSGGPEVRV
LLFNATGDRDPAALLKLLQPCQFDYAVFCPNLTEVSSTGNADQQNFTVTLDQVLLRCLEH
QQHWNHLDEEQASPDLWSAPSPEPGGSASLLLAPHPPHTCSASSLVFSCISHALQWISQG
RDPIFQPPSPPKGLLTHPVAHSGASILREAAAIHVLVTGSLHLVGGVLKLLEPALSQ
Enzyme 4 Number of Residues 537
Enzyme 4 Molecular Weight 59175
Enzyme 4 Theoretical pI 7.42
Enzyme 4 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 4 General Function Coenzyme transport and metabolism
Enzyme 4 Specific Function Not Available
Enzyme 4 Pathways Not Available
Enzyme 4 Reactions Not Available
Enzyme 4 Pfam Domain Function
Enzyme 4 Signals
  • None
Enzyme 4 Transmembrane Regions
  • None
Enzyme 4 Essentiality Not Available
Enzyme 4 GenBank ID Protein Not Available
Enzyme 4 UniProtKB/Swiss-Prot ID Q5JU19 Link Image
Enzyme 4 UniProtKB/Swiss-Prot Entry Name Q5JU19_HUMAN Link Image
Enzyme 4 PDB ID Not Available
Enzyme 4 Cellular Location Not Available
Enzyme 4 Gene Sequence Not Available
Enzyme 4 GenBank Gene ID AL162586 Link Image
Enzyme 4 GeneCard ID Q5JU19 Link Image
Enzyme 4 GenAtlas ID FPGS Link Image
Enzyme 4 HGNC ID HGNC:3824 Link Image
Enzyme 4 Chromosome Location Not Available
Enzyme 4 Locus Not Available
Enzyme 4 SNPs SNPJam Report Link Image
Enzyme 4 General References Not Available
Enzyme 4 Metabolite References Not Available
Enzyme 5 [top]
Enzyme 5 ID 13030
Enzyme 5 Name Dihydrofolate reductase (cDNA, FLJ93028, Homo sapiens dihydrofolate reductase (DHFR), mRNA)
Enzyme 5 Synonyms Not Available
Enzyme 5 Gene Name DYR
Enzyme 5 Protein Sequence >Dihydrofolate reductase (cDNA, FLJ93028, Homo sapiens dihydrofolate reductase (DHFR), mRNA) 
MVGSLNCIVAVSQNMGIGKNGDLPWPPLRNEFRYFQRMTTTSSVEGKQNLVIMGKKTWFS
IPEKNRPLKGRINLVLSRELKEPPQGAHFLSRSLDDALKLTEQPELANKVDMVWIVGGSS
VYKEAMNHPGHLKLFVTRIMQDFESDTFFPEIDLEKYKLLPEYPGVLSDVQEEKGIKYKF
EVYEKND
Enzyme 5 Number of Residues 187
Enzyme 5 Molecular Weight 21453
Enzyme 5 Theoretical pI Not Available
Enzyme 5 GO Classification Not Available
Enzyme 5 General Function Not Available
Enzyme 5 Specific Function Not Available
Enzyme 5 Pathways Not Available
Enzyme 5 Reactions Not Available
Enzyme 5 Pfam Domain Function
Enzyme 5 Signals
  • None
Enzyme 5 Transmembrane Regions
  • None
Enzyme 5 Essentiality Not Available
Enzyme 5 GenBank ID Protein Not Available
Enzyme 5 UniProtKB/Swiss-Prot ID B0YJ76 Link Image
Enzyme 5 UniProtKB/Swiss-Prot Entry Name B0YJ76_HUMAN Link Image
Enzyme 5 PDB ID Not Available
Enzyme 5 Cellular Location Not Available
Enzyme 5 Gene Sequence Not Available
Enzyme 5 GenBank Gene ID Not Available
Enzyme 5 GeneCard ID B0YJ76 Link Image
Enzyme 5 GenAtlas ID Not Available
Enzyme 5 HGNC ID Not Available
Enzyme 5 Chromosome Location Not Available
Enzyme 5 Locus Not Available
Enzyme 5 SNPs SNPJam Report Link Image
Enzyme 5 General References Not Available
Enzyme 5 Metabolite References Not Available