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Human Metabolome Database Version 2.5

 

Showing metabocard for 5-Phosphoribosylamine (HMDB01128)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2005-11-16 15:48:42
Update Date 2009-08-18 12:45:12
Accession Number HMDB01128
Secondary Accession Numbers HMDB02347
Common Name 5-Phosphoribosylamine
Description 5-Phosphoribosylamine is a substrate for Amidophosphoribosyltransferase and Trifunctional purine biosynthetic protein adenosine-3.
Synonyms
  1. 5-P-beta-D-ribosyl-amine
  2. 5-phospho-beta-D-ribosyl-amine
  3. 5-phosphoribosylamine
  4. PRA
  5. 5-P-beta-delta-ribosyl-amine
  6. 5-phospho-beta-delta-ribosyl-amine
  7. 5-phospho-beta-D-ribosylamine
  8. 5-phospho-D-ribosylamine
  9. 5-phospho-beta-delta-ribosylamine
  10. 5-phospho-delta-ribosylamine
Chemical IUPAC Name (5-amino-3,4-dihydroxy-oxolan-2-yl)methoxyphosphonic acid
Chemical Formula C5H12NO7P
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Carbohydrates and Carbohydrate conjugates
Class
  • Sugar Phosphates
Sub Class
  • Monosaccharide phosphates
Family
  • Mammalian Metabolite
Species
  • hemiaminal
  • secondary alcohol
  • 1,2-diol
  • phosphoric acid ester
  • heterocyclic compound
Biofunction
—
Application
—
Source
  • Endogenous
Average Molecular Weight 229.125
Monoisotopic Molecular Weight 229.035141
Isomeric SMILES N[C@@H]1O[C@H](COP(O)(O)=O)[C@@H](O)[C@H]1O
Canonical SMILES NC1OC(COP(O)(O)=O)C(O)C1O
KEGG Compound ID C03090 Link Image
BioCyc ID 5-P-BETA-D-RIBOSYL-AMINE Link Image
BiGG ID 41182 Link Image
Wikipedia Link 5-phosphoribosylamine Link Image
NuGOwiki Link HMDB01128 Link Image
Metagene Link HMDB01128 Link Image
METLIN ID 6023 Link Image
PubChem Compound 150 Link Image
PubChem Substance 7653282 Link Image
ChEBI ID 17284 Link Image
CAS Registry Number Not Available
InChI Identifier InChI=1/C5H12NO7P/c6-5-4(8)3(7)2(13-5)1-12-14(9,10)11/h2-5,7-8H,1,6H2,(H2,9,10,11)/t2-,3-,4-,5-/m1/s1
Synthesis Reference Not Available
Melting Point (Experimental) Not Available
Experimental Water Solubility Not Available Source: PhysProp
Predicted Water Solubility 38.2 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge -1
State Solid
Experimental LogP/Hydrophobicity Not Available Source: PhysProp
Predicted LogP/Hydrophobicity -2.39 [Predicted by ALOGPS]; -3.4 [Predicted by PubChem via XLOGP] Calculated using ALOGPS
Material Safety Data Sheet (MSDS) Not Available
MOL File Show Link Image
SDF File Show Link Image
PDB File Show Link Image
2D Structure
3D Structure
Experimental PDB ID Not Available
Experimental 1H NMR Spectrum Not Available
Experimental 13C NMR Spectrum Not Available
Experimental 13C HSQC Spectrum Not Available
Predicted 1H NMR Spectrum Show Image
Show Peaklist
Predicted 13C NMR Spectrum Show Image
Show Peaklist
Mass Spectrum Not Available
Simplified TOCSY Spectrum Not Available
BMRB Spectrum Not Available
Cellular Location Not Available
Biofluid Location Not Available
Tissue Location Not Available
Concentrations (Normal) Not Available
Concentrations (Abnormal) Not Available
Associated Disorders Not Available
OMIM ID Not Available
Pathways
Name SMPDB Link KEGG Link
Glutamate Metabolism SMP00072 Link Image map00250 Link Image
Purine Metabolism SMP00050 Link Image map00230 Link Image
General References
  1. Wikipedia Link Image
Metabolic Enzymes
  1. Trifunctional purine biosynthetic protein adenosine-3
  2. cDNA FLJ78616, highly similar to Homo sapiens phosphoribosylglycinamide formyltransferase, phosphoribosylglycinamide synthetase, phosphoribosylaminoimidazole synthetase
  3. Phosphoribosyl pyrophosphate amidotransferase, isoform CRA_b
Enzyme 1 [top]
Enzyme 1 ID 5566
Enzyme 1 Name Trifunctional purine biosynthetic protein adenosine-3
Enzyme 1 Synonyms
  1. Phosphoribosylamine--glycine ligase
  2. Glycinamide ribonucleotide synthetase
  3. GARS
  4. Phosphoribosylglycinamide synthetase
  5. Phosphoribosylformylglycinamidine cyclo-ligase
  6. AIR synthase
  7. AIRS
  8. Phosphoribosyl-aminoimidazole synthetase
  9. Phosphoribosylglycinamide formyltransferase
  10. 5'-phosphoribosylglycinamide transformylase
  11. GAR transformylase
  12. GART
Enzyme 1 Gene Name GART
Enzyme 1 Protein Sequence >Trifunctional purine biosynthetic protein adenosine-3 
MAARVLIIGSGGREHTLAWKLAQSHHVKQVLVAPGNAGTACSEKISNTAISISDHTALAQ
FCKEKKIEFVVVGPEAPLAAGIVGNLRSAGVQCFGPTAEAAQLESSKRFAKEFMDRHGIP
TAQWKAFTKPEEACSFILSADFPALVVKASGLAAGKGVIVAKSKEEACKAVQEIMQEKAF
GAAGETIVIEELLDGEEVSCLCFTDGKTVAPMPPAQDHKRLLEGDGGPNTGGMGAYCPAP
QVSNDLLLKIKDTVLQRTVDGMQQEGTPYTGILYAGIMLTKNGPKVLEFNCRFGDPECQV
ILPLLKSDLYEVIQSTLDGLLCTSLPVWLENHTALTVVMASKGYPGDYTKGVEITGFPEA
QALGLEVFHAGTALKNGKVVTHGGRVLAVTAIRENLISALEEAKKGLAAIKFEGAIYRKD
VGFRAIAFLQQPRSLTYKESGVDIAAGNMLVKKIQPLAKATSRSGCKVDLGGFAGLFDLK
AAGFKDPLLASGTDGVGTKLKIAQLCNKHDTIGQDLVAMCVNDILAQGAEPLFFLDYFSC
GKLDLSVTEAVVAGIAKACGKAGCALLGGETAEMPDMYPPGEYDLAGFAVGAMERDQKLP
HLERITEGDVVVGIASSGLHSNGFSLVRKIVAKSSLQYSSPAPDGCGDQTLGDLLLTPTR
IYSHSLLPVLRSGHVKAFAHITGGGLLENIPRVLPEKLGVDLDAQTWRIPRVFSWLQQEG
HLSEEEMARTFNCGVGAVLVVSKEQTEQILRDIQQHKEEAWVIGSVVARAEGSPRVKVKN
LIESMQINGSVLKNGSLTNHFSFEKKKARVAVLISGTGSNLQALIDSTREPNSSAQIDIV
ISNKAAVAGLDKAERAGIPTRVINHKLYKNRVEFDSAIDLVLEEFSIDIVCLAGFMRILS
GPFVQKWNGKMLNIHPSLLPSFKGSNAHEQALETGVTVTGCTVHFVAEDVDAGQIILQEA
VPVKRGDTVATLSERVKLAEHKIFPAALQLVASGTVQLGENGKICWVKEE
Enzyme 1 Number of Residues 1010
Enzyme 1 Molecular Weight 107766.3
Enzyme 1 Theoretical pI 6.68
Enzyme 1 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • adenyl ribonucleotide binding
  • binding
  • catalytic activity
  • cyclo-ligase activity
  • glycine hydroxymethyltransferase activity
  • hydroxymethyl-, formyl- and related transferase activity
  • ligase activity
  • ligase activity, forming carbon-nitrogen bonds
  • methyltransferase activity
  • nucleoside binding
  • phosphoribosylamine-glycine ligase activity
  • phosphoribosylformylglycinamidine cyclo-ligase activity
  • phosphoribosylglycinamide formyltransferase activity
  • purine nucleoside binding
  • transferase activity
  • transferase activity, transferring one-carbon groups
Process
  • 'de novo' IMP biosynthetic process
  • IMP biosynthetic process
  • biosynthetic process
  • cellular aromatic compound metabolic process
  • cellular metabolic process
  • cellular nitrogen compound metabolic process
  • metabolic process
  • nitrogen compound metabolic process
  • nucleobase metabolic process
  • nucleobase, nucleoside and nucleotide metabolic process
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
  • nucleoside phosphate metabolic process
  • nucleotide metabolic process
  • purine base biosynthetic process
  • purine base metabolic process
  • purine nucleoside monophosphate biosynthetic process
  • purine nucleotide biosynthetic process
  • purine nucleotide metabolic process
  • purine ribonucleoside monophosphate biosynthetic process
Component
  • cell part
  • cytoplasm
  • intracellular part
Enzyme 1 General Function Involved in catalytic activity
Enzyme 1 Specific Function ATP + 5-phospho-D-ribosylamine + glycine = ADP + phosphate + N(1)-(5-phospho-D-ribosyl)glycinamide
Enzyme 1 Pathways
Enzyme 1 Reactions
  • ATP + 5-phospho-D-ribosylamine + glycine = ADP + phosphate + N1-(5-phospho-D-ribosyl)glycinamide [RN:R04144]
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • None
Enzyme 1 Transmembrane Regions
  • None
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 31642 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID P22102 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name PUR2_HUMAN Link Image
Enzyme 1 PDB ID Not Available
Enzyme 1 Cellular Location Not Available
Enzyme 1 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 1 GenBank Gene ID X54199 Link Image
Enzyme 1 GeneCard ID GART Link Image
Enzyme 1 GenAtlas ID GART Link Image
Enzyme 1 HGNC ID HGNC:4163 Link Image
Enzyme 1 Chromosome Location 2
Enzyme 1 Locus 21q22.1|21q22.11
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 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. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. 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]
  5. 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]
  6. Rush J, Moritz A, Lee KA, Guo A, Goss VL, Spek EJ, Zhang H, Zha XM, Polakiewicz RD, Comb MJ: Immunoaffinity profiling of tyrosine phosphorylation in cancer cells. Nat Biotechnol. 2005 Jan;23(1):94-101. Epub 2004 Dec 12. [PubMed Link Image]
  7. Rikova K, Guo A, Zeng Q, Possemato A, Yu J, Haack H, Nardone J, Lee K, Reeves C, Li Y, Hu Y, Tan Z, Stokes M, Sullivan L, Mitchell J, Wetzel R, Macneill J, Ren JM, Yuan J, Bakalarski CE, Villen J, Kornhauser JM, Smith B, Li D, Zhou X, Gygi SP, Gu TL, Polakiewicz RD, Rush J, Comb MJ: Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer. Cell. 2007 Dec 14;131(6):1190-203. [PubMed Link Image]
  8. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed Link Image]
  9. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
  10. Zhang Y, Desharnais J, Greasley SE, Beardsley GP, Boger DL, Wilson IA: Crystal structures of human GAR Tfase at low and high pH and with substrate beta-GAR. Biochemistry. 2002 Dec 3;41(48):14206-15. [PubMed Link Image]
  11. Zhang Y, Desharnais J, Marsilje TH, Li C, Hedrick MP, Gooljarsingh LT, Tavassoli A, Benkovic SJ, Olson AJ, Boger DL, Wilson IA: Rational design, synthesis, evaluation, and crystal structure of a potent inhibitor of human GAR Tfase: 10-(trifluoroacetyl)-5,10-dideazaacyclic-5,6,7,8-tetrahydrofolic acid. Biochemistry. 2003 May 27;42(20):6043-56. [PubMed Link Image]
  12. Dahms TE, Sainz G, Giroux EL, Caperelli CA, Smith JL: The apo and ternary complex structures of a chemotherapeutic target: human glycinamide ribonucleotide transformylase. Biochemistry. 2005 Jul 26;44(29):9841-50. [PubMed Link Image]
Enzyme 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 13032
Enzyme 2 Name cDNA FLJ78616, highly similar to Homo sapiens phosphoribosylglycinamide formyltransferase, phosphoribosylglycinamide synthetase, phosphoribosylaminoimidazole synthetase
Enzyme 2 Synonyms
  1. GART, transcript variant 1, mRNA
  2. Phosphoribosylglycinamide formyltransferase, phosphoribosylglycinamide synthetase, phosphoribosylaminoimidazole synthetase, isoform CRA_b
Enzyme 2 Gene Name GART
Enzyme 2 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 2 Number of Residues 1010
Enzyme 2 Molecular Weight 107768
Enzyme 2 Theoretical pI 6.68
Enzyme 2 GO Classification Not Available
Enzyme 2 General Function Nucleotide transport and metabolism
Enzyme 2 Specific Function Not Available
Enzyme 2 Pathways Not Available
Enzyme 2 Reactions Not Available
Enzyme 2 Pfam Domain Function Not Available
Enzyme 2 Signals
  • None
Enzyme 2 Transmembrane Regions
  • None
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein 158259255 Link Image
Enzyme 2 UniProtKB/Swiss-Prot ID A8KA32 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name A8KA32_HUMAN Link Image
Enzyme 2 PDB ID Not Available
Enzyme 2 Cellular Location Not Available
Enzyme 2 Gene Sequence Not Available
Enzyme 2 GenBank Gene ID AK292897 Link Image
Enzyme 2 GeneCard ID A8KA32 Link Image
Enzyme 2 GenAtlas ID Not Available
Enzyme 2 HGNC ID Not Available
Enzyme 2 Chromosome Location Not Available
Enzyme 2 Locus Not Available
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 General References Not Available
Enzyme 2 Metabolite References Not Available
Enzyme 3 [top]
Enzyme 3 ID 13038
Enzyme 3 Name Phosphoribosyl pyrophosphate amidotransferase, isoform CRA_b
Enzyme 3 Synonyms
  1. SubName: cDNA FLJ78123, highly similar to Homo sapiens phosphoribosyl pyrophosphate amidotransferase (PPAT), mRNA
  2. SubName: cDNA, FLJ92602, highly similar to Homo sapiens phosphoribosyl pyrophosphate amidotransferase (PPAT), mRNA
Enzyme 3 Gene Name PPAT
Enzyme 3 Protein Sequence >Phosphoribosyl pyrophosphate amidotransferase, isoform CRA_b 
MELEELGIREECGVFGCIASGEWPTQLDVPHVITLGLVGLQHRGQESAGIVTSDGSSVPT
FKSHKGMGLVNHVFTEDNLKKLYVSNLGIGHTRYATTGKCELENCQPFVVETLHGKIAVA
HNGELVNAARLRKKLLRHGIGLSTSSDSEMITQLLAYTPPQEQDDTPDWVARIKNLMKEA
PTAYSLLIMHRDVIYAVRDPYGNRPLCIGRLIPVSDINDKEKKTSETEGWVVSSESCSFL
SIGARYYREVLPGEIVEISRHNVQTLDIISRSEGNPVAFCIFEYVYFARPDSMFEDQMVY
TVRYRCGQQLAIEAPVDADLVSTVPESATPAALAYAGKCGLPYVEVLCKNRYVGRTFIQP
NMRLRQLGVAKKFGVLSDNFKGKRIVLVDDSIVRGNTISPIIKLLKESGAKEVHIRVASP
PIKYPCFMGINIPTKEELIANKPEFDHLAEYLGANSVVYLSVEGLVSSVQEGIKFKKQKE
KKHDIMIQENGNGLECFEKSGHCTACLTGKYPVELEW
Enzyme 3 Number of Residues 517
Enzyme 3 Molecular Weight 57398.5
Enzyme 3 Theoretical pI 6.74
Enzyme 3 GO Classification
Function
  • amidophosphoribosyltransferase activity
  • catalytic activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
  • transferase activity, transferring pentosyl groups
Process
  • cellular aromatic compound metabolic process
  • cellular metabolic process
  • cellular nitrogen compound metabolic process
  • metabolic process
  • nitrogen compound metabolic process
  • nucleobase metabolic process
  • nucleobase, nucleoside and nucleotide metabolic process
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
  • nucleoside metabolic process
  • purine base biosynthetic process
  • purine base metabolic process
Component
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Enzyme 3 General Function Involved in amidophosphoribosyltransferase activity
Enzyme 3 Specific Function Not Available
Enzyme 3 Pathways Not Available
Enzyme 3 Reactions Not Available
Enzyme 3 Pfam Domain Function
Enzyme 3 Signals
  • None
Enzyme 3 Transmembrane Regions
  • None
Enzyme 3 Essentiality Not Available
Enzyme 3 GenBank ID Protein 158255320 Link Image
Enzyme 3 UniProtKB/Swiss-Prot ID A8K4H7 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name A8K4H7_HUMAN Link Image
Enzyme 3 PDB ID Not Available
Enzyme 3 Cellular Location Not Available
Enzyme 3 Gene Sequence >1554 bp 
ATGGAGCTGGAGGAGTTGGGGATCCGAGAGGAATGTGGCGTGTTCGGGTGCATCGCCTCA
GGAGAGTGGCCCACGCAGCTGGATGTACCGCATGTGATCACTCTGGGACTCGTGGGGCTG
CAGCACCGGGGTCAGGAGAGTGCTGGTATTGTGACTAGTGATGGGAGTTCCGTGCCAACA
TTCAAATCACACAAGGGAATGGGTCTTGTAAATCACGTCTTTACTGAAGACAATTTGAAA
AAATTATATGTTTCAAATCTTGGAATTGGACACACCAGGTATGCCACCACAGGAAAATGT
GAACTAGAAAATTGTCAGCCCTTCGTTGTTGAAACACTTCATGGGAAGATAGCTGTGGCA
CATAATGGCGAATTGGTAAATGCTGCTCGATTAAGGAAAAAGCTTCTGCGTCATGGTATT
GGTCTGTCTACAAGTTCTGATAGTGAAATGATTACCCAGTTACTGGCGTATACCCCTCCT
CAGGAACAAGATGACACCCCAGACTGGGTAGCCAGGATTAAAAACTTGATGAAGGAAGCA
CCCACAGCATACTCCCTGCTTATAATGCACAGAGATGTTATTTATGCAGTACGAGATCCT
TATGGAAATCGTCCCTTATGCATTGGTCGTCTTATTCCAGTGTCTGATATAAATGACAAA
GAGAAAAAAACATCAGAAACAGAAGGATGGGTGGTGTCTTCAGAATCTTGTAGCTTCTTA
TCTATTGGTGCAAGATATTACCGTGAAGTCTTGCCTGGAGAAATTGTGGAAATATCCAGA
CACAATGTCCAAACTCTTGATATTATATCAAGGTCTGAAGGAAACCCAGTGGCTTTTTGT
ATCTTTGAATATGTTTATTTTGCAAGACCAGACAGTATGTTCGAAGACCAAATGGTTTAT
ACAGTAAGATACCGTTGTGGCCAGCAGCTAGCGATTGAAGCACCTGTGGATGCAGATTTG
GTTAGCACTGTTCCAGAATCTGCTACGCCTGCTGCTCTTGCTTACGCAGGAAAGTGTGGA
CTTCCATATGTGGAGGTGCTGTGTAAAAACCGGTATGTAGGGAGAACCTTCATTCAGCCA
AACATGAGGTTAAGACAACTTGGTGTTGCAAAAAAATTTGGAGTATTGTCAGACAACTTT
AAAGGCAAAAGAATTGTTCTTGTAGATGATTCAATTGTCAGAGGCAATACCATCTCACCT
ATAATAAAACTGCTCAAAGAATCTGGTGCAAAAGAGGTACACATTCGAGTAGCTTCACCA
CCAATTAAATATCCATGCTTCATGGGAATAAACATTCCTACAAAAGAAGAGCTCATTGCC
AATAAACCAGAATTTGATCACCTTGCAGAATATCTAGGAGCAAACAGTGTTGTGTATCTG
TCAGTAGAAGGACTGGTTTCATCTGTACAAGAAGGGATAAAGTTTAAAAAACAGAAAGAG
AAAAAGCACGATATTATGATCCAAGAAAATGGAAATGGTCTGGAATGTTTTGAAAAGAGT
GGTCATTGTACAGCTTGTCTCACTGGAAAATATCCTGTAGAATTAGAATGGTAG
Enzyme 3 GenBank Gene ID AK290942 Link Image
Enzyme 3 GeneCard ID PPAT Link Image
Enzyme 3 GenAtlas ID PPAT Link Image
Enzyme 3 HGNC ID HGNC:9238 Link Image
Enzyme 3 Chromosome Location 4
Enzyme 3 Locus 4q12
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 General References Not Available
Enzyme 3 Metabolite References Not Available