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Human Metabolome Database Version 2.5

 

Showing metabocard for 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate (HMDB06273)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2007-05-22 21:52:31
Update Date 2009-05-05 21:00:47
Accession Number HMDB06273
Secondary Accession Numbers Not Available
Common Name 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate
Description 5-amino-1-(5-phospho-D-ribosyl) imidazole-4-carboxylate is an intermediate in purine metabolism. 5-amino-1-(5-phospho-D-ribosyl) imidazole-4-carboxylate is converted from aminoimidazole ribotide via phosphoribosylaminoimidazole carboxylase [EC: 4.1.1.21].
Synonyms
  1. 1-(5'-Phosphoribosyl)-4-carboxy-5-aminoimidazole
  2. 1-(5'-Phosphoribosyl)-5-amino-4-carboxyimidazole
  3. 1-(5'-Phosphoribosyl)-5-amino-4-imidazolecarboxylate
  4. 1-(5-Phospho-D-ribosyl)-5-amino-4-imidazolecarboxylate
  5. 4-Carboxy-5-aminoimidazole ribonucleotide
  6. 5'-Phosphoribosyl-4-carboxy-5-aminoimidazole
  7. 5'-Phosphoribosyl-5-amino-4-imidazolecarboxylate
  8. 5'Phosphoribosyl-4-carboxy-5-aminoimidazole
  9. 5-Amino-4-imidazolecarboxylic acid ribonucleotide
  10. 5-Aminoimidazole carboxilic acid ribonucleotice
  11. 5-Aminoimidazole-4-carboxilic acid ribonucleotide
  12. 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylic acid
  13. 5-amino-4-carboxyimidazole ribonucleotide
  14. Carboxyaminoimidazole ribonucleotide
Chemical IUPAC Name 5-amino-1-[(2R,3R,4S,5R)-3,4-dihydroxy-5-(phosphonooxymethyl)oxolan-2-yl]imidazole-4-carboxylic acid
Chemical Formula C9H14N3O9P
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Nucleosides and Nucleoside conjugates
Class
  • Nucleotides
Sub Class
  • Nucleotide monophosphates
Family
  • Mammalian Metabolite
Species
  • secondary alcohol
  • 1,2-diol
  • primary amine
  • primary aromatic amine
  • carboxylic acid
  • phosphoric acid ester
  • aromatic compound
  • heterocyclic compound
Biofunction
—
Application
—
Source
  • Endogenous
Average Molecular Weight 339.196
Monoisotopic Molecular Weight 339.046753
Isomeric SMILES NC1=C(N=CN1[C@@H]1O[C@H](COP(O)(O)=O)[C@@H](O)[C@H]1O)C(O)=O
Canonical SMILES NC1=C(N=CN1C1OC(COP(O)(O)=O)C(O)C1O)C(O)=O
KEGG Compound ID C04751 Link Image
BioCyc ID PHOSPHORIBOSYL-CARBOXY-AMINOIMIDAZOLE Link Image
BiGG ID 44477 Link Image
Wikipedia Link Not Available
NuGOwiki Link HMDB06273 Link Image
Metagene Link HMDB06273 Link Image
METLIN ID Not Available
PubChem Compound 165388 Link Image
PubChem Substance 10255898 Link Image
ChEBI ID 28413 Link Image
CAS Registry Number Not Available
InChI Identifier InChI=1/C9H14N3O9P/c10-7-4(9(15)16)11-2-12(7)8-6(14)5(13)3(21-8)1-20-22(17,18)19/h2-3,5-6,8,13-14H,1,10H2,(H,15,16)(H2,17,18,19)/t3-,5-,6-,8-/m1/s1
Synthesis Reference Not Available
Melting Point (Experimental) Not Available
Experimental Water Solubility Not Available Source: PhysProp
Predicted Water Solubility 2.81 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge -3
State Solid
Experimental LogP/Hydrophobicity Not Available Source: PhysProp
Predicted LogP/Hydrophobicity -2.05 [Predicted by ALOGPS]; -4.7 [Predicted by PubChem via XLOGP] Calculated using ALOGPS
Material Safety Data Sheet (MSDS) Not Available
MOL File Show Link Image
SDF File Show Link Image
PDB File Show Link Image
2D Structure
3D Structure
Experimental PDB ID Not Available
Experimental 1H NMR Spectrum Not Available
Experimental 13C NMR Spectrum Not Available
Experimental 13C HSQC Spectrum Not Available
Predicted 1H NMR Spectrum Show Image
Show Peaklist
Predicted 13C NMR Spectrum Show Image
Show Peaklist
Mass Spectrum Not Available
Simplified TOCSY Spectrum Not Available
BMRB Spectrum Not Available
Cellular Location
  • Cytoplasm
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
Purine Metabolism SMP00050 Link Image map00230 Link Image
General References Not Available
Metabolic Enzymes
  1. Multifunctional protein ADE2
Enzyme 1 [top]
Enzyme 1 ID 6176
Enzyme 1 Name Multifunctional protein ADE2
Enzyme 1 Synonyms
  1. Phosphoribosylaminoimidazole-succinocarboxamide synthase
  2. SAICAR synthetase
  3. Phosphoribosylaminoimidazole carboxylase
  4. AIR carboxylase
  5. AIRC
Enzyme 1 Gene Name PAICS
Enzyme 1 Protein Sequence >Multifunctional protein ADE2 
MATAEVLNIGKKLYEGKTKEVYELLDSPGKVLLQSKDQITAGNAARKNHLEGKAAISNKI
TSCIFQLLQEAGIKTAFTRKCGETAFIAPQCEMIPIEWVCRRIATGSFLKRNPGVKEGYK
FYPPKVELFFKDDANNDPQWSEEQLIAAKFCFAGLLIGQTEVDIMSHATQAIFEILEKSW
LPQNCTLVDMKIEFGVDVTTKEIVLADVIDNDSWRLWPSGDRSQQKDKQSYRDLKEVTPE
GLQMVKKNFEWVAERVELLLKSESQCRVVVLMGSTSDLGHCEKIKKACGNFGIPCELRVT
SAHKGPDETLRIKAEYEGDGIPTVFVAVAGRSNGLGPVMSGNTAYPVISCPPLTPDWGVQ
DVWSSLRLPSGLGCSTVLSPEGSAQFAAQIFGLSNHLVWSKLRASILNTWISLKQADKKI
RECNL
Enzyme 1 Number of Residues 425
Enzyme 1 Molecular Weight 47078.8
Enzyme 1 Theoretical pI 7.26
Enzyme 1 GO Classification
Function
  • ATP binding
  • acid-amino acid ligase activity
  • adenyl nucleotide binding
  • adenyl ribonucleotide binding
  • binding
  • carbon-carbon lyase activity
  • carboxy-lyase activity
  • catalytic activity
  • ligase activity
  • ligase activity, forming carbon-nitrogen bonds
  • lyase activity
  • nucleoside binding
  • phosphoribosylaminoimidazole carboxylase activity
  • phosphoribosylaminoimidazolesuccinocarboxamide synthase activity
  • purine nucleoside binding
Process
  • 'de novo' IMP biosynthetic process
  • IMP biosynthetic process
  • cellular nitrogen compound metabolic process
  • metabolic process
  • nitrogen compound metabolic process
  • nucleobase, nucleoside and nucleotide metabolic process
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
  • nucleoside phosphate metabolic process
  • nucleotide metabolic process
  • purine nucleoside monophosphate biosynthetic process
  • purine nucleotide biosynthetic process
  • purine nucleotide metabolic process
  • purine ribonucleoside monophosphate biosynthetic process
Component
—
Enzyme 1 General Function Involved in phosphoribosylaminoimidazole carboxylase activity
Enzyme 1 Specific Function ATP + 5-amino-1-(5-phospho-D- ribosyl)imidazole-4-carboxylate + L-aspartate = ADP + phosphate + (S)-2-(5-amino-1-(5-phospho-D-ribosyl)imidazole-4- carboxamido)succinate
Enzyme 1 Pathways
Enzyme 1 Reactions
  • ATP + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate + L-aspartate = ADP + phosphate + (S)-2-[5-amino-1-(5-phospho-D-ribosyl)imidazole-4- carboxamido]succinate [RN:R04591]
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • None
Enzyme 1 Transmembrane Regions
  • None
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 28384 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID P22234 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name PUR6_HUMAN Link Image
Enzyme 1 PDB ID Not Available
Enzyme 1 Cellular Location Not Available
Enzyme 1 Gene Sequence >1278 bp 
ATGGCGACAGCTGAGGTACTGAACATTGGTAAAAAATTATATGAGGGTAAAACAAAAGAA
GTCTACGAATTGTTAGACAGTCCAGGAAAAGTCCTCCTGCAGTCCAAGGACCAGATTACA
GCAGGAAATGCAGCTAGAAAAAACCACCTGGAAGGAAAAGCTGCAATCTCAAATAAAATC
ACCAGTTGTATTTTTCAGTTATTACAGGAAGCAGGTATTAAAACTGCCTTCACCAGAAAA
TGTGGGGAGACAGCTTTCATTGCACCGCAGTGTGAAATGATTCCAATTGAATGGGTTTGC
AGAAGAATAGCAACTGGTTCTTTTCTCAAAAGAAATCCTGGTGTCAAGGAAGGATATAAG
TTTTACCCACCTAAAGTGGAGTTGTTTTTCAAGGATGATGCCAATAATGACCCACAGTGG
TCTGAGGAACAGCTGATTGCTGCAAAATTTTGCTTTGCTGGACTTCTTATAGGCCAGACT
GAAGTGGATATCATGAGTCATGCTACACAGGCTATATTTGAAATACTGGAGAAATCCTGG
TTGCCCCAGAATTGTACACTGGTTGATATGAAGATTGAATTTGGTGTTGATGTAACCACC
AAAGAAATTGTTCTTGCTGATGTTATTGACAATGATTCCTGGAGACTCTGGCCATCAGGA
GATCGAAGCCAACAGAAAGACAAACAGTCTTATCGGGACCTCAAAGAAGTAACTCCTGAA
GGGCTCCAAATGGTAAAGAAAAACTTTGAGTGGGTTGCAGAGAGAGTAGAGTTGCTTTTG
AAATCAGAAAGTCAGTGCAGGGTTGTAGTGTTGATGGGCTCTACTTCTGATCTTGGTCAC
TGTGAAAAAATCAAGAAGGCCTGTGGAAATTTTGGCATTCCATGTGAACTTCGAGTAACA
TCTGCGCATAAAGGACCAGATGAAACTCTGAGGATTAAAGCTGAGTATGAAGGGGATGGC
ATTCCTACTGTATTTGTGGCAGTGGCAGGCAGAAGTAATGGTTTGGGACCAGTGATGTCT
GGGAACACTGCATATCCAGTTATCAGCTGTCCTCCCCTCACACCAGACTGGGGAGTTCAG
GATGTGTGGTCTTCTCTTCGACTACCCAGTGGTCTTGGCTGTTCAACCGTACTTTCTCCA
GAAGGATCAGCTCAATTTGCTGCTCAGATATTTGGGTTAAGCAACCATTTGGTATGGAGC
AAACTGCGAGCAAGCATTTTGAACACATGGATTTCCTTGAAGCAGGCTGACAAGAAAATC
AGAGAATGTAATTTATAA
Enzyme 1 GenBank Gene ID X53793 Link Image
Enzyme 1 GeneCard ID PAICS Link Image
Enzyme 1 GenAtlas ID PAICS Link Image
Enzyme 1 HGNC ID HGNC:8587 Link Image
Enzyme 1 Chromosome Location 4
Enzyme 1 Locus 4q12
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 General References
  1. Minet M, Lacroute F: Cloning and sequencing of a human cDNA coding for a multifunctional polypeptide of the purine pathway by complementation of the ade2-101 mutant in Saccharomyces cerevisiae. Curr Genet. 1990 Nov;18(4):287-91. [PubMed Link Image]
  2. 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]
  3. Beausoleil SA, Villen J, Gerber SA, Rush J, Gygi SP: A probability-based approach for high-throughput protein phosphorylation analysis and site localization. Nat Biotechnol. 2006 Oct;24(10):1285-92. Epub 2006 Sep 10. [PubMed Link Image]
  4. Yu LR, Zhu Z, Chan KC, Issaq HJ, Dimitrov DS, Veenstra TD: Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra. J Proteome Res. 2007 Nov;6(11):4150-62. Epub 2007 Oct 9. [PubMed Link Image]
  5. Daub H, Olsen JV, Bairlein M, Gnad F, Oppermann FS, Korner R, Greff Z, Keri G, Stemmann O, Mann M: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. Mol Cell. 2008 Aug 8;31(3):438-48. [PubMed Link Image]
  6. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed Link Image]
  7. 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]
  8. Oppermann FS, Gnad F, Olsen JV, Hornberger R, Greff Z, Keri G, Mann M, Daub H: Large-scale proteomics analysis of the human kinome. Mol Cell Proteomics. 2009 Jul;8(7):1751-64. Epub 2009 Apr 15. [PubMed Link Image]
  9. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed Link Image]
  10. 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]
  11. Li SX, Tong YP, Xie XC, Wang QH, Zhou HN, Han Y, Zhang ZY, Gao W, Li SG, Zhang XC, Bi RC: Octameric structure of the human bifunctional enzyme PAICS in purine biosynthesis. J Mol Biol. 2007 Mar 9;366(5):1603-14. Epub 2006 Dec 16. [PubMed Link Image]
Enzyme 1 Metabolite References Not Available