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Showing Protein Amidophosphoribosyltransferase (HMDBP00331)

IdentificationBiological propertiesGene propertiesProtein propertiesExternal linksReferencesXMLShow 7 metabolites
Identification
HMDB Protein ID HMDBP00331
Secondary Accession Numbers
  • 5567
  • HMDBP04853
Name Amidophosphoribosyltransferase
Synonyms
  1. ATase
  2. GPAT
  3. Glutamine phosphoribosylpyrophosphate amidotransferase
Gene Name PPAT
Protein Type Unknown
Biological Properties
General Function Involved in amidophosphoribosyltransferase activity
Specific Function Not Available
Pathways
  • 2-Hydroxyglutric Aciduria (D And L Form)
  • 4-Hydroxybutyric Aciduria/Succinic Semialdehyde Dehydrogenase Deficiency
  • Adenine phosphoribosyltransferase deficiency (APRT)
  • Adenosine Deaminase Deficiency
  • Adenylosuccinate Lyase Deficiency
  • AICA-Ribosiduria
  • Alanine, aspartate and glutamate metabolism
  • Azathioprine Action Pathway
  • Glutamate Metabolism
  • Gout or Kelley-Seegmiller Syndrome
  • Homocarnosinosis
  • Hyperinsulinism-Hyperammonemia Syndrome
  • IMP biosynthesis via de novo pathway
  • Lesch-Nyhan Syndrome (LNS)
  • Mercaptopurine Action Pathway
  • Mercaptopurine Metabolism Pathway
  • Mitochondrial DNA depletion syndrome
  • Molybdenum Cofactor Deficiency
  • Myoadenylate deaminase deficiency
  • Purine metabolism
  • Purine metabolism
  • Purine Nucleoside Phosphorylase Deficiency
  • Succinic semialdehyde dehydrogenase deficiency
  • Thioguanine Action Pathway
  • Xanthine Dehydrogenase Deficiency (Xanthinuria)
  • Xanthinuria type I
  • Xanthinuria type II
Reactions
5-Phosphoribosylamine + Pyrophosphate + L-Glutamic acid → L-Glutamine + Phosphoribosyl pyrophosphate + Water details
GO Classification
Biological Process
purine nucleobase metabolic process
glutamine metabolic process
organ regeneration
purine nucleotide biosynthetic process
cellular response to insulin stimulus
nucleoside metabolic process
'de novo' IMP biosynthetic process
protein homotetramerization
purine nucleobase biosynthetic process
lactation
maternal process involved in female pregnancy
purine ribonucleoside monophosphate biosynthetic process
Cellular Component
cytosol
Function
catalytic activity
transferase activity
transferase activity, transferring pentosyl groups
amidophosphoribosyltransferase activity
transferase activity, transferring glycosyl groups
Molecular Function
metal ion binding
4 iron, 4 sulfur cluster binding
amidophosphoribosyltransferase activity
Process
metabolic process
nitrogen compound metabolic process
cellular nitrogen compound metabolic process
nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
nucleobase, nucleoside and nucleotide metabolic process
cellular aromatic compound metabolic process
purine base metabolic process
purine base biosynthetic process
nucleoside metabolic process
cellular metabolic process
nucleobase metabolic process
Cellular Location Not Available
Gene Properties
Chromosome Location 4
Locus 4q12
SNPs PPAT
Gene Sequence 
>1554 bp
ATGGAGCTGGAGGAGTTGGGGATCCGAGAGGAATGTGGCGTGTTCGGGTGCATCGCCTCA
GGAGAGTGGCCCACGCAGCTGGATGTACCGCATGTGATCACTCTGGGACTCGTGGGGCTG
CAGCACCGGGGTCAGGAGAGTGCTGGTATTGTGACTAGTGATGGGAGTTCGGTGCCAACA
TTCAAATCACACAAGGGAATGGGTCTTGTAAATCACGTCTTTACTGAAGACAATTTGAAA
AAATTATATGTTTCAAATCTTGGAATTGGACACACCAGGTATGCCACCACAGGAAAATGT
GAACTAGAAAATTGTCAGCCCTTCGTTGTTGAAACACTTCATGGGAAGATAGCTGTGGCA
CATAATGGCGAATTGGTAAATGCTGCTCGATTAAGGAAAAAGCTTCTGCGTCATGGTATT
GGTCTGTCTACAAGTTCTGATAGTGAAATGATTACCCAGTTACTGGCGTATACCCCTCCT
CAGGAACAAGATGACACCCCAGACTGGGTAGCCAGGATTAAAAACTTGATGAAGGAAGCA
CCCACAGCATACTCCCTGCTTATAATGCACAGAGATGTTATTTATGCAGTACGAGATCCT
TATGGAAATCGTCCCTTATGCATTGGTCGTCTTATTCCAGTGTCTGATATAAATGACAAA
GAGAAAAAAACATCAGAAACAGAAGGATGGGTGGTGTCTTCAGAATCTTGTAGCTTCTTA
TCTATTGGTGCAAGATATTACCGTGAAGTCTTGCCTGGAGAAATTGTGGAAATATCCAGA
CACAATGTCCAAACTCTTGATATTATATCAAGGTCTGAAGGAAACCCAGTGGCTTTTTGT
ATCTTTGAATATGTTTATTTTGCAAGACCAGACAGTATGTTCGAAGACCAAATGGTTTAT
ACAGTAAGATACCGTTGTGGCCAGCAGCTAGCGATTGAAGCACCTGTGGATGCAGATTTG
GTTAGCACTGTTCCAGAATCTGCTACGCCTGCTGCTCTTGCTTACGCAGGAAAGTGTGGA
CTTCCATATGTGGAGGTGCTGTGTAAAAACCGGTATGTAGGGAGAACCTTCATTCAGCCA
AACATGAGGTTAAGACAACTTGGTGTTGCAAAAAAATTTGGAGTATTGTCAGACAACTTT
AAAGGCAAAAGAATTGTTCTTGTAGATGATTCAATTGTCAGAGGCAATACCATCTCACCT
ATAATAAAACTGCTCAAAGAATCTGGTGCAAAAGAGGTACACATTCGAGTAGCTTCACCA
CCAATTAAATATCCATGCTTCATGGGAATAAACATTCCTACAAAAGAAGAGCTCATTGCC
AATAAACCAGAATTTGATCACCTTGCAGAATATCTAGGAGCAAACAGTGTTGTGTATCTG
TCAGTAGAAGGACTGGTTTCATCTGTACAAGAAGGGATAAAGTTTAAAAAACAGAAAGAG
AAAAAGCACGATATTATGATCCAAGAAAATGGAAATGGTCTGGAATGTTTTGAAAAGAGT
GGTCATTGTACAGCTTGTCTCACTGGAAAATATCCTGTAGAATTAGAATGGTAG
Protein Properties
Number of Residues 517
Molecular Weight 57398.52
Theoretical pI 6.749
Pfam Domain Function
Signals Not Available
Transmembrane Regions Not Available
Protein Sequence 
>Amidophosphoribosyltransferase
MELEELGIREECGVFGCIASGEWPTQLDVPHVITLGLVGLQHRGQESAGIVTSDGSSVPT
FKSHKGMGLVNHVFTEDNLKKLYVSNLGIGHTRYATTGKCELENCQPFVVETLHGKIAVA
HNGELVNAARLRKKLLRHGIGLSTSSDSEMITQLLAYTPPQEQDDTPDWVARIKNLMKEA
PTAYSLLIMHRDVIYAVRDPYGNRPLCIGRLIPVSDINDKEKKTSETEGWVVSSESCSFL
SIGARYYREVLPGEIVEISRHNVQTLDIISRSEGNPVAFCIFEYVYFARPDSMFEDQMVY
TVRYRCGQQLAIEAPVDADLVSTVPESATPAALAYAGKCGLPYVEVLCKNRYVGRTFIQP
NMRLRQLGVAKKFGVLSDNFKGKRIVLVDDSIVRGNTISPIIKLLKESGAKEVHIRVASP
PIKYPCFMGINIPTKEELIANKPEFDHLAEYLGANSVVYLSVEGLVSSVQEGIKFKKQKE
KKHDIMIQENGNGLECFEKSGHCTACLTGKYPVELEW
GenBank ID Protein Not Available
UniProtKB/Swiss-Prot ID Q06203
UniProtKB/Swiss-Prot Entry Name PUR1_HUMAN
PDB IDs Not Available
GenBank Gene ID D13757
GeneCard ID PPAT
GenAtlas ID PPAT
HGNC ID HGNC:9238
References
General References
  1. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed:15489334 ]
  2. 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. doi: 10.1126/science.1175371. Epub 2009 Jul 16. [PubMed:19608861 ]
  3. Iwahana H, Oka J, Mizusawa N, Kudo E, Ii S, Yoshimoto K, Holmes EW, Itakura M: Molecular cloning of human amidophosphoribosyltransferase. Biochem Biophys Res Commun. 1993 Jan 15;190(1):192-200. [PubMed:8380692 ]
  4. Brayton KA, Chen Z, Zhou G, Nagy PL, Gavalas A, Trent JM, Deaven LL, Dixon JE, Zalkin H: Two genes for de novo purine nucleotide synthesis on human chromosome 4 are closely linked and divergently transcribed. J Biol Chem. 1994 Feb 18;269(7):5313-21. [PubMed:8106516 ]