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Identification
HMDB Protein ID HMDBP00566
Secondary Accession Numbers
  • 5838
Name Ribose-phosphate pyrophosphokinase 3
Synonyms
  1. PRPS1-like 1
  2. PRS-III
  3. Phosphoribosyl pyrophosphate synthase 1-like 1
  4. Phosphoribosyl pyrophosphate synthase III
Gene Name PRPS1L1
Protein Type Unknown
Biological Properties
General Function Involved in magnesium ion binding
Specific Function Catalyzes the synthesis of phosphoribosylpyrophosphate (PRPP) that is essential for nucleotide synthesis.
Pathways
  • 5-phospho-alpha-D-ribose 1-diphosphate biosynthesis
  • Adenine phosphoribosyltransferase deficiency (APRT)
  • Adenosine Deaminase Deficiency
  • Adenylosuccinate Lyase Deficiency
  • AICA-Ribosiduria
  • Azathioprine Action Pathway
  • Glucose-6-phosphate dehydrogenase deficiency
  • Gout or Kelley-Seegmiller Syndrome
  • Lesch-Nyhan Syndrome (LNS)
  • Mercaptopurine Action Pathway
  • Mitochondrial DNA depletion syndrome
  • Molybdenum Cofactor Deficiency
  • Myoadenylate deaminase deficiency
  • Pentose Phosphate Pathway
  • Pentose phosphate pathway
  • Purine Metabolism
  • Purine metabolism
  • Purine Nucleoside Phosphorylase Deficiency
  • Ribose-5-phosphate isomerase deficiency
  • Thioguanine Action Pathway
  • Transaldolase deficiency
  • Xanthine Dehydrogenase Deficiency (Xanthinuria)
  • Xanthinuria type I
  • Xanthinuria type II
Reactions
Adenosine triphosphate + D-Ribose 5-phosphate → Adenosine monophosphate + Phosphoribosyl pyrophosphate details
GO Classification
Biological Process
nucleotide biosynthetic process
5-phosphoribose 1-diphosphate biosynthetic process
ribonucleoside monophosphate biosynthetic process
nucleoside metabolic process
Function
ion binding
cation binding
metal ion binding
binding
catalytic activity
transferase activity
transferase activity, transferring phosphorus-containing groups
diphosphotransferase activity
ribose phosphate diphosphokinase activity
magnesium ion binding
Molecular Function
magnesium ion binding
kinase activity
ribose phosphate diphosphokinase activity
ATP binding
protein homodimerization 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
nucleoside phosphate metabolic process
nucleotide metabolic process
nucleotide biosynthetic process
nucleoside monophosphate metabolic process
nucleoside monophosphate biosynthetic process
ribonucleoside monophosphate biosynthetic process
nucleoside metabolic process
biosynthetic process
cellular biosynthetic process
Cellular Location Not Available
Gene Properties
Chromosome Location 7
Locus 7p21.1
SNPs PRPS1L1
Gene Sequence
>957 bp
ACGCCGAATATCAAAATCTTCAGCGGCAGCTCCCACCAGGACTTATCCCAGAAAATTGCT
GACCGCCTGGGCCTGGAGCTAGGCAAGGTGGTGACTAAGAAATTCAGCAACCAGGAGACC
TGCGTGGAAATTGATGAGAGTGTGCGTGGAGAGGATGTCTACATCGTTCAGAGTGGTTGT
GGCGAAATCAACGACAGTCTAATGGAGCTTTTGATCATGATTAATGCCTGCAAGATTGCT
TCAGCTAGCCGAGTTACTGCAGTCATCCCATGCTTCCCTTATGCCCGACAGGATAAGAAG
GATAAGAGCCGGTCCCCAATCTCTGCCAAGCTTGTTGCAAATATGCTCTCTATAGCAGGT
GCGGATCATATCATCACCATGGACCTACATGCTTCTCAAATTCAGGGCTTTTTTGATATC
CCAGTAGACAACTTGTATGCAGAGCCAACTGTCCTGAAGTGGATAAGGGAGAATATCCCT
GAGTGGAAGAACTGCATTATTGTCTCGCCAGATGCTGGTGGAGCTAAAAGAGTGACCTCC
ATTGCAGACCAGTTGAATGTGGACTTTGCTTTGATTCATAAAGAACGGAAGAAGGCCAAT
GAAGTGGACTGCATAGTGCTAGTGGGAGATGTGAATGATCGTGTGGCTATCCTTGTAGAT
GACATGGCAGACACTTGTGTTACAATCTGCCTCGCAGCTGACAAACTTCTCTCAGCTGGA
GCAACCAGAGTTTATGCTATCTTGACTCATGGAATCTTTTCTGGCCCAGCCATTTCTCGC
ATCAACACTGCATGCTTTGAAGCAGTGGTAGTCACCAATACCATACCTCAAGATGATAAG
ATGAAGCATTGCTCCAAAATACGAGTAATTGACATCTCCATGATCCTTGCAGAAGCCATA
AGGAGAACTCATAATGGGGAATCTGTTTCCTACCTGTTCAGCCATGTTCCTTTATAA
Protein Properties
Number of Residues 318
Molecular Weight 34838.915
Theoretical pI 6.353
Pfam Domain Function
Signals Not Available
Transmembrane Regions Not Available
Protein Sequence
>Ribose-phosphate pyrophosphokinase 3
MPNIKIFSGSSHQDLSQKIADRLGLELGKVVTKKFSNQETCVEIDESVRGEDVYIVQSGC
GEINDSLMELLIMINACKIASASRVTAVIPCFPYARQDKKDKSRSPISAKLVANMLSIAG
ADHIITMDLHASQIQGFFDIPVDNLYAEPTVLKWIRENIPEWKNCIIVSPDAGGAKRVTS
IADQLNVDFALIHKERKKANEVDCIVLVGDVNDRVAILVDDMADTCVTICLAADKLLSAG
ATRVYAILTHGIFSGPAISRINTACFEAVVVTNTIPQDEKMKHCSKIRVIDISMILAEAI
RRTHNGESVSYLFSHVPL
GenBank ID Protein 110611809
UniProtKB/Swiss-Prot ID P21108
UniProtKB/Swiss-Prot Entry Name PRPS3_HUMAN
PDB IDs Not Available
GenBank Gene ID BC062797
GeneCard ID PRPS1L1
GenAtlas ID PRPS1L1
HGNC ID HGNC:9463
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. Taira M, Iizasa T, Shimada H, Kudoh J, Shimizu N, Tatibana M: A human testis-specific mRNA for phosphoribosylpyrophosphate synthetase that initiates from a non-AUG codon. J Biol Chem. 1990 Sep 25;265(27):16491-7. [PubMed:2168892 ]