You are using an unsupported browser. Please upgrade your browser to a newer version to get the best experience on Human Metabolome Database.
Identification
HMDB Protein ID HMDBP00628
Secondary Accession Numbers
  • 5900
  • HMDBP07393
Name Ribose-phosphate pyrophosphokinase 1
Synonyms
  1. PPRibP
  2. PRS-I
  3. Phosphoribosyl pyrophosphate synthase I
Gene Name PRPS1
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
  • Pentose phosphate pathway
  • Purine Metabolism
  • Purine metabolism
Reactions
Adenosine triphosphate + D-Ribose 5-phosphate → Adenosine monophosphate + Phosphoribosyl pyrophosphate details
GO Classification
Biological Process
5-phosphoribose 1-diphosphate biosynthetic process
hypoxanthine biosynthetic process
ribonucleoside monophosphate biosynthetic process
purine nucleotide biosynthetic process
nervous system development
nucleoside metabolic process
urate biosynthetic process
carbohydrate metabolic process
pyrimidine nucleotide biosynthetic process
Cellular Component
cytosol
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
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 X
Locus Xq21.32-q24
SNPs PRPS1
Gene Sequence
>957 bp
ATGCCGAATATCAAAATCTTCAGCGGCAGCTCCCACCAGGACTTATCTCAGAAAATTGCT
GACCGCCTGGGCCTGGAGCTAGGCAAGGTGGTGACTAAGAAATTCAGCAACCAGGAGACC
TGTGTGGAAATTGGTGAAAGTGTACGTGGAGAGGATGTCTACATTGTTCAGAGTGGTTGT
GGCGAAATCAATGACAATTTAATGGAGCTTTTGATCATGATTAATGCCTGCAAGATTGCT
TCAGCCAGCCGGGTTACTGCAGTCATCCCATGCTTCCCTTATGCCCGGCAGGATAAGAAA
GATAAGAGCCGGGCGCCAATCTCAGCCAAGCTTGTTGCAAATATGCTATCTGTAGCAGGT
GCAGATCATATTATCACCATGGACCTACATGCTTCTCAAATTCAGGGCTTTTTTGATATC
CCAGTAGACAATTTGTATGCAGAGCCGGCTGTCCTAAAGTGGATAAGGGAGAATATCTCT
GAGTGGAGGAACTGCACTATTGTCTCACCTGATGCTGGTGGAGCTAAGAGAGTGACCTCC
ATTGCAGACAGGCTGAATGTGGACTTTGCCTTGATTCACAAAGAACGGAAGAAGGCCAAT
GAAGTGGACCGCATGGTGCTTGTGGGAGATGTGAAGGATCGGGTGGCCATCCTTGTGGAT
GACATGGCTGACACTTGTGGCACAATCTGCCATGCAGCTGACAAACTTCTCTCAGCTGGC
GCCACCAGAGTTTATGCCATCTTGACTCATGGAATCTTCTCCGGTCCTGCTATTTCTCGC
ATCAACAACGCATGCTTTGAGGCAGTAGTAGTCACCAATACCATACCTCAGGAGGACAAG
ATGAAGCATTGCTCCAAAATACAGGTGATTGACATCTCTATGATCCTTGCAGAAGCCATC
AGGAGAACTCACAATGGAGAATCCGTTTCTTACCTATTCAGCCATGTCCCTTTATAA
Protein Properties
Number of Residues 318
Molecular Weight 12324.195
Theoretical pI 6.662
Pfam Domain Function
Signals Not Available
Transmembrane Regions Not Available
Protein Sequence
>Ribose-phosphate pyrophosphokinase 1
MPNIKIFSGSSHQDLSQKIADRLGLELGKVVTKKFSNQETCVEIGESVRGEDVYIVQSGC
GEINDNLMELLIMINACKIASASRVTAVIPCFPYARQDKKDKSRAPISAKLVANMLSVAG
ADHIITMDLHASQIQGFFDIPVDNLYAEPAVLKWIRENISEWRNCTIVSPDAGGAKRVTS
IADRLNVDFALIHKERKKANEVDRMVLVGDVKDRVAILVDDMADTCGTICHAADKLLSAG
ATRVYAILTHGIFSGPAISRINNACFEAVVVTNTIPQEDKMKHCSKIQVIDISMILAEAI
RRTHNGESVSYLFSHVPL
GenBank ID Protein 57208781
UniProtKB/Swiss-Prot ID P60891
UniProtKB/Swiss-Prot Entry Name PRPS1_HUMAN
PDB IDs
GenBank Gene ID AL137787
GeneCard ID PRPS1
GenAtlas ID PRPS1
HGNC ID HGNC:9462
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. Deloukas P, Earthrowl ME, Grafham DV, Rubenfield M, French L, Steward CA, Sims SK, Jones MC, Searle S, Scott C, Howe K, Hunt SE, Andrews TD, Gilbert JG, Swarbreck D, Ashurst JL, Taylor A, Battles J, Bird CP, Ainscough R, Almeida JP, Ashwell RI, Ambrose KD, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Bates K, Beasley H, Bray-Allen S, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Cahill P, Camire D, Carter NP, Chapman JC, Clark SY, Clarke G, Clee CM, Clegg S, Corby N, Coulson A, Dhami P, Dutta I, Dunn M, Faulkner L, Frankish A, Frankland JA, Garner P, Garnett J, Gribble S, Griffiths C, Grocock R, Gustafson E, Hammond S, Harley JL, Hart E, Heath PD, Ho TP, Hopkins B, Horne J, Howden PJ, Huckle E, Hynds C, Johnson C, Johnson D, Kana A, Kay M, Kimberley AM, Kershaw JK, Kokkinaki M, Laird GK, Lawlor S, Lee HM, Leongamornlert DA, Laird G, Lloyd C, Lloyd DM, Loveland J, Lovell J, McLaren S, McLay KE, McMurray A, Mashreghi-Mohammadi M, Matthews L, Milne S, Nickerson T, Nguyen M, Overton-Larty E, Palmer SA, Pearce AV, Peck AI, Pelan S, Phillimore B, Porter K, Rice CM, Rogosin A, Ross MT, Sarafidou T, Sehra HK, Shownkeen R, Skuce CD, Smith M, Standring L, Sycamore N, Tester J, Thorpe A, Torcasso W, Tracey A, Tromans A, Tsolas J, Wall M, Walsh J, Wang H, Weinstock K, West AP, Willey DL, Whitehead SL, Wilming L, Wray PW, Young L, Chen Y, Lovering RC, Moschonas NK, Siebert R, Fechtel K, Bentley D, Durbin R, Hubbard T, Doucette-Stamm L, Beck S, Smith DR, Rogers J: The DNA sequence and comparative analysis of human chromosome 10. Nature. 2004 May 27;429(6990):375-81. [PubMed:15164054 ]
  3. Sjoblom T, Jones S, Wood LD, Parsons DW, Lin J, Barber TD, Mandelker D, Leary RJ, Ptak J, Silliman N, Szabo S, Buckhaults P, Farrell C, Meeh P, Markowitz SD, Willis J, Dawson D, Willson JK, Gazdar AF, Hartigan J, Wu L, Liu C, Parmigiani G, Park BH, Bachman KE, Papadopoulos N, Vogelstein B, Kinzler KW, Velculescu VE: The consensus coding sequences of human breast and colorectal cancers. Science. 2006 Oct 13;314(5797):268-74. Epub 2006 Sep 7. [PubMed:16959974 ]
  4. Roessler BJ, Bell G, Heidler S, Seino S, Becker M, Palella TD: Cloning of two distinct copies of human phosphoribosylpyrophosphate synthetase cDNA. Nucleic Acids Res. 1990 Jan 11;18(1):193. [PubMed:2155397 ]
  5. Sonoda T, Taira M, Ishijima S, Ishizuka T, Iizasa T, Tatibana M: Complete nucleotide sequence of human phosphoribosyl pyrophosphate synthetase subunit I (PRS I) cDNA and a comparison with human and rat PRPS gene families. J Biochem. 1991 Feb;109(2):361-4. [PubMed:1650777 ]
  6. Ishizuka T, Iizasa T, Taira M, Ishijima S, Sonoda T, Shimada H, Nagatake N, Tatibana M: Promoter regions of the human X-linked housekeeping genes PRPS1 and PRPS2 encoding phosphoribosylpyrophosphate synthetase subunit I and II isoforms. Biochim Biophys Acta. 1992 Mar 24;1130(2):139-48. [PubMed:1314091 ]
  7. Li S, Lu Y, Peng B, Ding J: Crystal structure of human phosphoribosylpyrophosphate synthetase 1 reveals a novel allosteric site. Biochem J. 2007 Jan 1;401(1):39-47. [PubMed:16939420 ]
  8. Becker MA, Smith PR, Taylor W, Mustafi R, Switzer RL: The genetic and functional basis of purine nucleotide feedback-resistant phosphoribosylpyrophosphate synthetase superactivity. J Clin Invest. 1995 Nov;96(5):2133-41. [PubMed:7593598 ]
  9. de Brouwer AP, Williams KL, Duley JA, van Kuilenburg AB, Nabuurs SB, Egmont-Petersen M, Lugtenberg D, Zoetekouw L, Banning MJ, Roeffen M, Hamel BC, Weaving L, Ouvrier RA, Donald JA, Wevers RA, Christodoulou J, van Bokhoven H: Arts syndrome is caused by loss-of-function mutations in PRPS1. Am J Hum Genet. 2007 Sep;81(3):507-18. Epub 2007 Aug 3. [PubMed:17701896 ]
  10. Kim HJ, Sohn KM, Shy ME, Krajewski KM, Hwang M, Park JH, Jang SY, Won HH, Choi BO, Hong SH, Kim BJ, Suh YL, Ki CS, Lee SY, Kim SH, Kim JW: Mutations in PRPS1, which encodes the phosphoribosyl pyrophosphate synthetase enzyme critical for nucleotide biosynthesis, cause hereditary peripheral neuropathy with hearing loss and optic neuropathy (cmtx5). Am J Hum Genet. 2007 Sep;81(3):552-8. Epub 2007 Jun 29. [PubMed:17701900 ]
  11. Liu X, Han D, Li J, Han B, Ouyang X, Cheng J, Li X, Jin Z, Wang Y, Bitner-Glindzicz M, Kong X, Xu H, Kantardzhieva A, Eavey RD, Seidman CE, Seidman JG, Du LL, Chen ZY, Dai P, Teng M, Yan D, Yuan H: Loss-of-function mutations in the PRPS1 gene cause a type of nonsyndromic X-linked sensorineural deafness, DFN2. Am J Hum Genet. 2010 Jan;86(1):65-71. doi: 10.1016/j.ajhg.2009.11.015. [PubMed:20021999 ]