Ribose-phosphate pyrophosphokinase

Details

Name
Ribose-phosphate pyrophosphokinase
Synonyms
  • 2.7.6.1
  • 5-phospho-D-ribosyl alpha-1-diphosphate
  • P-Rib-PP synthase
  • Phosphoribosyl diphosphate synthase
  • Phosphoribosyl pyrophosphate synthase
  • PPRibP synthase
  • PRPP synthase
  • PRPPase
  • RPPK
Gene Name
prs
Organism
Bacillus subtilis (strain 168)
Amino acid sequence
>lcl|BSEQ0011193|Ribose-phosphate pyrophosphokinase
MSNQYGDKNLKIFSLNSNPELAKEIADIVGVQLGKCSVTRFSDGEVQINIEESIRGCDCY
IIQSTSDPVNEHIMELLIMVDALKRASAKTINIVIPYYGYARQDRKARSREPITAKLFAN
LLETAGATRVIALDLHAPQIQGFFDIPIDHLMGVPILGEYFEGKNLEDIVIVSPDHGGVT
RARKLADRLKAPIAIIDKRRPRPNVAEVMNIVGNIEGKTAILIDDIIDTAGTITLAANAL
VENGAKEVYACCTHPVLSGPAVERINNSTIKELVVTNSIKLPEEKKIERFKQLSVGPLLA
EAIIRVHEQQSVSYLFS
Number of residues
317
Molecular Weight
34867.88
Theoretical pI
6.26
GO Classification
Functions
ATP binding / kinase activity / magnesium ion binding / ribose phosphate diphosphokinase activity
Processes
5-phosphoribose 1-diphosphate biosynthetic process / nucleotide biosynthetic process / ribonucleoside monophosphate biosynthetic process
Components
cytoplasm
General Function
Ribose phosphate diphosphokinase activity
Specific Function
Involved in the biosynthesis of ribose 1,5-bisphosphate. Catalyzes the transfer of pyrophosphoryl group from ATP to ribose-5-phosphate to yield phosphoribosyl diphosphate (PRPP) and AMP.
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Cytoplasm
Gene sequence
>lcl|BSEQ0011194|Ribose-phosphate pyrophosphokinase (prs)
ATGTCTAATCAATACGGAGATAAGAATTTAAAGATTTTTTCTTTGAATTCGAATCCAGAG
CTTGCAAAAGAAATCGCAGATATAGTTGGAGTTCAATTAGGGAAATGTTCTGTCACAAGA
TTTAGTGACGGGGAAGTCCAAATTAATATCGAAGAAAGTATTCGCGGATGTGATTGTTAC
ATCATCCAGTCTACAAGTGACCCCGTTAACGAGCATATTATGGAACTGCTGATTATGGTA
GATGCGTTAAAACGCGCTTCTGCAAAAACGATTAACATTGTTATTCCTTATTACGGTTAT
GCGCGTCAAGACAGAAAAGCAAGATCCCGTGAGCCAATCACAGCTAAACTTTTCGCTAAC
CTGCTTGAAACAGCCGGTGCGACTCGTGTGATTGCACTTGACCTGCATGCGCCGCAAATT
CAAGGATTCTTTGATATACCGATTGACCACTTAATGGGTGTTCCGATTTTAGGAGAATAT
TTTGAAGGCAAAAATCTTGAAGATATCGTCATTGTTTCACCAGACCATGGCGGTGTGACA
CGTGCCCGCAAACTGGCTGACCGACTAAAAGCGCCAATTGCGATTATCGATAAACGCCGT
CCGCGTCCAAACGTGGCGGAAGTCATGAATATTGTAGGTAACATCGAAGGGAAGACTGCT
ATCCTCATCGATGACATTATTGATACTGCAGGTACGATTACACTTGCTGCTAATGCGCTC
GTTGAAAACGGAGCGAAAGAAGTATATGCATGCTGTACACACCCTGTACTATCAGGCCCT
GCGGTTGAACGGATTAATAATTCAACAATTAAAGAGCTTGTTGTGACAAACAGCATCAAG
CTTCCTGAAGAAAAGAAAATTGAACGCTTTAAGCAGCTTTCAGTCGGACCGCTTCTGGCC
GAAGCGATTATTCGCGTTCATGAGCAGCAATCAGTCAGCTATCTGTTCAGCTAA
Chromosome Location
Not Available
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDP14193
UniProtKB Entry NameKPRS_BACSU
GenBank Protein ID40218
GenBank Gene IDX16518
General References
  1. Nilsson D, Hove-Jensen B, Arnvig K: Primary structure of the tms and prs genes of Bacillus subtilis. Mol Gen Genet. 1989 Sep;218(3):565-71. [Article]
  2. Ogasawara N, Nakai S, Yoshikawa H: Systematic sequencing of the 180 kilobase region of the Bacillus subtilis chromosome containing the replication origin. DNA Res. 1994;1(1):1-14. [Article]
  3. Kunst F, Ogasawara N, Moszer I, Albertini AM, Alloni G, Azevedo V, Bertero MG, Bessieres P, Bolotin A, Borchert S, Borriss R, Boursier L, Brans A, Braun M, Brignell SC, Bron S, Brouillet S, Bruschi CV, Caldwell B, Capuano V, Carter NM, Choi SK, Cordani JJ, Connerton IF, Cummings NJ, Daniel RA, Denziot F, Devine KM, Dusterhoft A, Ehrlich SD, Emmerson PT, Entian KD, Errington J, Fabret C, Ferrari E, Foulger D, Fritz C, Fujita M, Fujita Y, Fuma S, Galizzi A, Galleron N, Ghim SY, Glaser P, Goffeau A, Golightly EJ, Grandi G, Guiseppi G, Guy BJ, Haga K, Haiech J, Harwood CR, Henaut A, Hilbert H, Holsappel S, Hosono S, Hullo MF, Itaya M, Jones L, Joris B, Karamata D, Kasahara Y, Klaerr-Blanchard M, Klein C, Kobayashi Y, Koetter P, Koningstein G, Krogh S, Kumano M, Kurita K, Lapidus A, Lardinois S, Lauber J, Lazarevic V, Lee SM, Levine A, Liu H, Masuda S, Mauel C, Medigue C, Medina N, Mellado RP, Mizuno M, Moestl D, Nakai S, Noback M, Noone D, O'Reilly M, Ogawa K, Ogiwara A, Oudega B, Park SH, Parro V, Pohl TM, Portelle D, Porwollik S, Prescott AM, Presecan E, Pujic P, Purnelle B, Rapoport G, Rey M, Reynolds S, Rieger M, Rivolta C, Rocha E, Roche B, Rose M, Sadaie Y, Sato T, Scanlan E, Schleich S, Schroeter R, Scoffone F, Sekiguchi J, Sekowska A, Seror SJ, Serror P, Shin BS, Soldo B, Sorokin A, Tacconi E, Takagi T, Takahashi H, Takemaru K, Takeuchi M, Tamakoshi A, Tanaka T, Terpstra P, Togoni A, Tosato V, Uchiyama S, Vandebol M, Vannier F, Vassarotti A, Viari A, Wambutt R, Wedler H, Weitzenegger T, Winters P, Wipat A, Yamamoto H, Yamane K, Yasumoto K, Yata K, Yoshida K, Yoshikawa HF, Zumstein E, Yoshikawa H, Danchin A: The complete genome sequence of the gram-positive bacterium Bacillus subtilis. Nature. 1997 Nov 20;390(6657):249-56. [Article]
  4. Arnvig K, Hove-Jensen B, Switzer RL: Purification and properties of phosphoribosyl-diphosphate synthetase from Bacillus subtilis. Eur J Biochem. 1990 Aug 28;192(1):195-200. [Article]
  5. Nilsson D, Hove-Jensen B: Phosphoribosylpyrophosphate synthetase of Bacillus subtilis. Cloning, characterization and chromosomal mapping of the prs gene. Gene. 1987;53(2-3):247-55. [Article]
  6. Hove-Jensen B, Bentsen AK, Harlow KW: Catalytic residues Lys197 and Arg199 of Bacillus subtilis phosphoribosyl diphosphate synthase. Alanine-scanning mutagenesis of the flexible catalytic loop. FEBS J. 2005 Jul;272(14):3631-9. [Article]
  7. Eriksen TA, Kadziola A, Bentsen AK, Harlow KW, Larsen S: Structural basis for the function of Bacillus subtilis phosphoribosyl-pyrophosphate synthetase. Nat Struct Biol. 2000 Apr;7(4):303-8. [Article]
  8. Eriksen TA, Kadziola A, Larsen S: Binding of cations in Bacillus subtilis phosphoribosyldiphosphate synthetase and their role in catalysis. Protein Sci. 2002 Feb;11(2):271-9. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB02798Alpha-Methylene Adenosine MonophosphateexperimentalunknownDetails
DB03148Adenosine 5'-methylenediphosphateexperimentalunknownDetails