ID C5QLK6_9STAP Unreviewed; 321 AA. AC C5QLK6; DT 01-SEP-2009, integrated into UniProtKB/TrEMBL. DT 01-SEP-2009, sequence version 1. DT 19-FEB-2014, entry version 23. DE RecName: Full=Ribose-phosphate pyrophosphokinase; DE Short=RPPK; DE EC=2.7.6.1; DE AltName: Full=Phosphoribosyl pyrophosphate synthase; GN Name=prs; ORFNames=HMPREF0793_0112; OS Staphylococcus caprae M23864:W1. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=525378; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=M23864:W1; RA Qin X., Bachman B., Battles P., Bell A., Bess C., Bickham C., RA Chaboub L., Chen D., Coyle M., Deiros D.R., Dinh H., Forbes L., RA Fowler G., Francisco L., Fu Q., Gubbala S., Hale W., Han Y., RA Hemphill L., Highlander S.K., Hirani K., Hogues M., Jackson L., RA Jakkamsetti A., Javaid M., Jiang H., Korchina V., Kovar C., Lara F., RA Lee S., Mata R., Mathew T., Moen C., Morales K., Munidasa M., RA Nazareth L., Ngo R., Nguyen L., Okwuonu G., Ongeri F., Patil S., RA Petrosino J., Pham C., Pham P., Pu L.-L., Puazo M., Raj R., Reid J., RA Rouhana J., Saada N., Shang Y., Simmons D., Thornton R., Warren J., RA Weissenberger G., Zhang J., Zhang L., Zhou C., Zhu D., Muzny D., RA Worley K., Gibbs R.; RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: ATP + D-ribose 5-phosphate = AMP + 5-phospho- CC alpha-D-ribose 1-diphosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PATHWAY: Metabolic intermediate biosynthesis; 5-phospho-alpha-D- CC ribose 1-diphosphate biosynthesis; 5-phospho-alpha-D-ribose 1- CC diphosphate from D-ribose 5-phosphate (route I): step 1/1. CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). CC -!- SIMILARITY: Belongs to the ribose-phosphate pyrophosphokinase CC family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; ACJB01000005; EES42220.1; -; Genomic_DNA. DR ProteinModelPortal; C5QLK6; -. DR EnsemblBacteria; EES42220; EES42220; HMPREF0793_0112. DR PATRIC; 31399264; VBIStaEpi14170_2487. DR UniPathway; UPA00087; UER00172. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004749; F:ribose phosphate diphosphokinase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006015; P:5-phosphoribose 1-diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0009165; P:nucleotide biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009156; P:ribonucleoside monophosphate biosynthetic process; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00583_B; RibP_PPkinase_B; 1. DR InterPro; IPR000842; PRib_PP_synth_CS. DR InterPro; IPR005946; Rib-P_diPkinase. DR Pfam; PF14572; Pribosyl_synth; 1. DR TIGRFAMs; TIGR01251; ribP_PPkin; 1. DR PROSITE; PS00114; PRPP_SYNTHASE; 1. PE 3: Inferred from homology; KW ATP-binding; Cytoplasm; Kinase; Magnesium; Metal-binding; KW Nucleotide biosynthesis; Nucleotide-binding; Transferase. FT REGION 221 234 5-phosphoribose 1-diphosphate binding (By FT similarity). FT METAL 135 135 Magnesium (By similarity). FT METAL 137 137 Magnesium (By similarity). FT METAL 146 146 Magnesium (By similarity). FT METAL 150 150 Magnesium (By similarity). SQ SEQUENCE 321 AA; 35295 MW; 8AA99FB0FE088710 CRC64; MLNNEYKNSS LKIFSLKGNE PLAQEVADHV GIELGKCSVK RFSDGEIQIN IEESIRGCDV FIIQPTSYPV NLHLMELLIM IDACKRASAA NINIVVPYYG YARQDRKARS REPITAKLVA NLIETAGANR MIALDLHAPQ IQGFFDIPID HLMGVPILAQ HFENDPDINP EECVVVSPDH GGVTRARKLA DILKTPIAII DKRRPKPNVA EVMNIVGEIE GRTAIIIDDI IDTAGTITLA AQALKDKGAK EVYACCTHPV LSGPAKERIE NSAIKELIVT NSIQLEESRK PTNTKELSVA GLIGKAIIRV YERESVSVLF D //