ID KPRS_LEPIC Reviewed; 312 AA. AC Q72V73; DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2004, sequence version 1. DT 16-SEP-2015, entry version 83. DE RecName: Full=Ribose-phosphate pyrophosphokinase {ECO:0000255|HAMAP-Rule:MF_00583}; DE Short=RPPK {ECO:0000255|HAMAP-Rule:MF_00583}; DE EC=2.7.6.1 {ECO:0000255|HAMAP-Rule:MF_00583}; DE AltName: Full=5-phospho-D-ribosyl alpha-1-diphosphate {ECO:0000255|HAMAP-Rule:MF_00583}; DE AltName: Full=Phosphoribosyl diphosphate synthase {ECO:0000255|HAMAP-Rule:MF_00583}; DE AltName: Full=Phosphoribosyl pyrophosphate synthase {ECO:0000255|HAMAP-Rule:MF_00583}; DE Short=P-Rib-PP synthase {ECO:0000255|HAMAP-Rule:MF_00583}; DE Short=PRPP synthase {ECO:0000255|HAMAP-Rule:MF_00583}; DE Short=PRPPase {ECO:0000255|HAMAP-Rule:MF_00583}; GN Name=prs {ECO:0000255|HAMAP-Rule:MF_00583}; GN OrderedLocusNames=LIC_10429; OS Leptospira interrogans serogroup Icterohaemorrhagiae serovar OS copenhageni (strain Fiocruz L1-130). OC Bacteria; Spirochaetes; Leptospirales; Leptospiraceae; Leptospira. OX NCBI_TaxID=267671; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Fiocruz L1-130; RX PubMed=15028702; DOI=10.1128/JB.186.7.2164-2172.2004; RA Nascimento A.L.T.O., Ko A.I., Martins E.A.L., Monteiro-Vitorello C.B., RA Ho P.L., Haake D.A., Verjovski-Almeida S., Hartskeerl R.A., RA Marques M.V., Oliveira M.C., Menck C.F.M., Leite L.C.C., Carrer H., RA Coutinho L.L., Degrave W.M., Dellagostin O.A., El-Dorry H., RA Ferro E.S., Ferro M.I.T., Furlan L.R., Gamberini M., Giglioti E.A., RA Goes-Neto A., Goldman G.H., Goldman M.H.S., Harakava R., RA Jeronimo S.M.B., Junqueira-de-Azevedo I.L.M., Kimura E.T., RA Kuramae E.E., Lemos E.G.M., Lemos M.V.F., Marino C.L., Nunes L.R., RA de Oliveira R.C., Pereira G.G., Reis M.S., Schriefer A., RA Siqueira W.J., Sommer P., Tsai S.M., Simpson A.J.G., Ferro J.A., RA Camargo L.E.A., Kitajima J.P., Setubal J.C., Van Sluys M.A.; RT "Comparative genomics of two Leptospira interrogans serovars reveals RT novel insights into physiology and pathogenesis."; RL J. Bacteriol. 186:2164-2172(2004). CC -!- FUNCTION: Involved in the biosynthesis of ribose 1,5-bisphosphate. CC Catalyzes the transfer of pyrophosphoryl group from ATP to ribose- CC 5-phosphate to yield phosphoribosyl diphosphate (PRPP) and AMP. CC {ECO:0000255|HAMAP-Rule:MF_00583}. CC -!- CATALYTIC ACTIVITY: ATP + D-ribose 5-phosphate = AMP + 5-phospho- CC alpha-D-ribose 1-diphosphate. {ECO:0000255|HAMAP-Rule:MF_00583}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00583}; CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP- CC Rule:MF_00583}; 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 {ECO:0000255|HAMAP-Rule:MF_00583}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00583}. CC -!- SIMILARITY: Belongs to the ribose-phosphate pyrophosphokinase CC family. {ECO:0000255|HAMAP-Rule:MF_00583}. 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; AE016823; AAS69051.1; -; Genomic_DNA. DR RefSeq; WP_001012709.1; NC_005823.1. DR ProteinModelPortal; Q72V73; -. DR STRING; 267671.LIC10429; -. DR EnsemblBacteria; AAS69051; AAS69051; LIC_10429. DR KEGG; lic:LIC10429; -. DR PATRIC; 22372670; VBILepInt6257_0510. DR KO; K00948; -. DR OMA; PVNEHLM; -. DR OrthoDB; EOG6Z99XQ; -. DR BioCyc; LINT267671:GHQI-428-MONOMER; -. DR UniPathway; UPA00087; UER00172. DR Proteomes; UP000007037; Chromosome I. 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 Gene3D; 3.40.50.2020; -; 2. DR HAMAP; MF_00583_B; RibP_PPkinase_B; 1. DR InterPro; IPR000842; PRib_PP_synth_CS. DR InterPro; IPR029099; Pribosyltran_N. DR InterPro; IPR029057; PRTase-like. DR InterPro; IPR005946; Rib-P_diPkinase. DR Pfam; PF14572; Pribosyl_synth; 1. DR Pfam; PF13793; Pribosyltran_N; 1. DR SUPFAM; SSF53271; SSF53271; 1. DR TIGRFAMs; TIGR01251; ribP_PPkin; 1. DR PROSITE; PS00114; PRPP_SYNTHASE; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Cytoplasm; Kinase; Magnesium; KW Metal-binding; Nucleotide biosynthesis; Nucleotide-binding; KW Transferase. FT CHAIN 1 312 Ribose-phosphate pyrophosphokinase. FT /FTId=PRO_0000141150. FT NP_BIND 38 40 ATP. {ECO:0000255|HAMAP-Rule:MF_00583}. FT NP_BIND 97 100 ATP. {ECO:0000255|HAMAP-Rule:MF_00583}. FT REGION 193 195 Ribose-5-phosphate binding. FT {ECO:0000255|HAMAP-Rule:MF_00583}. FT REGION 220 227 Ribose-5-phosphate binding. FT {ECO:0000255|HAMAP-Rule:MF_00583}. FT REGION 306 308 Ribose-5-phosphate binding. FT {ECO:0000255|HAMAP-Rule:MF_00583}. FT METAL 129 129 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00583}. FT METAL 131 131 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00583}. FT METAL 144 144 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00583}. FT BINDING 105 105 Ribose-5-phosphate. {ECO:0000255|HAMAP- FT Rule:MF_00583}. FT BINDING 131 131 ATP. {ECO:0000255|HAMAP-Rule:MF_00583}. FT BINDING 136 136 ATP. {ECO:0000255|HAMAP-Rule:MF_00583}. FT BINDING 170 170 Ribose-5-phosphate. {ECO:0000255|HAMAP- FT Rule:MF_00583}. SQ SEQUENCE 312 AA; 33847 MW; 605454F791690F69 CRC64; MNGDIAVFAG NSNKQIAEEI CTHLGIQSGK INLKKFSDGE ISVKIEDNVR GKEVFIVQST SAPANDHLME LILIMDALRR ASVSSISVVI PYYGYGRQDR KVEPRVPISA RVVADLIEVV GLDRILTMDL HADQIQGFFR VPVDNLHFAP VLAEYVNTKK IDDLVIVSPD SGGAERARAF GKKVNGSLAI IDKRRPKANV SEVMNVIGEI EGKNCILLDD MIDTAGTICK AADVLLKHGA KSVYCAATHG VLSGEAVDRI NSTQFSEVVL ANTIAIPESK KINKLKSLSV APLFANAIQR IHTNQSVSTL FD //