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 10-APR-2019, entry version 99. 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 the central metabolite CC phospho-alpha-D-ribosyl-1-pyrophosphate (PRPP) via the transfer of CC pyrophosphoryl group from ATP to 1-hydroxyl of ribose-5-phosphate CC (Rib-5-P). {ECO:0000255|HAMAP-Rule:MF_00583}. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + D-ribose 5-phosphate = 5-phospho-alpha-D-ribose 1- CC diphosphate + AMP + H(+); Xref=Rhea:RHEA:15609, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:58017, CC ChEBI:CHEBI:78346, ChEBI:CHEBI:456215; EC=2.7.6.1; CC Evidence={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 2 Mg(2+) ions 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 -!- SUBUNIT: Homohexamer. {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. Class I subfamily. {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 SMR; Q72V73; -. DR PaxDb; Q72V73; -. DR EnsemblBacteria; AAS69051; AAS69051; LIC_10429. DR KEGG; lic:LIC_10429; -. DR eggNOG; ENOG4105C5T; Bacteria. DR eggNOG; COG0462; LUCA. DR KO; K00948; -. DR OMA; FGWARQD; -. 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-UniRule. DR GO; GO:0004749; F:ribose phosphate diphosphokinase activity; IEA:UniProtKB-UniRule. DR GO; GO:0006015; P:5-phosphoribose 1-diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0009116; P:nucleoside metabolic process; IEA:InterPro. DR GO; GO:0009165; P:nucleotide biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009156; P:ribonucleoside monophosphate biosynthetic process; IEA:UniProtKB-UniRule. DR CDD; cd06223; PRTases_typeI; 1. DR HAMAP; MF_00583_B; RibP_PPkinase_B; 1. DR InterPro; IPR000842; PRib_PP_synth_CS. DR InterPro; IPR029099; Pribosyltran_N. DR InterPro; IPR000836; PRibTrfase_dom. DR InterPro; IPR029057; PRTase-like. DR InterPro; IPR005946; Rib-P_diPkinase. DR InterPro; IPR037515; Rib-P_diPkinase_bac. DR PANTHER; PTHR10210; PTHR10210; 1. 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 98 ATP. {ECO:0000255|HAMAP-Rule:MF_00583}. FT REGION 223 227 Ribose-5-phosphate binding. FT {ECO:0000255|HAMAP-Rule:MF_00583}. FT ACT_SITE 193 193 {ECO:0000255|HAMAP-Rule:MF_00583}. FT METAL 131 131 Magnesium 1. {ECO:0000255|HAMAP- FT Rule:MF_00583}. FT METAL 170 170 Magnesium 2. {ECO:0000255|HAMAP- FT Rule:MF_00583}. FT BINDING 195 195 Ribose-5-phosphate. {ECO:0000255|HAMAP- FT Rule:MF_00583}. FT BINDING 219 219 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 //