ID B0SKG4_LEPBP Unreviewed; 313 AA. AC B0SKG4; DT 08-APR-2008, integrated into UniProtKB/TrEMBL. DT 08-APR-2008, sequence version 1. DT 11-NOV-2015, entry version 64. DE RecName: Full=Ribose-phosphate pyrophosphokinase {ECO:0000256|HAMAP-Rule:MF_00583}; DE Short=RPPK {ECO:0000256|HAMAP-Rule:MF_00583}; DE EC=2.7.6.1 {ECO:0000256|HAMAP-Rule:MF_00583}; DE AltName: Full=5-phospho-D-ribosyl alpha-1-diphosphate {ECO:0000256|HAMAP-Rule:MF_00583}; DE AltName: Full=Phosphoribosyl diphosphate synthase {ECO:0000256|HAMAP-Rule:MF_00583}; DE AltName: Full=Phosphoribosyl pyrophosphate synthase {ECO:0000256|HAMAP-Rule:MF_00583}; GN Name=prs {ECO:0000256|HAMAP-Rule:MF_00583, GN ECO:0000313|EMBL:ABZ96381.1}; GN OrderedLocusNames=LEPBI_I0236 {ECO:0000313|EMBL:ABZ96381.1}; OS Leptospira biflexa serovar Patoc (strain Patoc 1 / ATCC 23582 / OS Paris). OC Bacteria; Spirochaetes; Leptospirales; Leptospiraceae; Leptospira. OX NCBI_TaxID=456481 {ECO:0000313|EMBL:ABZ96381.1, ECO:0000313|Proteomes:UP000001847}; RN [1] {ECO:0000313|EMBL:ABZ96381.1, ECO:0000313|Proteomes:UP000001847} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Patoc 1 / ATCC 23582 / Paris RC {ECO:0000313|Proteomes:UP000001847}; RX PubMed=18270594; DOI=10.1371/journal.pone.0001607; RA Picardeau M., Bulach D.M., Bouchier C., Zuerner R.L., Zidane N., RA Wilson P.J., Creno S., Kuczek E.S., Bommezzadri S., Davis J.C., RA McGrath A., Johnson M.J., Boursaux-Eude C., Seemann T., Rouy Z., RA Coppel R.L., Rood J.I., Lajus A., Davies J.K., Medigue C., Adler B.; RT "Genome sequence of the saprophyte Leptospira biflexa provides RT insights into the evolution of Leptospira and the pathogenesis of RT leptospirosis."; RL PLoS ONE 3:E1607-E1607(2008). 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:0000256|HAMAP-Rule:MF_00583}. CC -!- CATALYTIC ACTIVITY: ATP + D-ribose 5-phosphate = AMP + 5-phospho- CC alpha-D-ribose 1-diphosphate. {ECO:0000256|HAMAP-Rule:MF_00583}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP- CC Rule:MF_00583}; CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|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:0000256|HAMAP-Rule:MF_00583}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00583}. CC -!- SIMILARITY: Belongs to the ribose-phosphate pyrophosphokinase CC family. {ECO:0000256|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; CP000786; ABZ96381.1; -; Genomic_DNA. DR RefSeq; WP_012387269.1; NC_010602.1. DR ProteinModelPortal; B0SKG4; -. DR STRING; 456481.LEPBI_I0236; -. DR EnsemblBacteria; ABZ96381; ABZ96381; LEPBI_I0236. DR KEGG; lbi:LEPBI_I0236; -. DR PATRIC; 22347166; VBILepBif123590_0238. DR eggNOG; ENOG4105C5T; Bacteria. DR eggNOG; COG0462; LUCA. DR HOGENOM; HOG000210449; -. DR KO; K00948; -. DR OMA; DGEIMVE; -. DR OrthoDB; EOG6Z99XQ; -. DR BioCyc; LBIF456481:GCM0-235-MONOMER; -. DR UniPathway; UPA00087; UER00172. DR Proteomes; UP000001847; 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; 2. DR TIGRFAMs; TIGR01251; ribP_PPkin; 1. DR PROSITE; PS00114; PRPP_SYNTHASE; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_00583}; KW Complete proteome {ECO:0000313|Proteomes:UP000001847}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00583}; KW Kinase {ECO:0000256|HAMAP-Rule:MF_00583, ECO:0000313|EMBL:ABZ96381.1}; KW Magnesium {ECO:0000256|HAMAP-Rule:MF_00583}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00583}; KW Nucleotide biosynthesis {ECO:0000256|HAMAP-Rule:MF_00583}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00583}; KW Reference proteome {ECO:0000313|Proteomes:UP000001847}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_00583, KW ECO:0000313|EMBL:ABZ96381.1}. FT NP_BIND 39 41 ATP. {ECO:0000256|HAMAP-Rule:MF_00583}. FT NP_BIND 98 101 ATP. {ECO:0000256|HAMAP-Rule:MF_00583}. FT NP_BIND 145 146 ATP. {ECO:0000256|HAMAP-Rule:MF_00583}. FT REGION 194 196 Ribose-5-phosphate binding. FT {ECO:0000256|HAMAP-Rule:MF_00583}. FT REGION 221 228 Ribose-5-phosphate binding. FT {ECO:0000256|HAMAP-Rule:MF_00583}. FT REGION 307 309 Ribose-5-phosphate binding. FT {ECO:0000256|HAMAP-Rule:MF_00583}. FT METAL 130 130 Magnesium. {ECO:0000256|HAMAP-Rule: FT MF_00583}. FT METAL 132 132 Magnesium. {ECO:0000256|HAMAP-Rule: FT MF_00583}. FT METAL 145 145 Magnesium. {ECO:0000256|HAMAP-Rule: FT MF_00583}. FT BINDING 106 106 Ribose-5-phosphate. {ECO:0000256|HAMAP- FT Rule:MF_00583}. FT BINDING 132 132 ATP. {ECO:0000256|HAMAP-Rule:MF_00583}. FT BINDING 137 137 ATP. {ECO:0000256|HAMAP-Rule:MF_00583}. FT BINDING 171 171 Ribose-5-phosphate. {ECO:0000256|HAMAP- FT Rule:MF_00583}. SQ SEQUENCE 313 AA; 34213 MW; 950A2469A64B5321 CRC64; MNPSEVVVFS GNANRPLAEE ICKNLKIPNG QISVKRFSDG ESSVKIEENV RGRDVFVVQS ISYPANDSLM ELLLIIDAAR RASARRITAV IPYYGYGRQD RKVEPRVPIS ARMVADLIET VGPDRVLTMD LHADQIQGFF RIPVDHLYFS PVLAEYINSL GMDDLVIVSP DSGGAERARN FGKKVNGSLA IIDKRRPKAN ESVVMHVIGD IKDKNCLLLD DMIDTGGTIA KAATALYENG AKSVLCCASH GVLSGEAPSK LNEAKFNPIV LSNSIVIPES KKINHLKTLS IAPLFAKAIE RIHNEESISS LFS //