ID A0A257CMJ3_9BURK Unreviewed; 325 AA. AC A0A257CMJ3; DT 20-DEC-2017, integrated into UniProtKB/TrEMBL. DT 20-DEC-2017, sequence version 1. DT 05-DEC-2018, entry version 5. 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}; DE Short=P-Rib-PP synthase {ECO:0000256|HAMAP-Rule:MF_00583}; DE Short=PRPP synthase {ECO:0000256|HAMAP-Rule:MF_00583}; DE Short=PRPPase {ECO:0000256|HAMAP-Rule:MF_00583}; GN Name=prs {ECO:0000256|HAMAP-Rule:MF_00583}; GN ORFNames=CFE43_19045 {ECO:0000313|EMBL:OYT90294.1}; OS Burkholderiales bacterium PBB3. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales. OX NCBI_TaxID=2015565 {ECO:0000313|EMBL:OYT90294.1, ECO:0000313|Proteomes:UP000216249}; RN [1] {ECO:0000313|EMBL:OYT90294.1, ECO:0000313|Proteomes:UP000216249} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PBB3 {ECO:0000313|EMBL:OYT90294.1}; RA Kojadinovic M., Villain A., Puppo C., Fon Sing S., Prioretti L., RA Hubert P., Gregori G., Zhang Y., Sassi J.-F., Claverie J.-M., RA Blanc G., Gontero B.; RT "A metagenomic investigation of the 'star' freshwater diatom RT Asterionella formosa and its bacterial cohort."; RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases. 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:0000256|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:456215, CC ChEBI:CHEBI:58017, ChEBI:CHEBI:78346; EC=2.7.6.1; CC Evidence={ECO:0000256|HAMAP-Rule:MF_00583, CC ECO:0000256|SAAS:SAAS00956745}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP- CC Rule:MF_00583}; CC Note=Binds 2 Mg(2+) ions 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, ECO:0000256|SAAS:SAAS00956751}. CC -!- SUBUNIT: Homohexamer. {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. Class I subfamily. {ECO:0000256|HAMAP-Rule:MF_00583}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:OYT90294.1}. 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; NKIK01000046; OYT90294.1; -; Genomic_DNA. DR UniPathway; UPA00087; UER00172. DR Proteomes; UP000216249; Unassembled WGS sequence. 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 {ECO:0000256|HAMAP-Rule:MF_00583, KW ECO:0000256|SAAS:SAAS00956731}; KW Complete proteome {ECO:0000313|Proteomes:UP000216249}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00583}; KW Kinase {ECO:0000256|HAMAP-Rule:MF_00583, KW ECO:0000256|SAAS:SAAS00956744, ECO:0000313|EMBL:OYT90294.1}; KW Magnesium {ECO:0000256|HAMAP-Rule:MF_00583, KW ECO:0000256|SAAS:SAAS00956743}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00583, KW ECO:0000256|SAAS:SAAS00956748}; KW Nucleotide biosynthesis {ECO:0000256|HAMAP-Rule:MF_00583, KW ECO:0000256|SAAS:SAAS00956760}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00583, KW ECO:0000256|SAAS:SAAS00956754}; KW Reference proteome {ECO:0000313|Proteomes:UP000216249}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_00583, KW ECO:0000256|SAAS:SAAS00956753, ECO:0000313|EMBL:OYT90294.1}. FT DOMAIN 10 126 Pribosyltran_N. {ECO:0000259|Pfam: FT PF13793}. FT NP_BIND 42 44 ATP. {ECO:0000256|HAMAP-Rule:MF_00583}. FT NP_BIND 101 102 ATP. {ECO:0000256|HAMAP-Rule:MF_00583}. FT REGION 228 232 Ribose-5-phosphate binding. FT {ECO:0000256|HAMAP-Rule:MF_00583}. FT ACT_SITE 198 198 {ECO:0000256|HAMAP-Rule:MF_00583}. FT METAL 136 136 Magnesium. {ECO:0000256|HAMAP-Rule: FT MF_00583}. FT METAL 175 175 Magnesium. {ECO:0000256|HAMAP-Rule: FT MF_00583}. FT BINDING 200 200 Ribose-5-phosphate. {ECO:0000256|HAMAP- FT Rule:MF_00583}. FT BINDING 224 224 Ribose-5-phosphate. {ECO:0000256|HAMAP- FT Rule:MF_00583}. SQ SEQUENCE 325 AA; 35112 MW; 0844537AEF0DA60A CRC64; MQAPNTPDFM VFTGNANPGM AADIAHHLGI SLGAATVGRF SDGEVTVEIN QNVRARDVFV VQSTCAPTNE NLMELLIMVD ALKRASAERI SAVIPYFGYA RQDRRPRSSR VPITAKVVAN MLQAVGVNRV LTMDLHADQI QGFFDIPVDN IYASPVLLGD LRQKNYEDLI VVSPDVGGVV RARALAKQLG CDLAIIDKRR PKANVSEVMH VIGEIEGRNC VIMDDMIDTA GTLVKAAEVL KARGAKKVYA YCTHPIFSGP AIERIANGGA LDEVVVTNTI PLSAAAAECK KIRQLTVAPL IAETIQRIAK GESVMSLFSD QDNLF //