ID A0A257CMJ3_9BURK Unreviewed; 325 AA. AC A0A257CMJ3; DT 20-DEC-2017, integrated into UniProtKB/TrEMBL. DT 20-DEC-2017, sequence version 1. DT 25-MAY-2022, entry version 13. 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., Hubert P., RA Gregori G., Zhang Y., Sassi J.-F., Claverie J.-M., Blanc G., Gontero B.; RT "A metagenomic investigation of the 'star' freshwater diatom Asterionella RT 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 (Rib- CC 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, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:58017, ChEBI:CHEBI:78346, CC ChEBI:CHEBI:456215; EC=2.7.6.1; Evidence={ECO:0000256|HAMAP- CC Rule:MF_00583}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|HAMAP-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-ribose CC 1-diphosphate biosynthesis; 5-phospho-alpha-D-ribose 1-diphosphate from CC D-ribose 5-phosphate (route I): step 1/1. {ECO:0000256|HAMAP- CC Rule:MF_00583}. 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 family. CC Class I subfamily. {ECO:0000256|HAMAP-Rule:MF_00583}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {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 EnsemblBacteria; OYT90294; OYT90294; CFE43_19045. 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: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 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; 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|ARBA:ARBA00022840, ECO:0000256|HAMAP- KW Rule:MF_00583}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00583}; KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|HAMAP-Rule:MF_00583}; KW Magnesium {ECO:0000256|HAMAP-Rule:MF_00583}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP- KW Rule:MF_00583}; KW Nucleotide biosynthesis {ECO:0000256|ARBA:ARBA00022727, ECO:0000256|HAMAP- KW Rule:MF_00583}; Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00583}; KW Reference proteome {ECO:0000313|Proteomes:UP000216249}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP- KW Rule:MF_00583}. FT DOMAIN 10..126 FT /note="Pribosyltran_N" FT /evidence="ECO:0000259|Pfam:PF13793" FT NP_BIND 42..44 FT /note="ATP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00583" FT NP_BIND 101..102 FT /note="ATP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00583" FT REGION 228..232 FT /note="Ribose-5-phosphate binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00583" FT ACT_SITE 198 FT /evidence="ECO:0000256|HAMAP-Rule:MF_00583" FT METAL 136 FT /note="Magnesium" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00583" FT METAL 175 FT /note="Magnesium" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00583" FT BINDING 200 FT /note="Ribose-5-phosphate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00583" FT BINDING 224 FT /note="Ribose-5-phosphate" FT /evidence="ECO:0000256|HAMAP-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 //