ID K7RV53_ACIA4 Unreviewed; 322 AA. AC K7RV53; DT 06-FEB-2013, integrated into UniProtKB/TrEMBL. DT 06-FEB-2013, sequence version 1. DT 15-FEB-2017, entry version 30. 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 OrderedLocusNames=PACID_09940 {ECO:0000313|EMBL:AFV88828.1}; OS Acidipropionibacterium acidipropionici (strain ATCC 4875 / DSM 20272 / OS JCM 6432 / NBRC 12425 / NCIMB 8070) (Propionibacterium OS acidipropionici). OC Bacteria; Actinobacteria; Propionibacteriales; Propionibacteriaceae; OC Acidipropionibacterium. OX NCBI_TaxID=1171373 {ECO:0000313|EMBL:AFV88828.1, ECO:0000313|Proteomes:UP000000214}; RN [1] {ECO:0000313|EMBL:AFV88828.1, ECO:0000313|Proteomes:UP000000214} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 4875 / DSM 20272 / JCM 6432 / NBRC 12425 / NCIMB 8070 RC {ECO:0000313|Proteomes:UP000000214}; RX PubMed=23083487; DOI=10.1186/1471-2164-13-562; RA Parizzi L.P., Grassi M.C., Llerena L.A., Carazzolle M.F., RA Queiroz V.L., Lunardi I., Zeidler A.F., Teixeira P.J., Mieczkowski P., RA Rincones J., Pereira G.A.; RT "The genome sequence of Propionibacterium acidipropionici provides RT insights into its biotechnological and industrial potential."; RL BMC Genomics 13:562-562(2012). 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; CP003493; AFV88828.1; -; Genomic_DNA. DR ProteinModelPortal; K7RV53; -. DR EnsemblBacteria; AFV88828; AFV88828; PACID_09940. DR KEGG; pbo:PACID_09940; -. DR KO; K00948; -. DR OMA; DGEIMVE; -. DR OrthoDB; POG091H018X; -. DR UniPathway; UPA00087; UER00172. DR Proteomes; UP000000214; Chromosome. 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: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-HAMAP. 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 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 Complete proteome {ECO:0000313|Proteomes:UP000000214}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00583}; KW Kinase {ECO:0000256|HAMAP-Rule:MF_00583, ECO:0000313|EMBL:AFV88828.1}; 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:UP000000214}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_00583, KW ECO:0000313|EMBL:AFV88828.1}. FT DOMAIN 13 128 Pribosyltran_N. {ECO:0000259|Pfam: FT PF13793}. FT NP_BIND 45 47 ATP. {ECO:0000256|HAMAP-Rule:MF_00583}. FT NP_BIND 104 107 ATP. {ECO:0000256|HAMAP-Rule:MF_00583}. FT NP_BIND 151 152 ATP. {ECO:0000256|HAMAP-Rule:MF_00583}. FT REGION 201 203 Ribose-5-phosphate binding. FT {ECO:0000256|HAMAP-Rule:MF_00583}. FT REGION 230 237 Ribose-5-phosphate binding. FT {ECO:0000256|HAMAP-Rule:MF_00583}. FT REGION 316 318 Ribose-5-phosphate binding. FT {ECO:0000256|HAMAP-Rule:MF_00583}. FT METAL 136 136 Magnesium. {ECO:0000256|HAMAP-Rule: FT MF_00583}. FT METAL 138 138 Magnesium. {ECO:0000256|HAMAP-Rule: FT MF_00583}. FT METAL 147 147 Magnesium. {ECO:0000256|HAMAP-Rule: FT MF_00583}. FT METAL 151 151 Magnesium. {ECO:0000256|HAMAP-Rule: FT MF_00583}. FT BINDING 112 112 Ribose-5-phosphate. {ECO:0000256|HAMAP- FT Rule:MF_00583}. FT BINDING 138 138 ATP. {ECO:0000256|HAMAP-Rule:MF_00583}. FT BINDING 143 143 ATP. {ECO:0000256|HAMAP-Rule:MF_00583}. FT BINDING 178 178 Ribose-5-phosphate. {ECO:0000256|HAMAP- FT Rule:MF_00583}. SQ SEQUENCE 322 AA; 35018 MW; 2BD26BECC263B671 CRC64; MSGATRPNNK HLMLCSGRAY PELAEEIGKE LGVELVPSRQ VTYANSEIYV QFEESVRGCD AFVVQSHCAP VNEAMMEQLI MVDALKRASA KRITVVAPFY PYARQDKKHL GREPISARLM ADLFTAAGAD RIMAVDLHAA QIQGFFDGPV DHLWALPVLS DYVKDKYGQE DIVVVSPDAG RVRLADQWTD KLGCQLAIIH KRRDPNKANE ATTHEVVGKV KGKTCILVDD MIDTAGTICQ AAKALEDHGA TKVIAAATHP VLSGPAADRI NASPIQELVV TNTLQVPDGV EIPKMTVLSI APLIAKAIQQ VFEDGSVAQL FR //