ID G5JUA5_9STRE Unreviewed; 326 AA. AC G5JUA5; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 26-NOV-2014, entry version 18. 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=Phosphoribosyl pyrophosphate synthase {ECO:0000256|HAMAP-Rule:MF_00583}; GN Name=prs_1 {ECO:0000313|EMBL:EHJ51729.1}; GN Synonyms=prs {ECO:0000256|HAMAP-Rule:MF_00583}; GN ORFNames=STRMA_0646 {ECO:0000313|EMBL:EHJ51729.1}; OS Streptococcus macacae NCTC 11558. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=764298 {ECO:0000313|EMBL:EHJ51729.1}; RN [1] {ECO:0000313|EMBL:EHJ51729.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=NCTC 11558 {ECO:0000313|EMBL:EHJ51729.1}; RX PubMed=24625962; DOI=10.1093/gbe/evu048; RA Richards V.P., Palmer S.R., Pavinski Bitar P.D., Qin X., RA Weinstock G.M., Highlander S.K., Town C.D., Burne R.A., Stanhope M.J.; RT "Phylogenomics and the dynamic genome evolution of the genus RT Streptococcus."; RL Genome Biol. Evol. 6:741-753(2014). 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 Note=Binds 1 magnesium 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 -!- 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:EHJ51729.1}. 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; AEUW02000001; EHJ51729.1; -; Genomic_DNA. DR ProteinModelPortal; G5JUA5; -. DR EnsemblBacteria; EHJ51729; EHJ51729; STRMA_0646. DR UniPathway; UPA00087; UER00172. 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 Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00583}; KW Kinase {ECO:0000256|HAMAP-Rule:MF_00583, ECO:0000313|EMBL:EHJ51729.1}; 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 Transferase {ECO:0000256|HAMAP-Rule:MF_00583, KW ECO:0000313|EMBL:EHJ51729.1}. FT REGION 219 232 5-phosphoribose 1-diphosphate binding. FT {ECO:0000256|HAMAP-Rule:MF_00583}. FT METAL 134 134 Magnesium. {ECO:0000256|HAMAP-Rule: FT MF_00583}. FT METAL 136 136 Magnesium. {ECO:0000256|HAMAP-Rule: FT MF_00583}. FT METAL 145 145 Magnesium. {ECO:0000256|HAMAP-Rule: FT MF_00583}. FT METAL 149 149 Magnesium. {ECO:0000256|HAMAP-Rule: FT MF_00583}. SQ SEQUENCE 326 AA; 35602 MW; 91DAF21FC9F0BC4A CRC64; MLNACSDKQL KLFSLTSNTA IAEKIAEAAG LPLGKLSSRQ FSDGEIMINI EESVRGSDIY IIQSTSNPVN DHLWELLIMV DACKRASANS VNVVIPYFGY SRQDRIAAAR EPITAKLVAN MLVKAGVDRV LTLDLHTVQV QGFFDIPVDN LFTIPLFAKH YIQQGLFGEE VVVVSPKNSG IKRARSLAQY LDAPIAIIDY AQDDDSLREE GYIIGEVEGK KAILIDDILN TGKTFAEASK IVERGGATDI YAVASHGLFA GGATEMLQSA PIKDILITDS VCTNEKLPDN VHYLSASKLI ADAIIRIQER KPLSPLFAYD RKGDES //