ID G5JUA5_9STRE Unreviewed; 326 AA. AC G5JUA5; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 01-APR-2015, entry version 20. 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_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 -!- 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 -!- 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 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: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 NP_BIND 43 45 ATP. {ECO:0000256|HAMAP-Rule:MF_00583}. FT NP_BIND 102 105 ATP. {ECO:0000256|HAMAP-Rule:MF_00583}. FT REGION 227 234 Ribose-5-phosphate 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}. FT BINDING 110 110 Ribose-5-phosphate. {ECO:0000256|HAMAP- FT Rule:MF_00583}. FT BINDING 136 136 ATP. {ECO:0000256|HAMAP-Rule:MF_00583}. FT BINDING 141 141 ATP. {ECO:0000256|HAMAP-Rule: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 //