ID A0A177P4T1_9RHIZ Unreviewed; 310 AA. AC A0A177P4T1; DT 07-SEP-2016, integrated into UniProtKB/TrEMBL. DT 07-SEP-2016, sequence version 1. DT 05-JUL-2017, entry version 7. 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=A1351_17075 {ECO:0000313|EMBL:OAI25255.1}; OS Methylosinus sp. R-45379. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Methylocystaceae; Methylosinus. OX NCBI_TaxID=980563 {ECO:0000313|EMBL:OAI25255.1, ECO:0000313|Proteomes:UP000078138}; RN [1] {ECO:0000313|EMBL:OAI25255.1, ECO:0000313|Proteomes:UP000078138} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=R-45379 {ECO:0000313|EMBL:OAI25255.1, RC ECO:0000313|Proteomes:UP000078138}; RA Ploux O.; RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases. 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 -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {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:OAI25255.1}. 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; LUUM01000274; OAI25255.1; -; Genomic_DNA. DR EnsemblBacteria; OAI25255; OAI25255; A1351_17075. DR UniPathway; UPA00087; UER00172. DR Proteomes; UP000078138; 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-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 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:UP000078138}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00583}; KW Kinase {ECO:0000256|HAMAP-Rule:MF_00583}; 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:UP000078138}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_00583}. FT DOMAIN 1 117 Pribosyltran_N. {ECO:0000259|Pfam: FT PF13793}. FT NP_BIND 34 36 ATP. {ECO:0000256|HAMAP-Rule:MF_00583}. FT NP_BIND 93 96 ATP. {ECO:0000256|HAMAP-Rule:MF_00583}. FT REGION 190 192 Ribose-5-phosphate binding. FT {ECO:0000256|HAMAP-Rule:MF_00583}. FT REGION 217 224 Ribose-5-phosphate binding. FT {ECO:0000256|HAMAP-Rule:MF_00583}. FT REGION 304 306 Ribose-5-phosphate binding. FT {ECO:0000256|HAMAP-Rule:MF_00583}. FT METAL 125 125 Magnesium. {ECO:0000256|HAMAP-Rule: FT MF_00583}. FT METAL 127 127 Magnesium. {ECO:0000256|HAMAP-Rule: FT MF_00583}. FT METAL 136 136 Magnesium. {ECO:0000256|HAMAP-Rule: FT MF_00583}. FT METAL 140 140 Magnesium. {ECO:0000256|HAMAP-Rule: FT MF_00583}. FT BINDING 101 101 Ribose-5-phosphate. {ECO:0000256|HAMAP- FT Rule:MF_00583}. FT BINDING 127 127 ATP. {ECO:0000256|HAMAP-Rule:MF_00583}. FT BINDING 132 132 ATP. {ECO:0000256|HAMAP-Rule:MF_00583}. FT BINDING 167 167 Ribose-5-phosphate. {ECO:0000256|HAMAP- FT Rule:MF_00583}. SQ SEQUENCE 310 AA; 32985 MW; 2AFC61173EF64E0D CRC64; MKILAGNSNR ALAETIAAYV GVPLCRAQVR RFADMEVFVE IQENVRGQDT FVVQSTSAPS NDHLMELLIM IDALRRASAR RITAVIPYFG YARQDRKGTS RTPISAKLVA NLITRAGADR VLTVDLHAGQ IQGFFDIPTD NLFAAPVMVA DIKSHAKVPN AMVVSPDTGG VVRARALAKR IDAPLAIVDK RRERAGESEV MNIIGDVSGR NCILVDDIVD SGGTLCNAAE ALLAQGATSV SAYITHGVLS GAAAERVAAS KLKELVLTDT IAATPAVQGA RNIRFIPIGP LIGEAIARTA REESVSSLFD //