ID A0A0W8GYC9_ACIJO Unreviewed; 317 AA. AC A0A0W8GYC9; DT 16-MAR-2016, integrated into UniProtKB/TrEMBL. DT 16-MAR-2016, sequence version 1. DT 18-JAN-2017, entry version 9. 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=AAU60_11580 {ECO:0000313|EMBL:KUG38169.1}; OS Acinetobacter johnsonii. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Moraxellaceae; Acinetobacter. OX NCBI_TaxID=40214 {ECO:0000313|EMBL:KUG38169.1, ECO:0000313|Proteomes:UP000053042}; RN [1] {ECO:0000313|EMBL:KUG38169.1, ECO:0000313|Proteomes:UP000053042} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MB44 {ECO:0000313|EMBL:KUG38169.1, RC ECO:0000313|Proteomes:UP000053042}; RA Tian S., Xie L., Ali M., Sun X., Li L.; RT "Sequencing and comparative genomics of Acinetobacter johnsonii RT MB44."; RL Submitted (APR-2015) 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:KUG38169.1}. 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; LBMO01000043; KUG38169.1; -; Genomic_DNA. DR RefSeq; WP_004695513.1; NZ_LVIB01000002.1. DR ProteinModelPortal; A0A0W8GYC9; -. DR EnsemblBacteria; KUG38169; KUG38169; AAU60_11580. DR GeneID; 29886849; -. DR UniPathway; UPA00087; UER00172. DR Proteomes; UP000053042; 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 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:UP000053042}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00583}; KW Kinase {ECO:0000256|HAMAP-Rule:MF_00583, ECO:0000313|EMBL:KUG38169.1}; 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:KUG38169.1}. FT DOMAIN 4 121 Pribosyltran_N. {ECO:0000259|Pfam: FT PF13793}. FT NP_BIND 37 39 ATP. {ECO:0000256|HAMAP-Rule:MF_00583}. FT NP_BIND 96 99 ATP. {ECO:0000256|HAMAP-Rule:MF_00583}. FT REGION 194 196 Ribose-5-phosphate binding. FT {ECO:0000256|HAMAP-Rule:MF_00583}. FT REGION 221 228 Ribose-5-phosphate binding. FT {ECO:0000256|HAMAP-Rule:MF_00583}. FT REGION 308 310 Ribose-5-phosphate binding. FT {ECO:0000256|HAMAP-Rule:MF_00583}. FT METAL 129 129 Magnesium. {ECO:0000256|HAMAP-Rule: FT MF_00583}. FT METAL 131 131 Magnesium. {ECO:0000256|HAMAP-Rule: FT MF_00583}. FT METAL 140 140 Magnesium. {ECO:0000256|HAMAP-Rule: FT MF_00583}. FT METAL 144 144 Magnesium. {ECO:0000256|HAMAP-Rule: FT MF_00583}. FT BINDING 105 105 Ribose-5-phosphate. {ECO:0000256|HAMAP- FT Rule:MF_00583}. FT BINDING 131 131 ATP. {ECO:0000256|HAMAP-Rule:MF_00583}. FT BINDING 136 136 ATP. {ECO:0000256|HAMAP-Rule:MF_00583}. FT BINDING 170 170 Ribose-5-phosphate. {ECO:0000256|HAMAP- FT Rule:MF_00583}. SQ SEQUENCE 317 AA; 34357 MW; E4DBC7355FA0A3EE CRC64; MPNLVVFSGS AHPQFAQKVV SHLHIPLGAA SIGQFSDGEI AVEITENVRG KDVFIVQPTC APTNDNLMEI LVMADALRRA SAGRITAVIP YFGYARQDRR PRSSRVPITA KVVADMLTTV GIDRVVMIDL HADQIQGFFD IPVDNIYGTP ALLADLRQQS HDNLMVVSPD VGGVVRARAV AKQMGDIDLA IIDKRRQKAN ESQVMHLIGD VKGRDCVIVD DMVDTAGTLC KAADALKTFG ARKVVAYATH PVLSGKAIEN LKNSVIDELV VTDTIPLSEE AQALGKIRQV SVASMVAETI RRINNEESIS AMFDSYL //