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-JUL-2018, entry version 17. 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 ECO:0000313|EMBL:SJX22280.1}; GN ORFNames=AAU60_11580 {ECO:0000313|EMBL:KUG38169.1}, ACNJC6_01913 GN {ECO:0000313|EMBL:SJX22280.1}, AJ0707_01193 GN {ECO:0000313|EMBL:SNU13768.1}; 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|Proteomes:UP000053042} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MB44 {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. RN [2] {ECO:0000313|EMBL:KUG38169.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=MB44 {ECO:0000313|EMBL:KUG38169.1}; RX PubMed=26893438; RA Tian S., Ali M., Xie L., Li L.; RT "Draft Genome Sequence of Acinetobacter johnsonii MB44, Exhibiting RT Nematicidal Activity against Caenorhabditis elegans."; RL Genome Announc. 4:e01772-15(2016). RN [3] {ECO:0000313|EMBL:SJX22280.1, ECO:0000313|Proteomes:UP000196240} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C6 {ECO:0000313|EMBL:SJX22280.1}; RA Peterson S.W.; RL Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases. RN [4] {ECO:0000313|EMBL:SNU13768.1, ECO:0000313|Proteomes:UP000214633} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AJ01M {ECO:0000313|EMBL:SNU13768.1}; RA Sun Z.S., Albrecht U., Echele G., Lee C.C.; RL Submitted (JUL-2017) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Involved in the biosynthesis of the central metabolite CC phospho-alpha-D-ribosyl-1-pyrophosphate (PRPP) via the transfer of CC pyrophosphoryl group from ATP to 1-hydroxyl of ribose-5-phosphate CC (Rib-5-P). {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 ECO:0000256|SAAS:SAAS00956745}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP- CC Rule:MF_00583}; CC Note=Binds 2 Mg(2+) ions 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, ECO:0000256|SAAS:SAAS00956751}. CC -!- SUBUNIT: Homohexamer. {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. Class I subfamily. {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; LBMO01000043; KUG38169.1; -; Genomic_DNA. DR EMBL; FUUY01000005; SJX22280.1; -; Genomic_DNA. DR EMBL; FZRG01000008; SNU13768.1; -; Genomic_DNA. DR RefSeq; WP_004695513.1; NZ_LVIB01000002.1. DR ProteinModelPortal; A0A0W8GYC9; -. DR EnsemblBacteria; KUG38169; KUG38169; AAU60_11580. DR GeneID; 29886849; -. DR PATRIC; fig|40214.16.peg.2361; -. DR UniPathway; UPA00087; UER00172. DR Proteomes; UP000053042; Unassembled WGS sequence. DR Proteomes; UP000196240; Unassembled WGS sequence. DR Proteomes; UP000214633; 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-UniRule. DR GO; GO:0004749; F:ribose phosphate diphosphokinase activity; IEA:UniProtKB-UniRule. 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-UniRule. 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 InterPro; IPR037515; Rib-P_diPkinase_bac. DR PANTHER; PTHR10210; PTHR10210; 1. 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 ECO:0000256|SAAS:SAAS00956731}; KW Complete proteome {ECO:0000313|Proteomes:UP000053042, KW ECO:0000313|Proteomes:UP000196240, ECO:0000313|Proteomes:UP000214633}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00583}; KW Kinase {ECO:0000256|HAMAP-Rule:MF_00583, KW ECO:0000256|SAAS:SAAS00956744, ECO:0000313|EMBL:KUG38169.1}; KW Magnesium {ECO:0000256|HAMAP-Rule:MF_00583, KW ECO:0000256|SAAS:SAAS00956743}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00583, KW ECO:0000256|SAAS:SAAS00956748}; KW Nucleotide biosynthesis {ECO:0000256|HAMAP-Rule:MF_00583, KW ECO:0000256|SAAS:SAAS00956760}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00583, KW ECO:0000256|SAAS:SAAS00956754}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_00583, KW ECO:0000256|SAAS:SAAS00956753, 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 97 ATP. {ECO:0000256|HAMAP-Rule:MF_00583}. FT REGION 224 228 Ribose-5-phosphate binding. FT {ECO:0000256|HAMAP-Rule:MF_00583}. FT ACT_SITE 194 194 {ECO:0000256|HAMAP-Rule:MF_00583}. FT METAL 131 131 Magnesium. {ECO:0000256|HAMAP-Rule: FT MF_00583}. FT METAL 170 170 Magnesium. {ECO:0000256|HAMAP-Rule: FT MF_00583}. FT BINDING 196 196 Ribose-5-phosphate. {ECO:0000256|HAMAP- FT Rule:MF_00583}. FT BINDING 220 220 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 //