ID A0A0W8GYC9_ACIJO Unreviewed; 317 AA. AC A0A0W8GYC9; DT 16-MAR-2016, integrated into UniProtKB/TrEMBL. DT 16-MAR-2016, sequence version 1. DT 28-JUN-2023, entry version 42. 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 synthase {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:GEK45576.1}; GN ORFNames=ACNJC6_01913 {ECO:0000313|EMBL:SJX22280.1}, AJ0707_01193 GN {ECO:0000313|EMBL:SNU13768.1}, AJO04nite_28340 GN {ECO:0000313|EMBL:GEK45576.1}, CFH90_12925 GN {ECO:0000313|EMBL:AZN64879.1}, DI542_15925 GN {ECO:0000313|EMBL:PZQ85565.1}, E0Z08_14080 GN {ECO:0000313|EMBL:QBK70576.1}, EGT73_01370 GN {ECO:0000313|EMBL:RSE26926.1}, FYN22_03840 GN {ECO:0000313|EMBL:QEK35054.1}, H0S57_12655 GN {ECO:0000313|EMBL:QPF34300.1}, I6G67_03860 GN {ECO:0000313|EMBL:QPS04633.1}, NCTC10308_01989 GN {ECO:0000313|EMBL:SUT96321.1}; OS Acinetobacter johnsonii. OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae; OC Acinetobacter. OX NCBI_TaxID=40214 {ECO:0000313|EMBL:PZQ85565.1, ECO:0000313|Proteomes:UP000249282}; RN [1] {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 [2] {ECO:0000313|EMBL:AZN64879.1, ECO:0000313|Proteomes:UP000276980} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=IC001 {ECO:0000313|EMBL:AZN64879.1, RC ECO:0000313|Proteomes:UP000276980}; RA Vejarano F., Suzuki-Minakuchi C., Ohtsubo Y., Tsuda M., Okada K., RA Nojiri H.; RT "Complete Genome Sequence of the Carbazole-Degrading Bacterium RT Acinetobacter johnsonii IC001."; RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases. RN [3] {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. RN [4] {ECO:0000313|EMBL:PZQ85565.1, ECO:0000313|Proteomes:UP000249282} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=S2_003_000_R3_20 {ECO:0000313|EMBL:PZQ85565.1}; RA Brooks B., Olm M.R., Firek B.A., Baker R., Thomas B.C., Morowitz M.J., RA Banfield J.F.; RT "Infants hospitalized years apart are colonized by the same room-sourced RT microbial strains."; RL Submitted (NOV-2017) to the EMBL/GenBank/DDBJ databases. RN [5] {ECO:0000313|EMBL:SUT96321.1, ECO:0000313|Proteomes:UP000254227} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NCTC10308 {ECO:0000313|EMBL:SUT96321.1, RC ECO:0000313|Proteomes:UP000254227}; RG Pathogen Informatics; RA Doyle S.; RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases. RN [6] {ECO:0000313|EMBL:RSE26926.1, ECO:0000313|Proteomes:UP000277537} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AJ_385 {ECO:0000313|EMBL:RSE26926.1, RC ECO:0000313|Proteomes:UP000277537}; RA D'Souza A.W., Potter R.F., Wallace M., Shupe A., Patel S., Sun S., Gul D., RA Kwon J.H., Andleeb S., Burnham C.-A.D., Dantas G.; RT "Transmission dynamics of multidrug resistant bacteria on intensive care RT unit surfaces."; RL Submitted (OCT-2018) to the EMBL/GenBank/DDBJ databases. RN [7] {ECO:0000313|EMBL:QBK70576.1, ECO:0000313|Proteomes:UP000292325} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=M19 {ECO:0000313|EMBL:QBK70576.1, RC ECO:0000313|Proteomes:UP000292325}; RA Cao G.; RT "Complete genome sequence of Acinetobacter johnsonii M19."; RL Submitted (MAR-2019) to the EMBL/GenBank/DDBJ databases. RN [8] {ECO:0000313|EMBL:GEK45576.1, ECO:0000313|Proteomes:UP000321274} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NBRC 102197 {ECO:0000313|EMBL:GEK45576.1, RC ECO:0000313|Proteomes:UP000321274}; RA Hosoyama A., Uohara A., Ohji S., Ichikawa N.; RT "Whole genome shotgun sequence of Acinetobacter johnsonii NBRC 102197."; RL Submitted (JUL-2019) to the EMBL/GenBank/DDBJ databases. RN [9] {ECO:0000313|EMBL:QEK35054.1, ECO:0000313|Proteomes:UP000323467} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Acsw19 {ECO:0000313|EMBL:QEK35054.1, RC ECO:0000313|Proteomes:UP000323467}; RA Zhou Y., Tang L.; RT "Whole-genome analysis of two copies of blaNDM-1 gene carrying RT Acinetobacter johnsonii Acsw19 strain isolated from Sichuan."; RL Submitted (AUG-2019) to the EMBL/GenBank/DDBJ databases. RN [10] {ECO:0000313|EMBL:QPF34300.1, ECO:0000313|Proteomes:UP000594629} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=E10B {ECO:0000313|EMBL:QPF34300.1, RC ECO:0000313|Proteomes:UP000594629}; RA Ghaly T.M., Sajjad A., Tetu S.G., Gillings M.R.; RT "A family of multi-drug resistance mega-plasmids in Acinetobacter RT species."; RL Submitted (JUL-2020) to the EMBL/GenBank/DDBJ databases. RN [11] {ECO:0000313|EMBL:QPS04633.1, ECO:0000313|Proteomes:UP000595107} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=FDAARGOS_910 {ECO:0000313|EMBL:QPS04633.1, RC ECO:0000313|Proteomes:UP000595107}; RA Sproer C., Gronow S., Severitt S., Schroder I., Tallon L., Sadzewicz L., RA Zhao X., Boylan J., Ott S., Bowen H., Vavikolanu K., Mehta A., RA Aluvathingal J., Nadendla S., Lowell S., Myers T., Yan Y., Sichtig H.; RT "FDA dAtabase for Regulatory Grade micrObial Sequences (FDA-ARGOS): RT Supporting development and validation of Infectious Disease Dx tests."; RL Submitted (DEC-2020) 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 (Rib- CC 5-P). {ECO:0000256|HAMAP-Rule:MF_00583}. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + D-ribose 5-phosphate = 5-phospho-alpha-D-ribose 1- CC diphosphate + AMP + H(+); Xref=Rhea:RHEA:15609, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:58017, ChEBI:CHEBI:78346, CC ChEBI:CHEBI:456215; EC=2.7.6.1; Evidence={ECO:0000256|HAMAP- CC Rule:MF_00583}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|HAMAP-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-ribose CC 1-diphosphate biosynthesis; 5-phospho-alpha-D-ribose 1-diphosphate from CC D-ribose 5-phosphate (route I): step 1/1. {ECO:0000256|HAMAP- CC Rule:MF_00583}. 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 family. CC 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; CP022298; AZN64879.1; -; Genomic_DNA. DR EMBL; BJUJ01000125; GEK45576.1; -; Genomic_DNA. DR EMBL; QFQJ01000118; PZQ85565.1; -; Genomic_DNA. DR EMBL; CP037424; QBK70576.1; -; Genomic_DNA. DR EMBL; CP043307; QEK35054.1; -; Genomic_DNA. DR EMBL; CP059080; QPF34300.1; -; Genomic_DNA. DR EMBL; CP065666; QPS04633.1; -; Genomic_DNA. DR EMBL; RHXE01000002; RSE26926.1; -; Genomic_DNA. DR EMBL; FUUY01000005; SJX22280.1; -; Genomic_DNA. DR EMBL; FZRG01000008; SNU13768.1; -; Genomic_DNA. DR EMBL; UFRV01000006; SUT96321.1; -; Genomic_DNA. DR RefSeq; WP_004695513.1; NZ_WURO01000002.1. DR AlphaFoldDB; A0A0W8GYC9; -. DR EnsemblBacteria; AZN64879; AZN64879; CFH90_12925. DR EnsemblBacteria; PZQ85565; PZQ85565; DI542_15925. DR EnsemblBacteria; QBK70576; QBK70576; E0Z08_14080. DR EnsemblBacteria; SJX22280; SJX22280; ACNJC6_01913. DR EnsemblBacteria; SNU13768; SNU13768; AJ0707_01193. DR EnsemblBacteria; SUT96321; SUT96321; NCTC10308_01989. DR GeneID; 56339682; -. DR UniPathway; UPA00087; UER00172. DR Proteomes; UP000196240; Unassembled WGS sequence. DR Proteomes; UP000214633; Unassembled WGS sequence. DR Proteomes; UP000249282; Unassembled WGS sequence. DR Proteomes; UP000254227; Unassembled WGS sequence. DR Proteomes; UP000276980; Chromosome. DR Proteomes; UP000277537; Unassembled WGS sequence. DR Proteomes; UP000292325; Chromosome. DR Proteomes; UP000321274; Unassembled WGS sequence. DR Proteomes; UP000323467; Chromosome. DR Proteomes; UP000594629; Chromosome. DR Proteomes; UP000595107; Chromosome. 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:0009165; P:nucleotide biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW. DR GO; GO:0009156; P:ribonucleoside monophosphate biosynthetic process; IEA:UniProtKB-UniRule. 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 InterPro; IPR037515; Rib-P_diPkinase_bac. DR PANTHER; PTHR10210; RIBOSE-PHOSPHATE DIPHOSPHOKINASE FAMILY MEMBER; 1. DR PANTHER; PTHR10210:SF41; RIBOSE-PHOSPHATE PYROPHOSPHOKINASE 5, CHLOROPLASTIC; 1. DR Pfam; PF14572; Pribosyl_synth; 1. DR Pfam; PF13793; Pribosyltran_N; 1. DR SMART; SM01400; Pribosyltran_N; 1. DR SUPFAM; SSF53271; PRTase-like; 1. DR TIGRFAMs; TIGR01251; ribP_PPkin; 1. DR PROSITE; PS00114; PRPP_SYNTHASE; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP- KW Rule:MF_00583}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00583}; KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|HAMAP-Rule:MF_00583}; KW Magnesium {ECO:0000256|HAMAP-Rule:MF_00583}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP- KW Rule:MF_00583}; KW Nucleotide biosynthesis {ECO:0000256|ARBA:ARBA00022727, ECO:0000256|HAMAP- KW Rule:MF_00583}; Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00583}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_00583, ECO:0000313|EMBL:PZQ85565.1}. FT DOMAIN 4..121 FT /note="Ribose-phosphate pyrophosphokinase N-terminal" FT /evidence="ECO:0000259|Pfam:PF13793" FT ACT_SITE 194 FT /evidence="ECO:0000256|HAMAP-Rule:MF_00583" FT BINDING 37..39 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00583" FT BINDING 96..97 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00583" FT BINDING 131 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00583" FT BINDING 170 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00583" FT BINDING 196 FT /ligand="D-ribose 5-phosphate" FT /ligand_id="ChEBI:CHEBI:78346" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00583" FT BINDING 220 FT /ligand="D-ribose 5-phosphate" FT /ligand_id="ChEBI:CHEBI:78346" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00583" FT BINDING 224..228 FT /ligand="D-ribose 5-phosphate" FT /ligand_id="ChEBI:CHEBI:78346" FT /evidence="ECO:0000256|HAMAP-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 //