ID A0A1Y2SN39_9GAMM Unreviewed; 336 AA. AC A0A1Y2SN39; DT 30-AUG-2017, integrated into UniProtKB/TrEMBL. DT 30-AUG-2017, sequence version 1. DT 25-OCT-2017, entry version 3. 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=Xbed_02221 {ECO:0000313|EMBL:OTA19543.1}; OS Xenorhabdus beddingii. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; OC Morganellaceae; Xenorhabdus. OX NCBI_TaxID=40578 {ECO:0000313|EMBL:OTA19543.1, ECO:0000313|Proteomes:UP000194204}; RN [1] {ECO:0000313|EMBL:OTA19543.1, ECO:0000313|Proteomes:UP000194204} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 4764 {ECO:0000313|EMBL:OTA19543.1, RC ECO:0000313|Proteomes:UP000194204}; RA Tobias N.J., Wolff H., Djahanschiri B., Ebersberger I., Bode H.B.; RT "Deconstructing symbiosis and pathogenesis requirements using a RT combined genomic-metabolomic approach."; RL Submitted (JAN-2017) 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:OTA19543.1}. 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; MUBK01000017; OTA19543.1; -; Genomic_DNA. DR UniPathway; UPA00087; UER00172. DR Proteomes; UP000194204; 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 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:UP000194204}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00583}; KW Kinase {ECO:0000256|HAMAP-Rule:MF_00583, ECO:0000313|EMBL:OTA19543.1}; 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 Reference proteome {ECO:0000313|Proteomes:UP000194204}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_00583, KW ECO:0000313|EMBL:OTA19543.1}. FT DOMAIN 25 142 Pribosyltran_N. {ECO:0000259|Pfam: FT PF13793}. FT NP_BIND 58 60 ATP. {ECO:0000256|HAMAP-Rule:MF_00583}. FT NP_BIND 117 120 ATP. {ECO:0000256|HAMAP-Rule:MF_00583}. FT REGION 215 217 Ribose-5-phosphate binding. FT {ECO:0000256|HAMAP-Rule:MF_00583}. FT REGION 242 249 Ribose-5-phosphate binding. FT {ECO:0000256|HAMAP-Rule:MF_00583}. FT REGION 329 331 Ribose-5-phosphate binding. FT {ECO:0000256|HAMAP-Rule:MF_00583}. FT METAL 150 150 Magnesium. {ECO:0000256|HAMAP-Rule: FT MF_00583}. FT METAL 152 152 Magnesium. {ECO:0000256|HAMAP-Rule: FT MF_00583}. FT METAL 161 161 Magnesium. {ECO:0000256|HAMAP-Rule: FT MF_00583}. FT METAL 165 165 Magnesium. {ECO:0000256|HAMAP-Rule: FT MF_00583}. FT BINDING 126 126 Ribose-5-phosphate. {ECO:0000256|HAMAP- FT Rule:MF_00583}. FT BINDING 152 152 ATP. {ECO:0000256|HAMAP-Rule:MF_00583}. FT BINDING 157 157 ATP. {ECO:0000256|HAMAP-Rule:MF_00583}. FT BINDING 191 191 Ribose-5-phosphate. {ECO:0000256|HAMAP- FT Rule:MF_00583}. SQ SEQUENCE 336 AA; 36645 MW; 5DB070A126D67768 CRC64; MSNVCLIGQQ YLSGRKPEVY PVPDMKLFAG NATPELAQRV ANRLYTSLGD AAVGRFSDGE VSVQINENVR GGDVFIIQST CAPTNDNLME LVVMVDALRR ASAGRITAVI PYFGYARQDR RVRSARVPIT AKVVADFLSS VGVDRVLTVD LHAEQIQGFF DVPVDNVFGS PILLEDMLQQ DLENPIVVSP DIGGVVRARA IAKLLNDTDM AIIDKRRPRA NVSQVMHIIG DVAGRDCVLV DDMIDTGGTL CKAAEALKER GAKRVFAYAT HPIFSGNAVE NIKNSVIDEF IVCDTIPLSD EIKALNKVRT LTLSGMLAEA IRRISNEESI SAMFEH //