ID A0A1Y2SN39_9GAMM Unreviewed; 336 AA. AC A0A1Y2SN39; DT 30-AUG-2017, integrated into UniProtKB/TrEMBL. DT 30-AUG-2017, sequence version 1. DT 02-OCT-2024, entry version 28. 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 ORFNames=Xbed_02221 {ECO:0000313|EMBL:OTA19543.1}; OS Xenorhabdus beddingii. OC Bacteria; Pseudomonadota; 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 combined RT genomic-metabolomic approach."; RL Submitted (JAN-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 (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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {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 AlphaFoldDB; A0A1Y2SN39; -. DR STRING; 40578.Xbed_02221; -. DR UniPathway; UPA00087; UER00172. DR Proteomes; UP000194204; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0002189; C:ribose phosphate diphosphokinase complex; IEA:TreeGrafter. 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-UniRule. DR GO; GO:0006164; P:purine nucleotide biosynthetic process; IEA:TreeGrafter. DR GO; GO:0009156; P:ribonucleoside monophosphate biosynthetic process; IEA:InterPro. 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 NCBIfam; TIGR01251; ribP_PPkin; 1. DR PANTHER; PTHR10210; RIBOSE-PHOSPHATE DIPHOSPHOKINASE FAMILY MEMBER; 1. DR PANTHER; PTHR10210:SF119; RIBOSE-PHOSPHATE PYROPHOSPHOKINASE; 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 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|ARBA:ARBA00022679, ECO:0000256|HAMAP- KW Rule:MF_00583}. FT DOMAIN 25..142 FT /note="Ribose-phosphate pyrophosphokinase N-terminal" FT /evidence="ECO:0000259|Pfam:PF13793" FT ACT_SITE 215 FT /evidence="ECO:0000256|HAMAP-Rule:MF_00583" FT BINDING 58..60 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00583" FT BINDING 117..118 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00583" FT BINDING 152 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00583" FT BINDING 191 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00583" FT BINDING 217 FT /ligand="D-ribose 5-phosphate" FT /ligand_id="ChEBI:CHEBI:78346" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00583" FT BINDING 241 FT /ligand="D-ribose 5-phosphate" FT /ligand_id="ChEBI:CHEBI:78346" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00583" FT BINDING 245..249 FT /ligand="D-ribose 5-phosphate" FT /ligand_id="ChEBI:CHEBI:78346" FT /evidence="ECO:0000256|HAMAP-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 //