ID A0A7T4QZT1_9GAMM Unreviewed; 314 AA. AC A0A7T4QZT1; DT 29-SEP-2021, integrated into UniProtKB/TrEMBL. DT 29-SEP-2021, sequence version 1. DT 25-MAY-2022, 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=I6N98_15060 {ECO:0000313|EMBL:QQD17652.1}; OS Spongiibacter nanhainus. OC Bacteria; Proteobacteria; Gammaproteobacteria; Cellvibrionales; OC Spongiibacteraceae; Spongiibacter. OX NCBI_TaxID=2794344 {ECO:0000313|EMBL:QQD17652.1, ECO:0000313|Proteomes:UP000596063}; RN [1] {ECO:0000313|EMBL:QQD17652.1, ECO:0000313|Proteomes:UP000596063} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=csc3.9 {ECO:0000313|Proteomes:UP000596063}; RA Shan Y.; 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; CP066167; QQD17652.1; -; Genomic_DNA. DR UniPathway; UPA00087; UER00172. DR Proteomes; UP000596063; Chromosome. DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW. DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro. DR GO; GO:0004749; F:ribose phosphate diphosphokinase activity; IEA:InterPro. DR GO; GO:0009165; P:nucleotide biosynthetic process; IEA:InterPro. 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 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|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 Reference proteome {ECO:0000313|Proteomes:UP000596063}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP- KW Rule:MF_00583}. FT DOMAIN 4..121 FT /note="Pribosyltran_N" FT /evidence="ECO:0000259|Pfam:PF13793" FT NP_BIND 37..39 FT /note="ATP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00583" FT NP_BIND 96..97 FT /note="ATP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00583" FT REGION 224..228 FT /note="Ribose-5-phosphate binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00583" FT ACT_SITE 194 FT /evidence="ECO:0000256|HAMAP-Rule:MF_00583" FT METAL 131 FT /note="Magnesium" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00583" FT METAL 170 FT /note="Magnesium" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00583" FT BINDING 196 FT /note="Ribose-5-phosphate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00583" FT BINDING 220 FT /note="Ribose-5-phosphate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00583" SQ SEQUENCE 314 AA; 33789 MW; C1B36D22E2B545BF CRC64; MHNMMVFTGN ANPELSTKVA KNLNLPLGDA TVSQFSDGEV FVEINDNVRG ADVFIIQPTC APTNDNIMEL VVMADAMRRA SAGRITAVVP YFGYARQDRR VRSQRVPISA KVVADIMSGV GIDRVLTVDL HAEQIQGFFD VPVDNVYGSP ILLDDISRQQ YDNQMVVSPD IGGVVRARAV AKQLNDADLA IIDKRRPKAG VAQVMHIIGE VEGKTCILVD DMVDTAGTLC KAAGALKANG AAKVVAYCTH PVLSGPAVDN INASELDELV VTDTIPLSEA ASQCARIRQL TLSNLLAESI RRVSNEESIS ALFR //