ID KPRS_FUSNN Reviewed; 316 AA. AC Q8RHM2; DT 25-OCT-2002, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2002, sequence version 1. DT 18-SEP-2019, entry version 108. DE RecName: Full=Ribose-phosphate pyrophosphokinase {ECO:0000255|HAMAP-Rule:MF_00583}; DE Short=RPPK {ECO:0000255|HAMAP-Rule:MF_00583}; DE EC=2.7.6.1 {ECO:0000255|HAMAP-Rule:MF_00583}; DE AltName: Full=5-phospho-D-ribosyl alpha-1-diphosphate {ECO:0000255|HAMAP-Rule:MF_00583}; DE AltName: Full=Phosphoribosyl diphosphate synthase {ECO:0000255|HAMAP-Rule:MF_00583}; DE AltName: Full=Phosphoribosyl pyrophosphate synthase {ECO:0000255|HAMAP-Rule:MF_00583}; DE Short=P-Rib-PP synthase {ECO:0000255|HAMAP-Rule:MF_00583}; DE Short=PRPP synthase {ECO:0000255|HAMAP-Rule:MF_00583}; DE Short=PRPPase {ECO:0000255|HAMAP-Rule:MF_00583}; GN Name=prs {ECO:0000255|HAMAP-Rule:MF_00583}; OrderedLocusNames=FN1992; OS Fusobacterium nucleatum subsp. nucleatum (strain ATCC 25586 / CIP OS 101130 / JCM 8532 / LMG 13131). OC Bacteria; Fusobacteria; Fusobacteriales; Fusobacteriaceae; OC Fusobacterium. OX NCBI_TaxID=190304; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 25586 / CIP 101130 / JCM 8532 / LMG 13131; RX PubMed=11889109; DOI=10.1128/jb.184.7.2005-2018.2002; RA Kapatral V., Anderson I., Ivanova N., Reznik G., Los T., Lykidis A., RA Bhattacharyya A., Bartman A., Gardner W., Grechkin G., Zhu L., RA Vasieva O., Chu L., Kogan Y., Chaga O., Goltsman E., Bernal A., RA Larsen N., D'Souza M., Walunas T., Pusch G., Haselkorn R., RA Fonstein M., Kyrpides N.C., Overbeek R.; RT "Genome sequence and analysis of the oral bacterium Fusobacterium RT nucleatum strain ATCC 25586."; RL J. Bacteriol. 184:2005-2018(2002). 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:0000255|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, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:58017, CC ChEBI:CHEBI:78346, ChEBI:CHEBI:456215; EC=2.7.6.1; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00583}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00583}; CC Note=Binds 2 Mg(2+) ions per subunit. {ECO:0000255|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:0000255|HAMAP-Rule:MF_00583}. CC -!- SUBUNIT: Homohexamer. {ECO:0000255|HAMAP-Rule:MF_00583}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00583}. CC -!- SIMILARITY: Belongs to the ribose-phosphate pyrophosphokinase CC family. Class I subfamily. {ECO:0000255|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; AE009951; AAL94082.1; -; Genomic_DNA. DR RefSeq; NP_602783.1; NC_003454.1. DR RefSeq; WP_005903312.1; NC_003454.1. DR SMR; Q8RHM2; -. DR STRING; 190304.FN1992; -. DR EnsemblBacteria; AAL94082; AAL94082; FN1992. DR GeneID; 992296; -. DR KEGG; fnu:FN1992; -. DR PATRIC; fig|190304.8.peg.460; -. DR eggNOG; ENOG4105C5T; Bacteria. DR eggNOG; COG0462; LUCA. DR HOGENOM; HOG000210449; -. DR InParanoid; Q8RHM2; -. DR KO; K00948; -. DR OMA; FGWARQD; -. DR BioCyc; FNUC190304:G1FZS-481-MONOMER; -. DR UniPathway; UPA00087; UER00172. DR Proteomes; UP000002521; Chromosome. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0002189; C:ribose phosphate diphosphokinase complex; IBA:GO_Central. 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; IBA:GO_Central. DR GO; GO:0006015; P:5-phosphoribose 1-diphosphate biosynthetic process; IBA:GO_Central. DR GO; GO:0009116; P:nucleoside metabolic process; IEA:InterPro. DR GO; GO:0009165; P:nucleotide biosynthetic process; IBA:GO_Central. DR GO; GO:0006164; P:purine nucleotide biosynthetic process; IBA:GO_Central. 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; Complete proteome; Cytoplasm; Kinase; Magnesium; KW Metal-binding; Nucleotide biosynthesis; Nucleotide-binding; KW Reference proteome; Transferase. FT CHAIN 1 316 Ribose-phosphate pyrophosphokinase. FT /FTId=PRO_0000141139. FT NP_BIND 40 42 ATP. {ECO:0000255|HAMAP-Rule:MF_00583}. FT NP_BIND 99 100 ATP. {ECO:0000255|HAMAP-Rule:MF_00583}. FT REGION 227 231 Ribose-5-phosphate binding. FT {ECO:0000255|HAMAP-Rule:MF_00583}. FT ACT_SITE 197 197 {ECO:0000255|HAMAP-Rule:MF_00583}. FT METAL 133 133 Magnesium 1. {ECO:0000255|HAMAP- FT Rule:MF_00583}. FT METAL 174 174 Magnesium 2. {ECO:0000255|HAMAP- FT Rule:MF_00583}. FT BINDING 199 199 Ribose-5-phosphate. {ECO:0000255|HAMAP- FT Rule:MF_00583}. FT BINDING 223 223 Ribose-5-phosphate. {ECO:0000255|HAMAP- FT Rule:MF_00583}. SQ SEQUENCE 316 AA; 35110 MW; 74E240407A01ED84 CRC64; MINFNNVKIF SGNSNLELAK KIAEKAGLQL GKAEIQRFKD GEVYIEIEET VRGRDVFVVQ STSEPVNENL MELLIFVDAL KRASAKTINV IIPYYGYARQ DRKSKPREPI TSKLVANLLT TAGVNRVVAM DLHADQIQGF FDIPLDHMQA LPLMARYFKE KGFKGDEVVV VSPDVGGVKR ARKLAEKLDC KIAIIDKRRP KPNMSEVMNL IGEVEGKIAI FIDDMIDTAG TITNGADAIA QRGAKEVYAC CTHAVFSDPA IERLEKSVLK EIVITDSIAL PERKKIDKIK ILSVDSVFAN AIDRITNNQS VSELFN //