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 22-JUL-2015, entry version 90. 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 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:0000255|HAMAP-Rule:MF_00583}. CC -!- CATALYTIC ACTIVITY: ATP + D-ribose 5-phosphate = AMP + 5-phospho- CC alpha-D-ribose 1-diphosphate. {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 1 Mg(2+) ion 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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00583}. CC -!- SIMILARITY: Belongs to the ribose-phosphate pyrophosphokinase CC family. {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 ProteinModelPortal; Q8RHM2; -. DR SMR; Q8RHM2; 6-315. DR STRING; 190304.FN1992; -. DR EnsemblBacteria; AAL94082; AAL94082; FN1992. DR GeneID; 992296; -. DR KEGG; fnu:FN1992; -. DR PATRIC; 21949509; VBIFusNuc122357_0460. DR eggNOG; COG0462; -. DR HOGENOM; HOG000210449; -. DR InParanoid; Q8RHM2; -. DR KO; K00948; -. DR OMA; PVNEHLM; -. DR OrthoDB; EOG6Z99XQ; -. DR UniPathway; UPA00087; UER00172. DR Proteomes; UP000002521; 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-HAMAP. DR GO; GO:0004749; F:ribose phosphate diphosphokinase activity; IEA:UniProtKB-HAMAP. 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:0009156; P:ribonucleoside monophosphate biosynthetic process; IEA:UniProtKB-HAMAP. 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; 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; 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 99 102 ATP. {ECO:0000255|HAMAP-Rule:MF_00583}. FT NP_BIND 146 147 ATP. {ECO:0000255|HAMAP-Rule:MF_00583}. FT REGION 197 199 Ribose-5-phosphate binding. FT {ECO:0000255|HAMAP-Rule:MF_00583}. FT REGION 224 231 Ribose-5-phosphate binding. FT {ECO:0000255|HAMAP-Rule:MF_00583}. FT REGION 310 312 Ribose-5-phosphate binding. FT {ECO:0000255|HAMAP-Rule:MF_00583}. FT METAL 131 131 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00583}. FT METAL 133 133 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00583}. FT METAL 142 142 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00583}. FT METAL 146 146 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00583}. FT BINDING 107 107 Ribose-5-phosphate. {ECO:0000255|HAMAP- FT Rule:MF_00583}. FT BINDING 133 133 ATP. {ECO:0000255|HAMAP-Rule:MF_00583}. FT BINDING 138 138 ATP. {ECO:0000255|HAMAP-Rule:MF_00583}. FT BINDING 174 174 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 //