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 07-APR-2021, entry version 114. 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 / DSM 15643 / OS BCRC 10681 / CIP 101130 / JCM 8532 / KCTC 2640 / LMG 13131 / VPI 4355). OC Bacteria; Fusobacteria; Fusobacteriales; Fusobacteriaceae; Fusobacterium. OX NCBI_TaxID=190304; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 25586 / DSM 15643 / BCRC 10681 / CIP 101130 / JCM 8532 / KCTC RC 2640 / LMG 13131 / VPI 4355; 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., Vasieva O., RA Chu L., Kogan Y., Chaga O., Goltsman E., Bernal A., Larsen N., D'Souza M., RA Walunas T., Pusch G., Haselkorn R., Fonstein M., Kyrpides N.C., RA Overbeek R.; RT "Genome sequence and analysis of the oral bacterium Fusobacterium nucleatum RT 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 (Rib- CC 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, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:58017, ChEBI:CHEBI:78346, CC ChEBI:CHEBI:456215; EC=2.7.6.1; Evidence={ECO:0000255|HAMAP- CC 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-ribose CC 1-diphosphate biosynthesis; 5-phospho-alpha-D-ribose 1-diphosphate from CC D-ribose 5-phosphate (route I): step 1/1. {ECO:0000255|HAMAP- CC 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 family. CC 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 SMR; Q8RHM2; -. DR STRING; 190304.FN1992; -. DR EnsemblBacteria; AAL94082; AAL94082; FN1992. DR KEGG; fnu:FN1992; -. DR PATRIC; fig|190304.8.peg.460; -. DR eggNOG; COG0462; Bacteria. DR HOGENOM; CLU_033546_1_0_0; -. DR InParanoid; Q8RHM2; -. 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: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 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; Cytoplasm; Kinase; Magnesium; Metal-binding; KW Nucleotide biosynthesis; Nucleotide-binding; Reference proteome; KW Transferase. FT CHAIN 1..316 FT /note="Ribose-phosphate pyrophosphokinase" FT /id="PRO_0000141139" FT NP_BIND 40..42 FT /note="ATP" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00583" FT NP_BIND 99..100 FT /note="ATP" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00583" FT REGION 227..231 FT /note="Ribose-5-phosphate binding" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00583" FT ACT_SITE 197 FT /evidence="ECO:0000255|HAMAP-Rule:MF_00583" FT METAL 133 FT /note="Magnesium 1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00583" FT METAL 174 FT /note="Magnesium 2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00583" FT BINDING 199 FT /note="Ribose-5-phosphate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00583" FT BINDING 223 FT /note="Ribose-5-phosphate" FT /evidence="ECO:0000255|HAMAP-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 //