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 20-JAN-2009, entry version 44. DE RecName: Full=Ribose-phosphate pyrophosphokinase; DE Short=RPPK; DE EC=2.7.6.1; DE AltName: Full=Phosphoribosyl pyrophosphate synthetase; DE Short=P-Rib-PP synthetase; DE Short=PRPP synthetase; GN Name=prs; OrderedLocusNames=FN1992; OS Fusobacterium nucleatum subsp. nucleatum. OC Bacteria; Fusobacteria; Fusobacteriales; Fusobacteriaceae; OC Fusobacterium. OX NCBI_TaxID=76856; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 25586 / CIP 101130 / JCM 8532 / LMG 13131; RX MEDLINE=21886394; PubMed=11889109; RX 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 -!- CATALYTIC ACTIVITY: ATP + D-ribose 5-phosphate = AMP + 5-phospho- CC alpha-D-ribose 1-diphosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). 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 -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). CC -!- SIMILARITY: Belongs to the ribose-phosphate pyrophosphokinase CC family. 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; -. DR HSSP; P14193; 1IBS. DR GeneID; 992296; -. DR GenomeReviews; AE009951_GR; FN1992. DR KEGG; fnu:FN1992; -. DR NMPDR; fig|190304.1.peg.462; -. DR HOGENOM; Q8RHM2; -. DR BioCyc; FNUC190304:FN1992-MON; -. DR BRENDA; 2.7.6.1; 289963. DR GO; GO:0005737; C:cytoplasm; IEA:HAMAP. DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW. DR GO; GO:0000287; F:magnesium ion binding; IEA:HAMAP. DR GO; GO:0004749; F:ribose phosphate diphosphokinase activity; IEA:HAMAP. DR GO; GO:0044249; P:cellular biosynthetic process; IEA:InterPro. DR GO; GO:0009116; P:nucleoside metabolic process; IEA:InterPro. DR GO; GO:0009156; P:ribonucleoside monophosphate biosynthetic p...; IEA:HAMAP. DR HAMAP; MF_00583; -; 1. DR InterPro; IPR000842; PRib-PP_synthetase_CS. DR InterPro; IPR000836; PRibTrfase. DR InterPro; IPR005946; PRPP_kinase. DR Pfam; PF00156; Pribosyltran; 1. DR TIGRFAMs; TIGR01251; ribP_PPkin; 1. DR PROSITE; PS00114; PRPP_SYNTHETASE; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Kinase; Magnesium; Metal-binding; KW Nucleotide biosynthesis; Transferase. FT CHAIN 1 316 Ribose-phosphate pyrophosphokinase. FT /FTId=PRO_0000141139. FT REGION 216 229 Binding of phosphoribosylpyrophosphate FT (Potential). FT METAL 131 131 Magnesium (Potential). FT METAL 133 133 Magnesium (Potential). FT METAL 142 142 Magnesium (Potential). FT METAL 146 146 Magnesium (Potential). 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 //