ID KPRS_LEPIC Reviewed; 312 AA. AC Q72V73; DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2004, sequence version 1. DT 12-JUN-2007, entry version 25. DE Ribose-phosphate pyrophosphokinase (EC 2.7.6.1) (RPPK) (Phosphoribosyl DE pyrophosphate synthetase) (P-Rib-PP synthetase) (PRPP synthetase). GN Name=prs; OrderedLocusNames=LIC_10429; OS Leptospira interrogans serogroup Icterohaemorrhagiae serovar OS copenhageni. OC Bacteria; Spirochaetes; Spirochaetales; Leptospiraceae; Leptospira. OX NCBI_TaxID=44275; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Fiocruz L1-130; RX PubMed=15028702; DOI=10.1128/JB.186.7.2164-2172.2004; RA Nascimento A.L.T.O., Ko A.I., Martins E.A.L., Monteiro-Vitorello C.B., RA Ho P.L., Haake D.A., Verjovski-Almeida S., Hartskeerl R.A., RA Marques M.V., Oliveira M.C., Menck C.F.M., Leite L.C.C., Carrer H., RA Coutinho L.L., Degrave W.M., Dellagostin O.A., El-Dorry H., RA Ferro E.S., Ferro M.I.T., Furlan L.R., Gamberini M., Giglioti E.A., RA Goes-Neto A., Goldman G.H., Goldman M.H.S., Harakava R., RA Jeronimo S.M.B., Junqueira-de-Azevedo I.L.M., Kimura E.T., RA Kuramae E.E., Lemos E.G.M., Lemos M.V.F., Marino C.L., Nunes L.R., RA de Oliveira R.C., Pereira G.G., Reis M.S., Schriefer A., RA Siqueira W.J., Sommer P., Tsai S.M., Simpson A.J.G., Ferro J.A., RA Camargo L.E.A., Kitajima J.P., Setubal J.C., Van Sluys M.A.; RT "Comparative genomics of two Leptospira interrogans serovars reveals RT novel insights into physiology and pathogenesis."; RL J. Bacteriol. 186:2164-2172(2004). 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; AE016823; AAS69051.1; -; Genomic_DNA. DR GenomeReviews; AE016823_GR; LIC_10429. DR KEGG; lic:LIC10429; -. DR GO; GO:0000287; F:magnesium ion binding; IEA:HAMAP. DR GO; GO:0004749; F:ribose phosphate diphosphokinase activity; IEA:HAMAP. DR GO; GO:0009156; P:ribonucleoside monophosphate biosynthetic p...; IEA:HAMAP. DR HAMAP; MF_00583; -; 1. DR InterPro; IPR000842; PRPP_synthetase. DR InterPro; IPR000836; PRtransferase. DR InterPro; IPR005946; RibP_Ppkin. DR Pfam; PF00156; Pribosyltran; 1. DR TIGRFAMs; TIGR01251; ribP_PPkin; 1. DR PROSITE; PS00114; PRPP_SYNTHETASE; 1. KW Complete proteome; Kinase; Magnesium; Metal-binding; KW Nucleotide biosynthesis; Transferase. FT CHAIN 1 312 Ribose-phosphate pyrophosphokinase. FT /FTId=PRO_0000141150. FT REGION 212 225 Binding of phosphoribosylpyrophosphate FT (Potential). FT METAL 129 129 Magnesium (Potential). FT METAL 131 131 Magnesium (Potential). FT METAL 144 144 Magnesium (Potential). SQ SEQUENCE 312 AA; 33847 MW; 605454F791690F69 CRC64; MNGDIAVFAG NSNKQIAEEI CTHLGIQSGK INLKKFSDGE ISVKIEDNVR GKEVFIVQST SAPANDHLME LILIMDALRR ASVSSISVVI PYYGYGRQDR KVEPRVPISA RVVADLIEVV GLDRILTMDL HADQIQGFFR VPVDNLHFAP VLAEYVNTKK IDDLVIVSPD SGGAERARAF GKKVNGSLAI IDKRRPKANV SEVMNVIGEI EGKNCILLDD MIDTAGTICK AADVLLKHGA KSVYCAATHG VLSGEAVDRI NSTQFSEVVL ANTIAIPESK KINKLKSLSV APLFANAIQR IHTNQSVSTL FD //