ID KPRS_LEPIC STANDARD; PRT; 312 AA. AC Q72V73; DT 13-SEP-2005 (Rel. 48, Created) DT 13-SEP-2005 (Rel. 48, Last sequence update) DT 13-SEP-2005 (Rel. 48, Last annotation update) DE Ribose-phosphate pyrophosphokinase (EC 2.7.6.1) (RPPK) (Phosphoribosyl DE pyrophosphate synthetase) (P-Rib-PP synthetase) (PRPP synthetase). GN Name=prs; OrderedLocusNames=LIC10429; 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: Utilized by both the de novo and the salvage pathways by CC which endogenously formed or exogenously added pyrimidine, purine, CC or pyridine bases are converted to the corresponding CC ribonucleoside monophosphates. CC -!- SUBCELLULAR LOCATION: Cytoplasmic (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; AE017288; AAS69051.1; -; Genomic_DNA. DR HAMAP; MF_00583; -; 1. DR InterPro; IPR002375; Pr/py_rp_transf. 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 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 //