ID URK_CLOPS Reviewed; 208 AA. AC Q0SS52; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 05-SEP-2006, sequence version 1. DT 16-JUN-2009, entry version 23. DE RecName: Full=Uridine kinase; DE EC=2.7.1.48; DE AltName: Full=Uridine monophosphokinase; DE AltName: Full=Cytidine monophosphokinase; GN Name=udk; OrderedLocusNames=CPR_1740; OS Clostridium perfringens (strain SM101 / Type A). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=289380; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16825665; DOI=10.1101/gr.5238106; RA Myers G.S.A., Rasko D.A., Cheung J.K., Ravel J., Seshadri R., RA DeBoy R.T., Ren Q., Varga J., Awad M.M., Brinkac L.M., Daugherty S.C., RA Haft D.H., Dodson R.J., Madupu R., Nelson W.C., Rosovitz M.J., RA Sullivan S.A., Khouri H., Dimitrov G.I., Watkins K.L., Mulligan S., RA Benton J., Radune D., Fisher D.J., Atkins H.S., Hiscox T., Jost B.H., RA Billington S.J., Songer J.G., McClane B.A., Titball R.W., Rood J.I., RA Melville S.B., Paulsen I.T.; RT "Skewed genomic variability in strains of the toxigenic bacterial RT pathogen, Clostridium perfringens."; RL Genome Res. 16:1031-1040(2006). CC -!- CATALYTIC ACTIVITY: ATP + uridine = ADP + UMP. CC -!- CATALYTIC ACTIVITY: ATP + cytidine = ADP + CMP. CC -!- PATHWAY: Pyrimidine metabolism; CTP biosynthesis via salvage CC pathway; CTP from cytidine: step 1/3. CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via salvage CC pathway; UMP from uridine: step 1/1. CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). CC -!- SIMILARITY: Belongs to the uridine kinase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000312; ABG85407.1; -; Genomic_DNA. DR RefSeq; YP_699055.1; -. DR GeneID; 4204462; -. DR GenomeReviews; CP000312_GR; CPR_1740. DR KEGG; cpr:CPR_1740; -. DR TIGR; CPR_1740; -. DR HOGENOM; Q0SS52; -. DR OMA; Q0SS52; NQFIEPT. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:HAMAP. DR GO; GO:0016773; F:phosphotransferase activity, alcohol group ...; IEA:InterPro. DR GO; GO:0004849; F:uridine kinase activity; IEA:HAMAP. DR GO; GO:0008655; P:pyrimidine salvage; IEA:HAMAP. DR HAMAP; MF_00551; -; 1. DR InterPro; IPR006083; PRK_URK. DR InterPro; IPR000764; Uridine_kinase. DR PANTHER; PTHR10285:SF6; Uridine_kin; 1. DR Pfam; PF00485; PRK; 1. DR PRINTS; PR00988; URIDINKINASE. DR TIGRFAMs; TIGR00235; udk; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Cytoplasm; Kinase; Nucleotide-binding; KW Transferase. FT CHAIN 1 208 Uridine kinase. FT /FTId=PRO_1000017872. FT NP_BIND 11 18 ATP (Potential). SQ SEQUENCE 208 AA; 23882 MW; DF1AB1B674A6B929 CRC64; MKRPIFIGIT GGTGSGKSTI AKEIYRQFGE ECIAMIEQDS YYKDQSHLSM DDRVKTNYDH PNAFDNNLLV SHLESLLNGH CIQKPSYDFS IHNRIEDTTK VEPKEIVIVE GILILEDPRI RELLDIKIYV DTDADVRIIR RMVRDINERG RTIESVINQY LNVVKPMHNQ FTEPTKKFAD IIIPEGGHNK VAIDIIVAKI KEVLGKYE //