ID   Q837L2_ENTFA            Unreviewed;       209 AA.
AC   Q837L2;
DT   01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2003, sequence version 1.
DT   01-MAY-2013, entry version 75.
DE   RecName: Full=Uridine kinase;
DE            EC=2.7.1.48;
DE   AltName: Full=Cytidine monophosphokinase;
DE   AltName: Full=Uridine monophosphokinase;
GN   Name=udk; OrderedLocusNames=EF_0825;
OS   Enterococcus faecalis (strain ATCC 700802 / V583).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae;
OC   Enterococcus.
OX   NCBI_TaxID=226185;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700802 / V583;
RX   PubMed=12663927; DOI=10.1126/science.1080613;
RA   Paulsen I.T., Banerjei L., Myers G.S.A., Nelson K.E., Seshadri R.,
RA   Read T.D., Fouts D.E., Eisen J.A., Gill S.R., Heidelberg J.F.,
RA   Tettelin H., Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J.,
RA   Daugherty S.C., DeBoy R.T., Durkin S.A., Kolonay J.F., Madupu R.,
RA   Nelson W.C., Vamathevan J.J., Tran B., Upton J., Hansen T., Shetty J.,
RA   Khouri H.M., Utterback T.R., Radune D., Ketchum K.A., Dougherty B.A.,
RA   Fraser C.M.;
RT   "Role of mobile DNA in the evolution of vancomycin-resistant
RT   Enterococcus faecalis.";
RL   Science 299:2071-2074(2003).
CC   -!- CATALYTIC ACTIVITY: ATP + cytidine = ADP + CMP.
CC   -!- CATALYTIC ACTIVITY: ATP + uridine = ADP + UMP.
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.
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DR   EMBL; AE016830; AAO80637.1; -; Genomic_DNA.
DR   RefSeq; NP_814567.1; NC_004668.1.
DR   ProteinModelPortal; Q837L2; -.
DR   STRING; 226185.EF0825; -.
DR   EnsemblBacteria; AAO80637; AAO80637; EF_0825.
DR   GeneID; 1199718; -.
DR   KEGG; efa:EF0825; -.
DR   PATRIC; 21852030; VBIEntFae7065_0764.
DR   KO; K00876; -.
DR   OMA; DICFMRR; -.
DR   ProtClustDB; PRK05480; -.
DR   BioCyc; EFAE226185:GHI1-928-MONOMER; -.
DR   UniPathway; UPA00574; UER00637.
DR   UniPathway; UPA00579; UER00640.
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 as acceptor; IEA:InterPro.
DR   GO; GO:0004849; F:uridine kinase activity; IEA:HAMAP.
DR   GO; GO:0044211; P:CTP salvage; IEA:UniProtKB-UniPathway.
DR   GO; GO:0044206; P:UMP salvage; IEA:UniProtKB-UniPathway.
DR   HAMAP; MF_00551; Uridine_kinase; 1; -.
DR   InterPro; IPR006083; PRK/URK.
DR   InterPro; IPR000764; Uridine_kinase.
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   Reference proteome; Transferase.
FT   NP_BIND      13     20       ATP (By similarity).
SQ   SEQUENCE   209 AA;  24261 MW;  C68D89ED1205B839 CRC64;
     MKDSQPIIIG VTGGSGSGKT SVSRAIFNNF PDHSIMMLEQ DSYYKDQSHL SFEERLNTNY
     DHPFAFDTDL LIQHVEQLLN YQAIEKPVYD YVAHTRSTET VIQEPKEVII LEGILILEDR
     RLRDLMDIKV YVDTDDDIRI IRRIKRDMEE RGRTLDSVIE QYLTVVKPMY HQFIEPTKRY
     ADIIVPEGGE NHVAIDLINT KVDSILTKM
//