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   03-AUG-2022, entry version 89.
DE   RecName: Full=Uridine kinase {ECO:0000255|HAMAP-Rule:MF_00551};
DE            EC=2.7.1.48 {ECO:0000255|HAMAP-Rule:MF_00551};
DE   AltName: Full=Cytidine monophosphokinase {ECO:0000255|HAMAP-Rule:MF_00551};
DE   AltName: Full=Uridine monophosphokinase {ECO:0000255|HAMAP-Rule:MF_00551};
GN   Name=udk {ECO:0000255|HAMAP-Rule:MF_00551}; OrderedLocusNames=CPR_1740;
OS   Clostridium perfringens (strain SM101 / Type A).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=289380;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SM101 / Type A;
RX   PubMed=16825665; DOI=10.1101/gr.5238106;
RA   Myers G.S.A., Rasko D.A., Cheung J.K., Ravel J., Seshadri R., DeBoy R.T.,
RA   Ren Q., Varga J., Awad M.M., Brinkac L.M., Daugherty S.C., Haft D.H.,
RA   Dodson R.J., Madupu R., Nelson W.C., Rosovitz M.J., Sullivan S.A.,
RA   Khouri H., Dimitrov G.I., Watkins K.L., Mulligan S., Benton J., Radune D.,
RA   Fisher D.J., Atkins H.S., Hiscox T., Jost B.H., Billington S.J.,
RA   Songer J.G., McClane B.A., Titball R.W., Rood J.I., Melville S.B.,
RA   Paulsen I.T.;
RT   "Skewed genomic variability in strains of the toxigenic bacterial pathogen,
RT   Clostridium perfringens.";
RL   Genome Res. 16:1031-1040(2006).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + uridine = ADP + H(+) + UMP; Xref=Rhea:RHEA:16825,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16704, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:57865, ChEBI:CHEBI:456216; EC=2.7.1.48;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00551};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + cytidine = ADP + CMP + H(+); Xref=Rhea:RHEA:24674,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:17562, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:60377, ChEBI:CHEBI:456216; EC=2.7.1.48;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00551};
CC   -!- PATHWAY: Pyrimidine metabolism; CTP biosynthesis via salvage pathway;
CC       CTP from cytidine: step 1/3. {ECO:0000255|HAMAP-Rule:MF_00551}.
CC   -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via salvage pathway;
CC       UMP from uridine: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00551}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00551}.
CC   -!- SIMILARITY: Belongs to the uridine kinase family. {ECO:0000255|HAMAP-
CC       Rule:MF_00551}.
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; CP000312; ABG85407.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q0SS52; -.
DR   SMR; Q0SS52; -.
DR   EnsemblBacteria; ABG85407; ABG85407; CPR_1740.
DR   KEGG; cpr:CPR_1740; -.
DR   OMA; TTLKPMH; -.
DR   UniPathway; UPA00574; UER00637.
DR   UniPathway; UPA00579; UER00640.
DR   Proteomes; UP000001824; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016773; F:phosphotransferase activity, alcohol group as acceptor; IEA:InterPro.
DR   GO; GO:0004849; F:uridine kinase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0044211; P:CTP salvage; IEA:UniProtKB-UniPathway.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0044206; P:UMP salvage; IEA:UniProtKB-UniPathway.
DR   CDD; cd02023; UMPK; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   HAMAP; MF_00551; Uridine_kinase; 1.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR006083; PRK/URK.
DR   InterPro; IPR026008; Uridine_kinase.
DR   InterPro; IPR000764; Uridine_kinase-like.
DR   Pfam; PF00485; PRK; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR00235; udk; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cytoplasm; Kinase; Nucleotide-binding; Transferase.
FT   CHAIN           1..208
FT                   /note="Uridine kinase"
FT                   /id="PRO_1000017872"
FT   BINDING         11..18
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00551"
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