ID   URK_BORBU               Reviewed;         206 AA.
AC   Q59190;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 132.
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=BB_0015;
OS   Borreliella burgdorferi (strain ATCC 35210 / DSM 4680 / CIP 102532 / B31)
OS   (Borrelia burgdorferi).
OC   Bacteria; Spirochaetes; Spirochaetales; Borreliaceae; Borreliella.
OX   NCBI_TaxID=224326;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-5.
RC   STRAIN=HB19;
RX   PubMed=9228761; DOI=10.1111/j.1574-6968.1997.tb12579.x;
RA   Boursaux-Eude C., Margarita D., Gilles A.M., Barzu O., Saint-Girons I.;
RT   "Borrelia burgdorferi uridine kinase: an enzyme of the pyrimidine salvage
RT   pathway for endogenous use of nucleotides.";
RL   FEMS Microbiol. Lett. 151:257-261(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35210 / DSM 4680 / CIP 102532 / B31;
RX   PubMed=9403685; DOI=10.1038/37551;
RA   Fraser C.M., Casjens S., Huang W.M., Sutton G.G., Clayton R.A.,
RA   Lathigra R., White O., Ketchum K.A., Dodson R.J., Hickey E.K., Gwinn M.L.,
RA   Dougherty B.A., Tomb J.-F., Fleischmann R.D., Richardson D.L.,
RA   Peterson J.D., Kerlavage A.R., Quackenbush J., Salzberg S.L., Hanson M.,
RA   van Vugt R., Palmer N., Adams M.D., Gocayne J.D., Weidman J.F.,
RA   Utterback T.R., Watthey L., McDonald L.A., Artiach P., Bowman C.,
RA   Garland S.A., Fujii C., Cotton M.D., Horst K., Roberts K.M., Hatch B.,
RA   Smith H.O., Venter J.C.;
RT   "Genomic sequence of a Lyme disease spirochaete, Borrelia burgdorferi.";
RL   Nature 390:580-586(1997).
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   -!- 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   -!- PATHWAY: Pyrimidine metabolism; CTP biosynthesis via salvage pathway;
CC       CTP from cytidine: step 1/3.
CC   -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via salvage pathway;
CC       UMP from uridine: step 1/1.
CC   -!- SUBUNIT: Monomer.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the uridine kinase family. {ECO:0000305}.
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DR   EMBL; X97449; CAA66081.1; -; Genomic_DNA.
DR   EMBL; AE000783; AAC66392.2; -; Genomic_DNA.
DR   PIR; G70101; G70101.
DR   RefSeq; NP_212149.2; NC_001318.1.
DR   RefSeq; WP_002655979.1; NC_001318.1.
DR   AlphaFoldDB; Q59190; -.
DR   SMR; Q59190; -.
DR   STRING; 224326.BB_0015; -.
DR   EnsemblBacteria; AAC66392; AAC66392; BB_0015.
DR   GeneID; 56568200; -.
DR   KEGG; bbu:BB_0015; -.
DR   PATRIC; fig|224326.49.peg.413; -.
DR   HOGENOM; CLU_021278_1_2_12; -.
DR   OMA; TTLKPMH; -.
DR   UniPathway; UPA00574; UER00637.
DR   UniPathway; UPA00579; UER00640.
DR   Proteomes; UP000001807; 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   1: Evidence at protein level;
KW   ATP-binding; Cytoplasm; Direct protein sequencing; Kinase;
KW   Nucleotide-binding; Reference proteome; Transferase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:9228761"
FT   CHAIN           2..206
FT                   /note="Uridine kinase"
FT                   /id="PRO_0000164465"
FT   BINDING         9..16
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   206 AA;  23874 MW;  2BB6A0075CB823E1 CRC64;
     MAKIIGISGG SGSGKTTVVS KISEFIPEFV LISQDNYYKS VGDYEHEFSK VNFDHPDAFD
     NNLFYEHLKN LKKNSPIDMP LYDFINHKRQ LKTVLVVPTP VVIVEGIMIF VEERVRNLID
     LKIYIDTPND IRFIRRLRRD ISKRGRTVES VIDQYLNTTR WGYYRFIEPT KEYADLIIPE
     GGHNDKALYV LSTFLKSLSK EGLDFT