ID   URK_BORAP               Reviewed;         207 AA.
AC   Q0SPE9; G0IQ45;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   04-NOV-2026, entry version 111.
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};
GN   OrderedLocusNames=BAPKO_0014, BafPKo_0015;
OS   Borreliella afzelii (strain PKo) (Borrelia afzelii).
OC   Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia; Spirochaetales;
OC   Borreliaceae; Borreliella.
OX   NCBI_TaxID=390236;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PKo;
RX   PubMed=16914037; DOI=10.1186/1471-2164-7-211;
RA   Gloeckner G., Schulte-Spechtel U., Schilhabel M., Felder M., Suehnel J.,
RA   Wilske B., Platzer M.;
RT   "Comparative genome analysis: selection pressure on the Borrelia vls
RT   cassettes is essential for infectivity.";
RL   BMC Genomics 7:211-211(2006).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PKo;
RX   PubMed=22123755; DOI=10.1128/jb.05951-11;
RA   Casjens S.R., Mongodin E.F., Qiu W.G., Dunn J.J., Luft B.J.,
RA   Fraser-Liggett C.M., Schutzer S.E.;
RT   "Whole-genome sequences of two Borrelia afzelii and two Borrelia garinii
RT   Lyme disease agent isolates.";
RL   J. Bacteriol. 193:6995-6996(2011).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=uridine + ATP = UMP + ADP + H(+); 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=cytidine + ATP = CMP + ADP + 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}.
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DR   EMBL; CP000395; ABH01279.1; -; Genomic_DNA.
DR   EMBL; CP002933; AEL69249.1; -; Genomic_DNA.
DR   RefSeq; WP_004790381.1; NC_008277.1.
DR   AlphaFoldDB; Q0SPE9; -.
DR   SMR; Q0SPE9; -.
DR   STRING; 29518.BLA32_04205; -.
DR   GeneID; 76831557; -.
DR   GeneID; 77264859; -.
DR   KEGG; baf:BAPKO_0014; -.
DR   KEGG; bafz:BafPKo_0015; -.
DR   PATRIC; fig|390236.22.peg.15; -.
DR   eggNOG; COG0572; Bacteria.
DR   HOGENOM; CLU_021278_1_2_12; -.
DR   OMA; AAINYDH; -.
DR   OrthoDB; 9777642at2; -.
DR   UniPathway; UPA00574; UER00637.
DR   UniPathway; UPA00579; UER00640.
DR   Proteomes; UP000005216; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0043771; F:cytidine kinase activity; IEA:RHEA.
DR   GO; GO:0004849; F:uridine kinase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0044211; P:CTP salvage; IEA:UniProtKB-UniRule.
DR   GO; GO:0044206; P:UMP salvage; IEA:UniProtKB-UniRule.
DR   CDD; cd02023; UMPK; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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   NCBIfam; NF004018; udk; 1.
DR   NCBIfam; TIGR00235; udk; 1.
DR   PANTHER; PTHR10285; URIDINE KINASE; 1.
DR   Pfam; PF00485; PRK; 1.
DR   PRINTS; PR00988; URIDINKINASE.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cytoplasm; Kinase; Nucleotide-binding; Reference proteome;
KW   Transferase.
FT   CHAIN           1..207
FT                   /note="Uridine kinase"
FT                   /id="PRO_1000017868"
FT   BINDING         9..16
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00551"
SQ   SEQUENCE   207 AA;  23998 MW;  3761FEE3551F9813 CRC64;
     MAKIIGISGG SGSGKTTVVS KISEFIPEFV LISQDNYYKS VGDYEYEFSK VNFDHPDAFD
     NNLFYEHLKN LKKNSPIDMP LYDFINHKRQ LKTVLVVPTP VIIVEGIMIF VEERVRNLID
     LKIYIDTPND IRFIRRLRRD ISKRGRTLES VIDQYLNTTR WGYYRFIEPT KEYADLIIPE
     GGHNDKALYV LSTFLKSLSK EGGLDFI
//