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URK_PECAS
ID   URK_PECAS               Reviewed;         213 AA.
AC   Q6D7B4;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   03-AUG-2022, entry version 97.
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=ECA1411;
OS   Pectobacterium atrosepticum (strain SCRI 1043 / ATCC BAA-672) (Erwinia
OS   carotovora subsp. atroseptica).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Pectobacteriaceae; Pectobacterium.
OX   NCBI_TaxID=218491;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SCRI 1043 / ATCC BAA-672;
RX   PubMed=15263089; DOI=10.1073/pnas.0402424101;
RA   Bell K.S., Sebaihia M., Pritchard L., Holden M.T.G., Hyman L.J.,
RA   Holeva M.C., Thomson N.R., Bentley S.D., Churcher L.J.C., Mungall K.,
RA   Atkin R., Bason N., Brooks K., Chillingworth T., Clark K., Doggett J.,
RA   Fraser A., Hance Z., Hauser H., Jagels K., Moule S., Norbertczak H.,
RA   Ormond D., Price C., Quail M.A., Sanders M., Walker D., Whitehead S.,
RA   Salmond G.P.C., Birch P.R.J., Parkhill J., Toth I.K.;
RT   "Genome sequence of the enterobacterial phytopathogen Erwinia carotovora
RT   subsp. atroseptica and characterization of virulence factors.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:11105-11110(2004).
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}.
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DR   EMBL; BX950851; CAG74321.1; -; Genomic_DNA.
DR   RefSeq; WP_011092995.1; NC_004547.2.
DR   AlphaFoldDB; Q6D7B4; -.
DR   SMR; Q6D7B4; -.
DR   STRING; 218491.ECA1411; -.
DR   EnsemblBacteria; CAG74321; CAG74321; ECA1411.
DR   GeneID; 57208226; -.
DR   KEGG; eca:ECA1411; -.
DR   PATRIC; fig|218491.5.peg.1447; -.
DR   eggNOG; COG0572; Bacteria.
DR   HOGENOM; CLU_021278_1_2_6; -.
DR   OMA; TTLKPMH; -.
DR   OrthoDB; 1793376at2; -.
DR   UniPathway; UPA00574; UER00637.
DR   UniPathway; UPA00579; UER00640.
DR   Proteomes; UP000007966; 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; Reference proteome;
KW   Transferase.
FT   CHAIN           1..213
FT                   /note="Uridine kinase"
FT                   /id="PRO_1000017874"
FT   BINDING         15..22
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00551"
SQ   SEQUENCE   213 AA;  24600 MW;  54750556951994D3 CRC64;
     MTDQSHQCVI IGISGASASG KSLISSTLYR ELRDQVGDQH IGVISEDSYY KDQSHLTMEE
     RVKTNYDHPS SMDHSLLIKH LQMLKSGQAI EVPQYSYVEH TRKQETVHIE LKKVIILEGI
     LLLTDARLRN EMNFSIFVDT PLDICLLRRM RRDVNERGRS MDSVMEQYQK TVRPMFLQFI
     EPSKQYADII VPRGGKNRIA IDILKAKISQ FFE
 
 
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