KTHY_YERPE
ID KTHY_YERPE Reviewed; 212 AA.
AC O69169; Q0WGH2;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Thymidylate kinase;
DE EC=2.7.4.9;
DE AltName: Full=dTMP kinase;
GN Name=tmk; OrderedLocusNames=YPO1605, y1764, YP_2249;
OS Yersinia pestis.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=632;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], CHARACTERIZATION, AND MASS SPECTROMETRY.
RC STRAIN=6/69C;
RX PubMed=10491164; DOI=10.1046/j.1432-1327.1999.00691.x;
RA Chenal-Francisque V., Tourneux L., Carniel E., Christova P.,
RA Li de la Sierra I., Barzu O., Gilles A.-M.;
RT "The highly similar TMP kinases of Yersinia pestis and Escherichia coli
RT differ markedly in their AZTMP phosphorylating activity.";
RL Eur. J. Biochem. 265:112-119(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CO-92 / Biovar Orientalis;
RX PubMed=11586360; DOI=10.1038/35097083;
RA Parkhill J., Wren B.W., Thomson N.R., Titball R.W., Holden M.T.G.,
RA Prentice M.B., Sebaihia M., James K.D., Churcher C.M., Mungall K.L.,
RA Baker S., Basham D., Bentley S.D., Brooks K., Cerdeno-Tarraga A.-M.,
RA Chillingworth T., Cronin A., Davies R.M., Davis P., Dougan G., Feltwell T.,
RA Hamlin N., Holroyd S., Jagels K., Karlyshev A.V., Leather S., Moule S.,
RA Oyston P.C.F., Quail M.A., Rutherford K.M., Simmonds M., Skelton J.,
RA Stevens K., Whitehead S., Barrell B.G.;
RT "Genome sequence of Yersinia pestis, the causative agent of plague.";
RL Nature 413:523-527(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KIM10+ / Biovar Mediaevalis;
RX PubMed=12142430; DOI=10.1128/jb.184.16.4601-4611.2002;
RA Deng W., Burland V., Plunkett G. III, Boutin A., Mayhew G.F., Liss P.,
RA Perna N.T., Rose D.J., Mau B., Zhou S., Schwartz D.C., Fetherston J.D.,
RA Lindler L.E., Brubaker R.R., Plano G.V., Straley S.C., McDonough K.A.,
RA Nilles M.L., Matson J.S., Blattner F.R., Perry R.D.;
RT "Genome sequence of Yersinia pestis KIM.";
RL J. Bacteriol. 184:4601-4611(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=91001 / Biovar Mediaevalis;
RX PubMed=15368893; DOI=10.1093/dnares/11.3.179;
RA Song Y., Tong Z., Wang J., Wang L., Guo Z., Han Y., Zhang J., Pei D.,
RA Zhou D., Qin H., Pang X., Han Y., Zhai J., Li M., Cui B., Qi Z., Jin L.,
RA Dai R., Chen F., Li S., Ye C., Du Z., Lin W., Wang J., Yu J., Yang H.,
RA Wang J., Huang P., Yang R.;
RT "Complete genome sequence of Yersinia pestis strain 91001, an isolate
RT avirulent to humans.";
RL DNA Res. 11:179-197(2004).
CC -!- FUNCTION: Phosphorylation of dTMP to form dTDP in both de novo and
CC salvage pathways of dTTP synthesis. 5-bromo-2'deoxyuridine
CC monophosphate is also a good phosphate acceptor.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + dTMP = ADP + dTDP; Xref=Rhea:RHEA:13517,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:58369, ChEBI:CHEBI:63528,
CC ChEBI:CHEBI:456216; EC=2.7.4.9;
CC -!- SUBUNIT: Homodimer.
CC -!- MASS SPECTROMETRY: Mass=23089.1; Mass_error=1.2; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:10491164};
CC -!- SIMILARITY: Belongs to the thymidylate kinase family. {ECO:0000305}.
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; AF065312; AAC18855.1; -; Genomic_DNA.
DR EMBL; AL590842; CAL20250.1; -; Genomic_DNA.
DR EMBL; AE009952; AAM85332.1; -; Genomic_DNA.
DR EMBL; AE017042; AAS62455.1; -; Genomic_DNA.
DR PIR; AH0195; AH0195.
DR RefSeq; WP_002213082.1; NZ_WUCM01000130.1.
DR RefSeq; YP_002346616.1; NC_003143.1.
DR AlphaFoldDB; O69169; -.
DR SMR; O69169; -.
DR STRING; 214092.YPO1605; -.
DR PaxDb; O69169; -.
DR DNASU; 1146711; -.
DR EnsemblBacteria; AAM85332; AAM85332; y1764.
DR EnsemblBacteria; AAS62455; AAS62455; YP_2249.
DR GeneID; 57976966; -.
DR KEGG; ype:YPO1605; -.
DR KEGG; ypk:y1764; -.
DR KEGG; ypm:YP_2249; -.
DR PATRIC; fig|214092.21.peg.1948; -.
DR eggNOG; COG0125; Bacteria.
DR HOGENOM; CLU_049131_0_1_6; -.
DR OMA; VMTREPG; -.
DR Proteomes; UP000000815; Chromosome.
DR Proteomes; UP000001019; Chromosome.
DR Proteomes; UP000002490; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004798; F:thymidylate kinase activity; IBA:GO_Central.
DR GO; GO:0009041; F:uridylate kinase activity; IBA:GO_Central.
DR GO; GO:0006233; P:dTDP biosynthetic process; IBA:GO_Central.
DR GO; GO:0006235; P:dTTP biosynthetic process; IBA:GO_Central.
DR GO; GO:0006227; P:dUDP biosynthetic process; IBA:GO_Central.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_00165; Thymidylate_kinase; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR039430; Thymidylate_kin-like_dom.
DR InterPro; IPR018095; Thymidylate_kin_CS.
DR InterPro; IPR018094; Thymidylate_kinase.
DR Pfam; PF02223; Thymidylate_kin; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00041; DTMP_kinase; 1.
DR PROSITE; PS01331; THYMIDYLATE_KINASE; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Kinase; Nucleotide biosynthesis; Nucleotide-binding;
KW Reference proteome; Transferase.
FT CHAIN 1..212
FT /note="Thymidylate kinase"
FT /id="PRO_0000155379"
FT BINDING 10..17
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 212 AA; 23088 MW; B4DB977818F7AF68 CRC64;
MNSKFIVIEG LEGAGKTTTR DTVVAVLRAQ GINDIVFTRE PGGTPLAEKL RDLIKQGIDG
EVLTDKAEVL MLYAARVQLV ENVIKPALAR GSWVVGDRHD LSSQAYQGGG RGIDSQLMAS
LRDTVLGEFR PDLTLYLDLP PAVGLARARA RGELDRIEQE SLAFFERTRA RYLELAASDA
SIKTIDASQP IEQVSASISQ ALAQWLTNQE PV
