ID KITH_ECOLI Reviewed; 205 AA.
AC P23331; Q0H0G7;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1991, sequence version 1.
DT 24-JAN-2024, entry version 169.
DE RecName: Full=Thymidine kinase {ECO:0000255|HAMAP-Rule:MF_00124};
DE EC=2.7.1.21 {ECO:0000255|HAMAP-Rule:MF_00124};
GN Name=tdk {ECO:0000255|HAMAP-Rule:MF_00124};
GN OrderedLocusNames=b1238, JW1226;
OS Escherichia coli (strain K12).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=2060797; DOI=10.1016/0378-1119(91)90218-z;
RA Bockamp E.O., Blasco R., Vinuela E.;
RT "Escherichia coli thymidine kinase: nucleotide sequence of the gene and
RT relationships to other thymidine kinases.";
RL Gene 101:9-14(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=2041474; DOI=10.1111/j.1365-2958.1991.tb02119.x;
RA Black M.E., Hruby D.E.;
RT "Nucleotide sequence of the Escherichia coli thymidine kinase gene provides
RT evidence for conservation of functional domains and quaternary structure.";
RL Mol. Microbiol. 5:373-379(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=7773397; DOI=10.1099/13500872-141-4-959;
RA Danchin A., Krin E.;
RT "Filling the gap between hns and adhE in Escherichia coli K12.";
RL Microbiology 141:959-960(1995).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=17615154; DOI=10.1093/jac/dkm240;
RA Sandrini M.P., Clausen A.R., On S.L., Aarestrup F.M., Munch-Petersen B.,
RA Piskur J.;
RT "Nucleoside analogues are activated by bacterial deoxyribonucleoside
RT kinases in a species-specific manner.";
RL J. Antimicrob. Chemother. 60:510-520(2007).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA Horiuchi T.;
RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 12.7-28.0 min region on the linkage map.";
RL DNA Res. 3:137-155(1996).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
CC -!- FUNCTION: Phosphorylates both thymidine and deoxyuridine.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + thymidine = ADP + dTMP + H(+); Xref=Rhea:RHEA:19129,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17748, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:63528, ChEBI:CHEBI:456216; EC=2.7.1.21;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00124};
CC -!- ACTIVITY REGULATION: Allosteric enzyme which is feedback inhibited by
CC dTTP and activated by a number of dNDP and dNTP.
CC -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_00124}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00124}.
CC -!- SIMILARITY: Belongs to the thymidine kinase family. {ECO:0000255|HAMAP-
CC Rule:MF_00124}.
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DR EMBL; X51523; CAA35907.1; -; Genomic_DNA.
DR EMBL; X53733; CAA37765.1; -; Genomic_DNA.
DR EMBL; X67326; CAA47741.1; -; Genomic_DNA.
DR EMBL; DQ384607; ABD37701.1; -; Genomic_DNA.
DR EMBL; U00096; AAC74320.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA36118.1; -; Genomic_DNA.
DR PIR; JS0519; JS0519.
DR RefSeq; NP_415754.1; NC_000913.3.
DR RefSeq; WP_000068077.1; NZ_SSZK01000031.1.
DR AlphaFoldDB; P23331; -.
DR SMR; P23331; -.
DR BioGRID; 4259556; 225.
DR IntAct; P23331; 6.
DR STRING; 511145.b1238; -.
DR jPOST; P23331; -.
DR PaxDb; 511145-b1238; -.
DR EnsemblBacteria; AAC74320; AAC74320; b1238.
DR GeneID; 945834; -.
DR KEGG; ecj:JW1226; -.
DR KEGG; eco:b1238; -.
DR PATRIC; fig|1411691.4.peg.1047; -.
DR EchoBASE; EB0987; -.
DR eggNOG; COG1435; Bacteria.
DR HOGENOM; CLU_064400_2_1_6; -.
DR InParanoid; P23331; -.
DR OMA; GTMDCGK; -.
DR OrthoDB; 9781579at2; -.
DR PhylomeDB; P23331; -.
DR BioCyc; EcoCyc:TDK-MONOMER; -.
DR BioCyc; MetaCyc:TDK-MONOMER; -.
DR PRO; PR:P23331; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0042802; F:identical protein binding; IDA:EcoCyc.
DR GO; GO:0004797; F:thymidine kinase activity; IDA:EcoCyc.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0071897; P:DNA biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0036198; P:dTMP salvage; IMP:EcoCyc.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0046104; P:thymidine metabolic process; IBA:GO_Central.
DR Gene3D; 3.30.60.20; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR HAMAP; MF_00124; Thymidine_kinase; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR001267; Thymidine_kinase.
DR InterPro; IPR020633; Thymidine_kinase_CS.
DR PANTHER; PTHR11441; THYMIDINE KINASE; 1.
DR PANTHER; PTHR11441:SF0; THYMIDINE KINASE, CYTOSOLIC; 1.
DR Pfam; PF00265; TK; 1.
DR PIRSF; PIRSF035805; TK_cell; 1.
DR SUPFAM; SSF57716; Glucocorticoid receptor-like (DNA-binding domain); 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS00603; TK_CELLULAR_TYPE; 1.
PE 3: Inferred from homology;
KW Allosteric enzyme; ATP-binding; Cytoplasm; DNA synthesis; Kinase;
KW Metal-binding; Nucleotide-binding; Reference proteome; Transferase; Zinc.
FT CHAIN 1..205
FT /note="Thymidine kinase"
FT /id="PRO_0000174971"
FT ACT_SITE 88
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00124"
FT BINDING 9..16
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305"
FT BINDING 87..90
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00124"
FT BINDING 145
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00124"
FT BINDING 147
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00124"
FT BINDING 182
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00124"
FT BINDING 185
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00124"
SQ SEQUENCE 205 AA; 23457 MW; 533166D9EAD20E16 CRC64;
MAQLYFYYSA MNAGKSTALL QSSYNYQERG MRTVVYTAEI DDRFGAGKVS SRIGLSSPAK
LFNQNSSLFD EIRAEHEQQA IHCVLVDECQ FLTRQQVYEL SEVVDQLDIP VLCYGLRTDF
RGELFIGSQY LLAWSDKLVE LKTICFCGRK ASMVLRLDQA GRPYNEGEQV VIGGNERYVS
VCRKHYKEAL QVDSLTAIQE RHRHD
//
