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Database: UniProt/SWISS-PROT
Entry: KITH_ECOLI
LinkDB: KITH_ECOLI
Original site: KITH_ECOLI 
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   12-SEP-2018, entry version 138.
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; Proteobacteria; 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
RT   and 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
RT   provides evidence for conservation of functional domains and
RT   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.,
RA   Munch-Petersen B., 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.,
RA   Ikemoto K., Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K.,
RA   Kimura S., Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K.,
RA   Mori H., Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N.,
RA   Sampei G., Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y.,
RA   Yano M., Horiuchi T.;
RT   "A 718-kb DNA sequence of the Escherichia coli K-12 genome
RT   corresponding to 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.,
RA   Mau B., 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
RT   MG1655 and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
CC   -!- FUNCTION: Phosphorylates both thymidine and deoxyuridine.
CC   -!- CATALYTIC ACTIVITY: ATP + thymidine = ADP + thymidine 5'-
CC       phosphate. {ECO:0000255|HAMAP-Rule:MF_00124}.
CC   -!- ACTIVITY REGULATION: Allosteric enzyme which is feedback inhibited
CC       by 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.
CC       {ECO:0000255|HAMAP-Rule:MF_00124}.
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_LN832404.1.
DR   ProteinModelPortal; P23331; -.
DR   BioGrid; 4259556; 225.
DR   IntAct; P23331; 6.
DR   STRING; 316385.ECDH10B_1298; -.
DR   PaxDb; P23331; -.
DR   PRIDE; P23331; -.
DR   EnsemblBacteria; AAC74320; AAC74320; b1238.
DR   EnsemblBacteria; BAA36118; BAA36118; BAA36118.
DR   GeneID; 945834; -.
DR   KEGG; ecj:JW1226; -.
DR   KEGG; eco:b1238; -.
DR   PATRIC; fig|1411691.4.peg.1047; -.
DR   EchoBASE; EB0987; -.
DR   EcoGene; EG10994; tdk.
DR   eggNOG; ENOG4107104; Bacteria.
DR   eggNOG; COG1435; LUCA.
DR   HOGENOM; HOG000076391; -.
DR   InParanoid; P23331; -.
DR   KO; K00857; -.
DR   OMA; KEQFGWI; -.
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-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004797; F:thymidine kinase activity; IDA:EcoCyc.
DR   GO; GO:0071897; P:DNA biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0006259; P:DNA metabolic process; IDA:EcoCyc.
DR   GO; GO:0046104; P:thymidine metabolic process; IBA:GO_Central.
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; PTHR11441; 1.
DR   Pfam; PF00265; TK; 1.
DR   PIRSF; PIRSF035805; TK_cell; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS00603; TK_CELLULAR_TYPE; 1.
PE   3: Inferred from homology;
KW   Allosteric enzyme; ATP-binding; Complete proteome; Cytoplasm;
KW   DNA synthesis; Kinase; Metal-binding; Nucleotide-binding;
KW   Reference proteome; Transferase; Zinc.
FT   CHAIN         1    205       Thymidine kinase.
FT                                /FTId=PRO_0000174971.
FT   NP_BIND       9     16       ATP. {ECO:0000305}.
FT   NP_BIND      87     90       ATP. {ECO:0000255|HAMAP-Rule:MF_00124}.
FT   ACT_SITE     88     88       Proton acceptor. {ECO:0000255|HAMAP-
FT                                Rule:MF_00124}.
FT   METAL       145    145       Zinc. {ECO:0000255|HAMAP-Rule:MF_00124}.
FT   METAL       147    147       Zinc. {ECO:0000255|HAMAP-Rule:MF_00124}.
FT   METAL       182    182       Zinc. {ECO:0000255|HAMAP-Rule:MF_00124}.
FT   METAL       185    185       Zinc. {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
//
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