ID KITH_CHRVO Reviewed; 184 AA. AC Q7NVK0; DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot. DT 15-DEC-2003, sequence version 1. DT 27-MAR-2024, entry version 111. 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}; OrderedLocusNames=CV_2342; OS Chromobacterium violaceum (strain ATCC 12472 / DSM 30191 / JCM 1249 / NBRC OS 12614 / NCIMB 9131 / NCTC 9757). OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; OC Chromobacteriaceae; Chromobacterium. OX NCBI_TaxID=243365; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 12472 / DSM 30191 / JCM 1249 / NBRC 12614 / NCIMB 9131 / RC NCTC 9757; RX PubMed=14500782; DOI=10.1073/pnas.1832124100; RA Vasconcelos A.T.R., de Almeida D.F., Hungria M., Guimaraes C.T., RA Antonio R.V., Almeida F.C., de Almeida L.G.P., de Almeida R., RA Alves-Gomes J.A., Andrade E.M., Araripe J., de Araujo M.F.F., RA Astolfi-Filho S., Azevedo V., Baptista A.J., Bataus L.A.M., Batista J.S., RA Belo A., van den Berg C., Bogo M., Bonatto S., Bordignon J., Brigido M.M., RA Brito C.A., Brocchi M., Burity H.A., Camargo A.A., Cardoso D.D.P., RA Carneiro N.P., Carraro D.M., Carvalho C.M.B., Cascardo J.C.M., Cavada B.S., RA Chueire L.M.O., Creczynski-Pasa T.B., Cunha-Junior N.C., Fagundes N., RA Falcao C.L., Fantinatti F., Farias I.P., Felipe M.S.S., Ferrari L.P., RA Ferro J.A., Ferro M.I.T., Franco G.R., Freitas N.S.A., Furlan L.R., RA Gazzinelli R.T., Gomes E.A., Goncalves P.R., Grangeiro T.B., RA Grattapaglia D., Grisard E.C., Hanna E.S., Jardim S.N., Laurino J., RA Leoi L.C.T., Lima L.F.A., Loureiro M.F., Lyra M.C.C.P., Madeira H.M.F., RA Manfio G.P., Maranhao A.Q., Martins W.S., di Mauro S.M.Z., RA de Medeiros S.R.B., Meissner R.V., Moreira M.A.M., Nascimento F.F., RA Nicolas M.F., Oliveira J.G., Oliveira S.C., Paixao R.F.C., Parente J.A., RA Pedrosa F.O., Pena S.D.J., Pereira J.O., Pereira M., Pinto L.S.R.C., RA Pinto L.S., Porto J.I.R., Potrich D.P., Ramalho-Neto C.E., Reis A.M.M., RA Rigo L.U., Rondinelli E., Santos E.B.P., Santos F.R., Schneider M.P.C., RA Seuanez H.N., Silva A.M.R., da Silva A.L.C., Silva D.W., Silva R., RA Simoes I.C., Simon D., Soares C.M.A., Soares R.B.A., Souza E.M., RA Souza K.R.L., Souza R.C., Steffens M.B.R., Steindel M., Teixeira S.R., RA Urmenyi T., Vettore A., Wassem R., Zaha A., Simpson A.J.G.; RT "The complete genome sequence of Chromobacterium violaceum reveals RT remarkable and exploitable bacterial adaptability."; RL Proc. Natl. Acad. Sci. U.S.A. 100:11660-11665(2003). 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 -!- 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}. 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; AE016825; AAQ60014.1; -; Genomic_DNA. DR RefSeq; WP_011135889.1; NC_005085.1. DR AlphaFoldDB; Q7NVK0; -. DR SMR; Q7NVK0; -. DR STRING; 243365.CV_2342; -. DR KEGG; cvi:CV_2342; -. DR eggNOG; COG1435; Bacteria. DR HOGENOM; CLU_064400_2_1_4; -. DR OrthoDB; 9781579at2; -. DR Proteomes; UP000001424; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0004797; F:thymidine kinase activity; IEA:UniProtKB-UniRule. 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:0016310; P:phosphorylation; IEA:UniProtKB-KW. 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 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. PE 3: Inferred from homology; KW ATP-binding; Cytoplasm; DNA synthesis; Kinase; Metal-binding; KW Nucleotide-binding; Reference proteome; Transferase; Zinc. FT CHAIN 1..184 FT /note="Thymidine kinase" FT /id="PRO_0000242789" FT ACT_SITE 83 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:0000255|HAMAP-Rule:MF_00124" FT BINDING 82..85 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00124" FT BINDING 140 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00124" FT BINDING 142 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00124" FT BINDING 177 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00124" FT BINDING 180 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00124" SQ SEQUENCE 184 AA; 20746 MW; 3206FA5D605A0C35 CRC64; MAKLFFRYAA MNSGKSTQLL QIANNYESMD KKVALYTSAI DDRYGVGMIT SRLNIQRESN TFDAGFDFLA HDYGDTACVL VDEAQFMTPE QAQQLHRLAH KRNIPVICFG LRTDFQGHPF PGSAWLLSLA DDVEEIKTIC HCGRKATMHI RIDGDGRRVK EGPQVEIGGE ARYRAVCGRC FHHD //