ID KITH_MYCCT Reviewed; 209 AA. AC Q2SSX9; DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot. DT 24-JAN-2006, sequence version 1. DT 02-SEP-2026, entry version 97. 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=MCAP_0143; OS Mycoplasma capricolum subsp. capricolum (strain California kid / ATCC 27343 OS / NCTC 10154). OC Bacteria; Bacillati; Mycoplasmatota; Mollicutes; Mycoplasmataceae; OC Mycoplasma. OX NCBI_TaxID=340047; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=California kid / ATCC 27343 / NCTC 10154; RA Glass J.I., Lartigue C., Pfannkoch C., Baden-Tillson H., Smith H.O., RA Venter J.C., Roske K., Wise K.S., Calcutt M.J., Nelson W.C., Nierman W.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: CC Reaction=thymidine + ATP = dTMP + ADP + 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; CP000123; ABC01477.1; -; Genomic_DNA. DR RefSeq; WP_011387039.1; NC_007633.1. DR AlphaFoldDB; Q2SSX9; -. DR SMR; Q2SSX9; -. DR GeneID; 23778904; -. DR KEGG; mcp:MCAP_0143; -. DR HOGENOM; CLU_064400_3_0_14; -. DR PhylomeDB; Q2SSX9; -. DR Proteomes; UP000001928; Chromosome. DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter. 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:0006259; P:DNA metabolic process; IEA:UniProtKB-UniRule. DR GO; GO:0046104; P:thymidine metabolic process; IEA:TreeGrafter. 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 NCBIfam; NF003296; PRK04296.1-1; 1. 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 ATP-binding; Cytoplasm; DNA synthesis; Kinase; Metal-binding; KW Nucleotide-binding; Reference proteome; Transferase; Zinc. FT CHAIN 1..209 FT /note="Thymidine kinase" FT /id="PRO_0000242795" FT ACT_SITE 104 FT /note="Proton acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00124" FT BINDING 25..32 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00124" FT BINDING 103..106 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00124" FT BINDING 160 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00124" FT BINDING 163 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00124" FT BINDING 198 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00124" FT BINDING 201 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00124" SQ SEQUENCE 209 AA; 23820 MW; 3570598B0F5A11E0 CRC64; MTELDINEIE AYNSNKMGWI ELITGCMFAG KTEEFIRRLK VLSYAKKRVL AFKPSIDNRY SVENIISHSG SKLDSYLVKS SDEIKQIVEK ENQIQQVDVI GIDEVQFFDE NVVDIIEQLA DNGIIVIVNG LDKDFRGLPF KNVDKLLVKA EFVTKLRARC HLCGSFANRS QRIVNGQPAL WDSPLILVDG KESYEARCRK CFISPKKDV //