ID B0TNH6_SHEHH Unreviewed; 192 AA. AC B0TNH6; DT 08-APR-2008, integrated into UniProtKB/TrEMBL. DT 08-APR-2008, sequence version 1. DT 27-MAR-2024, entry version 80. DE RecName: Full=Thymidine kinase {ECO:0000256|ARBA:ARBA00012118, ECO:0000256|HAMAP-Rule:MF_00124}; DE EC=2.7.1.21 {ECO:0000256|ARBA:ARBA00012118, ECO:0000256|HAMAP-Rule:MF_00124}; GN Name=tdk {ECO:0000256|HAMAP-Rule:MF_00124}; GN OrderedLocusNames=Shal_2941 {ECO:0000313|EMBL:ABZ77490.1}; OS Shewanella halifaxensis (strain HAW-EB4). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales; OC Shewanellaceae; Shewanella. OX NCBI_TaxID=458817 {ECO:0000313|EMBL:ABZ77490.1, ECO:0000313|Proteomes:UP000001317}; RN [1] {ECO:0000313|EMBL:ABZ77490.1, ECO:0000313|Proteomes:UP000001317} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HAW-EB4 {ECO:0000313|EMBL:ABZ77490.1, RC ECO:0000313|Proteomes:UP000001317}; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H., RA Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T., Detter J.C., Han C., RA Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., RA Kim E., Zhao J.-S., Richardson P.; RT "Complete sequence of Shewanella halifaxensis HAW-EB4."; RL Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases. 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:0000256|HAMAP-Rule:MF_00124, CC ECO:0000256|RuleBase:RU000544}; CC -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_00124}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00124}. CC -!- SIMILARITY: Belongs to the thymidine kinase family. CC {ECO:0000256|ARBA:ARBA00007587, ECO:0000256|HAMAP-Rule:MF_00124, CC ECO:0000256|RuleBase:RU004165}. 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; CP000931; ABZ77490.1; -; Genomic_DNA. DR RefSeq; WP_012278017.1; NC_010334.1. DR AlphaFoldDB; B0TNH6; -. DR STRING; 458817.Shal_2941; -. DR KEGG; shl:Shal_2941; -. DR eggNOG; COG1435; Bacteria. DR HOGENOM; CLU_064400_2_1_6; -. DR OrthoDB; 9781579at2; -. DR Proteomes; UP000001317; 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 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 ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP- KW Rule:MF_00124}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00124}; KW DNA synthesis {ECO:0000256|ARBA:ARBA00022634, ECO:0000256|HAMAP- KW Rule:MF_00124}; KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|HAMAP-Rule:MF_00124}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00124}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP- KW Rule:MF_00124}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP- KW Rule:MF_00124}; Zinc {ECO:0000256|HAMAP-Rule:MF_00124}. FT ACT_SITE 88 FT /note="Proton acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00124, FT ECO:0000256|PIRSR:PIRSR035805-1" FT BINDING 9..16 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00124" FT BINDING 87..90 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00124" FT BINDING 145 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00124" FT BINDING 147 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00124" FT BINDING 182 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00124" FT BINDING 185 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00124" SQ SEQUENCE 192 AA; 21700 MW; 6F00321214D9A59C CRC64; MAQLYFYYSA MNAGKSTSLL QSSYNYRERG MHTLVMTASI DDRYGVGKVA SRLGIETEAQ VFGSNDNLTQ MISTSHADKT LHCILIDESQ FLSKEQVKQL TYVVDILDIP VLCYGLKTDF QGELFSGSHY LLAWADKLVE LKTICHCGRK ANMVVRLDGD GKPMREGEQV AIGGNESYES VCRKHFREFI WD //