ID KITH_CLOAB Reviewed; 195 AA. AC Q97F65; DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2001, sequence version 1. DT 02-SEP-2026, entry version 127. 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=CA_C2887; OS Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / IAM OS 19013 / LMG 5710 / NBRC 13948 / NRRL B-527 / VKM B-1787 / 2291 / W). OC Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=272562; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 824 / DSM 792 / JCM 1419 / IAM 19013 / LMG 5710 / NBRC RC 13948 / NRRL B-527 / VKM B-1787 / 2291 / W; RX PubMed=11466286; DOI=10.1128/jb.183.16.4823-4838.2001; RA Noelling J., Breton G., Omelchenko M.V., Makarova K.S., Zeng Q., Gibson R., RA Lee H.M., Dubois J., Qiu D., Hitti J., Wolf Y.I., Tatusov R.L., Sabathe F., RA Doucette-Stamm L.A., Soucaille P., Daly M.J., Bennett G.N., Koonin E.V., RA Smith D.R.; RT "Genome sequence and comparative analysis of the solvent-producing RT bacterium Clostridium acetobutylicum."; RL J. Bacteriol. 183:4823-4838(2001). RN [2] RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 1-191 IN COMPLEX WITH ZINC IONS RP AND ADP. RG Northeast structural genomics consortium (NESG); RT "X-ray structure of clostridium acetobutylicum genomics target CAR26."; RL Submitted (FEB-2009) to the PDB data bank. 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 -!- 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; AE001437; AAK80830.1; -; Genomic_DNA. DR PIR; C97255; C97255. DR RefSeq; WP_010966171.1; NC_003030.1. DR PDB; 1XX6; X-ray; 2.00 A; A/B=1-191. DR AlphaFoldDB; Q97F65; -. DR SMR; Q97F65; -. DR STRING; 272562.CA_C2887; -. DR GeneID; 44999375; -. DR KEGG; cac:CA_C2887; -. DR PATRIC; fig|272562.8.peg.3071; -. DR eggNOG; COG1435; Bacteria. DR HOGENOM; CLU_064400_3_0_9; -. DR OrthoDB; 9781579at2; -. DR BRENDA; 2.7.1.21; 1452. DR EvolutionaryTrace; Q97F65; -. DR Proteomes; UP000000814; 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 FunFam; 3.30.60.20:FF:000026; Thymidine kinase; 1. DR FunFam; 3.40.50.300:FF:000384; Thymidine kinase; 1. 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. DR PDBsum; 1XX6; -. PE 1: Evidence at protein level; KW 3D-structure; ATP-binding; Cytoplasm; DNA synthesis; Kinase; Metal-binding; KW Nucleotide-binding; Reference proteome; Transferase; Zinc. FT CHAIN 1..195 FT /note="Thymidine kinase" FT /id="PRO_0000174967" FT ACT_SITE 89 FT /note="Proton acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00124" FT BINDING 15..22 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT BINDING 23 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT BINDING 57..58 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT BINDING 88..91 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00124" FT BINDING 120 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 145 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT BINDING 148 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT BINDING 179 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 183 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT BINDING 186 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT STRAND 9..14 FT /evidence="ECO:0007829|PDB:1XX6" FT HELIX 21..34 FT /evidence="ECO:0007829|PDB:1XX6" FT STRAND 39..44 FT /evidence="ECO:0007829|PDB:1XX6" FT STRAND 54..56 FT /evidence="ECO:0007829|PDB:1XX6" FT STRAND 62..64 FT /evidence="ECO:0007829|PDB:1XX6" FT STRAND 66..71 FT /evidence="ECO:0007829|PDB:1XX6" FT HELIX 73..77 FT /evidence="ECO:0007829|PDB:1XX6" FT STRAND 83..87 FT /evidence="ECO:0007829|PDB:1XX6" FT HELIX 90..92 FT /evidence="ECO:0007829|PDB:1XX6" FT HELIX 96..106 FT /evidence="ECO:0007829|PDB:1XX6" FT STRAND 110..115 FT /evidence="ECO:0007829|PDB:1XX6" FT HELIX 128..134 FT /evidence="ECO:0007829|PDB:1XX6" FT STRAND 136..140 FT /evidence="ECO:0007829|PDB:1XX6" FT TURN 146..148 FT /evidence="ECO:0007829|PDB:1XX6" FT STRAND 149..152 FT /evidence="ECO:0007829|PDB:1XX6" FT STRAND 154..159 FT /evidence="ECO:0007829|PDB:1XX6" FT STRAND 177..182 FT /evidence="ECO:0007829|PDB:1XX6" FT TURN 184..186 FT /evidence="ECO:0007829|PDB:1XX6" SQ SEQUENCE 195 AA; 22303 MW; 6EDB551986B203BA CRC64; MYRPKDHGWV EVIVGPMYSG KSEELIRRIR RAKIAKQKIQ VFKPEIDNRY SKEDVVSHMG EKEQAVAIKN SREILKYFEE DTEVIAIDEV QFFDDEIVEI VNKIAESGRR VICAGLDMDF RGKPFGPIPE LMAIAEFVDK IQAICVVCGN PATRTQRLIN GKPAFYDDPV VLIGAMESYE ARCRKCHVVP QKKEV //