ID E3DRG9_HALPG Unreviewed; 192 AA. AC E3DRG9; DT 11-JAN-2011, integrated into UniProtKB/TrEMBL. DT 11-JAN-2011, sequence version 1. DT 27-MAR-2024, entry version 55. 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=Hprae_1976 {ECO:0000313|EMBL:ADO78101.1}; OS Halanaerobium praevalens (strain ATCC 33744 / DSM 2228 / GSL). OC Bacteria; Bacillota; Clostridia; Halanaerobiales; Halanaerobiaceae; OC Halanaerobium. OX NCBI_TaxID=572479 {ECO:0000313|EMBL:ADO78101.1, ECO:0000313|Proteomes:UP000006866}; RN [1] {ECO:0000313|Proteomes:UP000006866} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33744 / DSM 2228 / GSL RC {ECO:0000313|Proteomes:UP000006866}; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., RA Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., Ivanova N., RA Ovchinnikova G., Chertkov O., Detter J.C., Han C., Larimer F., Land M., RA Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., RA Tindall B., Pomrenke H.G., Brambilla E., Klenk H.-P., Eisen J.A.; RT "The complete genome of Halanaerobium praevalens DSM 2228."; RL Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:ADO78101.1, ECO:0000313|Proteomes:UP000006866} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33744 / DSM 2228 / GSL RC {ECO:0000313|Proteomes:UP000006866}; RX PubMed=21886858; RA Ivanova N., Sikorski J., Chertkov O., Nolan M., Lucas S., Hammon N., RA Deshpande S., Cheng J.F., Tapia R., Han C., Goodwin L., Pitluck S., RA Huntemann M., Liolios K., Pagani I., Mavromatis K., Ovchinikova G., RA Pati A., Chen A., Palaniappan K., Land M., Hauser L., Brambilla E.M., RA Kannan K.P., Rohde M., Tindall B.J., Goker M., Detter J.C., Woyke T., RA Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., RA Klenk H.P., Lapidus A.; RT "Complete genome sequence of the extremely halophilic Halanaerobium RT praevalens type strain (GSL)."; RL Stand. Genomic Sci. 4:312-321(2011). 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; CP002175; ADO78101.1; -; Genomic_DNA. DR RefSeq; WP_014554117.1; NC_017455.1. DR AlphaFoldDB; E3DRG9; -. DR STRING; 572479.Hprae_1976; -. DR KEGG; hpk:Hprae_1976; -. DR PATRIC; fig|572479.3.peg.2011; -. DR eggNOG; COG1435; Bacteria. DR HOGENOM; CLU_064400_3_0_9; -. DR OrthoDB; 9781579at2; -. DR Proteomes; UP000006866; 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}; Reference proteome {ECO:0000313|Proteomes:UP000006866}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP- KW Rule:MF_00124}; Zinc {ECO:0000256|HAMAP-Rule:MF_00124}. FT ACT_SITE 89 FT /note="Proton acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00124, FT ECO:0000256|PIRSR:PIRSR035805-1" FT BINDING 15..22 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00124" FT BINDING 88..91 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 148 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00124" FT BINDING 183 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00124" FT BINDING 186 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00124" SQ SEQUENCE 192 AA; 21632 MW; 14E0DA779ECD278F CRC64; MYKITKSGWL EIITGPMYCG KSEELIRRLN RVKIAKQKVR VFKPVLDDRY SKKDVVSHSG NSIEAVPVDH PEEILKRIDK TVDVVGIDEA QFFHSDLVAI CEELADEGIR VILAGLDRDF RNQPFGPMPE LMARAEYVDK LHAICIQCGE PASRTQRLIN GQPARADDPV ILVGAAEVYE ARCRSCHSLR TD //