ID D1BTG9_XYLCX Unreviewed; 215 AA. AC D1BTG9; DT 19-JAN-2010, integrated into UniProtKB/TrEMBL. DT 19-JAN-2010, sequence version 1. DT 27-MAR-2024, entry version 73. 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=Xcel_1929 {ECO:0000313|EMBL:ACZ30948.1}; OS Xylanimonas cellulosilytica (strain DSM 15894 / CECT 5975 / LMG 20990 / OS XIL07). OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; OC Promicromonosporaceae; Xylanimonas. OX NCBI_TaxID=446471 {ECO:0000313|EMBL:ACZ30948.1, ECO:0000313|Proteomes:UP000002255}; RN [1] {ECO:0000313|Proteomes:UP000002255} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 15894 / CECT 5975 / LMG 20990 / XIL07 RC {ECO:0000313|Proteomes:UP000002255}; 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 Mikhailova N., Foster B., Clum A., Brettin T., Detter J.C., Han C., RA Larimer F., Land M., Hauser L., Markowitz V., Cheng J.F., Hugenholtz P., RA Woyke T., Wu D., Gehrich-Schroeter G., Schneider S., Pukall S.R., RA Klenk H.P., Eisen J.A.; RT "The complete chromosome of Xylanimonas cellulosilytica DSM 15894."; RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:ACZ30948.1, ECO:0000313|Proteomes:UP000002255} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 15894 / CECT 5975 / LMG 20990 / XIL07 RC {ECO:0000313|Proteomes:UP000002255}; RX PubMed=21304672; DOI=10.4056/sigs.571102; RA Foster B., Pukall R., Abt B., Nolan M., Glavina Del Rio T., Chen F., RA Lucas S., Tice H., Pitluck S., Cheng J.-F., Chertkov O., Brettin T., RA Han C., Detter J.C., Bruce D., Goodwin L., Ivanova N., Mavromatis K., RA Pati A., Mikhailova N., Chen A., Palaniappan K., Land M., Hauser L., RA Chang Y.-J., Jeffries C.D., Chain P., Rohde M., Goeker M., Bristow J., RA Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.-P., RA Lapidus A.; RT "Complete genome sequence of Xylanimonas cellulosilytica type strain RT (XIL07)."; RL Stand. Genomic Sci. 2:1-8(2010). 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 -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|HAMAP-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; CP001821; ACZ30948.1; -; Genomic_DNA. DR RefSeq; WP_012878690.1; NC_013530.1. DR AlphaFoldDB; D1BTG9; -. DR STRING; 446471.Xcel_1929; -. DR KEGG; xce:Xcel_1929; -. DR eggNOG; COG1435; Bacteria. DR HOGENOM; CLU_064400_2_0_11; -. DR OrthoDB; 9781579at2; -. DR Proteomes; UP000002255; 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: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 {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 Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP- KW Rule:MF_00124}; Reference proteome {ECO:0000313|Proteomes:UP000002255}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP- KW Rule:MF_00124}. FT ACT_SITE 87 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 86..89 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00124" SQ SEQUENCE 215 AA; 23757 MW; 2DCF6A74220C3DDC CRC64; MAELVFFSGT MDSGKSTLAL QTDYNYAARG RTGLVFTRHD RAGAARISSR LGLETDAREA DAATDFWELV AEEGRQGRPV DYLVCDEAQF YSPEQIEQLA RLVDEVEIDV FAFGITTDFR TKLFPGSARL LELADRIEVL QVPALCWCGR PATHQARTVD GVMVVEGEQV VVGDTAASAA VVAYEVLCRR HHMRRMTASS ARQHATTDEA RLDLV //