ID B1VAS4_PHYAS Unreviewed; 199 AA. AC B1VAS4; DT 20-MAY-2008, integrated into UniProtKB/TrEMBL. DT 20-MAY-2008, sequence version 1. DT 27-MAR-2024, entry version 85. 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 ECO:0000313|EMBL:CAM12047.1}; GN OrderedLocusNames=PA0713 {ECO:0000313|EMBL:CAM12047.1}; OS Phytoplasma australiense. OC Bacteria; Mycoplasmatota; Mollicutes; Acholeplasmatales; OC Acholeplasmataceae; Phytoplasma; 16SrXII (Stolbur group). OX NCBI_TaxID=59748 {ECO:0000313|EMBL:CAM12047.1, ECO:0000313|Proteomes:UP000008323}; RN [1] {ECO:0000313|EMBL:CAM12047.1, ECO:0000313|Proteomes:UP000008323} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=18359806; DOI=10.1128/JB.01301-07; RA Tran-Nguyen L.T., Kube M., Schneider B., Reinhardt R., Gibb K.S.; RT "Comparative genome analysis of 'Candidatus Phytoplasma australiense' RT (subgroup tuf-Australia I; rp-A) and 'Ca. Phytoplasma asteris' strains OY-M RT and AY-WB."; RL J. Bacteriol. 190:3979-3991(2008). 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; AM422018; CAM12047.1; -; Genomic_DNA. DR AlphaFoldDB; B1VAS4; -. DR STRING; 59748.PA0713; -. DR KEGG; pal:PA0713; -. DR eggNOG; COG1435; Bacteria. DR Proteomes; UP000008323; 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:UP000008323}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP- KW 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 14..21 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" SQ SEQUENCE 199 AA; 22397 MW; 69449E73F2E74516 CRC64; MPKEQQGFIE VICGPMFAGK TEALIKRYQE AQKLKKNILS FKPRIDNRYS SEGFIVSHSQ NKFPAILIDQ SRDILPFVTP ETDLIIIDEV QFLDNDIFGI VDYLANQNIQ IILAGLDLDF KGKPFGPMPY LLALAEVVTK LTAICAVSGK KATKTQRLIN GKPAKSNDST ILVGGQEYHE PRCRRHHELL DVDKKTINL //