ID Q4A5P2_MYCS5 Unreviewed; 183 AA. AC Q4A5P2; DT 13-SEP-2005, integrated into UniProtKB/TrEMBL. DT 13-SEP-2005, sequence version 1. DT 27-MAR-2024, entry version 99. 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:AAZ43929.1}; GN OrderedLocusNames=MS53_0521 {ECO:0000313|EMBL:AAZ43929.1}; OS Mycoplasmopsis synoviae (strain 53) (Mycoplasma synoviae). OC Bacteria; Mycoplasmatota; Mycoplasmoidales; Metamycoplasmataceae; OC Mycoplasmopsis. OX NCBI_TaxID=262723 {ECO:0000313|EMBL:AAZ43929.1, ECO:0000313|Proteomes:UP000000549}; RN [1] {ECO:0000313|EMBL:AAZ43929.1, ECO:0000313|Proteomes:UP000000549} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=53 {ECO:0000313|EMBL:AAZ43929.1, RC ECO:0000313|Proteomes:UP000000549}; RX PubMed=16077101; DOI=10.1128/JB.187.16.5568-5577.2005; RA Vasconcelos A.T., Ferreira H.B., Bizarro C.V., Bonatto S.L., Carvalho M.O., RA Pinto P.M., Almeida D.F., Almeida L.G., Almeida R., Alves-Filho L., RA Assuncao E.N., Azevedo V.A., Bogo M.R., Brigido M.M., Brocchi M., RA Burity H.A., Camargo A.A., Camargo S.S., Carepo M.S., Carraro D.M., RA de Mattos Cascardo J.C., Castro L.A., Cavalcanti G., Chemale G., RA Collevatti R.G., Cunha C.W., Dallagiovanna B., Dambros B.P., RA Dellagostin O.A., Falcao C., Fantinatti-Garboggini F., Felipe M.S., RA Fiorentin L., Franco G.R., Freitas N.S., Frias D., Grangeiro T.B., RA Grisard E.C., Guimaraes C.T., Hungria M., Jardim S.N., Krieger M.A., RA Laurino J.P., Lima L.F., Lopes M.I., Loreto E.L., Madeira H.M., RA Manfio G.P., Maranhao A.Q., Martinkovics C.T., Medeiros S.R., Moreira M.A., RA Neiva M., Ramalho-Neto C.E., Nicolas M.F., Oliveira S.C., Paixao R.F., RA Pedrosa F.O., Pena S.D., Pereira M., Pereira-Ferrari L., Piffer I., RA Pinto L.S., Potrich D.P., Salim A.C., Santos F.R., Schmitt R., RA Schneider M.P., Schrank A., Schrank I.S., Schuck A.F., Seuanez H.N., RA Silva D.W., Silva R., Silva S.C., Soares C.M., Souza K.R., Souza R.C., RA Staats C.C., Steffens M.B., Teixeira S.M., Urmenyi T.P., Vainstein M.H., RA Zuccherato L.W., Simpson A.J., Zaha A.; RT "Swine and poultry pathogens: the complete genome sequences of two strains RT of Mycoplasma hyopneumoniae and a strain of Mycoplasma synoviae."; RL J. Bacteriol. 187:5568-5577(2005). 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; AE017245; AAZ43929.1; -; Genomic_DNA. DR RefSeq; WP_011283658.1; NC_007294.1. DR AlphaFoldDB; Q4A5P2; -. DR STRING; 262723.MS53_0521; -. DR GeneID; 61970740; -. DR KEGG; msy:MS53_0521; -. DR eggNOG; COG1435; Bacteria. DR HOGENOM; CLU_064400_3_0_14; -. DR OrthoDB; 9781579at2; -. DR Proteomes; UP000000549; 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 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 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:UP000000549}; 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 176 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00124" FT BINDING 179 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00124" SQ SEQUENCE 183 AA; 21146 MW; CA97CF80A439C64E CRC64; MRWKYDIGSL EVITGPMFAG KSNEIIRILN VNQIAGFKPL SFKPDFDTRW SVNHIVSRTG SKMETINLKD PKDIWNHIKK DTQVIAFDEV HFFDMSIVAE IQKLIEKKYK VIVSGLDMDY LGKPFEVVSQ LCCLADKIKK LKAVCMNCHG VANMTYRKVD NNERNLLGDS EYEARCRNCH KLR //