ID KITH_UREPA Reviewed; 223 AA. AC Q9PPP5; DT 07-NOV-2003, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 27-MAR-2024, entry version 119. 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}; OrderedLocusNames=UU594; OS Ureaplasma parvum serovar 3 (strain ATCC 700970). OC Bacteria; Mycoplasmatota; Mycoplasmoidales; Mycoplasmoidaceae; Ureaplasma. OX NCBI_TaxID=273119; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700970; RX PubMed=11048724; DOI=10.1038/35037619; RA Glass J.I., Lefkowitz E.J., Glass J.S., Heiner C.R., Chen E.Y., RA Cassell G.H.; RT "The complete sequence of the mucosal pathogen Ureaplasma urealyticum."; RL Nature 407:757-762(2000). RN [2] RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) IN COMPLEX WITH ZINC IONS AND RP THYMIDINE, AND SUBUNIT. RX PubMed=15611477; DOI=10.1073/pnas.0406332102; RA Welin M., Kosinska U., Mikkelsen N.E., Carnrot C., Zhu C., Wang L., RA Eriksson S., Munch-Petersen B., Eklund H.; RT "Structures of thymidine kinase 1 of human and mycoplasmic origin."; RL Proc. Natl. Acad. Sci. U.S.A. 101:17970-17975(2004). RN [3] RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH ZINC IONS AND RP THYMIDINE, CATALYTIC ACTIVITY, AND SUBUNIT. RX PubMed=16336273; DOI=10.1111/j.1742-4658.2005.05030.x; RA Kosinska U., Carnrot C., Eriksson S., Wang L., Eklund H.; RT "Structure of the substrate complex of thymidine kinase from Ureaplasma RT urealyticum and investigations of possible drug targets for the enzyme."; RL FEBS J. 272:6365-6372(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:0000255|HAMAP-Rule:MF_00124, CC ECO:0000269|PubMed:16336273}; CC -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_00124, CC ECO:0000269|PubMed:15611477, ECO:0000269|PubMed:16336273}. 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; AF222894; AAF31008.1; -; Genomic_DNA. DR RefSeq; WP_006688765.1; NC_002162.1. DR PDB; 2B8T; X-ray; 2.00 A; A/B/C/D=1-223. DR PDB; 2UZ3; X-ray; 2.50 A; A/B/C/D=1-223. DR PDBsum; 2B8T; -. DR PDBsum; 2UZ3; -. DR AlphaFoldDB; Q9PPP5; -. DR SMR; Q9PPP5; -. DR STRING; 273119.UU594; -. DR BindingDB; Q9PPP5; -. DR ChEMBL; CHEMBL1075130; -. DR DrugBank; DB02452; Thymidine 5'-triphosphate. DR DrugCentral; Q9PPP5; -. DR EnsemblBacteria; AAF31008; AAF31008; UU594. DR GeneID; 29672699; -. DR KEGG; uur:UU594; -. DR eggNOG; COG1435; Bacteria. DR HOGENOM; CLU_064400_3_0_14; -. DR OrthoDB; 9781579at2; -. DR BRENDA; 2.7.1.21; 9209. DR EvolutionaryTrace; Q9PPP5; -. DR PRO; PR:Q9PPP5; -. DR Proteomes; UP000000423; 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 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..223 FT /note="Thymidine kinase" FT /id="PRO_0000175042" FT ACT_SITE 97 FT /note="Proton acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00124" FT BINDING 19..26 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00124" FT BINDING 96..99 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00124" FT BINDING 128 FT /ligand="substrate" FT BINDING 153 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT BINDING 156 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT BINDING 178..182 FT /ligand="substrate" FT BINDING 187 FT /ligand="substrate" FT BINDING 191 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT BINDING 194 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT STRAND 13..18 FT /evidence="ECO:0007829|PDB:2B8T" FT HELIX 25..38 FT /evidence="ECO:0007829|PDB:2B8T" FT STRAND 43..48 FT /evidence="ECO:0007829|PDB:2B8T" FT HELIX 52..54 FT /evidence="ECO:0007829|PDB:2B8T" FT STRAND 61..63 FT /evidence="ECO:0007829|PDB:2UZ3" FT STRAND 65..67 FT /evidence="ECO:0007829|PDB:2UZ3" FT STRAND 69..73 FT /evidence="ECO:0007829|PDB:2B8T" FT HELIX 75..82 FT /evidence="ECO:0007829|PDB:2B8T" FT STRAND 92..95 FT /evidence="ECO:0007829|PDB:2B8T" FT HELIX 98..100 FT /evidence="ECO:0007829|PDB:2B8T" FT HELIX 105..114 FT /evidence="ECO:0007829|PDB:2B8T" FT STRAND 118..122 FT /evidence="ECO:0007829|PDB:2B8T" FT STRAND 130..132 FT /evidence="ECO:0007829|PDB:2B8T" FT HELIX 136..142 FT /evidence="ECO:0007829|PDB:2B8T" FT STRAND 144..148 FT /evidence="ECO:0007829|PDB:2B8T" FT TURN 154..156 FT /evidence="ECO:0007829|PDB:2B8T" FT STRAND 158..160 FT /evidence="ECO:0007829|PDB:2B8T" FT STRAND 162..167 FT /evidence="ECO:0007829|PDB:2B8T" FT TURN 184..186 FT /evidence="ECO:0007829|PDB:2B8T" FT STRAND 187..190 FT /evidence="ECO:0007829|PDB:2B8T" FT HELIX 192..194 FT /evidence="ECO:0007829|PDB:2B8T" FT HELIX 207..215 FT /evidence="ECO:0007829|PDB:2B8T" SQ SEQUENCE 223 AA; 25367 MW; 27F3061B26979A0B CRC64; MAKVNAFSKK IGWIELITGP MFAGKTAELI RRLHRLEYAD VKYLVFKPKI DTRSIRNIQS RTGTSLPSVE VESAPEILNY IMSNSFNDET KVIGIDEVQF FDDRICEVAN ILAENGFVVI ISGLDKNFKG EPFGPIAKLF TYADKITKLT AICNECGAEA THSLRKIDGK HADYNDDIVK IGCQEFYSAV CRHHHKVPNR PYLNSNSEEF IKFFKNKKRN KNI //