ID A6GYI4_FLAPJ Unreviewed; 202 AA. AC A6GYI4; DT 24-JUL-2007, integrated into UniProtKB/TrEMBL. DT 24-JUL-2007, sequence version 1. DT 27-MAR-2024, entry version 88. 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:CAL43157.1}; GN OrderedLocusNames=FP1063 {ECO:0000313|EMBL:CAL43157.1}; OS Flavobacterium psychrophilum (strain ATCC 49511 / DSM 21280 / CIP 103535 / OS JIP02/86). OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae; Flavobacterium. OX NCBI_TaxID=402612 {ECO:0000313|EMBL:CAL43157.1, ECO:0000313|Proteomes:UP000006394}; RN [1] {ECO:0000313|EMBL:CAL43157.1, ECO:0000313|Proteomes:UP000006394} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 49511 / DSM 21280 / CIP 103535 / JIP02/86 RC {ECO:0000313|Proteomes:UP000006394}; RX PubMed=17592475; DOI=10.1038/nbt1313; RA Duchaud E., Boussaha M., Loux V., Bernardet J.F., Michel C., Kerouault B., RA Mondot S., Nicolas P., Bossy R., Caron C., Bessieres P., Gibrat J.F., RA Claverol S., Dumetz F., Le Henaff M., Benmansour A.; RT "Complete genome sequence of the fish pathogen Flavobacterium RT psychrophilum."; RL Nat. Biotechnol. 25:763-769(2007). 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; AM398681; CAL43157.1; -; Genomic_DNA. DR RefSeq; WP_011963208.1; NC_009613.3. DR RefSeq; YP_001295968.1; NC_009613.3. DR AlphaFoldDB; A6GYI4; -. DR STRING; 402612.FP1063; -. DR EnsemblBacteria; CAL43157; CAL43157; FP1063. DR GeneID; 66552461; -. DR KEGG; fps:FP1063; -. DR PATRIC; fig|402612.5.peg.1077; -. DR eggNOG; COG1435; Bacteria. DR HOGENOM; CLU_064400_3_0_10; -. DR OrthoDB; 9781579at2; -. DR Proteomes; UP000006394; 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:UP000006394}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP- KW Rule:MF_00124}. FT ACT_SITE 94 FT /note="Proton acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00124, FT ECO:0000256|PIRSR:PIRSR035805-1" FT BINDING 21..28 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00124" FT BINDING 93..96 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00124" SQ SEQUENCE 202 AA; 22748 MW; 5858A0C11E12CFF4 CRC64; MFLENTVNHK EQFGWIEVIC GSMFSGKTEE LIRRLKRAQF AKQKVEIFKP TIDTRYDDEM VVSHNKNEIR STPVPAAANI AILAQGCDVV GIDEAQFFDD EIVKICNDLA NSGIRVIVAG LDMDFKGNPF GPMPALMATA EYVTKVHAVC TRTGNLANYS FRKTDNDKLV MLGETEEYEP LSRAAYYNAM RENMIVKDAE HL //