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Database: UniProt
Entry: A0A223V592_9FLAO
LinkDB: A0A223V592_9FLAO
Original site: A0A223V592_9FLAO 
ID   A0A223V592_9FLAO        Unreviewed;       214 AA.
AC   A0A223V592;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   27-MAR-2024, entry version 19.
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:GGD77432.1};
GN   ORFNames=CJ263_08770 {ECO:0000313|EMBL:ASV30300.1}, GCM10011412_14040
GN   {ECO:0000313|EMBL:GGD77432.1};
OS   Maribacter cobaltidurans.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Maribacter.
OX   NCBI_TaxID=1178778 {ECO:0000313|EMBL:ASV30300.1, ECO:0000313|Proteomes:UP000215244};
RN   [1] {ECO:0000313|EMBL:ASV30300.1, ECO:0000313|Proteomes:UP000215244}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B1 {ECO:0000313|EMBL:ASV30300.1,
RC   ECO:0000313|Proteomes:UP000215244};
RA   Wu Y.-H., Cheng H., Xu X.-W.;
RT   "The complete genome sequence of Maribacter sp. B1, isolated from deep-sea
RT   sediment.";
RL   Submitted (AUG-2017) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:GGD77432.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CGMCC 1.15508 {ECO:0000313|EMBL:GGD77432.1};
RX   PubMed=30832757;
RA   Wu L., Ma J.;
RT   "The Global Catalogue of Microorganisms (GCM) 10K type strain sequencing
RT   project: providing services to taxonomists for standard genome sequencing
RT   and annotation.";
RL   Int. J. Syst. Evol. Microbiol. 69:895-898(2019).
RN   [3] {ECO:0000313|EMBL:GGD77432.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CGMCC 1.15508 {ECO:0000313|EMBL:GGD77432.1};
RA   Sun Q., Zhou Y.;
RL   Submitted (DEC-2022) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; CP022957; ASV30300.1; -; Genomic_DNA.
DR   EMBL; BMJL01000002; GGD77432.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A223V592; -.
DR   KEGG; marb:CJ263_08770; -.
DR   OrthoDB; 9781579at2; -.
DR   Proteomes; UP000215244; Chromosome.
DR   Proteomes; UP000603042; Unassembled WGS sequence.
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:UP000215244};
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   214 AA;  24035 MW;  458C5180EFE298C0 CRC64;
     MFLENTVNHK EQFGWIEVIA GSMFSGKTEE LIRRLKRAQF AKLKVEIFKP MVDTRYDDDM
     VVSHDANEIR STPVPAAANI RILADTCDVI GIDEAQFFDD EIVTVCNDLA NKGVRVIVAG
     LDMDFKGNPF GPMPALMATA EYVTKVHAIC TRTGNLANYS FRKSNNDKLV MLGETNEYEP
     LSRGAFYKAL LKQKVKGMEV DVEEIKYPNK KSNA
//
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