ID   Q5FUA6_GLUOX            Unreviewed;       180 AA.
AC   Q5FUA6;
DT   01-MAR-2005, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2005, sequence version 1.
DT   27-MAR-2024, entry version 102.
DE   RecName: Full=Thymidine kinase {ECO:0000256|ARBA:ARBA00012118, ECO:0000256|RuleBase:RU000544};
DE            EC=2.7.1.21 {ECO:0000256|ARBA:ARBA00012118, ECO:0000256|RuleBase:RU000544};
GN   OrderedLocusNames=GOX0257 {ECO:0000313|EMBL:AAW60040.1};
OS   Gluconobacter oxydans (strain 621H) (Gluconobacter suboxydans).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Acetobacteraceae; Gluconobacter.
OX   NCBI_TaxID=290633 {ECO:0000313|EMBL:AAW60040.1, ECO:0000313|Proteomes:UP000006375};
RN   [1] {ECO:0000313|EMBL:AAW60040.1, ECO:0000313|Proteomes:UP000006375}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=621H {ECO:0000313|EMBL:AAW60040.1,
RC   ECO:0000313|Proteomes:UP000006375};
RX   PubMed=15665824; DOI=10.1038/nbt1062;
RA   Prust C., Hoffmeister M., Liesegang H., Wiezer A., Fricke W.F.,
RA   Ehrenreich A., Gottschalk G., Deppenmeier U.;
RT   "Complete genome sequence of the acetic acid bacterium Gluconobacter
RT   oxydans.";
RL   Nat. Biotechnol. 23:195-200(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|RuleBase:RU000544};
CC   -!- SIMILARITY: Belongs to the thymidine kinase family.
CC       {ECO:0000256|ARBA:ARBA00007587, ECO:0000256|RuleBase:RU004165}.
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DR   EMBL; CP000009; AAW60040.1; -; Genomic_DNA.
DR   RefSeq; WP_011251843.1; NZ_LT900338.1.
DR   AlphaFoldDB; Q5FUA6; -.
DR   STRING; 290633.GOX0257; -.
DR   GeneID; 56904524; -.
DR   KEGG; gox:GOX0257; -.
DR   eggNOG; COG1435; Bacteria.
DR   HOGENOM; CLU_064400_3_1_5; -.
DR   Proteomes; UP000006375; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004797; F:thymidine kinase activity; IEA:UniProtKB-EC.
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   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|RuleBase:RU000544};
KW   DNA synthesis {ECO:0000256|ARBA:ARBA00022634,
KW   ECO:0000256|RuleBase:RU000544};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|RuleBase:RU000544};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU000544};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006375};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000544}.
FT   ACT_SITE        77
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR035805-1"
SQ   SEQUENCE   180 AA;  19791 MW;  D2EE672D897B1D3D CRC64;
     MTVRGRLVLY VGPMFAGKSA HLIAAAKRQT DVLALKPGFD TRDGSELVSR DGSHLAAVSA
     NAWPEDADRY SHIVLDEGQF WVAPHYHGDI VEDIRAARAR GADVTVGGLD TDYRRVPFDV
     MTRLMDEADE VIALTARCHV CGAPAAWTAK THETGHLLET GDQELYEARC DAHWTLPDRP
//