ID   F8A3R9_CELGA            Unreviewed;       229 AA.
AC   F8A3R9;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   27-MAR-2024, entry version 58.
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=Celgi_1453 {ECO:0000313|EMBL:AEI11972.1};
OS   Cellulomonas gilvus (strain ATCC 13127 / NRRL B-14078) (Cellvibrio gilvus).
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Cellulomonadaceae;
OC   Cellulomonas.
OX   NCBI_TaxID=593907 {ECO:0000313|EMBL:AEI11972.1, ECO:0000313|Proteomes:UP000000485};
RN   [1] {ECO:0000313|Proteomes:UP000000485}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 13127 / NRRL B-14078 {ECO:0000313|Proteomes:UP000000485};
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Munk A., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA   Kyrpides N., Ivanova N., Ovchinnikova G., Pagani I., Mead D., Brumm P.,
RA   Woyke T.;
RT   "Complete sequence of Cellvibrio gilvus ATCC 13127.";
RL   Submitted (APR-2011) 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|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; CP002665; AEI11972.1; -; Genomic_DNA.
DR   RefSeq; WP_013883491.1; NC_015671.1.
DR   AlphaFoldDB; F8A3R9; -.
DR   STRING; 593907.Celgi_1453; -.
DR   KEGG; cga:Celgi_1453; -.
DR   eggNOG; COG1435; Bacteria.
DR   HOGENOM; CLU_064400_2_0_11; -.
DR   OrthoDB; 9781579at2; -.
DR   Proteomes; UP000000485; 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:UP000000485};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000544}.
FT   ACT_SITE        87
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR035805-1"
SQ   SEQUENCE   229 AA;  24843 MW;  DD36676D5457BC53 CRC64;
     MAELVFFSGT MDCGKSTLAL QMHHNHAARG RDGVLFTRHD RAGTATISSR LGLTKQAHEV
     DDATDFWHEV IARRTHGRPV DYLIGDEAQF YTAAQVEQLA RVVDELGVDV YAFGISTDFR
     ARLFPGAQRF VELADRVDVL QVRALCWCGA RATHNARVVG GRMVVEGAQV VVGDVGGADG
     TAEAADEVQY EVLCRRHHMR RMTAATARAA APSPQTLTAA LLGAEAVEV
//