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Database: UniProt
Entry: A4ITL0
LinkDB: A4ITL0
Original site: A4ITL0 
ID   KITH_GEOTN              Reviewed;         207 AA.
AC   A4ITL0;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2007, sequence version 1.
DT   16-JAN-2019, entry version 74.
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};
GN   OrderedLocusNames=GTNG_3325;
OS   Geobacillus thermodenitrificans (strain NG80-2).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX   NCBI_TaxID=420246;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NG80-2;
RX   PubMed=17372208; DOI=10.1073/pnas.0609650104;
RA   Feng L., Wang W., Cheng J., Ren Y., Zhao G., Gao C., Tang Y., Liu X.,
RA   Han W., Peng X., Liu R., Wang L.;
RT   "Genome and proteome of long-chain alkane degrading Geobacillus
RT   thermodenitrificans NG80-2 isolated from a deep-subsurface oil
RT   reservoir.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:5602-5607(2007).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + thymidine = ADP + dTMP + H(+);
CC         Xref=Rhea:RHEA:19129, ChEBI:CHEBI:15378, ChEBI:CHEBI:17748,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:63528, ChEBI:CHEBI:456216;
CC         EC=2.7.1.21; Evidence={ECO:0000255|HAMAP-Rule:MF_00124};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_00124}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00124}.
CC   -!- SIMILARITY: Belongs to the thymidine kinase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00124}.
DR   EMBL; CP000557; ABO68664.1; -; Genomic_DNA.
DR   RefSeq; WP_008880714.1; NC_009328.1.
DR   ProteinModelPortal; A4ITL0; -.
DR   SMR; A4ITL0; -.
DR   STRING; 420246.GTNG_3325; -.
DR   EnsemblBacteria; ABO68664; ABO68664; GTNG_3325.
DR   GeneID; 31762558; -.
DR   KEGG; gtn:GTNG_3325; -.
DR   eggNOG; ENOG4107104; Bacteria.
DR   eggNOG; COG1435; LUCA.
DR   HOGENOM; HOG000076390; -.
DR   KO; K00857; -.
DR   OMA; CAGLDQD; -.
DR   OrthoDB; 1279539at2; -.
DR   BioCyc; GTHE420246:G1G82-3472-MONOMER; -.
DR   Proteomes; UP000001578; 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   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; PTHR11441; 1.
DR   Pfam; PF00265; TK; 1.
DR   PIRSF; PIRSF035805; TK_cell; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS00603; TK_CELLULAR_TYPE; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Complete proteome; Cytoplasm; DNA synthesis; Kinase;
KW   Metal-binding; Nucleotide-binding; Transferase; Zinc.
FT   CHAIN         1    207       Thymidine kinase.
FT                                /FTId=PRO_1000018155.
FT   NP_BIND      15     22       ATP. {ECO:0000255|HAMAP-Rule:MF_00124}.
FT   NP_BIND      88     91       ATP. {ECO:0000255|HAMAP-Rule:MF_00124}.
FT   ACT_SITE     89     89       Proton acceptor. {ECO:0000255|HAMAP-
FT                                Rule:MF_00124}.
FT   METAL       145    145       Zinc. {ECO:0000255|HAMAP-Rule:MF_00124}.
FT   METAL       148    148       Zinc. {ECO:0000255|HAMAP-Rule:MF_00124}.
FT   METAL       183    183       Zinc. {ECO:0000255|HAMAP-Rule:MF_00124}.
FT   METAL       186    186       Zinc. {ECO:0000255|HAMAP-Rule:MF_00124}.
SQ   SEQUENCE   207 AA;  22819 MW;  40C38E9BEA6CA824 CRC64;
     MYVMTQSGWL EVICGSMFSG KSEELIRRIR RAQFAKQEVK VFKPTIDNRY SEDAVVSHNG
     NSVIAIPVAT PAELFRYISA TTDVVAIDEV QFFSDDIIDV VQTLADRGYR VIAAGLDQDF
     RGEPFGPVPA LMALAESVTK LQAVCTVCGS PASRTQRLIN GAPASYDDPI ILVGASEAYE
     PRCRHHHEVP GKPKKQHDHP FAERASE
//
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