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Database: UniProt
Entry: Q8DU63
LinkDB: Q8DU63
Original site: Q8DU63 
ID   KITH_STRMU              Reviewed;         194 AA.
AC   Q8DU63;
DT   01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   05-DEC-2018, entry version 91.
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=SMU_1086;
OS   Streptococcus mutans serotype c (strain ATCC 700610 / UA159).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=210007;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700610 / UA159;
RX   PubMed=12397186; DOI=10.1073/pnas.172501299;
RA   Ajdic D.J., McShan W.M., McLaughlin R.E., Savic G., Chang J.,
RA   Carson M.B., Primeaux C., Tian R., Kenton S., Jia H.G., Lin S.P.,
RA   Qian Y., Li S., Zhu H., Najar F.Z., Lai H., White J., Roe B.A.,
RA   Ferretti J.J.;
RT   "Genome sequence of Streptococcus mutans UA159, a cariogenic dental
RT   pathogen.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:14434-14439(2002).
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; AE014133; AAN58784.1; -; Genomic_DNA.
DR   RefSeq; NP_721478.1; NC_004350.2.
DR   RefSeq; WP_011074582.1; NC_004350.2.
DR   ProteinModelPortal; Q8DU63; -.
DR   SMR; Q8DU63; -.
DR   STRING; 210007.SMU_1086; -.
DR   PRIDE; Q8DU63; -.
DR   EnsemblBacteria; AAN58784; AAN58784; SMU_1086.
DR   GeneID; 1029394; -.
DR   KEGG; smu:SMU_1086; -.
DR   PATRIC; fig|210007.7.peg.973; -.
DR   eggNOG; ENOG4107104; Bacteria.
DR   eggNOG; COG1435; LUCA.
DR   KO; K00857; -.
DR   OMA; KEQFGWI; -.
DR   PhylomeDB; Q8DU63; -.
DR   BioCyc; SMUT210007:G1FZX-1034-MONOMER; -.
DR   Proteomes; UP000002512; 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; Reference proteome; Transferase;
KW   Zinc.
FT   CHAIN         1    194       Thymidine kinase.
FT                                /FTId=PRO_0000175031.
FT   NP_BIND      12     19       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       146    146       Zinc. {ECO:0000255|HAMAP-Rule:MF_00124}.
FT   METAL       149    149       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   194 AA;  22231 MW;  18E8FE938D452CFE CRC64;
     MTVLAQLYYK YGTMNSGKTI EILKVAHNYE EQGKPVVIMT SSLDTRDGFG VVASRIGMRR
     EAVTITDDMD IFAYIENMFK KPYCILIDES QFLSQKNVYD LARIVDELDV PVMAFGLKND
     FQNHLFEGSR ELLLLADKIE EIKTICQFCS KKATMVLRTE NGRPVYKGNQ IQIGGNETYI
     PVCRRHYFHP PIKA
//
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