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Database: UniProt
Entry: Q7MVV7
LinkDB: Q7MVV7
Original site: Q7MVV7 
ID   KITH_PORGI              Reviewed;         204 AA.
AC   Q7MVV7;
DT   01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 1.
DT   16-JAN-2019, entry version 89.
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}; OrderedLocusNames=PG_0925;
OS   Porphyromonas gingivalis (strain ATCC BAA-308 / W83).
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales;
OC   Porphyromonadaceae; Porphyromonas.
OX   NCBI_TaxID=242619;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-308 / W83;
RX   PubMed=12949112; DOI=10.1128/JB.185.18.5591-5601.2003;
RA   Nelson K.E., Fleischmann R.D., DeBoy R.T., Paulsen I.T., Fouts D.E.,
RA   Eisen J.A., Daugherty S.C., Dodson R.J., Durkin A.S., Gwinn M.L.,
RA   Haft D.H., Kolonay J.F., Nelson W.C., Mason T.M., Tallon L., Gray J.,
RA   Granger D., Tettelin H., Dong H., Galvin J.L., Duncan M.J.,
RA   Dewhirst F.E., Fraser C.M.;
RT   "Complete genome sequence of the oral pathogenic bacterium
RT   Porphyromonas gingivalis strain W83.";
RL   J. Bacteriol. 185:5591-5601(2003).
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; AE015924; AAQ66060.1; -; Genomic_DNA.
DR   RefSeq; WP_004584156.1; NC_002950.2.
DR   ProteinModelPortal; Q7MVV7; -.
DR   SMR; Q7MVV7; -.
DR   STRING; 242619.PG0925; -.
DR   PRIDE; Q7MVV7; -.
DR   EnsemblBacteria; AAQ66060; AAQ66060; PG_0925.
DR   KEGG; pgi:PG_0925; -.
DR   eggNOG; ENOG4107T8J; Bacteria.
DR   eggNOG; COG1435; LUCA.
DR   KO; K00857; -.
DR   OMA; KEQFGWI; -.
DR   OrthoDB; 1279539at2; -.
DR   Proteomes; UP000000588; 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   PANTHER; PTHR11441; PTHR11441; 1.
DR   Pfam; PF00265; TK; 1.
DR   PIRSF; PIRSF035805; TK_cell; 1.
DR   SUPFAM; SSF52540; SSF52540; 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    204       Thymidine kinase.
FT                                /FTId=PRO_0000175005.
FT   NP_BIND      23     30       ATP. {ECO:0000255|HAMAP-Rule:MF_00124}.
FT   NP_BIND      95     98       ATP. {ECO:0000255|HAMAP-Rule:MF_00124}.
FT   ACT_SITE     96     96       Proton acceptor. {ECO:0000255|HAMAP-
FT                                Rule:MF_00124}.
FT   METAL       152    152       Zinc. {ECO:0000255|HAMAP-Rule:MF_00124}.
FT   METAL       155    155       Zinc. {ECO:0000255|HAMAP-Rule:MF_00124}.
FT   METAL       184    184       Zinc. {ECO:0000255|HAMAP-Rule:MF_00124}.
FT   METAL       187    187       Zinc. {ECO:0000255|HAMAP-Rule:MF_00124}.
SQ   SEQUENCE   204 AA;  22741 MW;  256F6C6396963C43 CRC64;
     MDYEIENNHA DSIRRGSIEV ICGSMFSGKT EELLRRLRRA KIARQTVEIF KPTIDIRYDE
     TDVVSHDKNA IASTPVDNSA NILLLSSQVD VVGIDEAQFF DEGLVEVAQQ LADQGVRVVI
     AGLDMDFRRQ PFGPMPGLCA IADSVTKVHA VCVECGRLAS YSFRRVQGDQ QVMLGELNEY
     SPLCRTCYRK CSSPPQTEEI HSTI
//
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