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Database: UniProt
Entry: O57203
LinkDB: O57203
Original site: O57203 
ID   KITH_VACCA              Reviewed;         177 AA.
AC   O57203; Q6J3E4;
DT   02-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   05-DEC-2018, entry version 74.
DE   RecName: Full=Thymidine kinase;
DE            EC=2.7.1.21;
GN   Name=TK; OrderedLocusNames=MVA086R, ACAM3000_MVA_086; ORFNames=J2R;
OS   Vaccinia virus (strain Ankara) (VACV).
OC   Viruses; dsDNA viruses, no RNA stage; Poxviridae; Chordopoxvirinae;
OC   Orthopoxvirus; Vaccinia virus.
OX   NCBI_TaxID=126794;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=9601507; DOI=10.1006/viro.1998.9123;
RA   Antoine G., Scheiflinger F., Dorner F., Falkner F.G.;
RT   "The complete genomic sequence of the modified vaccinia Ankara strain:
RT   comparison with other orthopoxviruses.";
RL   Virology 244:365-396(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Isolate Acambis 3000;
RA   Esposito J.J., Frace M., Sammons S.A., Olsen-Rasmussen M.S.,
RA   Osborne J., Khristova M., Wohlhueter R.M.;
RL   Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) IN COMPLEX WITH ZINC IONS AND
RP   TTP, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, ACTIVE SITE, AND DISULFIDE
RP   BONDS.
RX   PubMed=17062140; DOI=10.1186/1472-6807-6-22;
RA   El Omari K., Solaroli N., Karlsson A., Balzarini J., Stammers D.K.;
RT   "Structure of vaccinia virus thymidine kinase in complex with dTTP:
RT   insights for drug design.";
RL   BMC Struct. Biol. 6:22-22(2006).
CC   -!- FUNCTION: Phosphorylates thymidine and thymidine analogs, such as
CC       azidothymidine (AZT). Part of the salvage pathway for pyrimidine
CC       deoxyribonucleotide synthesis. {ECO:0000269|PubMed:17062140}.
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:0000269|PubMed:17062140};
CC   -!- SUBUNIT: Homotetramer. Two molecules of substrate bind to each
CC       enzyme tetramer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the thymidine kinase family. {ECO:0000305}.
DR   EMBL; U94848; AAB96503.1; -; Genomic_DNA.
DR   EMBL; AY603355; AAT10484.1; -; Genomic_DNA.
DR   PIR; T37362; T37362.
DR   PDB; 2J87; X-ray; 3.10 A; A/B/C/D=1-177.
DR   PDBsum; 2J87; -.
DR   ProteinModelPortal; O57203; -.
DR   SMR; O57203; -.
DR   BRENDA; 2.7.1.21; 6591.
DR   EvolutionaryTrace; O57203; -.
DR   Proteomes; UP000159908; Genome.
DR   Proteomes; UP000172909; Genome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion 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   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   1: Evidence at protein level;
KW   3D-structure; ATP-binding; Complete proteome; Disulfide bond;
KW   DNA synthesis; Kinase; Metal-binding; Nucleotide-binding; Transferase;
KW   Zinc.
FT   CHAIN         1    177       Thymidine kinase.
FT                                /FTId=PRO_0000174937.
FT   NP_BIND      11     18       ATP. {ECO:0000244|PDB:2J87,
FT                                ECO:0000269|PubMed:17062140}.
FT   REGION      157    161       Substrate binding. {ECO:0000244|PDB:2J87,
FT                                ECO:0000269|PubMed:17062140}.
FT   ACT_SITE     83     83       Proton acceptor. {ECO:0000244|PDB:2J87,
FT                                ECO:0000269|PubMed:17062140}.
FT   METAL       138    138       Zinc. {ECO:0000244|PDB:2J87,
FT                                ECO:0000269|PubMed:17062140}.
FT   METAL       141    141       Zinc. {ECO:0000244|PDB:2J87,
FT                                ECO:0000269|PubMed:17062140}.
FT   METAL       170    170       Zinc. {ECO:0000244|PDB:2J87,
FT                                ECO:0000269|PubMed:17062140}.
FT   METAL       173    173       Zinc. {ECO:0000244|PDB:2J87,
FT                                ECO:0000269|PubMed:17062140}.
FT   BINDING     113    113       Substrate; via amide nitrogen.
FT                                {ECO:0000244|PDB:2J87,
FT                                ECO:0000269|PubMed:17062140}.
FT   DISULFID    170    170       Interchain (with C-173).
FT                                {ECO:0000244|PDB:2J87,
FT                                ECO:0000269|PubMed:17062140}.
FT   DISULFID    173    173       Interchain (with C-170).
FT                                {ECO:0000244|PDB:2J87,
FT                                ECO:0000269|PubMed:17062140}.
FT   STRAND        5     10       {ECO:0000244|PDB:2J87}.
FT   HELIX        17     29       {ECO:0000244|PDB:2J87}.
FT   TURN         30     32       {ECO:0000244|PDB:2J87}.
FT   STRAND       35     40       {ECO:0000244|PDB:2J87}.
FT   STRAND       56     58       {ECO:0000244|PDB:2J87}.
FT   HELIX        66     69       {ECO:0000244|PDB:2J87}.
FT   TURN         70     72       {ECO:0000244|PDB:2J87}.
FT   HELIX        73     75       {ECO:0000244|PDB:2J87}.
FT   STRAND       77     82       {ECO:0000244|PDB:2J87}.
FT   HELIX        84     86       {ECO:0000244|PDB:2J87}.
FT   HELIX        90     99       {ECO:0000244|PDB:2J87}.
FT   STRAND      103    107       {ECO:0000244|PDB:2J87}.
FT   TURN        119    121       {ECO:0000244|PDB:2J87}.
FT   HELIX       122    126       {ECO:0000244|PDB:2J87}.
FT   STRAND      129    133       {ECO:0000244|PDB:2J87}.
FT   TURN        139    141       {ECO:0000244|PDB:2J87}.
FT   STRAND      143    145       {ECO:0000244|PDB:2J87}.
FT   STRAND      147    153       {ECO:0000244|PDB:2J87}.
FT   TURN        163    165       {ECO:0000244|PDB:2J87}.
FT   STRAND      166    169       {ECO:0000244|PDB:2J87}.
FT   HELIX       171    174       {ECO:0000244|PDB:2J87}.
SQ   SEQUENCE   177 AA;  20028 MW;  57E19BCEBE6F3C54 CRC64;
     MNGGHIQLII GPMFSGKSTE LIRRVRRYQI AQYKCVTIKY SNDNRYGTGL WTHDKNNFEA
     LEATKLCDVL ESITDFSVIG IDEGQFFPDI VEFCERMANE GKIVIVAALD GTFQRKPFNN
     ILNLIPLSEM VVKLTAVCMK CFKEASFSKR LGEETEIEII GGNDMYQSVC RKCYVGS
//
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