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Database: UniProt
Entry: Q9WYN2
LinkDB: Q9WYN2
Original site: Q9WYN2 
ID   KITH_THEMA              Reviewed;         184 AA.
AC   Q9WYN2;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   16-JAN-2019, entry version 118.
DE   RecName: Full=Thymidine kinase;
DE            EC=2.7.1.21;
GN   Name=tdk; OrderedLocusNames=TM_0401;
OS   Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099).
OC   Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX   NCBI_TaxID=243274;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43589 / MSB8 / DSM 3109 / JCM 10099;
RX   PubMed=10360571; DOI=10.1038/20601;
RA   Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J.,
RA   Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A.,
RA   McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M.,
RA   Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L.,
RA   Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O.,
RA   Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.;
RT   "Evidence for lateral gene transfer between Archaea and Bacteria from
RT   genome sequence of Thermotoga maritima.";
RL   Nature 399:323-329(1999).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) IN COMPLEX WITH ZINC IONS;
RP   THYMIDINE AND ATP ANALOGS, AND SUBUNIT.
RX   PubMed=17407781; DOI=10.1016/j.jmb.2007.02.104;
RA   Segura-Pena D., Lutz S., Monnerjahn C., Konrad M., Lavie A.;
RT   "Binding of ATP to TK1-like enzymes is associated with a
RT   conformational change in the quaternary structure.";
RL   J. Mol. Biol. 369:129-141(2007).
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) IN COMPLEX WITH ZINC IONS AND
RP   THYMIDINE, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF
RP   HIS-53; GLY-55 AND LEU-129.
RX   PubMed=18073106; DOI=10.1016/j.str.2007.09.025;
RA   Segura-Pena D., Lichter J., Trani M., Konrad M., Lavie A., Lutz S.;
RT   "Quaternary structure change as a mechanism for the regulation of
RT   thymidine kinase 1-like enzymes.";
RL   Structure 15:1555-1566(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;
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=40 uM for ATP {ECO:0000269|PubMed:18073106};
CC         KM=0.5 uM for thymidine {ECO:0000269|PubMed:18073106};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:17407781,
CC       ECO:0000269|PubMed:18073106}.
CC   -!- INTERACTION:
CC       Self; NbExp=2; IntAct=EBI-15674853, EBI-15674853;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the thymidine kinase family. {ECO:0000305}.
DR   EMBL; AE000512; AAD35486.1; -; Genomic_DNA.
DR   PIR; B72383; B72383.
DR   RefSeq; NP_228211.1; NC_000853.1.
DR   RefSeq; WP_004083238.1; NZ_CP011107.1.
DR   PDB; 2ORW; X-ray; 1.50 A; A/B=1-184.
DR   PDB; 2QPO; X-ray; 1.95 A; A/B/C/D=1-184.
DR   PDB; 2QQ0; X-ray; 1.50 A; A/B=1-184.
DR   PDB; 2QQE; X-ray; 1.90 A; A/B=1-184.
DR   PDBsum; 2ORW; -.
DR   PDBsum; 2QPO; -.
DR   PDBsum; 2QQ0; -.
DR   PDBsum; 2QQE; -.
DR   ProteinModelPortal; Q9WYN2; -.
DR   SMR; Q9WYN2; -.
DR   DIP; DIP-29527N; -.
DR   STRING; 243274.TM0401; -.
DR   EnsemblBacteria; AAD35486; AAD35486; TM_0401.
DR   GeneID; 897394; -.
DR   KEGG; tma:TM0401; -.
DR   eggNOG; ENOG4107104; Bacteria.
DR   eggNOG; COG1435; LUCA.
DR   InParanoid; Q9WYN2; -.
DR   KO; K00857; -.
DR   OMA; KEQFGWI; -.
DR   OrthoDB; 1279539at2; -.
DR   EvolutionaryTrace; Q9WYN2; -.
DR   Proteomes; UP000008183; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0004797; F:thymidine kinase activity; IBA:GO_Central.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0071897; P:DNA biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0006259; P:DNA metabolic process; IBA:GO_Central.
DR   GO; GO:0046104; P:thymidine metabolic process; IBA:GO_Central.
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   1: Evidence at protein level;
KW   3D-structure; ATP-binding; Complete proteome; Cytoplasm;
KW   DNA synthesis; Kinase; Metal-binding; Nucleotide-binding;
KW   Reference proteome; Transferase; Zinc.
FT   CHAIN         1    184       Thymidine kinase.
FT                                /FTId=PRO_0000175040.
FT   NP_BIND      10     17       ATP.
FT   NP_BIND      83     86       ATP. {ECO:0000250}.
FT   REGION      161    164       Substrate binding.
FT   ACT_SITE     84     84       Proton acceptor. {ECO:0000255}.
FT   METAL       140    140       Zinc.
FT   METAL       143    143       Zinc.
FT   METAL       173    173       Zinc.
FT   METAL       176    176       Zinc.
FT   BINDING      53     53       ATP.
FT   BINDING     115    115       Substrate; via amide nitrogen.
FT   BINDING     169    169       Substrate.
FT   MUTAGEN      53     53       H->A: Reduced affinity for ATP.
FT                                {ECO:0000269|PubMed:18073106}.
FT   MUTAGEN      55     55       G->W: Reduced affinity for ATP.
FT                                {ECO:0000269|PubMed:18073106}.
FT   MUTAGEN     129    129       L->W: Reduced affinity for thymidine.
FT                                {ECO:0000269|PubMed:18073106}.
FT   STRAND        5     11       {ECO:0000244|PDB:2ORW}.
FT   HELIX        16     29       {ECO:0000244|PDB:2ORW}.
FT   STRAND       33     39       {ECO:0000244|PDB:2ORW}.
FT   STRAND       61     65       {ECO:0000244|PDB:2ORW}.
FT   HELIX        66     72       {ECO:0000244|PDB:2ORW}.
FT   STRAND       77     82       {ECO:0000244|PDB:2ORW}.
FT   HELIX        85     87       {ECO:0000244|PDB:2ORW}.
FT   HELIX        92    101       {ECO:0000244|PDB:2ORW}.
FT   STRAND      105    113       {ECO:0000244|PDB:2ORW}.
FT   HELIX       121    129       {ECO:0000244|PDB:2ORW}.
FT   STRAND      131    135       {ECO:0000244|PDB:2ORW}.
FT   TURN        141    143       {ECO:0000244|PDB:2ORW}.
FT   STRAND      146    148       {ECO:0000244|PDB:2QQE}.
FT   STRAND      150    153       {ECO:0000244|PDB:2ORW}.
FT   TURN        166    168       {ECO:0000244|PDB:2ORW}.
FT   STRAND      169    172       {ECO:0000244|PDB:2ORW}.
FT   HELIX       174    180       {ECO:0000244|PDB:2ORW}.
SQ   SEQUENCE   184 AA;  20654 MW;  906B2C1BE3A7EDDA CRC64;
     MSGKLTVITG PMYSGKTTEL LSFVEIYKLG KKKVAVFKPK IDSRYHSTMI VSHSGNGVEA
     HVIERPEEMR KYIEEDTRGV FIDEVQFFNP SLFEVVKDLL DRGIDVFCAG LDLTHKQNPF
     ETTALLLSLA DTVIKKKAVC HRCGEYNATL TLKVAGGEEE IDVGGQEKYI AVCRDCYNTL
     KKRV
//
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