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Protein

Thymidine kinase

Gene

tdk

Organism
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

ATP + thymidine = ADP + thymidine 5'-phosphate.

Kineticsi

  1. KM=40 µM for ATP1 Publication
  2. KM=0.5 µM for thymidine1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei53 – 531ATP
    Active sitei84 – 841Proton acceptorSequence Analysis
    Binding sitei115 – 1151Substrate; via amide nitrogen
    Metal bindingi140 – 1401Zinc
    Metal bindingi143 – 1431Zinc
    Binding sitei169 – 1691Substrate
    Metal bindingi173 – 1731Zinc
    Metal bindingi176 – 1761Zinc

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi10 – 178ATP
    Nucleotide bindingi83 – 864ATPBy similarity

    GO - Molecular functioni

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Kinase, Transferase

    Keywords - Biological processi

    DNA synthesis

    Keywords - Ligandi

    ATP-binding, Metal-binding, Nucleotide-binding, Zinc

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Thymidine kinase (EC:2.7.1.21)
    Gene namesi
    Name:tdk
    Ordered Locus Names:TM_0401
    OrganismiThermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
    Taxonomic identifieri243274 [NCBI]
    Taxonomic lineageiBacteriaThermotogaeThermotogalesThermotogaceaeThermotoga
    ProteomesiUP000008183 Componenti: Chromosome

    Subcellular locationi

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi53 – 531H → A: Reduced affinity for ATP. 1 Publication
    Mutagenesisi55 – 551G → W: Reduced affinity for ATP. 1 Publication
    Mutagenesisi129 – 1291L → W: Reduced affinity for thymidine. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 184184Thymidine kinasePRO_0000175040Add
    BLAST

    Interactioni

    Subunit structurei

    Homotetramer.2 Publications

    Protein-protein interaction databases

    DIPiDIP-29527N.
    STRINGi243274.TM0401.

    Structurei

    Secondary structure

    1
    184
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi5 – 117Combined sources
    Helixi16 – 2914Combined sources
    Beta strandi33 – 397Combined sources
    Beta strandi61 – 655Combined sources
    Helixi66 – 727Combined sources
    Beta strandi77 – 826Combined sources
    Helixi85 – 873Combined sources
    Helixi92 – 10110Combined sources
    Beta strandi105 – 1139Combined sources
    Helixi121 – 1299Combined sources
    Beta strandi131 – 1355Combined sources
    Turni141 – 1433Combined sources
    Beta strandi146 – 1483Combined sources
    Beta strandi150 – 1534Combined sources
    Turni166 – 1683Combined sources
    Beta strandi169 – 1724Combined sources
    Helixi174 – 1807Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2ORWX-ray1.50A/B1-184[»]
    2QPOX-ray1.95A/B/C/D1-184[»]
    2QQ0X-ray1.50A/B1-184[»]
    2QQEX-ray1.90A/B1-184[»]
    ProteinModelPortaliQ9WYN2.
    SMRiQ9WYN2. Positions 2-182.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9WYN2.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni161 – 1644Substrate binding

    Sequence similaritiesi

    Belongs to the thymidine kinase family.Curated

    Phylogenomic databases

    eggNOGiCOG1435.
    InParanoidiQ9WYN2.
    KOiK00857.
    OMAiVTKVHAI.
    OrthoDBiEOG69D3J2.

    Family and domain databases

    Gene3Di3.40.50.300. 1 hit.
    HAMAPiMF_00124. Thymidine_kinase.
    InterProiIPR027417. P-loop_NTPase.
    IPR001267. Thymidine_kinase.
    IPR020633. Thymidine_kinase_CS.
    [Graphical view]
    PANTHERiPTHR11441. PTHR11441. 1 hit.
    PfamiPF00265. TK. 1 hit.
    [Graphical view]
    PIRSFiPIRSF035805. TK_cell. 1 hit.
    SUPFAMiSSF52540. SSF52540. 1 hit.
    PROSITEiPS00603. TK_CELLULAR_TYPE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q9WYN2-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MSGKLTVITG PMYSGKTTEL LSFVEIYKLG KKKVAVFKPK IDSRYHSTMI
    60 70 80 90 100
    VSHSGNGVEA HVIERPEEMR KYIEEDTRGV FIDEVQFFNP SLFEVVKDLL
    110 120 130 140 150
    DRGIDVFCAG LDLTHKQNPF ETTALLLSLA DTVIKKKAVC HRCGEYNATL
    160 170 180
    TLKVAGGEEE IDVGGQEKYI AVCRDCYNTL KKRV
    Length:184
    Mass (Da):20,654
    Last modified:November 1, 1999 - v1
    Checksum:i906B2C1BE3A7EDDA
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AE000512 Genomic DNA. Translation: AAD35486.1.
    PIRiB72383.
    RefSeqiNP_228211.1. NC_000853.1.
    WP_004083238.1. NZ_CP011107.1.

    Genome annotation databases

    EnsemblBacteriaiAAD35486; AAD35486; TM_0401.
    GeneIDi897394.
    KEGGitma:TM0401.
    tmi:THEMA_02720.
    tmm:Tmari_0398.
    PATRICi23935685. VBITheMar51294_0406.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AE000512 Genomic DNA. Translation: AAD35486.1.
    PIRiB72383.
    RefSeqiNP_228211.1. NC_000853.1.
    WP_004083238.1. NZ_CP011107.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2ORWX-ray1.50A/B1-184[»]
    2QPOX-ray1.95A/B/C/D1-184[»]
    2QQ0X-ray1.50A/B1-184[»]
    2QQEX-ray1.90A/B1-184[»]
    ProteinModelPortaliQ9WYN2.
    SMRiQ9WYN2. Positions 2-182.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    DIPiDIP-29527N.
    STRINGi243274.TM0401.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAD35486; AAD35486; TM_0401.
    GeneIDi897394.
    KEGGitma:TM0401.
    tmi:THEMA_02720.
    tmm:Tmari_0398.
    PATRICi23935685. VBITheMar51294_0406.

    Phylogenomic databases

    eggNOGiCOG1435.
    InParanoidiQ9WYN2.
    KOiK00857.
    OMAiVTKVHAI.
    OrthoDBiEOG69D3J2.

    Miscellaneous databases

    EvolutionaryTraceiQ9WYN2.

    Family and domain databases

    Gene3Di3.40.50.300. 1 hit.
    HAMAPiMF_00124. Thymidine_kinase.
    InterProiIPR027417. P-loop_NTPase.
    IPR001267. Thymidine_kinase.
    IPR020633. Thymidine_kinase_CS.
    [Graphical view]
    PANTHERiPTHR11441. PTHR11441. 1 hit.
    PfamiPF00265. TK. 1 hit.
    [Graphical view]
    PIRSFiPIRSF035805. TK_cell. 1 hit.
    SUPFAMiSSF52540. SSF52540. 1 hit.
    PROSITEiPS00603. TK_CELLULAR_TYPE. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 43589 / MSB8 / DSM 3109 / JCM 10099.
    2. "Binding of ATP to TK1-like enzymes is associated with a conformational change in the quaternary structure."
      Segura-Pena D., Lutz S., Monnerjahn C., Konrad M., Lavie A.
      J. Mol. Biol. 369:129-141(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) IN COMPLEX WITH ZINC IONS; THYMIDINE AND ATP ANALOGS, SUBUNIT.
    3. "Quaternary structure change as a mechanism for the regulation of thymidine kinase 1-like enzymes."
      Segura-Pena D., Lichter J., Trani M., Konrad M., Lavie A., Lutz S.
      Structure 15:1555-1566(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) IN COMPLEX WITH ZINC IONS AND THYMIDINE, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF HIS-53; GLY-55 AND LEU-129.

    Entry informationi

    Entry nameiKITH_THEMA
    AccessioniPrimary (citable) accession number: Q9WYN2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 30, 2000
    Last sequence update: November 1, 1999
    Last modified: July 22, 2015
    This is version 100 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.