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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

  1. ATP binding Source: UniProtKB-HAMAP
  2. metal ion binding Source: UniProtKB-KW
  3. thymidine kinase activity Source: UniProtKB-HAMAP

GO - Biological processi

  1. DNA biosynthetic process Source: UniProtKB-KW
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

Cytoplasm Curated

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
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.
OMAiVITGPMY.
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.
YP_007976748.1. NC_021214.1.
YP_008990629.1. NC_023151.1.

Genome annotation databases

EnsemblBacteriaiAAD35486; AAD35486; TM_0401.
GeneIDi897394.
KEGGitma:TM0401.
tmi:THEMA_02720.
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.
YP_007976748.1. NC_021214.1.
YP_008990629.1. NC_023151.1.

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.
PATRICi23935685. VBITheMar51294_0406.

Phylogenomic databases

eggNOGiCOG1435.
InParanoidiQ9WYN2.
KOiK00857.
OMAiVITGPMY.
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(2006) [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(2006) [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: April 1, 2015
This is version 98 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.