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Q9WYN2 (KITH_THEMA) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 73. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Thymidine kinase
EC=2.7.1.21
Gene names
Name:tdk
Ordered Locus Names:TM_0401
OrganismThermotoga maritima
Taxonomic identifier2336 [NCBI]
Taxonomic lineageBacteria › Thermotogae › Thermotogales › Thermotogaceae › Thermotoga

Protein attributes

Sequence length184 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

ATP + thymidine = ADP + thymidine 5'-phosphate. HAMAP MF_00124

Subunit structure

Homotetramer. Ref.2 Ref.3

Subcellular location

Cytoplasm Potential HAMAP MF_00124.

Sequence similarities

Belongs to the thymidine kinase family.

Biophysicochemical properties

Kinetic parameters:

KM=40 µM for ATP Ref.3

KM=0.5 µM for thymidine

Ontologies

Keywords
   Biological processDNA synthesis
   Cellular componentCytoplasm
   LigandATP-binding
Metal-binding
Nucleotide-binding
Zinc
   Molecular functionKinase
Transferase
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological processDNA replication

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

thymidine kinase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 184184Thymidine kinase HAMAP MF_00124
PRO_0000175040

Regions

Nucleotide binding10 – 178ATP HAMAP MF_00124
Nucleotide binding83 – 864ATP By similarity
Region161 – 1644Substrate binding HAMAP MF_00124

Sites

Active site841Proton acceptor Potential
Metal binding1401Zinc
Metal binding1431Zinc
Metal binding1731Zinc
Metal binding1761Zinc
Binding site531ATP
Binding site1151Substrate; via amide nitrogen
Binding site1691Substrate

Experimental info

Mutagenesis531H → A: Reduced affinity for ATP. Ref.3
Mutagenesis551G → W: Reduced affinity for ATP. Ref.3
Mutagenesis1291L → W: Reduced affinity for thymidine. Ref.3

Secondary structure

1 ............................... 184
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9WYN2 [UniParc].

Last modified November 1, 1999. Version 1.
Checksum: 906B2C1BE3A7EDDA

FASTA18420,654
        10         20         30         40         50         60 
MSGKLTVITG PMYSGKTTEL LSFVEIYKLG KKKVAVFKPK IDSRYHSTMI VSHSGNGVEA 

        70         80         90        100        110        120 
HVIERPEEMR KYIEEDTRGV FIDEVQFFNP SLFEVVKDLL DRGIDVFCAG LDLTHKQNPF 

       130        140        150        160        170        180 
ETTALLLSLA DTVIKKKAVC HRCGEYNATL TLKVAGGEEE IDVGGQEKYI AVCRDCYNTL 


KKRV

« Hide

References

« Hide 'large scale' references
[1]"Evidence for lateral gene transfer between Archaea and Bacteria from genome sequence of Thermotoga maritima."
Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M., Cotton M.D., Pratt M.S. expand/collapse author list , Phillips C.A., Richardson D.L., Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.
Nature 399:323-329(1999) [PubMed: 10360571] [Abstract]
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: 17407781] [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: 18073106] [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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE000512 Genomic DNA. Translation: AAD35486.1.
PIRB72383.
RefSeqNP_228211.1. NC_000853.1.

3D structure databases

PDBe
RCSB PDB
PDBj
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[»]
ProteinModelPortalQ9WYN2.
SMRQ9WYN2. Positions 2-182.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-29527N.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID897394.
GenomeReviewsGene locus TM_0401 in contig AE000512_GR.
KEGGtma:TM0401.
NMPDRfig|243274.1.peg.395.
PATRIC23935685. VBITheMar51294_0406.
TIGRTM_0401.

Phylogenomic databases

HOGENOMHBG522108.
OMAVITGPMY.
PhylomeDBQ9WYN2.
ProtClustDBPRK04296.

Enzyme and pathway databases

BioCycTMAR243274:TM_0401-MONOMER.

Family and domain databases

HAMAPMF_00124. Thymidine_kinase.
[Tree]
InterProIPR001267. Thymidine_kinase.
IPR020633. Thymidine_kinase_CS.
IPR020634. Thymidine_kinase_subgr.
[Graphical view]
KOK00857.
PANTHERPTHR11441. TK_cell. 1 hit.
PfamPF00265. TK. 1 hit.
[Graphical view]
PIRSFPIRSF035805. TK_cell. 1 hit.
PROSITEPS00603. TK_CELLULAR_TYPE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameKITH_THEMA
AccessionPrimary (citable) accession number: Q9WYN2
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: November 1, 1999
Last modified: January 25, 2012
This is version 73 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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