Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q8FHX4 (KITH_ECOL6) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 65. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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:c1703
OrganismEscherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC) [Complete proteome] [HAMAP]
Taxonomic identifier199310 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length205 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Phosphorylates both thymidine and deoxyuridine By similarity. HAMAP-Rule MF_00124

Catalytic activity

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

Enzyme regulation

Allosteric enzyme which is feedback inhibited by dTTP and activated by a number of dNDP and dNTP By similarity. HAMAP-Rule MF_00124

Subunit structure

Homotetramer By similarity. HAMAP-Rule MF_00124

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00124.

Sequence similarities

Belongs to the thymidine kinase family.

Ontologies

Keywords
   Biological processDNA synthesis
   Cellular componentCytoplasm
   LigandATP-binding
Metal-binding
Nucleotide-binding
Zinc
   Molecular functionKinase
Transferase
   Technical termAllosteric enzyme
Complete 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-HAMAP

thymidine kinase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

zinc ion binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 205205Thymidine kinase HAMAP-Rule MF_00124
PRO_0000174972

Regions

Nucleotide binding9 – 168ATP By similarity
Nucleotide binding87 – 904ATP By similarity

Sites

Active site881Proton acceptor Potential
Metal binding1451Zinc By similarity
Metal binding1471Zinc By similarity
Metal binding1821Zinc By similarity
Metal binding1851Zinc By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8FHX4 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: 533166D9E91D1F52

FASTA20523,400
        10         20         30         40         50         60 
MAQLYFYYSA MNAGKSTALL QSSYNYQERG MRTVVYTAEI DDRFGAGKVS SRIGLSSPAK 

        70         80         90        100        110        120 
LFNQNSSLFD EIRAEHEQQA IHCVLVDECQ FLTRQQVYEL SEVVDQLDIP VLCYGLRTDF 

       130        140        150        160        170        180 
RGELFIGSQY LLAWSDKLVE LKTICFCGRK ASMVLRLDQA GRPYNEGEQV VIGGNERYVS 

       190        200 
VCRKHYKEAL EVGSLTAIQE RHRHD 

« Hide

References

[1]"Extensive mosaic structure revealed by the complete genome sequence of uropathogenic Escherichia coli."
Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D., Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F., Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T., Donnenberg M.S., Blattner F.R.
Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CFT073 / ATCC 700928 / UPEC.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE014075 Genomic DNA. Translation: AAN80170.1.
RefSeqNP_753608.1. NC_004431.1.

3D structure databases

ProteinModelPortalQ8FHX4.
SMRQ8FHX4. Positions 1-189.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING199310.c1703.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAN80170; AAN80170; c1703.
GeneID1035485.
KEGGecc:c1703.
PATRIC18281330. VBIEscCol75197_1584.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000076391.
KOK00857.
OMARTICHCG.
OrthoDBEOG69D3J2.
ProtClustDBPRK04296.

Enzyme and pathway databases

BioCycECOL199310:C1703-MONOMER.

Family and domain databases

HAMAPMF_00124. Thymidine_kinase.
InterProIPR027417. P-loop_NTPase.
IPR001267. Thymidine_kinase.
IPR020633. Thymidine_kinase_CS.
IPR020634. Thymidine_kinase_subgr.
[Graphical view]
PANTHERPTHR11441. PTHR11441. 1 hit.
PfamPF00265. TK. 1 hit.
[Graphical view]
PIRSFPIRSF035805. TK_cell. 1 hit.
SUPFAMSSF52540. SSF52540. 1 hit.
PROSITEPS00603. TK_CELLULAR_TYPE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameKITH_ECOL6
AccessionPrimary (citable) accession number: Q8FHX4
Entry history
Integrated into UniProtKB/Swiss-Prot: March 1, 2005
Last sequence update: March 1, 2003
Last modified: April 16, 2014
This is version 65 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families