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Q9PPP5 (KITH_UREPA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 81. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:UU594
OrganismUreaplasma parvum serovar 3 (strain ATCC 700970) [Complete proteome] [HAMAP]
Taxonomic identifier273119 [NCBI]
Taxonomic lineageBacteriaTenericutesMollicutesMycoplasmataceaeUreaplasma

Protein attributes

Sequence length223 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

ATP + thymidine = ADP + thymidine 5'-phosphate. Ref.3

Subunit structure

Homotetramer. Ref.2 Ref.3

Subcellular location

Cytoplasm Potential 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 term3D-structure
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 – 223223Thymidine kinase HAMAP-Rule MF_00124
PRO_0000175042

Regions

Nucleotide binding19 – 268ATP By similarity
Nucleotide binding96 – 994ATP By similarity
Region178 – 1825Substrate binding HAMAP-Rule MF_00124

Sites

Active site971Proton acceptor Potential
Metal binding1531Zinc
Metal binding1561Zinc
Metal binding1911Zinc
Metal binding1941Zinc
Binding site1281Substrate; via amide nitrogen
Binding site1871Substrate

Secondary structure

........................................ 223
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9PPP5 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 27F3061B26979A0B

FASTA22325,367
        10         20         30         40         50         60 
MAKVNAFSKK IGWIELITGP MFAGKTAELI RRLHRLEYAD VKYLVFKPKI DTRSIRNIQS 

        70         80         90        100        110        120 
RTGTSLPSVE VESAPEILNY IMSNSFNDET KVIGIDEVQF FDDRICEVAN ILAENGFVVI 

       130        140        150        160        170        180 
ISGLDKNFKG EPFGPIAKLF TYADKITKLT AICNECGAEA THSLRKIDGK HADYNDDIVK 

       190        200        210        220 
IGCQEFYSAV CRHHHKVPNR PYLNSNSEEF IKFFKNKKRN KNI 

« Hide

References

« Hide 'large scale' references
[1]"The complete sequence of the mucosal pathogen Ureaplasma urealyticum."
Glass J.I., Lefkowitz E.J., Glass J.S., Heiner C.R., Chen E.Y., Cassell G.H.
Nature 407:757-762(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 700970.
[2]"Structures of thymidine kinase 1 of human and mycoplasmic origin."
Welin M., Kosinska U., Mikkelsen N.E., Carnrot C., Zhu C., Wang L., Eriksson S., Munch-Petersen B., Eklund H.
Proc. Natl. Acad. Sci. U.S.A. 101:17970-17975(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) IN COMPLEX WITH ZINC IONS AND THYMIDINE, SUBUNIT.
[3]"Structure of the substrate complex of thymidine kinase from Ureaplasma urealyticum and investigations of possible drug targets for the enzyme."
Kosinska U., Carnrot C., Eriksson S., Wang L., Eklund H.
FEBS J. 272:6365-6372(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH ZINC IONS AND THYMIDINE, CATALYTIC ACTIVITY, SUBUNIT.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF222894 Genomic DNA. Translation: AAF31008.1.
RefSeqNP_078433.1. NC_002162.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2B8TX-ray2.00A/B/C/D1-223[»]
2UZ3X-ray2.50A/B/C/D1-223[»]
ProteinModelPortalQ9PPP5.
SMRQ9PPP5. Positions 11-217.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING273119.UU594.

Chemistry

BindingDBQ9PPP5.
ChEMBLCHEMBL1075130.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAF31008; AAF31008; UU594.
GeneID876009.
KEGGuur:UU594.
PATRIC20534825. VBIUrePar45146_0617.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1435.
HOGENOMHOG000076390.
KOK00857.
OMAQAICLSC.
OrthoDBEOG69D3J2.

Enzyme and pathway databases

BioCycUPAR273119:GHVP-635-MONOMER.
BRENDA2.7.1.21. 9209.

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...

Other

EvolutionaryTraceQ9PPP5.

Entry information

Entry nameKITH_UREPA
AccessionPrimary (citable) accession number: Q9PPP5
Entry history
Integrated into UniProtKB/Swiss-Prot: November 7, 2003
Last sequence update: October 1, 2000
Last modified: May 14, 2014
This is version 81 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references