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Protein

Thymidine kinase

Gene

tdk

Organism
Ureaplasma parvum serovar 3 (strain ATCC 700970)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

ATP + thymidine = ADP + thymidine 5'-phosphate.UniRule annotation1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei97 – 971Proton acceptorUniRule annotation
Binding sitei128 – 1281Substrate; via amide nitrogen
Metal bindingi153 – 1531Zinc
Metal bindingi156 – 1561Zinc
Binding sitei187 – 1871Substrate
Metal bindingi191 – 1911Zinc
Metal bindingi194 – 1941Zinc

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi19 – 268ATPUniRule annotation
Nucleotide bindingi96 – 994ATPUniRule annotation

GO - Molecular functioni

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

Enzyme and pathway databases

BioCyciUPAR273119:GHVP-635-MONOMER.
BRENDAi2.7.1.21. 9209.

Names & Taxonomyi

Protein namesi
Recommended name:
Thymidine kinaseUniRule annotation (EC:2.7.1.21UniRule annotation)
Gene namesi
Name:tdkUniRule annotation
Ordered Locus Names:UU594
OrganismiUreaplasma parvum serovar 3 (strain ATCC 700970)
Taxonomic identifieri273119 [NCBI]
Taxonomic lineageiBacteriaTenericutesMollicutesMycoplasmataceaeUreaplasma
ProteomesiUP000000423: Chromosome

Subcellular locationi

Cytoplasm UniRule annotation

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 223223Thymidine kinasePRO_0000175042Add
BLAST

Interactioni

Subunit structurei

Homotetramer.UniRule annotation2 Publications

Protein-protein interaction databases

STRINGi273119.UU594.

Structurei

Secondary structure

1
223
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi13 – 186Combined sources
Helixi25 – 3814Combined sources
Beta strandi43 – 486Combined sources
Helixi52 – 543Combined sources
Beta strandi69 – 735Combined sources
Helixi75 – 828Combined sources
Beta strandi92 – 954Combined sources
Helixi98 – 1003Combined sources
Helixi105 – 11410Combined sources
Beta strandi118 – 1225Combined sources
Beta strandi130 – 1323Combined sources
Helixi136 – 1427Combined sources
Beta strandi144 – 1485Combined sources
Turni154 – 1563Combined sources
Beta strandi158 – 1603Combined sources
Beta strandi162 – 1676Combined sources
Turni184 – 1863Combined sources
Beta strandi187 – 1904Combined sources
Helixi192 – 1943Combined sources
Helixi207 – 2159Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2B8TX-ray2.00A/B/C/D1-223[»]
2UZ3X-ray2.50A/B/C/D1-223[»]
ProteinModelPortaliQ9PPP5.
SMRiQ9PPP5. Positions 11-217.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9PPP5.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni178 – 1825Substrate binding

Sequence similaritiesi

Belongs to the thymidine kinase family.UniRule annotation

Phylogenomic databases

eggNOGiCOG1435.
HOGENOMiHOG000076390.
KOiK00857.
OMAiVITGPMY.
OrthoDBiEOG69D3J2.

Family and domain databases

HAMAPiMF_00124. Thymidine_kinase.
InterProiIPR027417. P-loop_NTPase.
IPR001267. Thymidine_kinase.
IPR020633. Thymidine_kinase_CS.
IPR020634. Thymidine_kinase_subgr.
[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.

Q9PPP5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAKVNAFSKK IGWIELITGP MFAGKTAELI RRLHRLEYAD VKYLVFKPKI
60 70 80 90 100
DTRSIRNIQS RTGTSLPSVE VESAPEILNY IMSNSFNDET KVIGIDEVQF
110 120 130 140 150
FDDRICEVAN ILAENGFVVI ISGLDKNFKG EPFGPIAKLF TYADKITKLT
160 170 180 190 200
AICNECGAEA THSLRKIDGK HADYNDDIVK IGCQEFYSAV CRHHHKVPNR
210 220
PYLNSNSEEF IKFFKNKKRN KNI
Length:223
Mass (Da):25,367
Last modified:October 1, 2000 - v1
Checksum:i27F3061B26979A0B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF222894 Genomic DNA. Translation: AAF31008.1.
RefSeqiNP_078433.1. NC_002162.1.

Genome annotation databases

EnsemblBacteriaiAAF31008; AAF31008; UU594.
GeneIDi876009.
KEGGiuur:UU594.
PATRICi20534825. VBIUrePar45146_0617.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF222894 Genomic DNA. Translation: AAF31008.1.
RefSeqiNP_078433.1. NC_002162.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2B8TX-ray2.00A/B/C/D1-223[»]
2UZ3X-ray2.50A/B/C/D1-223[»]
ProteinModelPortaliQ9PPP5.
SMRiQ9PPP5. Positions 11-217.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi273119.UU594.

Chemistry

BindingDBiQ9PPP5.
ChEMBLiCHEMBL1075130.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAF31008; AAF31008; UU594.
GeneIDi876009.
KEGGiuur:UU594.
PATRICi20534825. VBIUrePar45146_0617.

Phylogenomic databases

eggNOGiCOG1435.
HOGENOMiHOG000076390.
KOiK00857.
OMAiVITGPMY.
OrthoDBiEOG69D3J2.

Enzyme and pathway databases

BioCyciUPAR273119:GHVP-635-MONOMER.
BRENDAi2.7.1.21. 9209.

Miscellaneous databases

EvolutionaryTraceiQ9PPP5.

Family and domain databases

HAMAPiMF_00124. Thymidine_kinase.
InterProiIPR027417. P-loop_NTPase.
IPR001267. Thymidine_kinase.
IPR020633. Thymidine_kinase_CS.
IPR020634. Thymidine_kinase_subgr.
[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. "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. 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.

Entry informationi

Entry nameiKITH_UREPA
AccessioniPrimary (citable) accession number: Q9PPP5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 7, 2003
Last sequence update: October 1, 2000
Last modified: January 7, 2015
This is version 84 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.