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O66893 (TOP1_AQUAE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 99. 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:
DNA topoisomerase 1

EC=5.99.1.2
Alternative name(s):
DNA topoisomerase I
Omega-protein
Relaxing enzyme
Swivelase
Untwisting enzyme
Gene names
Name:topA
Ordered Locus Names:aq_657
OrganismAquifex aeolicus (strain VF5) [Reference proteome] [HAMAP]
Taxonomic identifier224324 [NCBI]
Taxonomic lineageBacteriaAquificaeAquificalesAquificaceaeAquifex

Protein attributes

Sequence length540 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Releases the supercoiling and torsional tension of DNA, which is introduced during the DNA replication and transcription, by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at a target site in duplex DNA. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA-(5'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 3'-OH DNA strand. The free DNA strand then undergoes passage around the unbroken strand, thus removing DNA supercoils. Finally, in the religation step, the DNA 3'-OH attacks the covalent intermediate to expel the active-site tyrosine and restore the DNA phosphodiester backbone By similarity. HAMAP-Rule MF_00952

Catalytic activity

ATP-independent breakage of single-stranded DNA, followed by passage and rejoining. HAMAP-Rule MF_00952

Cofactor

Magnesium. Binds two Mg2+ per subunit By similarity. HAMAP-Rule MF_00952

Subunit structure

Monomer By similarity. HAMAP-Rule MF_00952

Sequence similarities

Belongs to the type IA topoisomerase family.

Contains 1 Toprim domain.

Ontologies

Keywords
   LigandDNA-binding
Magnesium
Metal-binding
   Molecular functionIsomerase
Topoisomerase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processDNA topological change

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Cellular_componentchromosome

Inferred from electronic annotation. Source: InterPro

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

DNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

DNA topoisomerase type I activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

magnesium ion binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 540540DNA topoisomerase 1 HAMAP-Rule MF_00952
PRO_0000145138

Regions

Domain1 – 110110Toprim
Region161 – 1666Interaction with DNA By similarity

Sites

Active site2811O-(5'-phospho-DNA)-tyrosine intermediate By similarity
Metal binding71Magnesium 1; catalytic By similarity
Metal binding791Magnesium 1; catalytic By similarity
Metal binding791Magnesium 2 By similarity
Metal binding811Magnesium 2 By similarity
Site311Interaction with DNA By similarity
Site1361Interaction with DNA By similarity
Site1371Interaction with DNA By similarity
Site1401Interaction with DNA By similarity
Site1451Interaction with DNA By similarity
Site1521Interaction with DNA By similarity
Site2831Interaction with DNA By similarity
Site4671Interaction with DNA By similarity

Sequences

Sequence LengthMass (Da)Tools
O66893 [UniParc].

Last modified August 1, 1998. Version 1.
Checksum: 89C0604DFF5B042E

FASTA54063,427
        10         20         30         40         50         60 
MELFIVESPT KAKTIQKFLG KGFLVKATLG HVKDLPEKEL GVDLRTLKAK YVYKRGKKKL 

        70         80         90        100        110        120 
VEQLKKLSRR SSIVYLGTDP DREGEAIAYF LKKDLEKVNK NIKRAVFYEI TPEAIRESIR 

       130        140        150        160        170        180 
NAGDVNMNLV YAQFARRILD RLIGYLISPI LWKEFKNYKL SAGRVQSPAL RLIVEREREI 

       190        200        210        220        230        240 
QNFKVKKYYY VKALLRKGSE EFWAIYDYRY ENPSDAKIIA KKLEKGYFSV YKVEKKKEKV 

       250        260        270        280        290        300 
SPPKPFITSD LQSEANAKFG FSSERTQKLA QELYEKGYIT YPRTDSYRMN EKKAKEFMNY 

       310        320        330        340        350        360 
IEKKYGKEYV GRLRRFREKA TAQGAHECIR PTSLREEIPE REELRLLYDL IFRRTIASLM 

       370        380        390        400        410        420 
KEMLLEREKV TVEAITPELK HPVYLVAKGL KIVFDGWSRV YPSEITEEKL PELYEGDLLD 

       430        440        450        460        470        480 
LVKTTLEERK TQPPPRYTEG TLIKTLEKLG IGRPSTYATI VKTLKERGYV EVKKKALVPT 

       490        500        510        520        530        540 
EIAFQVVEFL MERFPTLMDY KFTAQMEEKL DLVEEGKLNW KSVVYEFMEK IFGKELEMVR 

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References

[1]"The complete genome of the hyperthermophilic bacterium Aquifex aeolicus."
Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L., Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R., Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.
Nature 392:353-358(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: VF5.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE000657 Genomic DNA. Translation: AAC06848.1.
PIRA70358.
RefSeqNP_213453.1. NC_000918.1.

3D structure databases

ProteinModelPortalO66893.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING224324.aq_657.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC06848; AAC06848; aq_657.
GeneID1193955.
KEGGaae:aq_657.
PATRIC20958804. VBIAquAeo85532_0534.

Phylogenomic databases

eggNOGCOG0550.
HOGENOMHOG000004018.
KOK03168.
OMAWINKAKK.
OrthoDBEOG6S7XQ9.

Enzyme and pathway databases

BioCycAAEO224324:GJBH-476-MONOMER.

Family and domain databases

Gene3D1.10.290.10. 1 hit.
1.10.460.10. 2 hits.
3.40.50.140. 1 hit.
HAMAPMF_00952. Topoisom_1_prok.
InterProIPR000380. Topo_IA.
IPR003601. Topo_IA_2.
IPR023406. Topo_IA_AS.
IPR013497. Topo_IA_cen.
IPR013824. Topo_IA_cen_sub1.
IPR013826. Topo_IA_cen_sub3.
IPR023405. Topo_IA_core_domain.
IPR003602. Topo_IA_DNA-bd.
IPR005733. TopoI_bac-type.
IPR028612. Topoisom_1_IA.
IPR006171. Toprim_domain.
[Graphical view]
PANTHERPTHR11390. PTHR11390. 1 hit.
PfamPF01131. Topoisom_bac. 1 hit.
PF01751. Toprim. 1 hit.
[Graphical view]
PRINTSPR00417. PRTPISMRASEI.
SMARTSM00437. TOP1Ac. 1 hit.
SM00436. TOP1Bc. 1 hit.
SM00493. TOPRIM. 1 hit.
[Graphical view]
SUPFAMSSF56712. SSF56712. 1 hit.
TIGRFAMsTIGR01051. topA_bact. 1 hit.
PROSITEPS00396. TOPOISOMERASE_I_PROK. 1 hit.
PS50880. TOPRIM. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameTOP1_AQUAE
AccessionPrimary (citable) accession number: O66893
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: August 1, 1998
Last modified: July 9, 2014
This is version 99 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