A0A0N0ZUS4 · A0A0N0ZUS4_CHRID

Function

function

A type II topoisomerase that negatively supercoils closed circular double-stranded (ds) DNA in an ATP-dependent manner to modulate DNA topology and maintain chromosomes in an underwound state. Negative supercoiling favors strand separation, and DNA replication, transcription, recombination and repair, all of which involve strand separation. Also able to catalyze the interconversion of other topological isomers of dsDNA rings, including catenanes and knotted rings. Type II topoisomerases break and join 2 DNA strands simultaneously in an ATP-dependent manner.

Miscellaneous

Few gyrases are as efficient as E.coli at forming negative supercoils. Not all organisms have 2 type II topoisomerases; in organisms with a single type II topoisomerase this enzyme also has to decatenate newly replicated chromosomes.

Caution

Lacks conserved residue(s) required for the propagation of feature annotation.
The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

Catalytic activity

  • ATP-dependent breakage, passage and rejoining of double-stranded DNA.
    EC:5.6.2.2 (UniProtKB | ENZYME | Rhea)

Features

Showing features for active site.

TypeIDPosition(s)Description
Active site122O-(5'-phospho-DNA)-tyrosine intermediate

GO annotations

AspectTerm
Cellular Componentchromosome
Cellular Componentcytoplasm
Cellular ComponentDNA topoisomerase type II (double strand cut, ATP-hydrolyzing) complex
Molecular FunctionATP binding
Molecular FunctionDNA binding
Molecular FunctionDNA negative supercoiling activity
Biological ProcessDNA topological change
Biological ProcessDNA-templated DNA replication

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    DNA gyrase subunit A
  • EC number

Gene names

    • Name
      gyrA
    • ORF names
      AOB46_12845

Organism names

Accessions

  • Primary accession
    A0A0N0ZUS4

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Heterotetramer, composed of two GyrA and two GyrB chains. In the heterotetramer, GyrA contains the active site tyrosine that forms a transient covalent intermediate with DNA, while GyrB binds cofactors and catalyzes ATP hydrolysis.

Family & Domains

Features

Showing features for domain, coiled coil, region, compositional bias.

TypeIDPosition(s)Description
Domain11-466DNA topoisomerase type IIA
Coiled coil438-479
Region816-862Disordered
Compositional bias832-853Polar residues

Sequence similarities

Belongs to the type II topoisomerase GyrA/ParC subunit family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    862
  • Mass (Da)
    96,663
  • Last updated
    2015-12-09 v1
  • Checksum
    1851BC4200020915
MQKEGERLIPINIVDEMKSSYIDYSMSVIVSRALPDVRDGLKPVHRRVLYGMYGLGVFSNRKYLKSARIVGDVLGKYHPHGDSSVYDAMVRMAQDWSLRYPQVDGQGNFGSMDGDPPAAMRYTEARLKKISDEVLADLDKETVDFQNNFDDSLQEPTVLPTKVPNLLVNGTSGIAVGMATNMAPHNLSESINAICAYIDNKDITIDELMHHITAPDFPTGGIIYGYDGVRDAFHTGRGRVVLRAKVNFEEIGNRNAIIVTEVPYQVNKADMIARTAELVKDDKIQGIHEIRDESDRNGLRVVYELKNDAIPNVVLNLLYKYTALQTSFSVNNIALVNGRPEQLNLKDIIHHFVEHRHEVIVRRTRFELKKAKERAHILEGFMKVIGTQDALDKAISIIRHSANPQAAKEGLIEAFELSDIQAQAILDLRLARLTGMELDKIRDEYDAIMKEILNLEDILANESRRFEIIKEELIEIKEKYGDERRTEIDYSGGEMSIEDIIPNEAVVLTISHAGYVKRTSLSEYKIQSRGGVGNKAATTRDSDFLEYIVSATNHQYMLFFTEKGRCYWLRVFEIPEGSKTAKGRAVQNLINIEPDDKIKAYIRTNNLKDAEYVNQMSVVMVTKNGTIKKTSLEAYSRPRVNGVNAIEIRDNDQLLGAYLTNGTSQIMIATKNGKCIRFPEEKVREVGRGSIGVRGIAMEDNDEVIGMIVVNDVEKETVLVVSEKGYGKRTAVEDYRITNRGGKGVITLNITEKTGNLIAIQNVTDEDGLMIINKSGVAIRMGMDEMRVMGRNTQGVKLINLKKNDEIAAIAKVAMDKDVEEDSEENEEGIGNLFDNQENDNVEPQAENETPAEGNENSDSEE

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias832-853Polar residues

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
LJOD01000008
EMBL· GenBank· DDBJ
KPE50676.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp