A0A4Q3YVI6 · A0A4Q3YVI6_9RHOB

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

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 site136O-(5'-phospho-DNA)-tyrosine intermediate

GO annotations

AspectTerm
Cellular Componentchromosome
Cellular Componentcytoplasm
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
      EU805_09220

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • IMCC34102
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Alphaproteobacteria > Rhodobacterales > Roseobacteraceae > Salipiger

Accessions

  • Primary accession
    A0A4Q3YVI6

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 region, compositional bias, domain, motif.

TypeIDPosition(s)Description
Region1-25Disordered
Compositional bias10-25Basic and acidic residues
Domain25-504DNA topoisomerase type IIA
Motif565-571GyrA-box

Sequence similarities

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

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    916
  • Mass (Da)
    101,007
  • Last updated
    2019-07-31 v1
  • Checksum
    EDA7E35D7E3120E2
MTDIPDTPESDDDGPARPEYDGPSVSIEDELRTAYLDYAMSVIVSRAIPDLRDGLKPVHRRILYAMHDTNNTYDKPYRKSSRPVAETMGKYHPHGDSAIYDALVRMAQDFSMSLVLLDGQGNFGSMDGDKAAAYRYTEVRMQKVAGYLLDDIDKDTVDFQLNYDGKDREPSVLPARFPNMLVNGAGGIAVGMATNIPPHNLGEVIDATLALIDDPDLSTEALIDYIPGPDFPTGGIMLGRSGARKAYLEGRGSVVMRSRTHVEELRKDRYAIVIDDVPYQVNKSVMIDRIAEAAREKRIEGIAHVQDESDRNGVRVVVELKRDATAEVVLNQLFRFTPMQTNFACNMLALNGGKPETLTLRRFLTSFVDFREDVVARRTAFELRKARERSHILCGLAVAVTNIDEVVATIRRSTDAAEAREALMTRRWPAEEILEYIALIDDPTHTANDDGTYNLSEAQARAILELRLQRLTQIGVKEVTDELQELAKKIRDYLEILGSRERILQIIRDELTEVRDNHAVPRRTEIVDWAGDMMDEDLIEREDMVVTVTSGGYIKRTALADFRAQRRGGKGLSSMQTKEEDVVTTLFVANTHTQLLFFTTSGMVYKLKCWQLPLGSRTAKGKAIVNILPIEAGVSIAAIMPVDRDEAEWDDLQVVFATSAGTVRRNRLSDFTNVNRAGKIAMKFEEGEDIRLINARIASESDDVMLVTNSGRAIRFPATDVRVFNSRASTGVRGVRLNGDDEVVSMSIIPHFEAEASERAAYLKMRRAMAGLTDEAEGSDDEDDVAPGAITQERYAEMSAAETLILTITANGMGKLSSSHDYPVRGRGGMGVMATDKAMRGGPLVTSFPVDLSDQIMLVTSTGQSIRVPVEGISFRSRGAGGVKVFNTAKGEVVASVAWIADQGGEDATEGEAPAS

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias10-25Basic and acidic residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
SELQ01000003
EMBL· GenBank· DDBJ
RYH02772.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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