Q5WM25 · Q5WM25_SHOC1

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.

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.

1830100200300400500600700800
TypeIDPosition(s)Description
Active site123O-(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
    • Ordered locus names
      ABC0007

Organism names

Accessions

  • Primary accession
    Q5WM25

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.

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain, motif, region, compositional bias.

TypeIDPosition(s)Description
Domain12-464DNA topoisomerase type IIA
Motif525-531GyrA-box
Region807-830Disordered
Compositional bias809-830Acidic residues

Sequence similarities

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

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    830
  • Mass (Da)
    92,637
  • Last updated
    2004-11-23 v1
  • Checksum
    17E92C5B975DB773
MAEEDVPRLRERQIDEEMKESFIDYAMSVIVSRALPDVRDGMKPVHRRILYAMFELGMTPDKPYKKSARIVGEVLGKYHPHGDTSVYDAMVRMAQDFSYRYMLVNGHGNFGSIDGDSAAAMRYTESKMSKISMELVRDLNKDTVDFIDNYDGTEREPKVMPSRFPNLLVNGTSGIAVGMATNIPPHQLGEVIDGVLALAKNPDISIPELMEYIPGPDFPTGGEILGRSGIRKAYSTGRGSITVRAKTEIVENKGKQSIIVTELPYQVNKARLIEKIAELVRDKKIDGITELRDSSDRNGMNIVIDVRRDANPNVILNNLFKQTALQTSFGINMLALVNGRPEVLNLKQTLEQYLAHQVEVIRRRTQFDLNKAEARAHILEGLRIALDHIDEIIALIRGSDTAEIARNGLIERFELSYDQAQAILDMRLQRLTGLERDKLEQEYKDVLARIAELRAILASDEKVIDVIQEEILAIKEKFNDERRTVISASEEHLEDEDLIPRQNIVITITHNGYIKRLPISTYRAQKRGGKGVQGMGTNDDDFVQHLFTTNTHHTVLVFTNKGKAYRLKGYEIPELGRTAKGIPAINLLPFDPGETISTVIPIECFDDDSYLFFVTEHGIAKRTKLSAFANIRKGGLFAINLREGDSLHGVRLTDGNREVMIGTKQGMAIRFPETDVRLMGRTAGGVKGITLSENDGVVGMEVVDENQSVLVVTEKGYGKRTPLDEYRVQSRGGKGIKTCNITDKNGPLVSLKMVADEDDIMIVTANGIIIRTNVDGISTTGRNTQGVTLIRVNEGEEVATVARVNINDDEVDDLEDDDEQEQPTSEENAE

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias809-830Acidic residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AP006627
EMBL· GenBank· DDBJ
BAD62550.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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