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A0A0B7J984 · A0A0B7J984_9GAMM

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 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
      C9J27_01540

Organism names

  • Taxonomic identifier
  • Strain
    • FS-7.2
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Gammaproteobacteria > Vibrionales > Vibrionaceae > Photobacterium

Accessions

  • Primary accession
    A0A0B7J984
  • Secondary accessions
    • A0A2T3KP03

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 motif.

TypeIDPosition(s)Description
Motif559-565GyrA-box

Sequence similarities

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

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    889
  • Mass (Da)
    98,744
  • Last updated
    2015-04-01 v1
  • MD5 Checksum
    4C575219D863FB4439D68BFAF701461A
MSDLAKEITPINIEEELKSSYLDYAMSVIVGRALPDVRDGLKPVHRRVLFAMNVLGNDWNKAYKKSARVVGDVIGKYHPHGDSAVYDTIVRMAQPFSLRYMLVDGQGNFGSIDGDSAAAMRYTEVRMSKIAHELLADLDKETVDYVPNYDGTEQIPAVLPTKIPNLLVNGSSGIAVGMATNIPPHNLGEVINGCLAYINDESITIDQLMEYIPGPDFPTAAMINGRKGIVDAYHTGRGKVYMRAKAEIETEKNGRETILVHEIPYQVNKARLIEKIAELVKDKKVEGISALRDESDKDGMRIVIECKRDAVGEVVLNNLYAQTQLQTTFGINMVALDNGQPKIFNLKEMIKCFVNHRREVVTRRTIYELRKARDRAHILEGLALALANIDEIIELIRQENTPAEAKAALVARGWQLGNVAAMLERAGTDAARPDWLEEQFGIRDNRYYLTEQQAQAILDLRLHKLTGLEHGKILEEYKQLLEEIAELMFILSSSERLMEVIREELELVKEQFSDERRTEITAASNDIDLEDLIPKEDVVVTLSHEGYVKYQILSDYEAQRRGGKGKAATRMKQEDFIERLLVANTHDTILCFSSRGRMYWLKVYQLPLASRTARGKPIVNILPLEENERITAILPVREYTEDKFVFMATADGTVKKTPLTDFSRPRSAGIIAVNLREGDSLIGVDVTDGDCDIMLFSAFGKVVRFYESPVVIDDEGNTKGGVRGMGRTAAGVRGIKLAEGDKVVSLIVPHNEGDILTVTENGYGKRTGLAEYPAKSRATQGVVSIKVSDRNGSVVGAVQAEDGDEFMMITNGGTLVRTRVAEVSRVGRNTQGVTLIRTAEDEKVVGLQRIDEPAEEELIEDAELVDGETVENTEQPAADAESGDSTEQE

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
PYNF01000001
EMBL· GenBank· DDBJ
PSV01770.1
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.
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