A0A6A9QBG8 · A0A6A9QBG8_ACIIN

  • Protein
    Reverse gyrase
  • Gene
    rgy
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    4/5

Function

function

Modifies the topological state of DNA by introducing positive supercoils in an ATP-dependent process, increasing the linking number in steps of +1. Binds to single-stranded DNA, transiently cleaves and then rejoins the ends, introducing a positive supercoil in the process. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA-(5'-phosphotyrosyl)-enzyme intermediate. Involved in rewinding DNA strands in regions of the chromosome that have opened up to allow replication, transcription, DNA repair and/or for DNA protection.
Modifies the topological state of DNA by introducing positive supercoils in an ATP-dependent process, increasing the linking number in steps of +1. Binds to single-stranded DNA, transiently cleaves and then rejoins the ends, introducing a positive supercoil in the process. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA-(5'-phosphotyrosyl)-enzyme intermediate. Probably involved in rewinding DNA strands in regions of the chromosome that have opened up to allow replication, transcription, DNA repair and/or for DNA protection.

Miscellaneous

This enzyme is the only unique feature of hyperthermophilic bacteria/archaea known and seems to be essential for adaptation to life at high temperatures. It may play a role in stabilization of DNA at high temperatures.

Caution

The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

Catalytic activity

Cofactor

Protein has several cofactor binding sites:
Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

Zn2+ (UniProtKB | Rhea| CHEBI:29105 )

Note: Binds 1 or 2 zinc ions per subunit.

Features

Showing features for binding site, active site.

TypeIDPosition(s)Description
Binding site90ATP (UniProtKB | ChEBI)
Active site945O-(5'-phospho-DNA)-tyrosine intermediate

GO annotations

AspectTerm
Cellular Componentcytoplasm
Molecular FunctionATP binding
Molecular FunctionATP hydrolysis activity
Molecular FunctionDNA binding
Molecular FunctionDNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity
Molecular Functionreverse gyrase activity
Molecular Functionzinc ion binding
Biological ProcessDNA topological change
Biological ProcessDNA unwinding involved in DNA replication

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Reverse gyrase
  • EC number

Gene names

    • Name
      rgy
    • ORF names
      D1867_04780

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • DSM 3191
  • Taxonomic lineage
    Archaea > Thermoproteota > Thermoprotei > Sulfolobales > Sulfolobaceae > Acidianus

Accessions

  • Primary accession
    A0A6A9QBG8

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Monomer.

Family & Domains

Features

Showing features for domain, region.

TypeIDPosition(s)Description
Domain94-256Helicase ATP-binding
Region608-1232Topoisomerase I
Domain612-774Toprim

Domain

Introduction of positive supercoils requires the cooperation of both domains. The helicase-like domain probably does not directly unwind DNA, but more likely acts by driving ATP-dependent conformational changes within the whole enzyme. A beta hairpin in the 'latch' region of the N-terminal domain plays a regulatory role in the enzyme, repressing topoisomerase activity in the absence of ATP and preventing the enzyme from acting as an ATP-independent relaxing enzyme; it also helps to coordinate nucleotide hydrolysis by the ATPase domain with the supercoiling activity of the topoisomerase domain.

Sequence similarities

In the C-terminal section; belongs to the type IA topoisomerase family.
In the N-terminal section; belongs to the DEAD box helicase family. DDVD subfamily.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    1,232
  • Mass (Da)
    139,946
  • Last updated
    2020-06-17 v1
  • Checksum
    D4436F23FE153C7F
MSEELPNLVYMNSCPNCGGEITANRLYRGSVCEKCIKEDIQFNSVYDLALYLLKNKSLINLRSSYEILKELKEVERLFKRVLGSPPLGPQRSWIVRALRGESFAIIAPPGLGKTTFGILMSLYFSEKQRKTLMIFPTKTLVNQVVQRIQEMSKNLEEVPKLAYYYSGITQSQKDELNKILESGDFDIFVSTSRYIINNVDYISTKDYKYLFVDDVDSVLKSSKSANAVLKLVGFTEDDIQNVRELLRKSKNSEEVYDEIRKIREKKTGDKIAIFSSATITKGNPVFSALMGFRPGSAVIYLRNVIDSYVQLSSATDEEIIDIVNKIVNKLGSGGLIFVPIDKGVSFANEIASNISGLKAEAISSTSITKLDKFEKGEIDVLVGVATHYGILVRGIDIPWRIRYAIFAGIPRFRFKIGETMHPLAMLKMLTLISLVTKDEEVTKILRIVRNKLRRISPAALAMLANSVKSGKIEDKYIQEAYDLTNKYLRNEEILEKIAEIGEISINNGYISTPDYLTYIQASGRTSRIFGGELTTGLSVLLVDNPRLFELLNRRLSIVLDEVTWNPFDIDNDKIGNNNLHEILKRIDSEREKIRKIKKEGLLTSTSVKNIKTVLFIVESPNKARTISNFFSKPSIRVFNGAIIYETVIGDKVLMVTASGGHVYDLTTKNIGIHGIEVRKNSNLEFIPYYNTIKRCNNGHQFTEYAEGNKCPTCGSTIIKDKIDVINSFRQLALEADEILIGTDPDVEGEKISWDLYLALKPYNPNIKRAEFHEVTRRAIVEAINNSRQFSIPLLQSQVVRRVEDRWIGFSLSTKLQTVFWPQYCSDVLKRTDCGENKNLSAGRVQTPVLGWVINRYNKYNETKRMVFVVKFLNSLSVLVPKQADLDRNDVKVVVYNISKSSETFGPMPPYTTDEMLSDASNLYGISAPEAMRVAQDLFEMGLITYHRTDSTRISNTGIAVAENYLKEVLEDKYKEIFKPRTWGEGGAHEAIRPTRPLDENQLRALIEEGELELPKRLTLNHYRIYGLIFSRFISSQIVPLNVDKLKFNIKVLSNGKELKVENPEIELITNVSLPGGIDVRKLSLYYPRSYFASRDSSYADTIKKLEECSNSSQCEFTGSIVSSFVKSDYQLYTQGELITEMKNKKIGRPSTYATIIATLLKRGYMLESKKVKRLVPSKLGINVYNFLTSKYFKFVSEERTRQLLELMDLIEDGKEDYRQVLKQLYDEIQSIG

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
WFIY01000004
EMBL· GenBank· DDBJ
MUM64572.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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