A0A0E3GUZ3 · A0A0E3GUZ3_SACSO

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.

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 site93ATP (UniProtKB | ChEBI)
Active site965O-(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
      HFC64_13635
      , SSOP1_0401
      , SULA_1442
      , SULB_1443
      , SULC_1441
      , SULG_07170
      , SULH_07170
      , SULI_07170
      , SULM_07170
      , SULN_07170
      , SULO_07180
      , SULZ_07410

Organism names

Accessions

  • Primary accession
    A0A0E3GUZ3

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Monomer.

Family & Domains

Features

Showing features for domain, region.

TypeIDPosition(s)Description
Domain97-298Helicase ATP-binding
Region615-1242Topoisomerase I
Domain619-785Toprim

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
    1,242
  • Mass (Da)
    141,668
  • Last updated
    2015-06-24 v1
  • Checksum
    EE4C1990F01F26FB
MTSINKVPPSIYTRSCPNCGGNISSQRLFNGSVCESCLKDDREFSNLSDLINILSENSNLKNLTQIRDVLEEYKKVEEIFGKLLNNSKPIGPQRSWTIRFLRGESFAIIAPPGLGKTTFGLIMSLYNATRNRKSIIIFPTRTLISQTVDKLAKFSELYSYSPRILYNKQSPTQTENILDQLKSGNFDIFISTNRFVIQNLSELSNIKFDFIFVDDVDAALKSGKSAKAILRLVGFTDEDIQTTMKLLRENIGEEEKFGKIQEIRESRLKDKIVIFSSATISRGNPILSSLMGFRPGSSVIYLRNIYDSYIDLTQTCKGQDFEECTLGTVIKLLKRLNDGTLIFVPIDKGAQYADYLASNLRDHGINVESVASSSISKLEKFERGEVSSLVGVATHYGVLVRGIDLPWRVKYSIFVGIPKFKFKIGEYMHPLALTRLLSLVYLVKNDDKVRGLLSYIRKRLRKISPAALAMLAKDIREGKIDDERLKEAYNLVNEYLKDNEFLKKVSDVGDLVIEGDYILMPDYLTYIQASGRTSRLYGANLTTGLSVLLIDNSRLFELLNKKLNLILDEVKWYSLDIDADKLGQVSLSDISAKITEERESLSKIKKEGNVESSSLSVKTTLFIVESPNKAKTISNFFSRPSTRSYGKLRVYETVLGDRVLIVAASGGHIYDLITEDESEKQDDNYVYGVLVKDSKFIPIYSTIKKCEKGHQIVKDLSQNKCPICGSRIVTDKTEVVDILRKLALEVDEVLIGTDPDTEGEKIAWDIYLAIRPFNGNIKRAEFHEVTRRAILNAIKNPREFNDNLVKSQIVRRIEDRWIGFKLSRKLQTEFWEQHCTSISKKNSKDEECKENRNLSAGRVQTPVLDWVVNRYQKYNENKKKYLIIESQDKSIFPFSVLALKKNGLSKNTQIIIHLEDINIKEEEFGPLPPYTTDTLLSDAANLLRIPASDTMRVAQDLFELGLITYHRTDSTRVSNVGISVAETYLKSKQVDISKIFRPRSWGEGGAHEAIRPTKPLDETMLKASIEQGDLELSKQLTFNHFRVYNLIFRRFITSQLPPLVVTKQIVRIRAYTKDNIELELDENKKEFVIGYKLKEGDEFRQTLQDAIYTLFRLYQPLDEKMKGKELSATITGTLNKSDVQLYTEGELISEMKSKQIGRPSTYAVIISTLKKRRYIIESKNLKKIIPTKLGMAVKEYLMENYKQIVSEKRTVKLLEKMNEVEEGKVDYLVLLKELYNEIQTIS

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP011055
EMBL· GenBank· DDBJ
AKA73724.1
EMBL· GenBank· DDBJ
Genomic DNA
CP011056
EMBL· GenBank· DDBJ
AKA76421.1
EMBL· GenBank· DDBJ
Genomic DNA
CP011057
EMBL· GenBank· DDBJ
AKA79114.1
EMBL· GenBank· DDBJ
Genomic DNA
CP033235
EMBL· GenBank· DDBJ
AZF68195.1
EMBL· GenBank· DDBJ
Genomic DNA
CP033236
EMBL· GenBank· DDBJ
AZF70815.1
EMBL· GenBank· DDBJ
Genomic DNA
CP033237
EMBL· GenBank· DDBJ
AZF73435.1
EMBL· GenBank· DDBJ
Genomic DNA
CP033238
EMBL· GenBank· DDBJ
AZF76059.1
EMBL· GenBank· DDBJ
Genomic DNA
CP033239
EMBL· GenBank· DDBJ
AZF78670.1
EMBL· GenBank· DDBJ
Genomic DNA
CP033240
EMBL· GenBank· DDBJ
AZF81273.1
EMBL· GenBank· DDBJ
Genomic DNA
CP033241
EMBL· GenBank· DDBJ
AZF83909.1
EMBL· GenBank· DDBJ
Genomic DNA
CP050869
EMBL· GenBank· DDBJ
QPG50715.1
EMBL· GenBank· DDBJ
Genomic DNA
LT549890
EMBL· GenBank· DDBJ
SAI83956.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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