G4RM03 · G4RM03_THETK

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

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 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
    • Ordered locus names
      TTX_1984

Organism names

Accessions

  • Primary accession
    G4RM03

Proteomes

Subcellular Location

Keywords

PTM/Processing

Proteomic databases

Interaction

Subunit

Monomer.

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain, region.

TypeIDPosition(s)Description
Domain94-254Helicase ATP-binding
Region629-1223Topoisomerase I
Domain633-807Toprim

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
    1,223
  • Mass (Da)
    138,603
  • Last updated
    2011-12-14 v1
  • Checksum
    86D358A5779FDB2E
MDFKTIRAIYLHSCPNCGGAVDSSRLAQGLPCSECLPRALKLENLKSVIQALKSEGSLKELATLDEVLRRYEELNVLFEKVVGFRMWGAQRLWAKRLAAGKSFAVVAPTGSGKTTFLLVSSLYMARGGKVLLVFPTSALAYQAYKKLLDYSARANYSGRIISYNTMLREQEREEALKRIEEGDFDILIITSAFLPKYFDVLAKYKFIFIATDDVDSVLRATSKNIERLLRLLGATDEALNLALDIIELNKKRARQMLGGDEKGLEESDVEIKRKREELRRLKARLKLGVFIASGALAKARRTTRLLLFRELLGFDVGGRAEGLRNVYDVYAKLSEDPRAQVAALVKRLGSGGIIYVQDKDLGRELVEYLKGEGIKAEHFFRPRRKVLEAFERGELDALVGLASARSALVRGIDMPHVIRYVIFVGIPKFKFRVKLDEFSAPAYLAFLYNVRGVLPQELKFKADRLIAQLRRIAPYTAGLEKVLTEGPKNSFEEYLLNVVKSAVEFVGLILSRDDVKRAIETSTEVKLTYIDGQLYVLLPDVTTYIQGSGRTSRLYAGGLSRGLSVILVDDEKVLHALRRELELRFDEVKFYDLAETDLDKILREVDSDRETIRRILSGSFKPEELSARDIMKSVLLVVESPTKARTIASFFGRPNMLIVGGVPAYEVSTGDMMLTVIATMGHIYELPTSLAKIEPSEKERVLRAVGRTLSEIYSPEDYAVFKTEDGYIPVYNRIYKCPGASYVDDTEVPENCQPLDIISTLRNLASEVDLVLLGTDPDSEGEKIAYDVYLALRPYVGSIKRIEFHEVTRRAIVNALSSPRDVNLPMVAAQMVRRVEDRWIGFGLSRRVQEAHGLAFLSAGRVQSPVLGWIVERYQSSRAERKFDVTIELEDGSIRLTLPEDSYKALKSEGRVRIKRLEGREVVLQPPPPYTTDEYMRDAVNKLGITAEQAMAIAQDLFESGFITYHRTDSTRVSATGIGIAREYISKRFGADLFKARPWATGEEGAHEAIRPTRPIDAEELRGLVAAGVIQPTIRLTRNHYAAYELIFRRFMSSQMREALVRVEKYEVEAGGYKAEVERVVEIKEEGFLRMYRTVEEARPLREGESPIKITYAKRHVELLSQADVLRLMKERGIGRPSTYAKILEVLSKRGYVVVRGRRKFMIPTKRGIEVYQYLKSNFGKLVSEERTRLIERFMDDVENGRRDYRAVLDELFEEFIEEVLKR

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
FN869859
EMBL· GenBank· DDBJ
CCC82598.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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