A0A6A9QBG8 · A0A6A9QBG8_ACIIN
- ProteinReverse gyrase
- Genergy
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids1232 (go to sequence)
- Protein existenceInferred from homology
- Annotation score4/5
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.
Catalytic activity
- ATP + H2O = ADP + H+ + phosphate
Cofactor
Protein has several cofactor binding sites:
Note: Binds 1 or 2 zinc ions per subunit.
Features
Showing features for binding site, active site.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | ATP binding | |
Molecular Function | ATP hydrolysis activity | |
Molecular Function | DNA binding | |
Molecular Function | DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity | |
Molecular Function | reverse gyrase activity | |
Molecular Function | zinc ion binding | |
Biological Process | DNA topological change | |
Biological Process | DNA unwinding involved in DNA replication |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameReverse gyrase
- EC number
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageArchaea > Thermoproteota > Thermoprotei > Sulfolobales > Sulfolobaceae > Acidianus
Accessions
- Primary accessionA0A6A9QBG8
Proteomes
Subcellular Location
Interaction
Subunit
Monomer.
Structure
Family & Domains
Features
Showing features for domain, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 94-256 | Helicase ATP-binding | ||||
Sequence: IVRALRGESFAIIAPPGLGKTTFGILMSLYFSEKQRKTLMIFPTKTLVNQVVQRIQEMSKNLEEVPKLAYYYSGITQSQKDELNKILESGDFDIFVSTSRYIINNVDYISTKDYKYLFVDDVDSVLKSSKSANAVLKLVGFTEDDIQNVRELLRKSKNSEEVY | ||||||
Region | 608-1232 | Topoisomerase I | ||||
Sequence: KNIKTVLFIVESPNKARTISNFFSKPSIRVFNGAIIYETVIGDKVLMVTASGGHVYDLTTKNIGIHGIEVRKNSNLEFIPYYNTIKRCNNGHQFTEYAEGNKCPTCGSTIIKDKIDVINSFRQLALEADEILIGTDPDVEGEKISWDLYLALKPYNPNIKRAEFHEVTRRAIVEAINNSRQFSIPLLQSQVVRRVEDRWIGFSLSTKLQTVFWPQYCSDVLKRTDCGENKNLSAGRVQTPVLGWVINRYNKYNETKRMVFVVKFLNSLSVLVPKQADLDRNDVKVVVYNISKSSETFGPMPPYTTDEMLSDASNLYGISAPEAMRVAQDLFEMGLITYHRTDSTRISNTGIAVAENYLKEVLEDKYKEIFKPRTWGEGGAHEAIRPTRPLDENQLRALIEEGELELPKRLTLNHYRIYGLIFSRFISSQIVPLNVDKLKFNIKVLSNGKELKVENPEIELITNVSLPGGIDVRKLSLYYPRSYFASRDSSYADTIKKLEECSNSSQCEFTGSIVSSFVKSDYQLYTQGELITEMKNKKIGRPSTYATIIATLLKRGYMLESKKVKRLVPSKLGINVYNFLTSKYFKFVSEERTRQLLELMDLIEDGKEDYRQVLKQLYDEIQSIG | ||||||
Domain | 612-774 | Toprim | ||||
Sequence: TVLFIVESPNKARTISNFFSKPSIRVFNGAIIYETVIGDKVLMVTASGGHVYDLTTKNIGIHGIEVRKNSNLEFIPYYNTIKRCNNGHQFTEYAEGNKCPTCGSTIIKDKIDVINSFRQLALEADEILIGTDPDVEGEKISWDLYLALKPYNPNIKRAEFHEV |
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
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length1,232
- Mass (Da)139,946
- Last updated2020-06-17 v1
- ChecksumD4436F23FE153C7F