A0A0E3GUZ3 · A0A0E3GUZ3_SACSO
- ProteinReverse gyrase
- Genergy
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids1242 (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
- Strains
- Taxonomic lineageArchaea > Thermoproteota > Thermoprotei > Sulfolobales > Sulfolobaceae > Saccharolobus
Accessions
- Primary accessionA0A0E3GUZ3
Proteomes
Subcellular Location
Interaction
Subunit
Monomer.
Structure
Family & Domains
Features
Showing features for domain, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 97-298 | Helicase ATP-binding | ||||
Sequence: TIRFLRGESFAIIAPPGLGKTTFGLIMSLYNATRNRKSIIIFPTRTLISQTVDKLAKFSELYSYSPRILYNKQSPTQTENILDQLKSGNFDIFISTNRFVIQNLSELSNIKFDFIFVDDVDAALKSGKSAKAILRLVGFTDEDIQTTMKLLRENIGEEEKFGKIQEIRESRLKDKIVIFSSATISRGNPILSSLMGFRPGSS | ||||||
Region | 615-1242 | Topoisomerase I | ||||
Sequence: LSVKTTLFIVESPNKAKTISNFFSRPSTRSYGKLRVYETVLGDRVLIVAASGGHIYDLITEDESEKQDDNYVYGVLVKDSKFIPIYSTIKKCEKGHQIVKDLSQNKCPICGSRIVTDKTEVVDILRKLALEVDEVLIGTDPDTEGEKIAWDIYLAIRPFNGNIKRAEFHEVTRRAILNAIKNPREFNDNLVKSQIVRRIEDRWIGFKLSRKLQTEFWEQHCTSISKKNSKDEECKENRNLSAGRVQTPVLDWVVNRYQKYNENKKKYLIIESQDKSIFPFSVLALKKNGLSKNTQIIIHLEDINIKEEEFGPLPPYTTDTLLSDAANLLRIPASDTMRVAQDLFELGLITYHRTDSTRVSNVGISVAETYLKSKQVDISKIFRPRSWGEGGAHEAIRPTKPLDETMLKASIEQGDLELSKQLTFNHFRVYNLIFRRFITSQLPPLVVTKQIVRIRAYTKDNIELELDENKKEFVIGYKLKEGDEFRQTLQDAIYTLFRLYQPLDEKMKGKELSATITGTLNKSDVQLYTEGELISEMKSKQIGRPSTYAVIISTLKKRRYIIESKNLKKIIPTKLGMAVKEYLMENYKQIVSEKRTVKLLEKMNEVEEGKVDYLVLLKELYNEIQTIS | ||||||
Domain | 619-785 | Toprim | ||||
Sequence: TTLFIVESPNKAKTISNFFSRPSTRSYGKLRVYETVLGDRVLIVAASGGHIYDLITEDESEKQDDNYVYGVLVKDSKFIPIYSTIKKCEKGHQIVKDLSQNKCPICGSRIVTDKTEVVDILRKLALEVDEVLIGTDPDTEGEKIAWDIYLAIRPFNGNIKRAEFHEV |
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
- Length1,242
- Mass (Da)141,668
- Last updated2015-06-24 v1
- ChecksumEE4C1990F01F26FB
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
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 |