HAMAP rule MF_01125
General rule information
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| Accession | MF_01125 |
| Dates | 31-JAN-2004 (Created)
3-NOV-2023 (Last updated, Version 34) |
| Name | Reverse_gyrase |
| Scope(s) |
Bacteria Archaea |
| Template(s) | Q08582 (RGYR1_SULAC); O29238 (RGYR_ARCFU); [ Recover all ] |
| Triggered by |
HAMAP; MF_01125 (Get profile general information and statistics) |
Propagated annotation
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Identifier, protein and gene names
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| Identifier | RGYR |
| Protein name | RecName: Full=Reverse gyrase; EC=5.6.2.-; |
| Gene name | Name=rgy; |
Comments
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| 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. 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. |
| CATALYTIC ACTIVITY | Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; |
| COFACTOR | Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Note=Binds 1 or 2 zinc ions per subunit.; |
| SUBUNIT | Monomer. |
| SUBCELLULAR LOCATION | Cytoplasm. |
| 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. |
| 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. |
| SIMILARITY | In the N-terminal section; belongs to the DEAD box helicase family. DDVD subfamily. |
| SIMILARITY | In the C-terminal section; belongs to the type IA topoisomerase family. |
Keywords
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| Cytoplasm |
| Hydrolase |
| Isomerase |
| Topoisomerase |
| DNA-binding |
| ATP-binding |
| Nucleotide-binding |
| Metal-binding |
| Zinc |
| Zinc-finger |
Gene Ontology
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| GO:0005524; Molecular function:ATP binding |
| GO:0003677; Molecular function:DNA binding |
| GO:0008094; Molecular function:ATP-dependent activity, acting on DNA |
| GO:0005737; Cellular component:cytoplasm |
| GO:0160097; Molecular function:reverse gyrase activity |
| GO:0003916; Molecular function:DNA topoisomerase activity |
| GO:0008270; Molecular function:zinc ion binding |
| GO:0006265; Biological process:DNA topological change |
| GO:0006268; Biological process:DNA unwinding involved in DNA replication |
Cross-references
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| Pfam | PF00270; DEAD; 1; |
| Pfam | PF01131; Topoisom_bac; 1; |
| Pfam | PF01751; Toprim; 1; |
| Pfam | PF00271; Helicase_C; 1; |
| PRINTS | PR00417; PRTPISMRASEI; 1; |
| PROSITE | PS51192; HELICASE_ATP_BIND_1; 1; |
| PROSITE | PS51194; HELICASE_CTER; 0-1; |
| PROSITE | PS52039; TOPO_IA_2; 1; |
| PROSITE | PS50880; TOPRIM; 1; |
| PROSITE | PS52037; ZF_RG_C; 0-1; |
| PROSITE | PS52036; ZF_RG_N; 1; |
| NCBIfam | TIGR01054; rgy; 1; |
Features
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| From: RGYR_THEMA (O51934) | ||||||||||||
| Key | From | To | Description | Tag | Condition | FTGroup | ||||||
| REGION | 538 | Cter | /note="Topoisomerase I" | |||||||||
| ACT_SITE | 851 | 851 | /note="O-(5'-phospho-DNA)-tyrosine intermediate" | Y | ||||||||
| BINDING | 83 | 83 | /ligand="ATP" /ligand_id="ChEBI:CHEBI:30616" |
Q | ||||||||
Additional information
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| Size range | 1054-1624 amino acids |
| Related rules |
None |
| Fusion | Nter: None Cter: None |
| Comments | Several reverse gyrases contain inteins; for M.jannaschii the intein was excised in the seed alignment. Duplicated in most Thermoprotei and some bacteria. In a few organisms (for example Methanopyrus kandleri and Nanoarchaeum equitans) the enzyme is encoded by 2 separated genes. Does not have helicase activity despite the helicase-like domain. |