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HAMAP rule MF_01125

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General rule information [?]

Accession MF_01125
Dates 31-JAN-2004 (Created)
3-NOV-2023 (Last updated, Version 34)
Name Reverse_gyrase
Scope(s) Bacteria
Template(s) Q08582 (RGYR1_SULAC); O29238 (RGYR_ARCFU); [ Recover all ]
Triggered by HAMAP; MF_01125 (Get profile general information and statistics)

Propagated annotation [?]

Identifier, protein and gene names [?]

Identifier RGYR
Protein name RecName: Full=Reverse gyrase;
Gene name Name=rgy;

Comments [?]

FUNCTIONModifies 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.;
DOMAINIntroduction 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.
MISCELLANEOUSThis 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.
SIMILARITYIn the N-terminal section; belongs to the DEAD box helicase family. DDVD subfamily.
SIMILARITYIn the C-terminal section; belongs to the type IA topoisomerase family.

Keywords [?]

Gene Ontology [?]

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 [?]

Pfam PF00270; DEAD; 1;
Pfam PF01131; Topoisom_bac; 1;
Pfam PF01751; Toprim; 1;
Pfam PF00271; Helicase_C; 1;
PROSITE PS52039; TOPO_IA_2; 1;
PROSITE PS52037; ZF_RG_C; 0-1;
PROSITE PS52036; ZF_RG_N; 1;
NCBIfam TIGR01054; rgy; 1;

Features [?]

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"

Additional information [?]

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.

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