HAMAP rule MF_01125

General rule information [?]

Accession	MF_01125
Dates	31-JAN-2004 (Created) 1-JUN-2023 (Last updated, Version 30)

Name	Reverse_gyrase

Scope

Bacteria

Archaea

Templates

Q08582 (RGYR_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;
Includes:
	RecName:		Full=Helicase;
			EC 3.6.4.12;
Includes:
	RecName:		Full=Topoisomerase;
			EC 5.6.2.2;

Gene name

rgy

Comments [?]

Function	Modifies the topological state of DNA by introducing positive supercoils in an ATP-dependent process. It cleaves transiently a single DNA strand and remains covalently bound to the 5' DNA end through a tyrosine residue. May be involved in rewinding the DNA strands in the regions of the chromosome that have opened up to allow transcription or replication.
Catalytic activity	RHEA:13065: ATP + H2O = ADP + H(+) + phosphate EC 3.6.4.12
	Reaction=ATP-dependent breakage, passage and rejoining of double-stranded DNA.; EC=5.6.2.2;
Subunit	Monomer.
Domain	Both the DNA unwinding and positive supercoiling activities require the cooperation of both domains. The cooperative action between the helicase-like and the topoisomerase domains is specific. The helicase-like domain probably does not directly unwind DNA but acts more likely by driving ATP-dependent conformational changes within the whole enzyme, functioning more like a protein motor. The 'latch' region of the N-terminal domain plays a regulatory role in the enzyme, repressing topoisomerase activity in the absence of ATP and therefore 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 discovered so far. It appears to be essential for adaptation to life at high temperatures.
Similarity	In the N-terminal section; belongs to the DEAD box helicase family. DDVD subfamily.
	In the C-terminal section; belongs to the prokaryotic type I/III topoisomerase family.

Keywords [?]

Hydrolase
Isomerase
Topoisomerase
Helicase
DNA-binding
ATP-binding
Nucleotide-binding

case <FT:2> or <FT:4>

Metal-binding
Zinc
Zinc-finger

end case

Gene Ontology [?]

GO:0005524; Molecular function: ATP binding.
GO:0003677; Molecular function: DNA binding.
GO:0003918; Molecular function: DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity.
GO:0004386; Molecular function: helicase activity.

case <FT:2> or <FT:4>

GO:0008270; Molecular function: zinc ion binding.

end case

GO:0006265; Biological process: DNA topological change.
GO:0006268; Biological process: DNA unwinding involved in DNA replication.

Cross-references [?]

Pfam	PF00270; DEAD; 1;
	PF01131; Topoisom_bac; 1;
	PF01751; Toprim; 1;
	PF00271; Helicase_C; 1;
PRINTS	PR00417; PRTPISMRASEI; 1;
PROSITE	PS51192; HELICASE_ATP_BIND_1; 1; trigger=PRU00541;
	PS51194; HELICASE_CTER; 0-1; trigger=PRU00542;
	PS50880; TOPRIM; 1; trigger=PRU00995;
NCBIfam	TIGR01054; rgy; 1;

Features [?]

From: RGYR_PYRFU (P95479)

Key From To Description Tag Condition FTGroup

ZN_FING 9 30 C4-type 1 C-x-x-C-x(10,18)-[CH]-x-x-C

BINDING 106 113 /ligand="ATP" /ligand_id="ChEBI:CHEBI:30616 x-P-x-G-x-G-K-[ST]

ZN_FING 722 741 C4-type 2 C-x-x-C-x(10,18)-C-x-x-C

REGION 645 Cter Topoisomerase I

ACT_SITE 955 955 For DNA cleavage activity Y

BINDING 89 89 /ligand="ATP" /ligand_id="ChEBI:CHEBI:30616 Q

Additional information [?]

Size range	1054-1624 amino acids
Related rules	None
Fusion	None
Comments	The reverse gyrases of M. jannaschii and P. horikoshii contain inteins which were excised in the alignment

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