AC MF_01125; DC Protein; auto TR HAMAP; MF_01125; -; 1; level=0 XX Names: Reverse_gyrase XX ID RGYR DE RecName: Full=Reverse gyrase; DE EC=5.6.2.-; GN Name=rgy; XX CC -!- FUNCTION: Modifies the topological state of DNA by introducing positive CC supercoils in an ATP-dependent process, increasing the linking number CC in steps of +1. Binds to single-stranded DNA, transiently cleaves and CC then rejoins the ends, introducing a positive supercoil in the process. CC The scissile phosphodiester is attacked by the catalytic tyrosine of CC the enzyme, resulting in the formation of a DNA-(5'-phosphotyrosyl)- CC enzyme intermediate. Probably involved in rewinding DNA strands in CC regions of the chromosome that have opened up to allow replication, CC transcription, DNA repair and/or for DNA protection. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Note=Binds 1 or 2 zinc ions per subunit.; CC -!- SUBUNIT: Monomer. CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- DOMAIN: Introduction of positive supercoils requires the cooperation of CC both domains. The helicase-like domain probably does not directly CC unwind DNA, but more likely acts by driving ATP-dependent CC conformational changes within the whole enzyme. A beta hairpin in the CC 'latch' region of the N-terminal domain plays a regulatory role in the CC enzyme, repressing topoisomerase activity in the absence of ATP and CC preventing the enzyme from acting as an ATP-independent relaxing CC enzyme; it also helps to coordinate nucleotide hydrolysis by the ATPase CC domain with the supercoiling activity of the topoisomerase domain. CC -!- MISCELLANEOUS: This enzyme is the only unique feature of CC hyperthermophilic bacteria/archaea known and seems to be essential for CC adaptation to life at high temperatures. It may play a role in CC stabilization of DNA at high temperatures. CC -!- SIMILARITY: In the N-terminal section; belongs to the DEAD box helicase CC family. DDVD subfamily. CC -!- SIMILARITY: In the C-terminal section; belongs to the type IA CC topoisomerase family. XX DR Pfam; PF00270; DEAD; 1; trigger=no DR Pfam; PF01131; Topoisom_bac; 1; trigger=no DR Pfam; PF01751; Toprim; 1; trigger=no DR Pfam; PF00271; Helicase_C; 1; trigger=no DR PRINTS; PR00417; PRTPISMRASEI; 1; trigger=no DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1; trigger=yes DR PROSITE; PS51194; HELICASE_CTER; 0-1; trigger=yes DR PROSITE; PS52039; TOPO_IA_2; 1; trigger=yes DR PROSITE; PS50880; TOPRIM; 1; trigger=yes DR PROSITE; PS52037; ZF_RG_C; 0-1; trigger=yes DR PROSITE; PS52036; ZF_RG_N; 1; trigger=yes DR NCBIfam; TIGR01054; rgy; 1; trigger=no XX KW Cytoplasm KW Hydrolase KW Isomerase KW Topoisomerase KW DNA-binding KW ATP-binding KW Nucleotide-binding KW Metal-binding KW Zinc KW Zinc-finger XX GO GO:0005524; F:ATP binding GO GO:0003677; F:DNA binding GO GO:0008094; F:ATP-dependent activity, acting on DNA GO GO:0005737; C:cytoplasm GO GO:0160097; F:reverse gyrase activity GO GO:0003916; F:DNA topoisomerase activity GO GO:0008270; F:zinc ion binding GO GO:0006265; P:DNA topological change GO GO:0006268; P:DNA unwinding involved in DNA replication XX FT From: RGYR_THEMA (O51934) FT REGION 538..Cter FT /note="Topoisomerase I" FT ACT_SITE 851 FT /note="O-(5'-phospho-DNA)-tyrosine intermediate" FT Condition: Y FT BINDING 83 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT Condition: Q XX Size: 1054-1624; Related: None; Template: Q08582; O29238; Scope: Bacteria Archaea Fusion: Nter: None Cter: None Duplicate: in AERPE, AQUAE, SACS2, SULTO Plasmid: 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. XX # Revision 1.34 2023/11/03 //