RGYR1_AQUAE
ID RGYR1_AQUAE Reviewed; 1146 AA.
AC O67037;
DT 16-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Reverse gyrase 1 {ECO:0000255|HAMAP-Rule:MF_01125};
DE Includes:
DE RecName: Full=Helicase {ECO:0000255|HAMAP-Rule:MF_01125};
DE EC=3.6.4.12 {ECO:0000255|HAMAP-Rule:MF_01125};
DE Includes:
DE RecName: Full=Topoisomerase {ECO:0000255|HAMAP-Rule:MF_01125};
DE EC=5.6.2.2 {ECO:0000255|HAMAP-Rule:MF_01125};
GN Name=rgy1 {ECO:0000255|HAMAP-Rule:MF_01125}; Synonyms=topG1;
GN OrderedLocusNames=aq_886;
OS Aquifex aeolicus (strain VF5).
OC Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX NCBI_TaxID=224324;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VF5;
RX PubMed=9537320; DOI=10.1038/32831;
RA Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
RL Nature 392:353-358(1998).
CC -!- FUNCTION: Modifies the topological state of DNA by introducing positive
CC supercoils in an ATP-dependent process. It cleaves transiently a single
CC DNA strand and remains covalently bound to the 5' DNA end through a
CC tyrosine residue. May be involved in rewinding the DNA strands in the
CC regions of the chromosome that have opened up to allow transcription or
CC replication. {ECO:0000255|HAMAP-Rule:MF_01125}.
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; EC=3.6.4.12;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01125};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP-dependent breakage, passage and rejoining of double-
CC stranded DNA.; EC=5.6.2.2; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01125};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01125};
CC Note=Binds two Mg(2+) per subunit. {ECO:0000255|HAMAP-Rule:MF_01125};
CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_01125}.
CC -!- DOMAIN: Both the DNA unwinding and positive supercoiling activities
CC require the cooperation of both domains. The cooperative action between
CC the helicase-like and the topoisomerase domains is specific. The
CC helicase-like domain probably does not directly unwind DNA but acts
CC more likely by driving ATP-dependent conformational changes within the
CC whole enzyme, functioning more like a protein motor. The 'latch' region
CC of the N-terminal domain plays a regulatory role in the enzyme,
CC repressing topoisomerase activity in the absence of ATP and therefore
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 {ECO:0000255|HAMAP-Rule:MF_01125}.
CC -!- MISCELLANEOUS: This enzyme is the only unique feature of
CC hyperthermophilic bacteria/archaea discovered so far. It appears to be
CC essential for adaptation to life at high temperatures.
CC -!- SIMILARITY: In the N-terminal section; belongs to the DEAD box helicase
CC family. DDVD subfamily. {ECO:0000255|HAMAP-Rule:MF_01125}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the prokaryotic type
CC I/III topoisomerase family. {ECO:0000255|HAMAP-Rule:MF_01125}.
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DR EMBL; AE000657; AAC07000.1; -; Genomic_DNA.
DR PIR; B70376; B70376.
DR RefSeq; NP_213599.1; NC_000918.1.
DR RefSeq; WP_010880537.1; NC_000918.1.
DR AlphaFoldDB; O67037; -.
DR SMR; O67037; -.
DR STRING; 224324.aq_886; -.
DR PRIDE; O67037; -.
DR EnsemblBacteria; AAC07000; AAC07000; aq_886.
DR KEGG; aae:aq_886; -.
DR PATRIC; fig|224324.8.peg.689; -.
DR eggNOG; COG1110; Bacteria.
DR HOGENOM; CLU_002886_0_0_0; -.
DR InParanoid; O67037; -.
DR OMA; GVATYYG; -.
DR OrthoDB; 223233at2; -.
DR Proteomes; UP000000798; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0003918; F:DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006265; P:DNA topological change; IEA:UniProtKB-UniRule.
DR GO; GO:0006268; P:DNA unwinding involved in DNA replication; IEA:UniProtKB-UniRule.
DR CDD; cd00186; TOP1Ac; 1.
DR Gene3D; 1.10.290.10; -; 1.
DR Gene3D; 1.10.460.10; -; 1.
DR Gene3D; 3.40.50.300; -; 3.
DR HAMAP; MF_01125; Reverse_gyrase; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005736; Reverse_gyrase.
DR InterPro; IPR003601; Topo_IA_2.
DR InterPro; IPR013497; Topo_IA_cen.
DR InterPro; IPR013824; Topo_IA_cen_sub1.
DR InterPro; IPR013826; Topo_IA_cen_sub3.
DR InterPro; IPR023405; Topo_IA_core_domain.
DR InterPro; IPR003602; Topo_IA_DNA-bd_dom.
DR InterPro; IPR006171; TOPRIM_domain.
DR InterPro; IPR040569; Znf_Rg.
DR PANTHER; PTHR43505; PTHR43505; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF01131; Topoisom_bac; 1.
DR Pfam; PF01751; Toprim; 1.
DR Pfam; PF17915; zf_Rg; 1.
DR PRINTS; PR00417; PRTPISMRASEI.
DR SMART; SM00382; AAA; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00437; TOP1Ac; 1.
DR SMART; SM00436; TOP1Bc; 1.
DR SMART; SM00493; TOPRIM; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR SUPFAM; SSF56712; SSF56712; 1.
DR TIGRFAMs; TIGR01054; rgy; 2.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS50880; TOPRIM; 1.
PE 3: Inferred from homology;
KW ATP-binding; DNA-binding; Helicase; Hydrolase; Isomerase; Magnesium;
KW Metal-binding; Nucleotide-binding; Reference proteome; Topoisomerase; Zinc;
KW Zinc-finger.
FT CHAIN 1..1146
FT /note="Reverse gyrase 1"
FT /id="PRO_0000158080"
FT DOMAIN 83..240
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01125"
FT DOMAIN 412..565
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01125"
FT DOMAIN 596..728
FT /note="Toprim"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01125"
FT ZN_FING 10..31
FT /note="C4-type"
FT /evidence="ECO:0000250"
FT REGION 602..1146
FT /note="Topoisomerase I"
FT MOTIF 197..200
FT /note="DEAD box"
FT ACT_SITE 891
FT /note="For DNA cleavage activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01125"
FT BINDING 79
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01125"
FT BINDING 96..103
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01125"
FT BINDING 602
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01125"
FT BINDING 697
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01125"
FT BINDING 697
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01125"
FT BINDING 699
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01125"
SQ SEQUENCE 1146 AA; 132518 MW; 26C7FF7A0F9C66E9 CRC64;
MIKAIFDTLC PNCGGEISAE RLLKGLPCEK CLPEEVNREE VCQKLENGSF KEFCELLSEL
KDWEDFFKEI LGTSPWSLQK SWARKVFLGR SFAMLAPTGV GKTTFGLSMA SYLAKQGKKS
YIILPTQLLV EQVSERIKTF GVDEDRLIVW GKLSEKKKKE LKERIQKGDF DILITTSMFL
YKNYEILPKD FSFIFVDDVD SFLKTAKNVD KVLYLLGFSE EDIHKAFELI RLKEKPNKSE
EDWEEIKKRS EELREIAKKK KGVLAVSSAT GNPRSNRIKL FRELLGFEVG KPSVLLRNIV
ETYEETQNLK ETLLKRVKEF GKGGLVFVSS DYGREAVEEV KKFLESHGVK AVTYEEDLKL
FEKGEAQVAI GISSFKNPLA RGIDLPHVVR YAIFYGVPKI RVPLKVETSV SHLLWALLSL
RPIILKDEKL KSEVKKVDTW IQRLRRYSFL SDDFVEERPD LKDRIENLRK EVQEFLLRED
IVEKIKNSEE LTLRLGEEGF ELVVADVTGY LQASGRTSRM YAGGLTKGLS HVLVDDRRAF
KNLEKKVRWF NQDINFKKIE EVDLKEVLRE IDEDRKKVRE ILEGKVKAEQ KEHVKPVLVV
VESPNKARTI ANFFGKPMGR KIGGIDVLEV MVGDLYIMIT ASLGHVFDLV KDKEFHGVIA
KNGEYVPIYE VIEGKENIVK GLRELAQEVD TVLIGTDPDT EGEKIGWDLG ALLSPYIPNV
ERIEFHEVTR KAIKHAVENP RDFNENLVKA QLVRRIADRW VGFEVSRIVQ QAFDKHWLSG
GRVQIPVLGW IIEREKLYRK KKHVVQITFK ENGRWLRLGF EFQDKKEAKE FYENLKEIDV
EVLEEREELK NPPPPFTTDT MLKEASDRYR ISVPKLMQLA QELFEYGLIT YHRTDSTRVS
DVGIGVAKEW ISEELGKELF YPRVWGEGGA HECIRPTKPL DVEDLRSMML AGQLQNLTRE
HLLLYELIFK RFMASQMKPV KVKTKKVKVK ALGREQELIL TTEILEEGFN KVYPLELQPD
LKGSVYVEDK KELKSVPMAY LYTQGSLVEE MKRRGIGRPS TYATIVSKLL ERGYVIERHG
FLIPTKLGKQ VYEFLKSREK IMPFVSEEFT RKLEELMDKV EEGKEDYLQV LDELYKKVNE
FEKANV
