OGG1_AQUAE
ID OGG1_AQUAE Reviewed; 226 AA.
AC O66612;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=8-oxoguanine DNA glycosylase/AP lyase {ECO:0000255|HAMAP-Rule:MF_00241};
DE Includes:
DE RecName: Full=8-oxoguanine DNA glycosylase {ECO:0000255|HAMAP-Rule:MF_00241};
DE Short=8-oxoG DNA glycosylase {ECO:0000255|HAMAP-Rule:MF_00241};
DE EC=3.2.2.- {ECO:0000255|HAMAP-Rule:MF_00241};
DE Includes:
DE RecName: Full=DNA-(apurinic or apyrimidinic site) lyase {ECO:0000255|HAMAP-Rule:MF_00241};
DE Short=AP lyase {ECO:0000255|HAMAP-Rule:MF_00241};
DE EC=4.2.99.18 {ECO:0000255|HAMAP-Rule:MF_00241};
GN Name=ogg {ECO:0000255|HAMAP-Rule:MF_00241}; OrderedLocusNames=aq_251;
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: Catalyzes the excision of an oxidatively damaged form of
CC guanine (7,8-dihydro-8-oxoguanine = 8-oxoG) from DNA. Also cleaves the
CC DNA backbone at apurinic/apyrimidinic sites (AP sites).
CC {ECO:0000255|HAMAP-Rule:MF_00241}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2'-deoxyribonucleotide-(2'-deoxyribose 5'-phosphate)-2'-
CC deoxyribonucleotide-DNA = a 3'-end 2'-deoxyribonucleotide-(2,3-
CC dehydro-2,3-deoxyribose 5'-phosphate)-DNA + a 5'-end 5'-monophospho-
CC 2'-deoxyribonucleoside-DNA + H(+); Xref=Rhea:RHEA:66592, Rhea:RHEA-
CC COMP:13180, Rhea:RHEA-COMP:16897, Rhea:RHEA-COMP:17067,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:136412, ChEBI:CHEBI:157695,
CC ChEBI:CHEBI:167181; EC=4.2.99.18; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00241};
CC -!- SIMILARITY: Belongs to the type-2 OGG1 family. {ECO:0000255|HAMAP-
CC Rule:MF_00241, ECO:0000305}.
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DR EMBL; AE000657; AAC06576.1; -; Genomic_DNA.
DR PIR; H70322; H70322.
DR RefSeq; NP_213172.1; NC_000918.1.
DR RefSeq; WP_010880110.1; NC_000918.1.
DR AlphaFoldDB; O66612; -.
DR SMR; O66612; -.
DR STRING; 224324.aq_251; -.
DR EnsemblBacteria; AAC06576; AAC06576; aq_251.
DR KEGG; aae:aq_251; -.
DR eggNOG; COG1059; Bacteria.
DR HOGENOM; CLU_104937_0_0_0; -.
DR InParanoid; O66612; -.
DR OMA; FCILTAN; -.
DR OrthoDB; 1534544at2; -.
DR Proteomes; UP000000798; Chromosome.
DR GO; GO:0140078; F:class I DNA-(apurinic or apyrimidinic site) endonuclease activity; IEA:UniProtKB-EC.
DR GO; GO:0016799; F:hydrolase activity, hydrolyzing N-glycosyl compounds; IEA:UniProtKB-UniRule.
DR GO; GO:0006284; P:base-excision repair; IEA:UniProtKB-UniRule.
DR CDD; cd00056; ENDO3c; 1.
DR Gene3D; 1.10.1670.10; -; 1.
DR HAMAP; MF_00241; Ogg; 1.
DR InterPro; IPR012092; DNA_glyclase/AP_lyase_Ogg.
DR InterPro; IPR011257; DNA_glycosylase.
DR InterPro; IPR003265; HhH-GPD_domain.
DR InterPro; IPR023170; HhH_base_excis_C.
DR PIRSF; PIRSF005954; Thrmst_ogg; 1.
DR SMART; SM00478; ENDO3c; 1.
DR SUPFAM; SSF48150; SSF48150; 1.
PE 3: Inferred from homology;
KW DNA damage; DNA repair; Glycosidase; Hydrolase; Lyase;
KW Multifunctional enzyme; Reference proteome.
FT CHAIN 1..226
FT /note="8-oxoguanine DNA glycosylase/AP lyase"
FT /id="PRO_0000159570"
FT ACT_SITE 149
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00241"
FT ACT_SITE 167
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00241"
FT SITE 226
FT /note="Important for guanine/8-oxoguanine distinction"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00241"
SQ SEQUENCE 226 AA; 26306 MW; 90DE4DCED18FC20D CRC64;
MDAIQEVKRI IPEVQKYVNQ RMEEFERLGR EGWTHFDFRP FLDIDYDAGL FSELSFCILT
ANSSATLGIK IQAHLGEEGF LNKTKEELEE VFRKFGHRYA GQRAERIVEA REKFPKVKSL
IEKEKNSKVI RELLADPKSP YKIKGFGYKE ASHFLRNIGF KDLAIIDRHI SRFLMEKGLL
RQVKSITPKV YLEAEKALES LAKELGLSLG ELDLYIFYIK TKKVLK