ID   OGG1_SULTO              Reviewed;         204 AA.
AC   Q972A8;
DT   10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   25-MAY-2022, entry version 101.
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=STK_12190;
OS   Sulfurisphaera tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)
OS   (Sulfolobus tokodaii).
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Sulfurisphaera.
OX   NCBI_TaxID=273063;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16993 / JCM 10545 / NBRC 100140 / 7;
RX   PubMed=11572479; DOI=10.1093/dnares/8.4.123;
RA   Kawarabayasi Y., Hino Y., Horikawa H., Jin-no K., Takahashi M., Sekine M.,
RA   Baba S., Ankai A., Kosugi H., Hosoyama A., Fukui S., Nagai Y.,
RA   Nishijima K., Otsuka R., Nakazawa H., Takamiya M., Kato Y., Yoshizawa T.,
RA   Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K.,
RA   Masuda S., Yanagii M., Nishimura M., Yamagishi A., Oshima T., Kikuchi H.;
RT   "Complete genome sequence of an aerobic thermoacidophilic Crenarchaeon,
RT   Sulfolobus tokodaii strain7.";
RL   DNA Res. 8:123-140(2001).
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}.
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DR   EMBL; BA000023; BAB66261.1; -; Genomic_DNA.
DR   RefSeq; WP_010979239.1; NC_003106.2.
DR   AlphaFoldDB; Q972A8; -.
DR   SMR; Q972A8; -.
DR   STRING; 273063.STK_12190; -.
DR   EnsemblBacteria; BAB66261; BAB66261; STK_12190.
DR   GeneID; 1459218; -.
DR   KEGG; sto:STK_12190; -.
DR   PATRIC; fig|273063.9.peg.1377; -.
DR   eggNOG; arCOG04357; Archaea.
DR   OMA; FCILTAN; -.
DR   OrthoDB; 95301at2157; -.
DR   Proteomes; UP000001015; 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..204
FT                   /note="8-oxoguanine DNA glycosylase/AP lyase"
FT                   /id="PRO_0000159567"
FT   ACT_SITE        128
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00241"
FT   ACT_SITE        146
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00241"
FT   SITE            204
FT                   /note="Important for guanine/8-oxoguanine distinction"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00241"
SQ   SEQUENCE   204 AA;  23886 MW;  42A27A11B7CE5FCF CRC64;
     MLRELVKNKK LRARVLERAE EFKLNNRAEE NVWFRELILC ILTSNSSFIS AYKALNYIMD
     EIFSLSEDQM SKRLRLAGYR FYNLKAKYIA NARKLYGNLK TKIKPIADYS QEEARQYIIN
     NIDGLGLKES SHFLRNVGYF DLAIIDRHVL HFLNEIGTSN LKIKNKKDYY LAESILKSIS
     INLGIQVGLL DLYIFFKQTN TIVK