ID   OGG1_SULIN              Reviewed;         207 AA.
AC   C3NHM4;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2009, sequence version 1.
DT   25-MAY-2022, entry version 61.
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=YN1551_1546;
OS   Sulfolobus islandicus (strain Y.N.15.51 / Yellowstone #2).
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Sulfolobus.
OX   NCBI_TaxID=419942;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Y.N.15.51 / Yellowstone #2;
RX   PubMed=19435847; DOI=10.1073/pnas.0808945106;
RA   Reno M.L., Held N.L., Fields C.J., Burke P.V., Whitaker R.J.;
RT   "Biogeography of the Sulfolobus islandicus pan-genome.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:8605-8610(2009).
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; CP001404; ACP48634.1; -; Genomic_DNA.
DR   RefSeq; WP_012717491.1; NC_012623.1.
DR   AlphaFoldDB; C3NHM4; -.
DR   SMR; C3NHM4; -.
DR   EnsemblBacteria; ACP48634; ACP48634; YN1551_1546.
DR   GeneID; 7809137; -.
DR   KEGG; sin:YN1551_1546; -.
DR   HOGENOM; CLU_104937_0_0_2; -.
DR   OMA; FCILTAN; -.
DR   Proteomes; UP000006818; 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.
FT   CHAIN           1..207
FT                   /note="8-oxoguanine DNA glycosylase/AP lyase"
FT                   /id="PRO_1000204473"
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            207
FT                   /note="Important for guanine/8-oxoguanine distinction"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00241"
SQ   SEQUENCE   207 AA;  24083 MW;  2C5EDB4A5C41CF4A CRC64;
     MLRSLVQNPR VRARVLERVD EFRLNNLSNE EVWFRELTLC LLTANSSFIS AYQALNCLGD
     KIYYANEEVI RSILKSCKYR FYNLKAKYII MAREKVYGKL KEEITPLADS DQQLAREKLL
     NIKGIGMKEA SHFLRNVGYF DLAIIDRHLI DFMRRIGAIG EINVKHLSKS RYISLESVLK
     SIALNLNISV GILDLFIWYK ETNTIVK