ID   OGG1_SULAC              Reviewed;         203 AA.
AC   Q4J929;
DT   27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2005, sequence version 1.
DT   27-MAR-2024, entry version 88.
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};
GN   OrderedLocusNames=Saci_1367;
OS   Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC
OS   15157 / NCIMB 11770).
OC   Archaea; Thermoproteota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Sulfolobus.
OX   NCBI_TaxID=330779;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770;
RX   PubMed=15995215; DOI=10.1128/jb.187.14.4992-4999.2005;
RA   Chen L., Bruegger K., Skovgaard M., Redder P., She Q., Torarinsson E.,
RA   Greve B., Awayez M., Zibat A., Klenk H.-P., Garrett R.A.;
RT   "The genome of Sulfolobus acidocaldarius, a model organism of the
RT   Crenarchaeota.";
RL   J. Bacteriol. 187:4992-4999(2005).
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; CP000077; AAY80701.1; -; Genomic_DNA.
DR   RefSeq; WP_011278203.1; NZ_CP046615.1.
DR   AlphaFoldDB; Q4J929; -.
DR   SMR; Q4J929; -.
DR   STRING; 330779.Saci_1367; -.
DR   GeneID; 78441713; -.
DR   KEGG; sai:Saci_1367; -.
DR   PATRIC; fig|330779.12.peg.1319; -.
DR   eggNOG; arCOG04357; Archaea.
DR   HOGENOM; CLU_104937_0_0_2; -.
DR   Proteomes; UP000001018; 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; Helix-hairpin-Helix base-excision DNA repair enzymes (C-terminal); 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; DNA-glycosylase; 1.
PE   3: Inferred from homology;
KW   DNA damage; DNA repair; Glycosidase; Hydrolase; Lyase;
KW   Multifunctional enzyme; Reference proteome.
FT   CHAIN           1..203
FT                   /note="8-oxoguanine DNA glycosylase/AP lyase"
FT                   /id="PRO_0000159565"
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            203
FT                   /note="Important for guanine/8-oxoguanine distinction"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00241"
SQ   SEQUENCE   203 AA;  23869 MW;  28AF6E867FC8D207 CRC64;
     MLRSLVLNEK LRARVLERAE EFLLNNKADE EVWFRELVLC ILTSNSSFIS AYKSMNYILD
     KILYMDEKEI SILLQESGYR FYNLKAKYLY RAKNLYGKVK KTIKEIADKD QMQAREFIAT
     HIYGIGYKEA SHFLRNVGYL DLAIIDRHIL RFINNLGIPI KLKSKREYLL AESLLRSIAN
     NLNVQVGLLD LFIFFKQTNT IVK
//