ID   OGG1_THEAC              Reviewed;         204 AA.
AC   Q9HM55;
DT   10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT   10-OCT-2002, sequence version 2.
DT   27-MAR-2024, entry version 104.
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=Ta0014;
OS   Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC
OS   15155 / AMRC-C165).
OC   Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC   Thermoplasmataceae; Thermoplasma.
OX   NCBI_TaxID=273075;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165;
RX   PubMed=11029001; DOI=10.1038/35035069;
RA   Ruepp A., Graml W., Santos-Martinez M.-L., Koretke K.K., Volker C.,
RA   Mewes H.-W., Frishman D., Stocker S., Lupas A.N., Baumeister W.;
RT   "The genome sequence of the thermoacidophilic scavenger Thermoplasma
RT   acidophilum.";
RL   Nature 407:508-513(2000).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAC11163.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AL445063; CAC11163.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_010900441.1; NC_002578.1.
DR   AlphaFoldDB; Q9HM55; -.
DR   SMR; Q9HM55; -.
DR   STRING; 273075.gene:9571229; -.
DR   PaxDb; 273075-Ta0014m; -.
DR   EnsemblBacteria; CAC11163; CAC11163; CAC11163.
DR   GeneID; 1456957; -.
DR   KEGG; tac:Ta0014; -.
DR   eggNOG; arCOG04357; Archaea.
DR   HOGENOM; CLU_104937_0_0_2; -.
DR   InParanoid; Q9HM55; -.
DR   OrthoDB; 35941at2157; -.
DR   Proteomes; UP000001024; 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..204
FT                   /note="8-oxoguanine DNA glycosylase/AP lyase"
FT                   /id="PRO_0000159568"
FT   ACT_SITE        129
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00241"
FT   ACT_SITE        147
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;  23690 MW;  B66235138976AE20 CRC64;
     MDSLISIPFL NDESVRSTIY RKVEEFRSIG KSSKEVLFKE LVFCILAANT SASMSLRMQE
     SIGDGFLYLS RDDLRKALKE NKYRFYNVRS DFIVKSRNII DDLPALVASP DHEGSRDYLV
     ENVYGIGYKE ASHFLRNVGI FDFAILDKHI MKWMAQYYPV KKNTSRKNYL YNEEIFRNIS
     AGFGIEPGIL DLFIWYEETG TVIK
//