ID   OGG1_THEVO              Reviewed;         204 AA.
AC   Q97CP1;
DT   10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2001, sequence version 1.
DT   27-MAR-2024, entry version 105.
DE   RecName: Full=8-oxoguanine DNA glycosylase/AP lyase {ECO:0000255|HAMAP-Rule:MF_00241, ECO:0000305};
DE   Includes:
DE     RecName: Full=8-oxoguanine DNA glycosylase {ECO:0000255|HAMAP-Rule:MF_00241, ECO:0000303|PubMed:27799846};
DE              Short=8-oxoG DNA glycosylase {ECO:0000255|HAMAP-Rule:MF_00241};
DE              EC=3.2.2.- {ECO:0000255|HAMAP-Rule:MF_00241, ECO:0000269|PubMed:27799846};
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, ECO:0000303|PubMed:27799846};
DE              EC=4.2.99.18 {ECO:0000255|HAMAP-Rule:MF_00241, ECO:0000269|PubMed:27799846};
GN   Name=ogg {ECO:0000255|HAMAP-Rule:MF_00241}; OrderedLocusNames=TV0060;
GN   ORFNames=TVG0063493;
OS   Thermoplasma volcanium (strain ATCC 51530 / DSM 4299 / JCM 9571 / NBRC
OS   15438 / GSS1).
OC   Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC   Thermoplasmataceae; Thermoplasma.
OX   NCBI_TaxID=273116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51530 / DSM 4299 / JCM 9571 / NBRC 15438 / GSS1;
RX   PubMed=11121031; DOI=10.1073/pnas.97.26.14257;
RA   Kawashima T., Amano N., Koike H., Makino S., Higuchi S., Kawashima-Ohya Y.,
RA   Watanabe K., Yamazaki M., Kanehori K., Kawamoto T., Nunoshiba T.,
RA   Yamamoto Y., Aramaki H., Makino K., Suzuki M.;
RT   "Archaeal adaptation to higher temperatures revealed by genomic sequence of
RT   Thermoplasma volcanium.";
RL   Proc. Natl. Acad. Sci. U.S.A. 97:14257-14262(2000).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC   STRAIN=ATCC 51530 / DSM 4299 / JCM 9571 / NBRC 15438 / GSS1;
RX   PubMed=27799846; DOI=10.1155/2016/8734894;
RA   Fujii M., Hata C., Ukita M., Fukushima C., Matsuura C., Kawashima-Ohya Y.,
RA   Tomobe K., Kawashima T.;
RT   "Characterization of a thermostable 8-oxoguanine DNA glycosylase specific
RT   for GO/N mismatches from the thermoacidophilic archaeon Thermoplasma
RT   volcanium.";
RL   Archaea 2016:8734894-8734894(2016).
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). Prefers
CC       oligomers containing 8-oxoG:C, 8-oxoG:T and 8-oxoG:G base pairs, and is
CC       less effective on oligomers containing 8-oxoG:A mispairs.
CC       {ECO:0000269|PubMed:27799846}.
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, ECO:0000269|PubMed:27799846};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is about 7.5. {ECO:0000269|PubMed:27799846};
CC       Temperature dependence:
CC         Optimum temperature is 60 degrees Celsius.
CC         {ECO:0000269|PubMed:27799846};
CC   -!- SIMILARITY: Belongs to the type-2 OGG1 family. {ECO:0000255|HAMAP-
CC       Rule:MF_00241}.
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DR   EMBL; BA000011; BAB59202.1; -; Genomic_DNA.
DR   RefSeq; WP_010916318.1; NC_002689.2.
DR   AlphaFoldDB; Q97CP1; -.
DR   SMR; Q97CP1; -.
DR   PaxDb; 273116-14324274; -.
DR   GeneID; 1441548; -.
DR   KEGG; tvo:TVG0063493; -.
DR   eggNOG; arCOG04357; Archaea.
DR   HOGENOM; CLU_104937_0_0_2; -.
DR   OrthoDB; 35941at2157; -.
DR   PhylomeDB; Q97CP1; -.
DR   Proteomes; UP000001017; 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   1: Evidence at protein level;
KW   DNA damage; DNA repair; Glycosidase; Hydrolase; Lyase;
KW   Multifunctional enzyme.
FT   CHAIN           1..204
FT                   /note="8-oxoguanine DNA glycosylase/AP lyase"
FT                   /id="PRO_0000159569"
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;  24267 MW;  D5CF15B12D55E49D CRC64;
     MDFNQYFLPL FQGEASLIIN KKVEEFKLFD RKNKDALFEE LCFCILAANT SARMALDMQN
     RIGKGFLYLS ENELREKLKA FKYRFYNVRP RYIVESRDIV DELPYIVSMD NKEEARDLLV
     ENVYGFGYKE ASHFLRNVGV FDFAILDKHI LEWLSRYFQV KKNTSRKNYL YNESIFREIA
     KSVGMEPGVL DLYIWYMETG TVIK
//