OGG1_THEVO
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 25-MAY-2022, entry version 99.
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 STRING; 273116.14324274; -.
DR EnsemblBacteria; BAB59202; BAB59202; BAB59202.
DR GeneID; 1441548; -.
DR KEGG; tvo:TVG0063493; -.
DR eggNOG; arCOG04357; Archaea.
DR HOGENOM; CLU_104937_0_0_2; -.
DR OMA; FCILTAN; -.
DR OrthoDB; 95301at2157; -.
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; -; 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 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
