OGG1_THEAC
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 25-MAY-2022, entry version 97.
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.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 OMA; FCILTAN; -.
DR OrthoDB; 95301at2157; -.
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; -; 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; 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