OGG1_YEAST
ID OGG1_YEAST Reviewed; 376 AA.
AC P53397; D6VZB3;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=N-glycosylase/DNA lyase;
DE Includes:
DE RecName: Full=8-oxoguanine DNA glycosylase;
DE EC=3.2.2.-;
DE Includes:
DE RecName: Full=DNA-(apurinic or apyrimidinic site) lyase;
DE Short=AP lyase;
DE EC=4.2.99.18;
GN Name=OGG1; OrderedLocusNames=YML060W; ORFNames=YM9958.02;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 28383 / FL100 / VTT C-80102;
RX PubMed=8643552; DOI=10.1073/pnas.93.11.5197;
RA van der Kemp P.A., Thomas D., Barbey R., de Oliveira R., Boiteux S.;
RT "Cloning and expression in Escherichia coli of the OGG1 gene of
RT Saccharomyces cerevisiae, which codes for a DNA glycosylase that excises
RT 7,8-dihydro-8-oxoguanine and 2,6-diamino-4-hydroxy-5-N-
RT methylformamidopyrimidine.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:5197-5202(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169872;
RA Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL Nature 387:90-93(1997).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP CHARACTERIZATION, AND MUTAGENESIS OF LYS-241.
RX PubMed=9241232; DOI=10.1093/nar/25.16.3204;
RA Girard P.-M., Guibourt N., Boiteux S.;
RT "The Ogg1 protein of Saccharomyces cerevisiae: a 7,8-dihydro-8-oxoguanine
RT DNA glycosylase/AP lyase whose lysine 241 is a critical residue for
RT catalytic activity.";
RL Nucleic Acids Res. 25:3204-3211(1997).
RN [5]
RP CHARACTERIZATION, AND MUTAGENESIS OF LYS-241.
RX PubMed=10677220; DOI=10.1021/bi992262n;
RA Guibourt N., Castaing B., Van Der Kemp P.A., Boiteux S.;
RT "Catalytic and DNA binding properties of the ogg1 protein of Saccharomyces
RT cerevisiae: comparison between the wild type and the K241R and K241Q
RT active-site mutant proteins.";
RL Biochemistry 39:1716-1724(2000).
RN [6]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
CC -!- FUNCTION: DNA repair enzyme that incises DNA at 8-oxoG residues.
CC Excises 7,8-dihydro-8-oxoguanine and 2,6-diamino-4-hydroxy-5-N-
CC methylformamidopyrimidine (FAPY) from damaged DNA. Has a beta-lyase
CC activity that nicks DNA 3' to the lesion.
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;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- MISCELLANEOUS: Present with 3690 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the type-1 OGG1 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U44855; AAC49312.1; -; Genomic_DNA.
DR EMBL; Z46729; CAA86715.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA09837.1; -; Genomic_DNA.
DR PIR; S49801; S49801.
DR RefSeq; NP_013651.1; NM_001182419.1.
DR AlphaFoldDB; P53397; -.
DR SMR; P53397; -.
DR BioGRID; 35106; 90.
DR DIP; DIP-4538N; -.
DR MINT; P53397; -.
DR STRING; 4932.YML060W; -.
DR CarbonylDB; P53397; -.
DR MaxQB; P53397; -.
DR PaxDb; P53397; -.
DR PRIDE; P53397; -.
DR TopDownProteomics; P53397; -.
DR EnsemblFungi; YML060W_mRNA; YML060W; YML060W.
DR GeneID; 854942; -.
DR KEGG; sce:YML060W; -.
DR SGD; S000004525; OGG1.
DR VEuPathDB; FungiDB:YML060W; -.
DR eggNOG; KOG2875; Eukaryota.
DR GeneTree; ENSGT00640000091554; -.
DR HOGENOM; CLU_027543_3_1_1; -.
DR InParanoid; P53397; -.
DR OMA; YAQTYVF; -.
DR BioCyc; YEAST:G3O-32655-MON; -.
DR Reactome; R-SCE-110329; Cleavage of the damaged pyrimidine.
DR Reactome; R-SCE-110330; Recognition and association of DNA glycosylase with site containing an affected purine.
DR Reactome; R-SCE-110331; Cleavage of the damaged purine.
DR PRO; PR:P53397; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; P53397; protein.
DR GO; GO:0005739; C:mitochondrion; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0034039; F:8-oxo-7,8-dihydroguanine DNA N-glycosylase activity; IBA:GO_Central.
DR GO; GO:0140078; F:class I DNA-(apurinic or apyrimidinic site) endonuclease activity; IEA:UniProtKB-EC.
DR GO; GO:0003684; F:damaged DNA binding; IEA:InterPro.
DR GO; GO:0008534; F:oxidized purine nucleobase lesion DNA N-glycosylase activity; IDA:SGD.
DR GO; GO:0006285; P:base-excision repair, AP site formation; IDA:SGD.
DR GO; GO:0006281; P:DNA repair; IMP:SGD.
DR GO; GO:0070987; P:error-free translesion synthesis; IGI:SGD.
DR GO; GO:0006289; P:nucleotide-excision repair; IEA:InterPro.
DR GO; GO:0007004; P:telomere maintenance via telomerase; IMP:SGD.
DR CDD; cd00056; ENDO3c; 1.
DR Gene3D; 1.10.1670.10; -; 1.
DR InterPro; IPR011257; DNA_glycosylase.
DR InterPro; IPR003265; HhH-GPD_domain.
DR InterPro; IPR023170; HhH_base_excis_C.
DR InterPro; IPR004577; Ogg1.
DR InterPro; IPR012904; OGG_N.
DR Pfam; PF00730; HhH-GPD; 1.
DR Pfam; PF07934; OGG_N; 1.
DR SMART; SM00478; ENDO3c; 1.
DR SUPFAM; SSF48150; SSF48150; 1.
DR TIGRFAMs; TIGR00588; ogg; 1.
PE 1: Evidence at protein level;
KW DNA damage; DNA repair; Glycosidase; Hydrolase; Lyase;
KW Multifunctional enzyme; Nucleus; Reference proteome.
FT CHAIN 1..376
FT /note="N-glycosylase/DNA lyase"
FT /id="PRO_0000058595"
FT ACT_SITE 241
FT /note="Schiff-base intermediate with DNA"
FT BINDING 134
FT /ligand="DNA"
FT /ligand_id="ChEBI:CHEBI:16991"
FT /evidence="ECO:0000250"
FT BINDING 139
FT /ligand="DNA"
FT /ligand_id="ChEBI:CHEBI:16991"
FT /evidence="ECO:0000250"
FT BINDING 189
FT /ligand="DNA"
FT /ligand_id="ChEBI:CHEBI:16991"
FT /evidence="ECO:0000250"
FT BINDING 258
FT /ligand="8-oxoguanine"
FT /ligand_id="ChEBI:CHEBI:52617"
FT /evidence="ECO:0000250"
FT BINDING 260
FT /ligand="8-oxoguanine"
FT /ligand_id="ChEBI:CHEBI:52617"
FT /evidence="ECO:0000250"
FT BINDING 262
FT /ligand="DNA"
FT /ligand_id="ChEBI:CHEBI:16991"
FT /evidence="ECO:0000250"
FT BINDING 320
FT /ligand="8-oxoguanine"
FT /ligand_id="ChEBI:CHEBI:52617"
FT /evidence="ECO:0000250"
FT BINDING 324
FT /ligand="8-oxoguanine"
FT /ligand_id="ChEBI:CHEBI:52617"
FT /evidence="ECO:0000250"
FT MUTAGEN 241
FT /note="K->Q: Abolishes both DNA glycosylase and AP lyase
FT activity."
FT /evidence="ECO:0000269|PubMed:10677220,
FT ECO:0000269|PubMed:9241232"
FT MUTAGEN 241
FT /note="K->R: Diminishes both DNA glycosylase and AP lyase
FT activity."
FT /evidence="ECO:0000269|PubMed:10677220,
FT ECO:0000269|PubMed:9241232"
SQ SEQUENCE 376 AA; 42781 MW; 4ADB72EB20E4BF20 CRC64;
MSYKFGKLAI NKSELCLANV LQAGQSFRWI WDEKLNQYST TMKIGQQEKY SVVILRQDEE
NEILEFVAVG DCGNQDALKT HLMKYFRLDV SLKHLFDNVW IPSDKAFAKL SPQGIRILAQ
EPWETLISFI CSSNNNISRI TRMCNSLCSN FGNLITTIDG VAYHSFPTSE ELTSRATEAK
LRELGFGYRA KYIIETARKL VNDKAEANIT SDTTYLQSIC KDAQYEDVRE HLMSYNGVGP
KVADCVCLMG LHMDGIVPVD VHVSRIAKRD YQISANKNHL KELRTKYNAL PISRKKINLE
LDHIRLMLFK KWGSYAGWAQ GVLFSKEIGG TSGSTTTGTI KKRKWDMIKE TEAIVTKQMK
LKVELSDLHI KEAKID
