ID   OGG1_SACS2              Reviewed;         207 AA.
AC   Q97ZK2;
DT   10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2001, sequence version 1.
DT   27-MAR-2024, entry version 112.
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:19446526};
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,
GN   ECO:0000303|PubMed:19446526}; OrderedLocusNames=SSO0904;
OS   Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
OS   (Sulfolobus solfataricus).
OC   Archaea; Thermoproteota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Saccharolobus.
OX   NCBI_TaxID=273057;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX   PubMed=11427726; DOI=10.1073/pnas.141222098;
RA   She Q., Singh R.K., Confalonieri F., Zivanovic Y., Allard G., Awayez M.J.,
RA   Chan-Weiher C.C.-Y., Clausen I.G., Curtis B.A., De Moors A., Erauso G.,
RA   Fletcher C., Gordon P.M.K., Heikamp-de Jong I., Jeffries A.C., Kozera C.J.,
RA   Medina N., Peng X., Thi-Ngoc H.P., Redder P., Schenk M.E., Theriault C.,
RA   Tolstrup N., Charlebois R.L., Doolittle W.F., Duguet M., Gaasterland T.,
RA   Garrett R.A., Ragan M.A., Sensen C.W., Van der Oost J.;
RT   "The complete genome of the crenarchaeon Sulfolobus solfataricus P2.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:7835-7840(2001).
RN   [2] {ECO:0007744|PDB:3FHG}
RP   X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF MUTANT GLN-128, AND ACTIVE SITE.
RX   PubMed=19446526; DOI=10.1016/j.str.2009.03.007;
RA   Faucher F., Duclos S., Bandaru V., Wallace S.S., Doublie S.;
RT   "Crystal structures of two archaeal 8-oxoguanine DNA glycosylases provide
RT   structural insight into guanine/8-oxoguanine distinction.";
RL   Structure 17:703-712(2009).
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}.
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DR   EMBL; AE006641; AAK41186.1; -; Genomic_DNA.
DR   PIR; C90241; C90241.
DR   RefSeq; WP_009992328.1; NC_002754.1.
DR   PDB; 3FHG; X-ray; 1.90 A; A=1-207.
DR   PDBsum; 3FHG; -.
DR   AlphaFoldDB; Q97ZK2; -.
DR   SMR; Q97ZK2; -.
DR   STRING; 273057.SSO0904; -.
DR   PaxDb; 273057-SSO0904; -.
DR   EnsemblBacteria; AAK41186; AAK41186; SSO0904.
DR   GeneID; 72912657; -.
DR   KEGG; sso:SSO0904; -.
DR   PATRIC; fig|273057.12.peg.906; -.
DR   eggNOG; arCOG04357; Archaea.
DR   HOGENOM; CLU_104937_0_0_2; -.
DR   InParanoid; Q97ZK2; -.
DR   PhylomeDB; Q97ZK2; -.
DR   BRENDA; 3.2.2.B5; 6163.
DR   EvolutionaryTrace; Q97ZK2; -.
DR   Proteomes; UP000001974; 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   3D-structure; DNA damage; DNA repair; Glycosidase; Hydrolase; Lyase;
KW   Multifunctional enzyme; Reference proteome.
FT   CHAIN           1..207
FT                   /note="8-oxoguanine DNA glycosylase/AP lyase"
FT                   /id="PRO_0000159566"
FT   ACT_SITE        128
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00241,
FT                   ECO:0000305|PubMed:19446526"
FT   ACT_SITE        146
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00241,
FT                   ECO:0000305|PubMed:19446526"
FT   SITE            207
FT                   /note="Important for guanine/8-oxoguanine distinction"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00241,
FT                   ECO:0000269|PubMed:19446526"
FT   HELIX           3..7
FT                   /evidence="ECO:0007829|PDB:3FHG"
FT   HELIX           9..26
FT                   /evidence="ECO:0007829|PDB:3FHG"
FT   HELIX           30..43
FT                   /evidence="ECO:0007829|PDB:3FHG"
FT   HELIX           48..58
FT                   /evidence="ECO:0007829|PDB:3FHG"
FT   HELIX           59..63
FT                   /evidence="ECO:0007829|PDB:3FHG"
FT   HELIX           67..76
FT                   /evidence="ECO:0007829|PDB:3FHG"
FT   HELIX           82..96
FT                   /evidence="ECO:0007829|PDB:3FHG"
FT   TURN            97..99
FT                   /evidence="ECO:0007829|PDB:3FHG"
FT   HELIX           100..110
FT                   /evidence="ECO:0007829|PDB:3FHG"
FT   HELIX           112..119
FT                   /evidence="ECO:0007829|PDB:3FHG"
FT   HELIX           127..136
FT                   /evidence="ECO:0007829|PDB:3FHG"
FT   HELIX           147..155
FT                   /evidence="ECO:0007829|PDB:3FHG"
FT   HELIX           169..185
FT                   /evidence="ECO:0007829|PDB:3FHG"
FT   HELIX           190..202
FT                   /evidence="ECO:0007829|PDB:3FHG"
SQ   SEQUENCE   207 AA;  24253 MW;  823B754303F3F950 CRC64;
     MLRSLVQNPK VRARVLERVD EFRLNNLSNE EVWFRELTLC LLTANSSFIS AYQALNCLGQ
     KIYYANEEEI RNILKSCKYR FYNLKAKYII MAREKVYGRL KEEIKPLADE DQQLARERLL
     NIKGIGMKEA SHFLRNVGYF DLAIIDRHII DFMRRIGAIG ETNVKQLSKS LYISFENILK
     SIASNLNMSV GILDLFIWYK ETNTIVK
//