OGG1_SACS2
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 25-MAY-2022, entry version 106.
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, ECO:0000303|PubMed:19446526};
GN OrderedLocusNames=SSO0904;
OS Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
OS (Sulfolobus solfataricus).
OC Archaea; Crenarchaeota; 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 EnsemblBacteria; AAK41186; AAK41186; SSO0904.
DR GeneID; 44129834; -.
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 OMA; FCILTAN; -.
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; -; 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 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
