OGG1_METJA
ID OGG1_METJA Reviewed; 207 AA.
AC Q58134;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 122.
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, ECO:0000269|PubMed:10521423, ECO:0000269|PubMed:19446526};
DE Includes:
DE RecName: Full=DNA-(apurinic or apyrimidinic site) lyase {ECO:0000255|HAMAP-Rule:MF_00241, ECO:0000305};
DE Short=AP lyase {ECO:0000255|HAMAP-Rule:MF_00241, ECO:0000305};
DE EC=4.2.99.18 {ECO:0000255|HAMAP-Rule:MF_00241, ECO:0000269|PubMed:10521423, ECO:0000269|PubMed:19446526};
GN Name=ogg {ECO:0000255|HAMAP-Rule:MF_00241, ECO:0000303|PubMed:19446526};
GN OrderedLocusNames=MJ0724;
OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS 10045 / NBRC 100440) (Methanococcus jannaschii).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanocaldococcaceae; Methanocaldococcus.
OX NCBI_TaxID=243232;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT jannaschii.";
RL Science 273:1058-1073(1996).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP MUTAGENESIS OF LYS-129.
RX PubMed=10521423; DOI=10.1074/jbc.274.43.30447;
RA Gogos A., Clarke N.D.;
RT "Characterization of an 8-oxoguanine DNA glycosylase from Methanococcus
RT jannaschii.";
RL J. Biol. Chem. 274:30447-30450(1999).
RN [3] {ECO:0007744|PDB:3FHF}
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS), FUNCTION, CATALYTIC ACTIVITY,
RP ACTIVE SITE, AND MUTAGENESIS OF 205-VAL--LYS-207.
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).
RN [4] {ECO:0007744|PDB:3KNT}
RP X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF MUTANT GLN-129 IN COMPLEX WITH
RP DNA CONTAINING 8-OXOGUANINE, AND DOMAIN.
RX PubMed=20083120; DOI=10.1016/j.jmb.2010.01.024;
RA Faucher F., Wallace S.S., Doublie S.;
RT "The C-terminal lysine of Ogg2 DNA glycosylases is a major molecular
RT determinant for guanine/8-oxoguanine distinction.";
RL J. Mol. Biol. 397:46-56(2010).
CC -!- FUNCTION: Catalyzes the excision of an oxidatively damaged form of
CC guanine (7,8-dihydro-8-oxoguanine = 8-oxoG) from DNA (PubMed:10521423,
CC PubMed:19446526). Also cleaves the DNA backbone at
CC apurinic/apyrimidinic sites (AP sites) (PubMed:10521423,
CC PubMed:19446526). Has little specificity for the base opposite oxoG
CC (PubMed:10521423). {ECO:0000269|PubMed:10521423,
CC ECO:0000269|PubMed:19446526}.
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:10521423,
CC ECO:0000269|PubMed:19446526};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 8.5. {ECO:0000269|PubMed:10521423};
CC -!- DOMAIN: Contains two domains separated by the central HhH motif. The C-
CC terminal domain undergoes a conformational change upon DNA binding.
CC {ECO:0000269|PubMed:20083120}.
CC -!- SIMILARITY: Belongs to the type-2 OGG1 family. {ECO:0000255|HAMAP-
CC Rule:MF_00241, ECO:0000305}.
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DR EMBL; L77117; AAB98720.1; -; Genomic_DNA.
DR PIR; D64390; D64390.
DR PDB; 3FHF; X-ray; 2.00 A; A=1-207.
DR PDB; 3KNT; X-ray; 2.70 A; A/B/C/D=1-207.
DR PDBsum; 3FHF; -.
DR PDBsum; 3KNT; -.
DR AlphaFoldDB; Q58134; -.
DR SMR; Q58134; -.
DR STRING; 243232.MJ_0724; -.
DR PRIDE; Q58134; -.
DR EnsemblBacteria; AAB98720; AAB98720; MJ_0724.
DR KEGG; mja:MJ_0724; -.
DR eggNOG; arCOG04357; Archaea.
DR HOGENOM; CLU_104937_0_0_2; -.
DR InParanoid; Q58134; -.
DR OMA; FCILTAN; -.
DR PhylomeDB; Q58134; -.
DR BRENDA; 3.2.2.B5; 3260.
DR BRENDA; 4.2.99.18; 3260.
DR EvolutionaryTrace; Q58134; -.
DR Proteomes; UP000000805; 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_0000159562"
FT ACT_SITE 129
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00241,
FT ECO:0000305|PubMed:19446526"
FT ACT_SITE 147
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, ECO:0000269|PubMed:20083120"
FT MUTAGEN 129
FT /note="K->S: Loss of activity."
FT /evidence="ECO:0000269|PubMed:10521423"
FT MUTAGEN 205..207
FT /note="Missing: Unable to excise the damaged base. Slight
FT decrease in lyase activity."
FT /evidence="ECO:0000269|PubMed:19446526"
FT HELIX 1..11
FT /evidence="ECO:0007829|PDB:3FHF"
FT HELIX 15..27
FT /evidence="ECO:0007829|PDB:3FHF"
FT HELIX 28..31
FT /evidence="ECO:0007829|PDB:3FHF"
FT HELIX 34..47
FT /evidence="ECO:0007829|PDB:3FHF"
FT HELIX 52..62
FT /evidence="ECO:0007829|PDB:3FHF"
FT HELIX 65..68
FT /evidence="ECO:0007829|PDB:3FHF"
FT HELIX 71..80
FT /evidence="ECO:0007829|PDB:3FHF"
FT HELIX 86..96
FT /evidence="ECO:0007829|PDB:3FHF"
FT HELIX 97..99
FT /evidence="ECO:0007829|PDB:3FHF"
FT HELIX 102..108
FT /evidence="ECO:0007829|PDB:3FHF"
FT STRAND 109..111
FT /evidence="ECO:0007829|PDB:3FHF"
FT HELIX 112..122
FT /evidence="ECO:0007829|PDB:3FHF"
FT HELIX 128..137
FT /evidence="ECO:0007829|PDB:3FHF"
FT HELIX 148..156
FT /evidence="ECO:0007829|PDB:3FHF"
FT STRAND 159..162
FT /evidence="ECO:0007829|PDB:3FHF"
FT HELIX 169..185
FT /evidence="ECO:0007829|PDB:3FHF"
FT HELIX 190..202
FT /evidence="ECO:0007829|PDB:3FHF"
SQ SEQUENCE 207 AA; 24827 MW; D17747917BF10B45 CRC64;
MMLIKKIEEL KNSEIKDIID KRIQEFKSFK NKSNEEWFKE LCFCILTANF TAEGGIRIQK
EIGDGFLTLP REELEEKLKN LGHRFYRKRA EYIVLARRFK NIKDIVESFE NEKVAREFLV
RNIKGIGYKE ASHFLRNVGY DDVAIIDRHI LRELYENNYI DEIPKTLSRR KYLEIENILR
DIGEEVNLKL SELDLYIWYL RTGKVLK
