OGG1_THEMA
ID OGG1_THEMA Reviewed; 207 AA.
AC Q9X2E1;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, 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};
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=TM_1821;
OS Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS / MSB8).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX NCBI_TaxID=243274;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=10360571; DOI=10.1038/20601;
RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA Smith H.O., Venter J.C., Fraser C.M.;
RT "Evidence for lateral gene transfer between Archaea and Bacteria from
RT genome sequence of Thermotoga maritima.";
RL Nature 399:323-329(1999).
RN [2] {ECO:0007744|PDB:3N0U}
RP X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS).
RA Cooper D.R., Roy A., Derewenda Z.S.;
RT "Crystal structure of Tm1821, the 8-oxoguanine DNA glycosylase of
RT Thermotoga maritima.";
RL Submitted (MAY-2010) to the PDB data bank.
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; AE000512; AAD36884.1; -; Genomic_DNA.
DR PIR; H72206; H72206.
DR RefSeq; NP_229618.1; NC_000853.1.
DR RefSeq; WP_004082367.1; NZ_CP011107.1.
DR PDB; 3N0U; X-ray; 1.50 A; A/B/C=1-207.
DR PDBsum; 3N0U; -.
DR AlphaFoldDB; Q9X2E1; -.
DR SMR; Q9X2E1; -.
DR STRING; 243274.THEMA_05090; -.
DR EnsemblBacteria; AAD36884; AAD36884; TM_1821.
DR KEGG; tma:TM1821; -.
DR eggNOG; COG1059; Bacteria.
DR InParanoid; Q9X2E1; -.
DR OMA; FCILTAN; -.
DR OrthoDB; 1534544at2; -.
DR EvolutionaryTrace; Q9X2E1; -.
DR Proteomes; UP000008183; 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_0000159572"
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 207
FT /note="Important for guanine/8-oxoguanine distinction"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00241"
FT HELIX 1..32
FT /evidence="ECO:0007829|PDB:3N0U"
FT HELIX 35..47
FT /evidence="ECO:0007829|PDB:3N0U"
FT TURN 48..50
FT /evidence="ECO:0007829|PDB:3N0U"
FT HELIX 53..63
FT /evidence="ECO:0007829|PDB:3N0U"
FT HELIX 66..69
FT /evidence="ECO:0007829|PDB:3N0U"
FT HELIX 72..81
FT /evidence="ECO:0007829|PDB:3N0U"
FT HELIX 87..97
FT /evidence="ECO:0007829|PDB:3N0U"
FT HELIX 98..100
FT /evidence="ECO:0007829|PDB:3N0U"
FT TURN 101..103
FT /evidence="ECO:0007829|PDB:3N0U"
FT HELIX 104..109
FT /evidence="ECO:0007829|PDB:3N0U"
FT HELIX 112..122
FT /evidence="ECO:0007829|PDB:3N0U"
FT HELIX 128..136
FT /evidence="ECO:0007829|PDB:3N0U"
FT TURN 137..139
FT /evidence="ECO:0007829|PDB:3N0U"
FT HELIX 148..156
FT /evidence="ECO:0007829|PDB:3N0U"
FT HELIX 169..186
FT /evidence="ECO:0007829|PDB:3N0U"
FT HELIX 190..202
FT /evidence="ECO:0007829|PDB:3N0U"
SQ SEQUENCE 207 AA; 24210 MW; DB4F7E3EF71C6204 CRC64;
MEELLKELER IREEAKPLVE QRFEEFKRLG EEGTEEDLFC ELSFCVLTAN WSAEGGIRAQ
KEIGKGFVHL PLEELAEKLR EVGHRYPQKR AEFIVENRKL LGKLKNLVKG DPFQSREFLV
RNAKGIGWKE ASHFLRNTGV EDLAILDKHV LRLMKRHGLI QEIPKGWSKK RYLYVEEILR
KVAEAFGESP GKFDLYLWYL VKGKVDK
