OGG1_ARCFU
ID OGG1_ARCFU Reviewed; 198 AA.
AC O29876;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 25-MAY-2022, 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:11425515};
DE Short=8-oxoG DNA glycosylase {ECO:0000255|HAMAP-Rule:MF_00241, ECO:0000303|PubMed:11425515};
DE EC=3.2.2.- {ECO:0000255|HAMAP-Rule:MF_00241, ECO:0000269|PubMed:11425515};
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, ECO:0000303|PubMed:11425515};
DE EC=4.2.99.18 {ECO:0000255|HAMAP-Rule:MF_00241, ECO:0000269|PubMed:11425515};
GN Name=ogg {ECO:0000255|HAMAP-Rule:MF_00241}; OrderedLocusNames=AF_0371;
OS Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC
OS 100126 / VC-16).
OC Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; Archaeoglobaceae;
OC Archaeoglobus.
OX NCBI_TaxID=224325;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16;
RX PubMed=9389475; DOI=10.1038/37052;
RA Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E., Ketchum K.A.,
RA Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D., Richardson D.L.,
RA Kerlavage A.R., Graham D.E., Kyrpides N.C., Fleischmann R.D.,
RA Quackenbush J., Lee N.H., Sutton G.G., Gill S.R., Kirkness E.F.,
RA Dougherty B.A., McKenney K., Adams M.D., Loftus B.J., Peterson S.N.,
RA Reich C.I., McNeil L.K., Badger J.H., Glodek A., Zhou L., Overbeek R.,
RA Gocayne J.D., Weidman J.F., McDonald L.A., Utterback T.R., Cotton M.D.,
RA Spriggs T., Artiach P., Kaine B.P., Sykes S.M., Sadow P.W., D'Andrea K.P.,
RA Bowman C., Fujii C., Garland S.A., Mason T.M., Olsen G.J., Fraser C.M.,
RA Smith H.O., Woese C.R., Venter J.C.;
RT "The complete genome sequence of the hyperthermophilic, sulphate-reducing
RT archaeon Archaeoglobus fulgidus.";
RL Nature 390:364-370(1997).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RX PubMed=11425515; DOI=10.1016/s0921-8777(01)00081-7;
RA Chung J.H., Suh M.J., Park Y.I., Tainer J.A., Han Y.S.;
RT "Repair activities of 8-oxoguanine DNA glycosylase from Archaeoglobus
RT fulgidus, a hyperthermophilic archaeon.";
RL Mutat. Res. 486:99-111(2001).
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). Efficiently
CC cleaves oligomers containing 8-oxoG:C and 8-oxoG:G base pairs, and is
CC less effective on oligomers containing 8-oxoG:T and 8-oxoG:A mispairs.
CC {ECO:0000269|PubMed:11425515}.
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:11425515};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 8.5. {ECO:0000269|PubMed:11425515};
CC Temperature dependence:
CC Optimum temperature is 60 degrees Celsius.
CC {ECO:0000269|PubMed:11425515};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:11425515}.
CC -!- SIMILARITY: Belongs to the type-2 OGG1 family. {ECO:0000255|HAMAP-
CC Rule:MF_00241}.
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DR EMBL; AE000782; AAB90876.1; -; Genomic_DNA.
DR PIR; C69296; C69296.
DR RefSeq; WP_010877878.1; NC_000917.1.
DR AlphaFoldDB; O29876; -.
DR SMR; O29876; -.
DR STRING; 224325.AF_0371; -.
DR EnsemblBacteria; AAB90876; AAB90876; AF_0371.
DR GeneID; 24793910; -.
DR KEGG; afu:AF_0371; -.
DR eggNOG; arCOG04357; Archaea.
DR HOGENOM; CLU_104937_0_0_2; -.
DR OMA; FCILTAN; -.
DR OrthoDB; 95301at2157; -.
DR PhylomeDB; O29876; -.
DR BRENDA; 3.2.2.B5; 414.
DR BRENDA; 4.2.99.18; 414.
DR Proteomes; UP000002199; 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 DNA damage; DNA repair; Glycosidase; Hydrolase; Lyase;
KW Multifunctional enzyme; Reference proteome.
FT CHAIN 1..198
FT /note="8-oxoguanine DNA glycosylase/AP lyase"
FT /id="PRO_0000159563"
FT ACT_SITE 122
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00241"
FT ACT_SITE 140
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00241"
FT SITE 198
FT /note="Important for guanine/8-oxoguanine distinction"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00241"
SQ SEQUENCE 198 AA; 22639 MW; 3A5C033AA12F3FFB CRC64;
MIEKAISRRI KEFRQLGEKG EVEFDFRPFL DFSVKATIRT ELAFCISTAN SSATAGLKFQ
RLLGQGVGVK EALTLAGVRF HNRKAEYIRE AFKSFKLVEK ALEAESSKAR EILLKIKGLG
MKEASHFLRN VGREDVAIID RHILRWLERQ GYEVPGTMTA KKYLEVEKIL MEISEERGES
LAEMDLRIWA EMTGKVLK
