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 27-MAR-2024, entry version 117. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 PaxDb; 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 OrthoDB; 35941at2157; -. 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; 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 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 //