AGOG_THEKO
ID AGOG_THEKO Reviewed; 263 AA.
AC Q5JI79;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=N-glycosylase/DNA lyase {ECO:0000255|HAMAP-Rule:MF_01168};
DE AltName: Full=8-oxoguanine DNA glycosylase {ECO:0000255|HAMAP-Rule:MF_01168};
DE EC=3.2.2.- {ECO:0000255|HAMAP-Rule:MF_01168};
DE AltName: Full=AGOG {ECO:0000255|HAMAP-Rule:MF_01168};
DE AltName: Full=DNA-(apurinic or apyrimidinic site) lyase {ECO:0000255|HAMAP-Rule:MF_01168};
DE Short=AP lyase {ECO:0000255|HAMAP-Rule:MF_01168};
DE EC=4.2.99.18 {ECO:0000255|HAMAP-Rule:MF_01168};
GN OrderedLocusNames=TK0940;
OS Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)
OS (Pyrococcus kodakaraensis (strain KOD1)).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Thermococcus.
OX NCBI_TaxID=69014;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-918 / JCM 12380 / KOD1;
RX PubMed=15710748; DOI=10.1101/gr.3003105;
RA Fukui T., Atomi H., Kanai T., Matsumi R., Fujiwara S., Imanaka T.;
RT "Complete genome sequence of the hyperthermophilic archaeon Thermococcus
RT kodakaraensis KOD1 and comparison with Pyrococcus genomes.";
RL Genome Res. 15:352-363(2005).
CC -!- FUNCTION: DNA repair enzyme that is part of the base excision repair
CC (BER) pathway; protects from oxidative damage by removing the major
CC product of DNA oxidation, 8-oxoguanine (GO), from single- and double-
CC stranded DNA substrates. {ECO:0000255|HAMAP-Rule:MF_01168}.
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_01168};
CC -!- DOMAIN: Contains two alpha-helical subdomains, with the 8-oxoguanine
CC binding site located in a cleft at their interface. Contains a helix-
CC hairpin-helix (HhH) structural motif and a Gly/Pro-rich sequence
CC followed by a conserved Asp (HhH-GPD motif).
CC -!- SIMILARITY: Belongs to the archaeal N-glycosylase/DNA lyase (AGOG)
CC family. {ECO:0000255|HAMAP-Rule:MF_01168}.
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DR EMBL; AP006878; BAD85129.1; -; Genomic_DNA.
DR RefSeq; WP_011249891.1; NC_006624.1.
DR AlphaFoldDB; Q5JI79; -.
DR SMR; Q5JI79; -.
DR STRING; 69014.TK0940; -.
DR EnsemblBacteria; BAD85129; BAD85129; TK0940.
DR GeneID; 3234448; -.
DR KEGG; tko:TK0940; -.
DR PATRIC; fig|69014.16.peg.918; -.
DR eggNOG; arCOG04144; Archaea.
DR HOGENOM; CLU_085935_0_0_2; -.
DR InParanoid; Q5JI79; -.
DR OMA; VKMFGYA; -.
DR OrthoDB; 108705at2157; -.
DR PhylomeDB; Q5JI79; -.
DR Proteomes; UP000000536; Chromosome.
DR GO; GO:0140078; F:class I DNA-(apurinic or apyrimidinic site) endonuclease activity; IEA:UniProtKB-EC.
DR GO; GO:0000702; F:oxidized base lesion DNA N-glycosylase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006284; P:base-excision repair; IEA:UniProtKB-UniRule.
DR HAMAP; MF_01168; AGOG; 1.
DR InterPro; IPR016544; AGOG.
DR InterPro; IPR015254; AGOG-like.
DR InterPro; IPR011257; DNA_glycosylase.
DR Pfam; PF09171; AGOG; 1.
DR PIRSF; PIRSF008955; AGOG; 1.
DR SUPFAM; SSF48150; SSF48150; 1.
PE 3: Inferred from homology;
KW DNA damage; DNA excision; DNA repair; Hydrolase; Lyase; Reference proteome.
FT CHAIN 1..263
FT /note="N-glycosylase/DNA lyase"
FT /id="PRO_0000185116"
FT REGION 139..204
FT /note="Helix-hairpin-helix"
FT ACT_SITE 164
FT /note="Schiff-base intermediate with DNA"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01168"
FT ACT_SITE 196
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01168"
FT BINDING 43
FT /ligand="8-oxoguanine"
FT /ligand_id="ChEBI:CHEBI:52617"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01168"
FT BINDING 71
FT /ligand="8-oxoguanine"
FT /ligand_id="ChEBI:CHEBI:52617"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01168"
FT BINDING 82
FT /ligand="8-oxoguanine"
FT /ligand_id="ChEBI:CHEBI:52617"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01168"
FT BINDING 168
FT /ligand="8-oxoguanine"
FT /ligand_id="ChEBI:CHEBI:52617"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01168"
FT BINDING 194
FT /ligand="8-oxoguanine"
FT /ligand_id="ChEBI:CHEBI:52617"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01168"
FT BINDING 230
FT /ligand="8-oxoguanine"
FT /ligand_id="ChEBI:CHEBI:52617"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01168"
FT BINDING 234
FT /ligand="8-oxoguanine"
FT /ligand_id="ChEBI:CHEBI:52617"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01168"
SQ SEQUENCE 263 AA; 30553 MW; DBBD7B55740CDBDB CRC64;
MSLERFVKIK YQTNEEKADK LVEGLKELGI ECARIIEEKV DLQFDALRHL RENLNDDETF
IKLVIANSIV SYQLSGKGED WWWEFSKYFS QNPPEKSIVE ACSKFLPSSR TNRRLVAGKI
KRLEKLEPFL NSLTLQELRR YYFENMMGLR NDIAEALGSP KTAKTVVFAV KMFGYAGRIA
FGEFVPYPME IDIPEDVRIK AYTERITNEP PVSFWRRVAE ETGIPPLHID SILWPVLGGK
REVMERLKKV CEKWELVLEL GSL
