AC   MF_01168;
DC   Protein; auto
TR   HAMAP; MF_01168; -; 1; level=0
XX
Names: AGOG
XX
ID   AGOG
DE   RecName: Full=N-glycosylase/DNA lyase;
DE   AltName: Full=8-oxoguanine DNA glycosylase;
DE            EC=3.2.2.-;
DE   AltName: Full=AGOG;
DE   AltName: Full=DNA-(apurinic or apyrimidinic site) lyase;
DE            Short=AP lyase;
DE            EC=4.2.99.18;
XX
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.
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'-phospho-2'-
CC         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;
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.
XX
DR   Pfam; PF09171; DUF1886; 1; trigger=no
DR   PIRSF; PIRSF008955; AGOG; 1; trigger=no
XX
KW   DNA damage
KW   DNA excision
KW   DNA repair
KW   Hydrolase
KW   Lyase
XX
GO   GO:0003906; F:DNA-(apurinic or apyrimidinic site) endonuclease activity
GO   GO:0000702; F:oxidized base lesion DNA N-glycosylase activity
GO   GO:0006284; P:base-excision repair
GO   GO:0006281; P:DNA repair
XX
FT   From: AGOG_PYRAE (Q8ZVK6)
FT   ACT_SITE        140
FT                   /note="Schiff-base intermediate with DNA"
FT   Condition: K
FT   ACT_SITE        172
FT   Condition: D
FT   BINDING         31
FT                   /ligand="8-oxoguanine"
FT                   /ligand_id="ChEBI:CHEBI:52617"
FT   Condition: Q
FT   BINDING         58
FT                   /ligand="8-oxoguanine"
FT                   /ligand_id="ChEBI:CHEBI:52617"
FT   Condition: S
FT   BINDING         69
FT                   /ligand="8-oxoguanine"
FT                   /ligand_id="ChEBI:CHEBI:52617"
FT   Condition: W
FT   BINDING         144
FT                   /ligand="8-oxoguanine"
FT                   /ligand_id="ChEBI:CHEBI:52617"
FT   Condition: F
FT   BINDING         170
FT                   /ligand="8-oxoguanine"
FT                   /ligand_id="ChEBI:CHEBI:52617"
FT   Condition: P
FT   BINDING         218
FT                   /ligand="8-oxoguanine"
FT                   /ligand_id="ChEBI:CHEBI:52617"
FT   Condition: D
FT   BINDING         222
FT                   /ligand="8-oxoguanine"
FT                   /ligand_id="ChEBI:CHEBI:52617"
FT   Condition: W
FT   REGION          125..184
FT                   /note="Helix-hairpin-helix"
XX
Size: 216-291;
Related: None;
Template: Q8ZVK6;
Scope:
 Archaea
Fusion:
 Nter: None
 Cter: None
Duplicate: None
Plasmid: None
Comments: None
XX
# Revision 1.18 2024/01/30
//