AC   MF_00103;
DC   Protein; auto
TR   HAMAP; MF_00103; -; 1; level=0
XX
Names: Fapy_DNA_glycosyl
XX
ID   FPG
DE   RecName: Full=Formamidopyrimidine-DNA glycosylase;
DE            Short=Fapy-DNA glycosylase;
DE            EC=3.2.2.23;
DE   AltName: Full=DNA-(apurinic or apyrimidinic site) lyase MutM;
DE            Short=AP lyase MutM;
DE            EC=4.2.99.18;
GN   Name=mutM; Synonyms=fpg;
XX
CC   -!- FUNCTION: Involved in base excision repair of DNA damaged by oxidation
CC       or by mutagenic agents. Acts as DNA glycosylase that recognizes and
CC       removes damaged bases. Has a preference for oxidized purines, such as
CC       7,8-dihydro-8-oxoguanine (8-oxoG). Has AP (apurinic/apyrimidinic) lyase
CC       activity and introduces nicks in the DNA strand. Cleaves the DNA
CC       backbone by beta-delta elimination to generate a single-strand break at
CC       the site of the removed base with both 3'- and 5'-phosphates.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of DNA containing ring-opened 7-methylguanine
CC         residues, releasing 2,6-diamino-4-hydroxy-5-(N-
CC         methyl)formamidopyrimidine.; EC=3.2.2.23;
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   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC       Note=Binds 1 zinc ion per subunit.;
CC   -!- SUBUNIT: Monomer.
CC   -!- SIMILARITY: Belongs to the FPG family.
XX
DR   Pfam; PF01149; Fapy_DNA_glyco; 1; trigger=no
DR   Pfam; PF06827; zf-FPG_IleRS; 1; trigger=no
DR   NCBIfam; TIGR00577; Fpg; 1; trigger=no
DR   PROSITE; PS51068; FPG_CAT; 1; trigger=no
DR   PROSITE; PS01242; ZF_FPG_1; 1; trigger=no
DR   PROSITE; PS51066; ZF_FPG_2; 1; trigger=yes
XX
KW   DNA damage
KW   DNA repair
KW   DNA-binding
KW   Hydrolase
KW   Glycosidase
KW   Lyase
KW   Multifunctional enzyme
case <Feature:PS51066>
KW   Metal-binding
KW   Zinc
KW   Zinc-finger
end case
XX
GO   GO:0003906; F:DNA-(apurinic or apyrimidinic site) endonuclease activity
GO   GO:0008534; F:oxidized purine nucleobase lesion DNA N-glycosylase activity
case <Feature:PS51066>
GO   GO:0008270; F:zinc ion binding
end case
GO   GO:0006281; P:DNA repair
XX
FT   From: FPG_ECOLI (P05523)
FT   ACT_SITE        2
FT                   /note="Schiff-base intermediate with DNA"
FT   Condition: P
FT   ACT_SITE        3
FT                   /note="Proton donor"
FT   Condition: E
FT   ACT_SITE        57
FT                   /note="Proton donor; for beta-elimination activity"
FT   Condition: K
FT   ACT_SITE        259
FT                   /note="Proton donor; for delta-elimination activity"
FT   Condition: R
FT   BINDING         90
FT                   /ligand="DNA"
FT                   /ligand_id="ChEBI:CHEBI:16991"
FT   Condition: H
FT   BINDING         109
FT                   /ligand="DNA"
FT                   /ligand_id="ChEBI:CHEBI:16991"
FT   Condition: R
FT   BINDING         150
FT                   /ligand="DNA"
FT                   /ligand_id="ChEBI:CHEBI:16991"
FT   Condition: [KR]
XX
Size: 262-309;
Related: None;
Template: P05523; P42371; O50606;
Scope:
 Bacteria
Fusion:
 Nter: None
 Cter: None
Duplicate: None
Plasmid: None
Comments: Weird insert in DESVH (not taken into account in size range)
XX
# Revision 1.49 2024/01/30
//