ID   MUTY_AERHY              Reviewed;          99 AA.
AC   P46230;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   25-MAY-2022, entry version 80.
DE   RecName: Full=Adenine DNA glycosylase;
DE            EC=3.2.2.31 {ECO:0000250|UniProtKB:P17802};
DE   Flags: Fragment;
GN   Name=mutY;
OS   Aeromonas hydrophila.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Aeromonadales;
OC   Aeromonadaceae; Aeromonas.
OX   NCBI_TaxID=644;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Ah65;
RX   PubMed=7961440; DOI=10.1128/jb.176.22.6819-6826.1994;
RA   Jahagirdar R., Howard S.P.;
RT   "Isolation and characterization of a second exe operon required for
RT   extracellular protein secretion in Aeromonas hydrophila.";
RL   J. Bacteriol. 176:6819-6826(1994).
CC   -!- FUNCTION: Adenine glycosylase active on G-A mispairs. MutY also
CC       corrects error-prone DNA synthesis past GO lesions which are due to the
CC       oxidatively damaged form of guanine: 7,8-dihydro-8-oxoguanine (8-oxo-
CC       dGTP). {ECO:0000250|UniProtKB:P17802}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolyzes free adenine bases from 7,8-dihydro-8-
CC         oxoguanine:adenine mismatched double-stranded DNA, leaving an
CC         apurinic site.; EC=3.2.2.31; Evidence={ECO:0000250|UniProtKB:P17802};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000250|UniProtKB:P17802};
CC       Note=Binds 1 [4Fe-4S] cluster. The cluster does not appear to play a
CC       role in catalysis, but is probably involved in the proper positioning
CC       of the enzyme along the DNA strand. {ECO:0000250|UniProtKB:P17802};
CC   -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P17802}.
CC   -!- SIMILARITY: Belongs to the Nth/MutY family. {ECO:0000305}.
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DR   EMBL; X81473; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; P46230; -.
DR   SMR; P46230; -.
DR   STRING; 1448139.AI20_00270; -.
DR   eggNOG; COG1194; Bacteria.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0000701; F:purine-specific mismatch base pair DNA N-glycosylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006284; P:base-excision repair; IEA:InterPro.
DR   CDD; cd00056; ENDO3c; 1.
DR   InterPro; IPR011257; DNA_glycosylase.
DR   InterPro; IPR003265; HhH-GPD_domain.
DR   InterPro; IPR044298; MIG/MutY.
DR   PANTHER; PTHR42944; PTHR42944; 1.
DR   Pfam; PF00730; HhH-GPD; 1.
DR   SUPFAM; SSF48150; SSF48150; 1.
PE   3: Inferred from homology;
KW   4Fe-4S; DNA damage; DNA repair; Glycosidase; Hydrolase; Iron; Iron-sulfur;
KW   Metal-binding.
FT   CHAIN           1..>99
FT                   /note="Adenine DNA glycosylase"
FT                   /id="PRO_0000102230"
FT   ACT_SITE        40
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P83847"
FT   NON_TER         99
SQ   SEQUENCE   99 AA;  11692 MW;  0806BDC67E1B0CB6 CRC64;
     MSNSDNTTFA TRILDWYQIH GRKTLPWQQD KTPYRVWVSE IMLQQTQVAT VIPYYQRFMA
     RFPDVQALAQ APIDEVLHHW TGLGYYARAR NLHKAAQQI