ID   MUTY_BUCBP              Reviewed;         351 AA.
AC   Q89A45;
DT   16-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 121.
DE   RecName: Full=Adenine DNA glycosylase;
DE            EC=3.2.2.31 {ECO:0000250|UniProtKB:P17802};
GN   Name=mutY; OrderedLocusNames=bbp_500;
OS   Buchnera aphidicola subsp. Baizongia pistaciae (strain Bp).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=224915;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bp;
RX   PubMed=12522265; DOI=10.1073/pnas.0235981100;
RA   van Ham R.C.H.J., Kamerbeek J., Palacios C., Rausell C., Abascal F.,
RA   Bastolla U., Fernandez J.M., Jimenez L., Postigo M., Silva F.J.,
RA   Tamames J., Viguera E., Latorre A., Valencia A., Moran F., Moya A.;
RT   "Reductive genome evolution in Buchnera aphidicola.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:581-586(2003).
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}.
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; AE016826; AAO27205.1; -; Genomic_DNA.
DR   RefSeq; WP_011091606.1; NC_004545.1.
DR   AlphaFoldDB; Q89A45; -.
DR   SMR; Q89A45; -.
DR   STRING; 224915.bbp_500; -.
DR   EnsemblBacteria; AAO27205; AAO27205; bbp_500.
DR   GeneID; 56471035; -.
DR   KEGG; bab:bbp_500; -.
DR   eggNOG; COG1194; Bacteria.
DR   HOGENOM; CLU_012862_0_2_6; -.
DR   OMA; RDPYRVW; -.
DR   OrthoDB; 1274533at2; -.
DR   Proteomes; UP000000601; Chromosome.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
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; cd03431; DNA_Glycosylase_C; 1.
DR   CDD; cd00056; ENDO3c; 1.
DR   Gene3D; 1.10.1670.10; -; 1.
DR   InterPro; IPR005760; A/G_AdeGlyc_MutY.
DR   InterPro; IPR011257; DNA_glycosylase.
DR   InterPro; IPR004036; Endonuclease-III-like_CS2.
DR   InterPro; IPR003651; Endonuclease3_FeS-loop_motif.
DR   InterPro; IPR004035; Endouclease-III_FeS-bd_BS.
DR   InterPro; IPR003265; HhH-GPD_domain.
DR   InterPro; IPR023170; HhH_base_excis_C.
DR   InterPro; IPR000445; HhH_motif.
DR   InterPro; IPR044298; MIG/MutY.
DR   InterPro; IPR029119; MutY_C.
DR   InterPro; IPR015797; NUDIX_hydrolase-like_dom_sf.
DR   PANTHER; PTHR42944; PTHR42944; 1.
DR   Pfam; PF00633; HHH; 1.
DR   Pfam; PF00730; HhH-GPD; 1.
DR   Pfam; PF14815; NUDIX_4; 1.
DR   SMART; SM00478; ENDO3c; 1.
DR   SMART; SM00525; FES; 1.
DR   SUPFAM; SSF48150; SSF48150; 1.
DR   SUPFAM; SSF55811; SSF55811; 1.
DR   TIGRFAMs; TIGR01084; mutY; 1.
DR   PROSITE; PS00764; ENDONUCLEASE_III_1; 1.
DR   PROSITE; PS01155; ENDONUCLEASE_III_2; 1.
PE   3: Inferred from homology;
KW   4Fe-4S; DNA damage; DNA repair; Glycosidase; Hydrolase; Iron; Iron-sulfur;
KW   Metal-binding; Reference proteome.
FT   CHAIN           1..351
FT                   /note="Adenine DNA glycosylase"
FT                   /id="PRO_0000102233"
FT   ACT_SITE        37
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P83847"
FT   BINDING         190
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
FT   BINDING         197
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
FT   BINDING         200
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
FT   BINDING         206
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
FT   SITE            138
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250|UniProtKB:P83847"
SQ   SEQUENCE   351 AA;  41563 MW;  2A7255140EED35DC CRC64;
     MTTLVFYQTI LNWYHHFGRK TLPWQIKKNP YKTWISEIML QQTQVKTVIP YYCKFIKRFP
     NIDTLSDSPL DSILNLWSGL GYYTRARNIY KTAKILKQKF NGIFPNSYAE IIKLPGIGKS
     TAGAILSFGF NLYSCILDGN IKRVLIRYYS ININNKYIEK LLWKTIESIT PIYHTNKFNQ
     ALIDIGALIC LKSNPKCNIC PLKSTCKSYL NNKLFQINCK KNKKHIIPKT KYWFLILQYK
     NYIFLEKRQN LGIWKKLFCF PQFIRQNDIL SWIQKNNTKI KKINILNEFK HKLSHLTLYI
     NPIWIIINKI SIFSNNNKTI WYNLNNPQCI GLPTPVTKII TKIKKFNTHH E