ID   MUTY_BUCAP              Reviewed;         347 AA.
AC   Q8K926;
DT   08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 127.
DE   RecName: Full=Adenine DNA glycosylase;
DE            EC=3.2.2.31 {ECO:0000250|UniProtKB:P17802};
GN   Name=mutY; OrderedLocusNames=BUsg_534;
OS   Buchnera aphidicola subsp. Schizaphis graminum (strain Sg).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=198804;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Sg;
RX   PubMed=12089438; DOI=10.1126/science.1071278;
RA   Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S.,
RA   Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.;
RT   "50 million years of genomic stasis in endosymbiotic bacteria.";
RL   Science 296:2376-2379(2002).
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; AE013218; AAM68075.1; -; Genomic_DNA.
DR   RefSeq; WP_011054041.1; NC_004061.1.
DR   AlphaFoldDB; Q8K926; -.
DR   SMR; Q8K926; -.
DR   STRING; 198804.BUsg_534; -.
DR   EnsemblBacteria; AAM68075; AAM68075; BUsg_534.
DR   KEGG; bas:BUsg_534; -.
DR   eggNOG; COG1194; Bacteria.
DR   HOGENOM; CLU_012862_0_2_6; -.
DR   OMA; RDPYRVW; -.
DR   OrthoDB; 1274533at2; -.
DR   Proteomes; UP000000416; 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.
FT   CHAIN           1..347
FT                   /note="Adenine DNA glycosylase"
FT                   /id="PRO_0000102232"
FT   ACT_SITE        37
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P83847"
FT   BINDING         192
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
FT   BINDING         199
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
FT   BINDING         202
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
FT   BINDING         208
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   347 AA;  41301 MW;  D6F6279175293587 CRC64;
     MTIYVFSQLI LNWYHINGRK NLPWKKDKTL YKVWISEIML QQTTVKTAIP YFKNFISRFP
     NIQSLNQSKL DDILCLWSGL GYYKRAENIY KTVKIIKEEF QEKFPTGFSD LIKLPGIGRS
     TAGAILSLSL DYFFPILEGN VKRILMRYYG IIGYVTEKKI EQKLWYLIEL ITPIHNTGSF
     NQGIMDIGAL ICTPKNPKCN LCPLIQKCIA YKEKNWIKYP LKKKKKIILE KKSWFVVIKY
     QNQFWIEKNT EKKIWKNLFC FPNFDTKIKT IEWLKKNKIN IDKKHKKIQS FYHKFSHFTL
     HIIPILVNLS FFKNFQNSKK TGIWYDLKNT HDIGLPKPVQ KILEIFK