ID   MUTY_BUCAI              Reviewed;         350 AA.
AC   P57617;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2000, sequence version 1.
DT   03-AUG-2022, entry version 124.
DE   RecName: Full=Adenine DNA glycosylase;
DE            EC=3.2.2.31 {ECO:0000250|UniProtKB:P17802};
GN   Name=mutY; OrderedLocusNames=BU552;
OS   Buchnera aphidicola subsp. Acyrthosiphon pisum (strain APS) (Acyrthosiphon
OS   pisum symbiotic bacterium).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=107806;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=APS;
RX   PubMed=10993077; DOI=10.1038/35024074;
RA   Shigenobu S., Watanabe H., Hattori M., Sakaki Y., Ishikawa H.;
RT   "Genome sequence of the endocellular bacterial symbiont of aphids Buchnera
RT   sp. APS.";
RL   Nature 407:81-86(2000).
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; BA000003; BAB13244.1; -; Genomic_DNA.
DR   RefSeq; NP_240358.1; NC_002528.1.
DR   RefSeq; WP_010896160.1; NC_002528.1.
DR   AlphaFoldDB; P57617; -.
DR   SMR; P57617; -.
DR   STRING; 107806.10039210; -.
DR   EnsemblBacteria; BAB13244; BAB13244; BAB13244.
DR   KEGG; buc:BU552; -.
DR   PATRIC; fig|107806.10.peg.556; -.
DR   eggNOG; COG1194; Bacteria.
DR   HOGENOM; CLU_012862_0_2_6; -.
DR   OMA; RDPYRVW; -.
DR   Proteomes; UP000001806; 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; 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   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..350
FT                   /note="Adenine DNA glycosylase"
FT                   /id="PRO_0000102231"
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   350 AA;  41589 MW;  F4567EFEF9B92BD1 CRC64;
     MTKYIFSQLV LNWYHKNGRK DLPWQINKTL YTVWISEIML QQTTVKSAIP YFKKFILNFP
     NIKSLNDSKL DDVLYLWSGL GYYNRAKNIY KSAQIIKKKY KGIFPDQFSN IIQLPGIGRS
     TAGAILSLSL NFFYPILDGN VKRILVRYYG ISGLLKDKKI EKKLWNIIES ITPIHNTGKF
     NQGMMDIGAS ICISIKPKCT ICPLKKECIA QIEKKWEKYP LKNIKKTLPQ KISWFIIIKH
     ENNFWLKKNT EQEIWKELFC FPKFKNKEEA LIWLKEKKIN INTCENMISF FHKFSHFILH
     INPILIRLPY ISEFFKENHK KIWYNLKNPQ HIGLPRPVQK ILENFKKNIF