ID   MUTY_MYCTO              Reviewed;         304 AA.
AC   P9WQ08; F2GKC9; O53574; Q7D581;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 41.
DE   RecName: Full=Adenine DNA glycosylase;
DE            EC=3.2.2.31 {ECO:0000250|UniProtKB:A0R567};
GN   Name=mutY; OrderedLocusNames=MT3695;
OS   Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 1551 / Oshkosh;
RX   PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA   Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA   Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA   Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA   Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA   Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT   "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT   laboratory strains.";
RL   J. Bacteriol. 184:5479-5490(2002).
CC   -!- FUNCTION: Adenine glycosylase active on G:A and C:A mispairs, as well
CC       as processing 7,8-dihydro-8-oxoguanine:A (8-oxoG) mismatches.
CC       {ECO:0000250|UniProtKB:A0R567}.
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:A0R567};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000305};
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:0000305};
CC   -!- SIMILARITY: Belongs to the Nth/MutY family. {ECO:0000305}.
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DR   EMBL; AE000516; AAK48053.1; -; Genomic_DNA.
DR   PIR; F70804; F70804.
DR   RefSeq; WP_003419495.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WQ08; -.
DR   SMR; P9WQ08; -.
DR   EnsemblBacteria; AAK48053; AAK48053; MT3695.
DR   KEGG; mtc:MT3695; -.
DR   PATRIC; fig|83331.31.peg.3978; -.
DR   HOGENOM; CLU_012862_2_0_11; -.
DR   Proteomes; UP000001020; 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; cd00056; ENDO3c; 1.
DR   Gene3D; 1.10.1670.10; -; 1.
DR   InterPro; IPR011257; DNA_glycosylase.
DR   InterPro; IPR003651; Endonuclease3_FeS-loop_motif.
DR   InterPro; IPR003265; HhH-GPD_domain.
DR   InterPro; IPR023170; HhH_base_excis_C.
DR   InterPro; IPR000445; HhH_motif.
DR   InterPro; IPR044298; MIG/MutY.
DR   PANTHER; PTHR42944; PTHR42944; 1.
DR   Pfam; PF00633; HHH; 1.
DR   Pfam; PF00730; HhH-GPD; 1.
DR   SMART; SM00478; ENDO3c; 1.
DR   SMART; SM00525; FES; 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..304
FT                   /note="Adenine DNA glycosylase"
FT                   /id="PRO_0000426858"
FT   DOMAIN          111..139
FT                   /note="HhH"
FT   ACT_SITE        48
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P83847"
FT   BINDING         203
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
FT   BINDING         210
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
FT   BINDING         213
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
FT   BINDING         218
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
FT   SITE            149
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250|UniProtKB:P83847"
SQ   SEQUENCE   304 AA;  33684 MW;  89B86C2F4AA7131E CRC64;
     MPHILPEPSV TGPRHISDTN LLAWYQRSHR DLPWREPGVS PWQILVSEFM LQQTPAARVL
     AIWPDWVRRW PTPSATATAS TADVLRAWGK LGYPRRAKRL HECATVIARD HNDVVPDDIE
     ILVTLPGVGS YTARAVACFA YRQRVPVVDT NVRRVVARAV HGRADAGAPS VPRDHADVLA
     LLPHRETAPE FSVALMELGA TVCTARTPRC GLCPLDWCAW RHAGYPPSDG PPRRGQAYTG
     TDRQVRGRLL DVLRAAEFPV TRAELDVAWL TDTAQRDRAL ESLLADALVT RTVDGRFALP
     GEGF