ID   MUTY_MYCTU              Reviewed;         304 AA.
AC   P9WQ09; 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 40.
DE   RecName: Full=Adenine DNA glycosylase;
DE            EC=3.2.2.31 {ECO:0000269|PubMed:17698424, ECO:0000269|PubMed:19778963};
GN   Name=mutY; OrderedLocusNames=Rv3589;
OS   Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83332;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=9634230; DOI=10.1038/31159;
RA   Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA   Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA   Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA   Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA   Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA   Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA   Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA   Barrell B.G.;
RT   "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT   genome sequence.";
RL   Nature 393:537-544(1998).
RN   [2]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=17698424; DOI=10.1016/j.dnarep.2007.06.009;
RA   Jain R., Kumar P., Varshney U.;
RT   "A distinct role of formamidopyrimidine DNA glycosylase (MutM) in down-
RT   regulation of accumulation of G, C mutations and protection against
RT   oxidative stress in mycobacteria.";
RL   DNA Repair 6:1774-1785(2007).
RN   [3]
RP   FUNCTION, DNA-BINDING, AND CATALYTIC ACTIVITY.
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=19778963; DOI=10.1099/mic.0.033621-0;
RA   Kurthkoti K., Srinath T., Kumar P., Malshetty V.S., Sang P.B., Jain R.,
RA   Manjunath R., Varshney U.;
RT   "A distinct physiological role of MutY in mutation prevention in
RT   mycobacteria.";
RL   Microbiology 156:88-93(2010).
RN   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA   Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA   Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA   Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA   Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT   "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT   mass spectrometry.";
RL   Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
RN   [5]
RP   REVIEW.
RX   PubMed=21764637; DOI=10.1016/j.tube.2011.06.005;
RA   Kurthkoti K., Varshney U.;
RT   "Base excision and nucleotide excision repair pathways in mycobacteria.";
RL   Tuberculosis 91:533-543(2011).
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. Minor
CC       activity against 8-oxoG:G and 8-oxo:T mismatches is also seen. Bind
CC       dsDNA oligonucleotides containing the above mismatches.
CC       {ECO:0000269|PubMed:17698424, ECO:0000269|PubMed:19778963}.
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:0000269|PubMed:17698424,
CC         ECO:0000269|PubMed:19778963};
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; AL123456; CCP46412.1; -; Genomic_DNA.
DR   PIR; F70804; F70804.
DR   RefSeq; NP_218106.1; NC_000962.3.
DR   RefSeq; WP_003419495.1; NZ_NVQJ01000014.1.
DR   AlphaFoldDB; P9WQ09; -.
DR   SMR; P9WQ09; -.
DR   STRING; 83332.Rv3589; -.
DR   PaxDb; P9WQ09; -.
DR   PRIDE; P9WQ09; -.
DR   DNASU; 886639; -.
DR   GeneID; 886639; -.
DR   KEGG; mtu:Rv3589; -.
DR   PATRIC; fig|83332.111.peg.3999; -.
DR   TubercuList; Rv3589; -.
DR   eggNOG; COG1194; Bacteria.
DR   OMA; WNNAIME; -.
DR   PhylomeDB; P9WQ09; -.
DR   Proteomes; UP000001584; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0034039; F:8-oxo-7,8-dihydroguanine DNA N-glycosylase activity; IBA:GO_Central.
DR   GO; GO:0035485; F:adenine/guanine mispair binding; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0032357; F:oxidized purine DNA binding; IBA:GO_Central.
DR   GO; GO:0000701; F:purine-specific mismatch base pair DNA N-glycosylase activity; IBA:GO_Central.
DR   GO; GO:0006284; P:base-excision repair; IBA:GO_Central.
DR   GO; GO:0006298; P:mismatch repair; IBA:GO_Central.
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   1: Evidence at protein level;
KW   4Fe-4S; DNA damage; DNA repair; Glycosidase; Hydrolase; Iron; Iron-sulfur;
KW   Metal-binding; Reference proteome.
FT   CHAIN           1..304
FT                   /note="Adenine DNA glycosylase"
FT                   /id="PRO_0000421385"
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