MUTY_MYCS2
ID MUTY_MYCS2 Reviewed; 293 AA.
AC A0R567; I7GFE6;
DT 06-MAR-2013, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Adenine DNA glycosylase;
DE EC=3.2.2.31 {ECO:0000269|PubMed:17698424};
GN Name=mutY; OrderedLocusNames=MSMEG_6083, MSMEI_5923;
OS Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium
OS smegmatis).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=246196;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RA Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA Fraser C.M.;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=17295914; DOI=10.1186/gb-2007-8-2-r20;
RA Deshayes C., Perrodou E., Gallien S., Euphrasie D., Schaeffer C.,
RA Van-Dorsselaer A., Poch O., Lecompte O., Reyrat J.-M.;
RT "Interrupted coding sequences in Mycobacterium smegmatis: authentic
RT mutations or sequencing errors?";
RL Genome Biol. 8:R20.1-R20.9(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=18955433; DOI=10.1101/gr.081901.108;
RA Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.-M.,
RA Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O.;
RT "Ortho-proteogenomics: multiple proteomes investigation through orthology
RT and a new MS-based protocol.";
RL Genome Res. 19:128-135(2009).
RN [4]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=ATCC 700084 / mc(2)155;
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 [5]
RP DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 700084 / mc(2)155;
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 [6]
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.
CC {ECO:0000269|PubMed:17698424}.
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 -!- 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 -!- DISRUPTION PHENOTYPE: Loss of adenine glycosylase activity. No overall
CC significant change in the mutation rate; an increase in C to A and A to
CC C mutations (with a reduction in other mutations) is seen after
CC rifampicin treatment. No change in susceptibility to H(2)O(2).
CC {ECO:0000269|PubMed:19778963}.
CC -!- SIMILARITY: Belongs to the Nth/MutY family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AFP42356.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; CP000480; ABK72600.1; -; Genomic_DNA.
DR EMBL; CP001663; AFP42356.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_011731026.1; NZ_SIJM01000046.1.
DR RefSeq; YP_890305.1; NC_008596.1.
DR AlphaFoldDB; A0R567; -.
DR SMR; A0R567; -.
DR STRING; 246196.MSMEI_5923; -.
DR EnsemblBacteria; ABK72600; ABK72600; MSMEG_6083.
DR EnsemblBacteria; AFP42356; AFP42356; MSMEI_5923.
DR GeneID; 66737367; -.
DR KEGG; msg:MSMEI_5923; -.
DR KEGG; msm:MSMEG_6083; -.
DR PATRIC; fig|246196.19.peg.5921; -.
DR eggNOG; COG1194; Bacteria.
DR OMA; WNNAIME; -.
DR OrthoDB; 1274533at2; -.
DR Proteomes; UP000000757; Chromosome.
DR Proteomes; UP000006158; 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; PF10576; EndIII_4Fe-2S; 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..293
FT /note="Adenine DNA glycosylase"
FT /id="PRO_0000421386"
FT DOMAIN 98..126
FT /note="HhH"
FT ACT_SITE 35
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:P83847"
FT BINDING 188
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 195
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 198
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 203
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT SITE 136
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P83847"
SQ SEQUENCE 293 AA; 31880 MW; E2892FE9619798B9 CRC64;
MSISPVELLS WYDHARRDLP WRRPGVSAWQ ILVSEFMLQQ TPVSRVEPIW SAWIERWPTA
SATAAAGPAE VLRAWGKLGY PRRAKRLHEC AVVIASEYDD VVPRDVDTLL TLPGIGAYTA
RAVACFAYQA SVPVVDTNVR RVVTRAVHGA ADAPASTRDL DMVAALLPPD TTAPTFSAAL
MELGATVCTA RSPRCGICPL SHCRWRSAGF PAGTVARRVQ RYAGTDRQVR GKLLDVLRDS
TTPVTRAQLD VVWLSDPAQR DRALDSLLVD GLVEQTADGR FALAGEGETG RPA
