MUTY_BACSU
ID MUTY_BACSU Reviewed; 369 AA.
AC O31584; Q79EV3;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Adenine DNA glycosylase;
DE EC=3.2.2.31 {ECO:0000250|UniProtKB:P83847};
GN Name=mutY {ECO:0000312|EMBL:CAB12691.1}; Synonyms=yfhQ;
GN OrderedLocusNames=BSU08630;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8946165; DOI=10.1093/dnares/3.4.257;
RA Yamamoto H., Uchiyama S., Sekiguchi J.;
RT "Cloning and sequencing of a 27.8-kb nucleotide sequence of the 79 degrees-
RT 81 degrees region of the Bacillus subtilis genome containing the sspE
RT locus.";
RL DNA Res. 3:257-262(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [3]
RP OPERON STRUCTURE, AND INDUCTION.
RC STRAIN=168;
RX PubMed=10463184; DOI=10.1099/13500872-145-8-2171;
RA Yamamoto H., Mori M., Sekiguchi J.;
RT "Transcription of genes near the sspE locus of the Bacillus subtilis
RT genome.";
RL Microbiology 145:2171-2180(1999).
RN [4]
RP DISRUPTION PHENOTYPE.
RC STRAIN=168;
RX PubMed=12483591; DOI=10.2323/jgam.46.183;
RA Sasaki M., Yonemura Y., Kurusu Y.;
RT "Genetic analysis of Bacillus subtilis mutator genes.";
RL J. Gen. Appl. Microbiol. 46:183-187(2000).
RN [5]
RP DISRUPTION PHENOTYPE IN STATIONARY PHASE CELLS.
RC STRAIN=168 / YB955;
RX PubMed=19011023; DOI=10.1128/jb.01210-08;
RA Vidales L.E., Cardenas L.C., Robleto E., Yasbin R.E., Pedraza-Reyes M.;
RT "Defects in the error prevention oxidized guanine system potentiate
RT stationary-phase mutagenesis in Bacillus subtilis.";
RL J. Bacteriol. 191:506-513(2009).
CC -!- FUNCTION: Base excision repair (BER) glycosylase that initiates repair
CC of A:oxoG to C:G by removing the inappropriately paired adenine base
CC from the DNA backbone, generating an abasic site product. 8-oxoguanine
CC (oxoG) is a genotoxic DNA lesion resulting from oxidation of guanine;
CC this residue is misread by replicative DNA polymerases, that insert
CC adenine instead of cytosine opposite the oxidized damaged base. Shows a
CC powerful dicrimination of A versus C, since it does not cleave cytosine
CC in oxoG:C pairs. May also be able to remove adenine from A:G mispairs,
CC although this activity may not be physiologically relevant.
CC {ECO:0000250|UniProtKB:P83847}.
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:P83847};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000250|UniProtKB:P83847};
CC Note=Binds 1 [4Fe-4S] cluster. The cluster has a structural role.
CC {ECO:0000250|UniProtKB:P83847};
CC -!- INDUCTION: Expressed during exponential growth. Expressed as both a
CC monocistronic transcript and a mutY-fabL-sspE transcript.
CC {ECO:0000269|PubMed:10463184}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene have a 100-fold increased
CC spontaneous mutation frequency. A double mutM/mutY disruption has a
CC 1000-fold increased spontaneous mutation frequency (PubMed:12483591).
CC Triple ytkD/mutM/mutY disrupted strains show increased mutation rates
CC during exponential and stationary phase (PubMed:19011023).
CC {ECO:0000269|PubMed:12483591, ECO:0000269|PubMed:19011023}.
CC -!- SIMILARITY: Belongs to the Nth/MutY family. {ECO:0000305}.
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DR EMBL; D85082; BAA24483.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB12691.1; -; Genomic_DNA.
DR PIR; A69802; A69802.
DR RefSeq; NP_388743.1; NC_000964.3.
DR RefSeq; WP_003243838.1; NZ_JNCM01000032.1.
DR AlphaFoldDB; O31584; -.
DR SMR; O31584; -.
DR STRING; 224308.BSU08630; -.
DR PaxDb; O31584; -.
DR PRIDE; O31584; -.
DR EnsemblBacteria; CAB12691; CAB12691; BSU_08630.
DR GeneID; 939222; -.
DR KEGG; bsu:BSU08630; -.
DR PATRIC; fig|224308.179.peg.931; -.
DR eggNOG; COG1194; Bacteria.
DR InParanoid; O31584; -.
DR OMA; RDPYRVW; -.
DR PhylomeDB; O31584; -.
DR BioCyc; BSUB:BSU08630-MON; -.
DR Proteomes; UP000001570; Chromosome.
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; 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; IPR003651; Endonuclease3_FeS-loop_motif.
DR InterPro; IPR003265; HhH-GPD_domain.
DR InterPro; IPR023170; HhH_base_excis_C.
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; 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.
PE 2: Evidence at transcript level;
KW 4Fe-4S; DNA damage; DNA repair; DNA-binding; Glycosidase; Hydrolase; Iron;
KW Iron-sulfur; Metal-binding; Reference proteome.
FT CHAIN 1..369
FT /note="Adenine DNA glycosylase"
FT /id="PRO_0000379974"
FT DOMAIN 108..137
FT /note="HhH"
FT /evidence="ECO:0000255"
FT ACT_SITE 46
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:P83847"
FT BINDING 33..34
FT /ligand="DNA"
FT /ligand_id="ChEBI:CHEBI:16991"
FT /ligand_note="substrate"
FT /ligand_part="adenine group"
FT /ligand_part_id="ChEBI:CHEBI:30756"
FT /ligand_part_note="mispaired A"
FT /evidence="ECO:0000250|UniProtKB:P83847"
FT BINDING 51..52
FT /ligand="DNA"
FT /ligand_id="ChEBI:CHEBI:16991"
FT /ligand_note="substrate"
FT /ligand_part="8-oxoguanine group"
FT /ligand_part_id="ChEBI:CHEBI:176966"
FT /evidence="ECO:0000250|UniProtKB:P83847"
FT BINDING 89..91
FT /ligand="DNA"
FT /ligand_id="ChEBI:CHEBI:16991"
FT /ligand_note="substrate"
FT /ligand_part="8-oxoguanine group"
FT /ligand_part_id="ChEBI:CHEBI:176966"
FT /evidence="ECO:0000250|UniProtKB:P83847"
FT BINDING 129
FT /ligand="DNA"
FT /ligand_id="ChEBI:CHEBI:16991"
FT /ligand_note="substrate"
FT /ligand_part="adenine group"
FT /ligand_part_id="ChEBI:CHEBI:30756"
FT /ligand_part_note="mispaired A"
FT /evidence="ECO:0000250|UniProtKB:P83847"
FT BINDING 201
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P83847"
FT BINDING 208
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P83847"
FT BINDING 211
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P83847"
FT BINDING 217
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P83847"
FT BINDING 313
FT /ligand="DNA"
FT /ligand_id="ChEBI:CHEBI:16991"
FT /ligand_note="substrate"
FT /ligand_part="8-oxoguanine group"
FT /ligand_part_id="ChEBI:CHEBI:176966"
FT /evidence="ECO:0000250|UniProtKB:P83847"
FT SITE 147
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P83847"
SQ SEQUENCE 369 AA; 41963 MW; FEF1FF70018579B1 CRC64;
MNVLEDKLKQ KDIQQFRDDL ISWFEREQRV LPWREDQDPY KVWVSEVMLQ QTRVETVIPY
FLRFVEQFPT VEALADADEE KVLKAWEGLG YYSRVRNLQS AVKEVKQEYG GIVPPDEKDF
GGLKGVGPYT KGAVLSIAYN KPIPAVDGNV MRVMSRILSI WDDIAKPKTR TIFEDAIRAF
ISKEKPSEFN QGLMELGALI CTPKSPSCLL CPVQQHCSAF EEGTERELPV KSKKKKPGIK
TMAAIVLTDE DGQVYIHKRP SKGLLANLWE FPNLETQKGI KTEREQLIAF LENEYGIQAD
ISDLQGVVEH VFTHLVWNIS VFFGKVKQVS DTSKLKKVTK EELEQFAFPV SHQKIWKMAG
EAAAISAAP
