MUTY_SALTY
ID MUTY_SALTY Reviewed; 350 AA.
AC Q05869;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Adenine DNA glycosylase;
DE EC=3.2.2.31 {ECO:0000250|UniProtKB:P17802};
GN Name=mutY; Synonyms=mutB; OrderedLocusNames=STM3110;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=GW1803;
RX PubMed=8419300; DOI=10.1128/jb.175.2.541-543.1993;
RA Desiraju V., Shanabruch W.G., Lu A.L.;
RT "Nucleotide sequence of the Salmonella typhimurium mutB gene, the homolog
RT of Escherichia coli mutY.";
RL J. Bacteriol. 175:541-543(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
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; M86634; AAA27165.1; -; Genomic_DNA.
DR EMBL; AE006468; AAL21985.1; -; Genomic_DNA.
DR PIR; A40647; A40647.
DR RefSeq; NP_462026.1; NC_003197.2.
DR RefSeq; WP_001148956.1; NC_003197.2.
DR AlphaFoldDB; Q05869; -.
DR SMR; Q05869; -.
DR STRING; 99287.STM3110; -.
DR PaxDb; Q05869; -.
DR EnsemblBacteria; AAL21985; AAL21985; STM3110.
DR GeneID; 1254633; -.
DR KEGG; stm:STM3110; -.
DR PATRIC; fig|99287.12.peg.3296; -.
DR HOGENOM; CLU_012862_0_2_6; -.
DR OMA; RDPYRVW; -.
DR PhylomeDB; Q05869; -.
DR BioCyc; SENT99287:STM3110-MON; -.
DR Proteomes; UP000001014; 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; IPR004036; Endonuclease-III-like_CS2.
DR InterPro; IPR003651; Endonuclease3_FeS-loop_motif.
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 SMART; SM00525; FES; 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_0000102235"
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; 39409 MW; 5C55DB4D7B7BB69F CRC64;
MQASQFSAQV LDWYDKYGRK TLPWQINKTP YKVWLSEVML QQTQVTTVIP YFERFMARFP
TVTDLANAPL DEVLHLWTGL GYYARARNLH KAAQQVATLH GGEFPQTFAE IAALPGVGRS
TAGAILSLAL GKHYPILDGN VKRVLARCYA VSGWPGKKEV ENTLWTLSEQ VTPARGVERF
NQAMMDLGAM VCTRSKPKCT LCPLQNGCIA AAHESWSRYP GKKPKQTLPE RTGYFLLLQH
NQEIFLAQRP PSGLWGGLYC FPQFAREDEL REWLAQRHVN ADNLTQLNAF RHTFSHFHLD
IVPMWLPVSS LDACMDEGSA LWYNLAQPPS VGLAAPVERL LQQLRTGAPV
