MUTY_ECOLI
ID MUTY_ECOLI Reviewed; 350 AA.
AC P17802; Q2M9N2;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1990, sequence version 1.
DT 03-AUG-2022, entry version 193.
DE RecName: Full=Adenine DNA glycosylase;
DE EC=3.2.2.31 {ECO:0000269|PubMed:1445834, ECO:0000269|PubMed:2682664};
DE AltName: Full=A/G-specific adenine glycosylase;
GN Name=mutY; Synonyms=micA; OrderedLocusNames=b2961, JW2928;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=2197596; DOI=10.1093/nar/18.13.3841;
RA Michaels M.L., Pham L., Nghiem Y., Cruz C., Miller J.H.;
RT "MutY, an adenine glycosylase active on G-A mispairs, has homology to
RT endonuclease III.";
RL Nucleic Acids Res. 18:3841-3845(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=2001994; DOI=10.1128/jb.173.6.1902-1910.1991;
RA Tsai-Wu J.-J., Radicella J.P., Lu A.-L.;
RT "Nucleotide sequence of the Escherichia coli micA gene required for A/G-
RT specific mismatch repair: identity of micA and mutY.";
RL J. Bacteriol. 173:1902-1910(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBUNIT.
RX PubMed=2682664; DOI=10.1073/pnas.86.22.8877;
RA Au K.G., Clark S., Miller J.H., Modrich P.;
RT "Escherichia coli mutY gene encodes an adenine glycosylase active on G-A
RT mispairs.";
RL Proc. Natl. Acad. Sci. U.S.A. 86:8877-8881(1989).
RN [6]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=1445834; DOI=10.1021/bi00160a004;
RA Michaels M.L., Tchou J., Grollman A.P., Miller J.H.;
RT "A repair system for 8-oxo-7,8-dihydrodeoxyguanine.";
RL Biochemistry 31:10964-10968(1992).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.2 ANGSTROMS), AND COFACTOR.
RX PubMed=9846876; DOI=10.1038/4168;
RA Guan Y., Manuel R.C., Arvai A.S., Parikh S.S., Mol C.D., Miller J.H.,
RA Lloyd S., Tainer J.A.;
RT "MutY catalytic core, mutant and bound adenine structures define
RT specificity for DNA repair enzyme superfamily.";
RL Nat. Struct. Biol. 5:1058-1064(1998).
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:0000269|PubMed:1445834, ECO:0000269|PubMed:2682664}.
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:1445834,
CC ECO:0000269|PubMed:2682664};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000269|PubMed:9846876};
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.;
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:2682664}.
CC -!- SIMILARITY: Belongs to the Nth/MutY family. {ECO:0000305}.
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DR EMBL; X52391; CAA36624.1; -; Genomic_DNA.
DR EMBL; M59471; AAA72957.1; -; Genomic_DNA.
DR EMBL; U28377; AAA69128.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75998.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77024.1; -; Genomic_DNA.
DR PIR; B38535; B38535.
DR RefSeq; NP_417436.1; NC_000913.3.
DR RefSeq; WP_001321419.1; NZ_SSUV01000019.1.
DR PDB; 1KG2; X-ray; 1.20 A; A=1-225.
DR PDB; 1KG3; X-ray; 1.55 A; A=1-225.
DR PDB; 1KG4; X-ray; 1.60 A; A=1-225.
DR PDB; 1KG5; X-ray; 1.35 A; A=1-225.
DR PDB; 1KG6; X-ray; 1.50 A; A=1-225.
DR PDB; 1KG7; X-ray; 1.50 A; A=1-225.
DR PDB; 1KQJ; X-ray; 1.70 A; A=1-225.
DR PDB; 1MUD; X-ray; 1.80 A; A=1-225.
DR PDB; 1MUN; X-ray; 1.20 A; A=1-225.
DR PDB; 1MUY; X-ray; 1.40 A; A=1-225.
DR PDB; 1WEF; X-ray; 1.90 A; A=1-225.
DR PDB; 1WEG; X-ray; 1.80 A; A=1-225.
DR PDB; 1WEI; X-ray; 1.45 A; A=1-225.
DR PDBsum; 1KG2; -.
DR PDBsum; 1KG3; -.
DR PDBsum; 1KG4; -.
DR PDBsum; 1KG5; -.
DR PDBsum; 1KG6; -.
DR PDBsum; 1KG7; -.
DR PDBsum; 1KQJ; -.
DR PDBsum; 1MUD; -.
DR PDBsum; 1MUN; -.
DR PDBsum; 1MUY; -.
DR PDBsum; 1WEF; -.
DR PDBsum; 1WEG; -.
DR PDBsum; 1WEI; -.
DR AlphaFoldDB; P17802; -.
DR BMRB; P17802; -.
DR SMR; P17802; -.
DR BioGRID; 4262359; 411.
DR BioGRID; 851767; 3.
DR DIP; DIP-10289N; -.
DR IntAct; P17802; 11.
DR STRING; 511145.b2961; -.
DR DrugBank; DB00173; Adenine.
DR DrugBank; DB02379; Beta-D-Glucose.
DR DrugBank; DB09462; Glycerin.
DR DrugBank; DB03366; Imidazole.
DR jPOST; P17802; -.
DR PaxDb; P17802; -.
DR PRIDE; P17802; -.
DR EnsemblBacteria; AAC75998; AAC75998; b2961.
DR EnsemblBacteria; BAE77024; BAE77024; BAE77024.
DR GeneID; 947447; -.
DR KEGG; ecj:JW2928; -.
DR KEGG; eco:b2961; -.
DR PATRIC; fig|1411691.4.peg.3770; -.
DR EchoBASE; EB0622; -.
DR eggNOG; COG1194; Bacteria.
DR HOGENOM; CLU_012862_0_2_6; -.
DR InParanoid; P17802; -.
DR OMA; RDPYRVW; -.
DR PhylomeDB; P17802; -.
DR BioCyc; EcoCyc:EG10627-MON; -.
DR BioCyc; MetaCyc:EG10627-MON; -.
DR BRENDA; 3.2.2.31; 2026.
DR EvolutionaryTrace; P17802; -.
DR PRO; PR:P17802; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; 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; PF10576; EndIII_4Fe-2S; 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 1: Evidence at protein level;
KW 3D-structure; 4Fe-4S; DNA damage; DNA repair; Glycosidase; Hydrolase; Iron;
KW Iron-sulfur; Metal-binding; Reference proteome.
FT CHAIN 1..350
FT /note="Adenine DNA glycosylase"
FT /id="PRO_0000102234"
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 BINDING 199
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT BINDING 202
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT BINDING 208
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT SITE 138
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P83847"
FT HELIX 3..17
FT /evidence="ECO:0007829|PDB:1KG2"
FT HELIX 23..25
FT /evidence="ECO:0007829|PDB:1KG2"
FT HELIX 30..40
FT /evidence="ECO:0007829|PDB:1KG2"
FT STRAND 41..43
FT /evidence="ECO:0007829|PDB:1WEF"
FT HELIX 45..58
FT /evidence="ECO:0007829|PDB:1KG2"
FT HELIX 62..67
FT /evidence="ECO:0007829|PDB:1KG2"
FT HELIX 70..77
FT /evidence="ECO:0007829|PDB:1KG2"
FT HELIX 84..99
FT /evidence="ECO:0007829|PDB:1KG2"
FT HELIX 108..112
FT /evidence="ECO:0007829|PDB:1KG2"
FT HELIX 119..130
FT /evidence="ECO:0007829|PDB:1KG2"
FT HELIX 139..149
FT /evidence="ECO:0007829|PDB:1KG2"
FT HELIX 158..171
FT /evidence="ECO:0007829|PDB:1KG2"
FT HELIX 177..190
FT /evidence="ECO:0007829|PDB:1KG2"
FT STRAND 194..196
FT /evidence="ECO:0007829|PDB:1KG2"
FT HELIX 199..201
FT /evidence="ECO:0007829|PDB:1KG2"
FT TURN 203..207
FT /evidence="ECO:0007829|PDB:1KG2"
FT HELIX 209..213
FT /evidence="ECO:0007829|PDB:1KG2"
FT HELIX 216..218
FT /evidence="ECO:0007829|PDB:1KG2"
SQ SEQUENCE 350 AA; 39149 MW; C7D3657C03EBBF4F CRC64;
MQASQFSAQV LDWYDKYGRK TLPWQIDKTP YKVWLSEVML QQTQVATVIP YFERFMARFP
TVTDLANAPL DEVLHLWTGL GYYARARNLH KAAQQVATLH GGKFPETFEE VAALPGVGRS
TAGAILSLSL GKHFPILDGN VKRVLARCYA VSGWPGKKEV ENKLWSLSEQ VTPAVGVERF
NQAMMDLGAM ICTRSKPKCS LCPLQNGCIA AANNSWALYP GKKPKQTLPE RTGYFLLLQH
EDEVLLAQRP PSGLWGGLYC FPQFADEESL RQWLAQRQIA ADNLTQLTAF RHTFSHFHLD
IVPMWLPVSS FTGCMDEGNA LWYNLAQPPS VGLAAPVERL LQQLRTGAPV
