ID   3MG1_ECOLI              Reviewed;         187 AA.
AC   P05100; Q2M7L0;
DT   13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT   13-AUG-1987, sequence version 1.
DT   02-SEP-2026, entry version 191.
DE   RecName: Full=DNA-3-methyladenine glycosylase 1;
DE            EC=3.2.2.20 {ECO:0000269|PubMed:3536912};
DE   AltName: Full=3-methyladenine-DNA glycosylase I, constitutive;
DE            Short=TAG I;
DE   AltName: Full=DNA-3-methyladenine glycosidase I;
DE   AltName: Full=DNA-3-methyladenine glycosylase I;
GN   Name=tag {ECO:0000303|PubMed:3520491, ECO:0000303|PubMed:3536912};
GN   OrderedLocusNames=b3549, JW3518;
OS   Escherichia coli (strain K12).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Enterobacterales; Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-29, FUNCTION,
RP   CATALYTIC ACTIVITY, AND ACTIVITY REGULATION.
RX   PubMed=3536912; DOI=10.1016/s0021-9258(18)66783-3;
RA   Sakumi K., Nakabeppu Y., Yamamoto Y., Kawabata S., Iwanaga S.,
RA   Sekiguchi M.;
RT   "Purification and structure of 3-methyladenine-DNA glycosylase I of
RT   Escherichia coli.";
RL   J. Biol. Chem. 261:15761-15766(1986).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3520491; DOI=10.1093/nar/14.9.3763;
RA   Steinum A.-L., Seeberg E.;
RT   "Nucleotide sequence of the tag gene from Escherichia coli.";
RL   Nucleic Acids Res. 14:3763-3772(1986).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=8041620; DOI=10.1093/nar/22.13.2576;
RA   Sofia H.J., Burland V., Daniels D.L., Plunkett G. III, Blattner F.R.;
RT   "Analysis of the Escherichia coli genome. V. DNA sequence of the region
RT   from 76.0 to 81.5 minutes.";
RL   Nucleic Acids Res. 22:2576-2586(1994).
RN   [4]
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   [5]
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   [6]
RP   IDENTIFICATION BY 2D-GEL.
RX   PubMed=9298644; DOI=10.1002/elps.1150180805;
RA   VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.;
RT   "Escherichia coli proteome analysis using the gene-protein database.";
RL   Electrophoresis 18:1243-1251(1997).
RN   [7] {ECO:0007744|PDB:1LMZ}
RP   STRUCTURE BY NMR.
RX   PubMed=12161745; DOI=10.1038/nsb829;
RA   Drohat A.C., Kwon K., Krosky D.J., Stivers J.T.;
RT   "3-Methyladenine DNA glycosylase I is an unexpected helix-hairpin-helix
RT   superfamily member.";
RL   Nat. Struct. Biol. 9:659-664(2002).
RN   [8] {ECO:0007744|PDB:1NKU}
RP   STRUCTURE BY NMR IN COMPLEX WITH ZINC, AND ZINC-BINDING SITES.
RX   PubMed=12654914; DOI=10.1074/jbc.m300934200;
RA   Kwon K., Cao C., Stivers J.T.;
RT   "A novel zinc snap motif conveys structural stability to 3-methyladenine
RT   DNA glycosylase I.";
RL   J. Biol. Chem. 278:19442-19446(2003).
RN   [9] {ECO:0007744|PDB:1P7M}
RP   STRUCTURE BY NMR IN COMPLEX WITH 3-METHYLADENINE AND ZINC, AND ZINC-BINDING
RP   SITES.
RX   PubMed=13129925; DOI=10.1074/jbc.m307500200;
RA   Cao C., Kwon K., Jiang Y.L., Drohat A.C., Stivers J.T.;
RT   "Solution structure and base perturbation studies reveal a novel mode of
RT   alkylated base recognition by 3-methyladenine DNA glycosylase I.";
RL   J. Biol. Chem. 278:48012-48020(2003).
CC   -!- FUNCTION: Hydrolysis of the deoxyribose N-glycosidic bond to excise 3-
CC       methyladenine from the damaged DNA polymer formed by alkylation
CC       lesions. {ECO:0000269|PubMed:3536912}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of alkylated DNA, releasing 3-methyladenine.;
CC         EC=3.2.2.20; Evidence={ECO:0000269|PubMed:3536912};
CC   -!- ACTIVITY REGULATION: Activity is controlled by product inhibition.
CC       {ECO:0000269|PubMed:3536912}.
CC   -!- INTERACTION:
CC       P05100; P0AFG8: aceE; NbExp=2; IntAct=EBI-558722, EBI-542683;
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DR   EMBL; J02606; AAA24658.1; -; Genomic_DNA.
DR   EMBL; X03845; CAA27472.1; -; Genomic_DNA.
DR   EMBL; U00039; AAB18526.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC76573.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAE77746.1; -; Genomic_DNA.
DR   PIR; A24604; DGECM1.
DR   RefSeq; NP_418005.1; NC_000913.3.
DR   RefSeq; WP_000438957.1; NZ_CP009789.1.
DR   PDB; 1LMZ; NMR; -; A=1-187.
DR   PDB; 1NKU; NMR; -; A=1-187.
DR   PDB; 1P7M; NMR; -; A=1-187.
DR   AlphaFoldDB; P05100; -.
DR   BMRB; P05100; -.
DR   MDRepo; P05100; -.
DR   SMR; P05100; -.
DR   BioGRID; 4261555; 196.
DR   BioGRID; 851471; 1.
DR   DIP; DIP-10950N; -.
DR   FunCoup; P05100; 235.
DR   IntAct; P05100; 5.
DR   STRING; 511145.b3549; -.
DR   BindingDB; P05100; -.
DR   ChEMBL; CHEMBL2295563; -.
DR   DrugBank; DB04104; 3-Methyladenine.
DR   jPOST; P05100; -.
DR   PaxDb; 511145-b3549; -.
DR   EnsemblBacteria; AAC76573; AAC76573; b3549.
DR   GeneID; 947137; -.
DR   KEGG; ecj:JW3518; -.
DR   KEGG; eco:b3549; -.
DR   KEGG; ecoc:C3026_19240; -.
DR   PATRIC; fig|1411691.4.peg.3165; -.
DR   EchoBASE; EB0979; -.
DR   eggNOG; COG2818; Bacteria.
DR   HOGENOM; CLU_083758_1_0_6; -.
DR   InParanoid; P05100; -.
DR   OMA; HMQATGM; -.
DR   OrthoDB; 9807664at2; -.
DR   PhylomeDB; P05100; -.
DR   BioCyc; EcoCyc:EG10986-MONOMER; -.
DR   BioCyc; MetaCyc:EG10986-MONOMER; -.
DR   BRENDA; 3.2.2.20; 2026.
DR   EvolutionaryTrace; P05100; -.
DR   PRO; PR:P05100; -.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0008725; F:DNA-3-methyladenine glycosylase activity; EXP:UniProtKB.
DR   GO; GO:0006284; P:base-excision repair; IEA:InterPro.
DR   GO; GO:0006307; P:DNA alkylation repair; EXP:EcoCyc.
DR   FunFam; 1.10.340.30:FF:000009; DNA-3-methyladenine glycosylase I; 1.
DR   Gene3D; 1.10.340.30; Hypothetical protein, domain 2; 1.
DR   InterPro; IPR005019; Adenine_glyco.
DR   InterPro; IPR052891; DNA-3mA_glycosylase.
DR   InterPro; IPR011257; DNA_glycosylase.
DR   InterPro; IPR004597; Tag.
DR   NCBIfam; NF007678; PRK10353.1; 1.
DR   NCBIfam; TIGR00624; tag; 1.
DR   PANTHER; PTHR30037; DNA-3-METHYLADENINE GLYCOSYLASE 1; 1.
DR   PANTHER; PTHR30037:SF4; DNA-3-METHYLADENINE GLYCOSYLASE I; 1.
DR   Pfam; PF03352; Adenine_glyco; 1.
DR   SUPFAM; SSF48150; DNA-glycosylase; 1.
DR   PDBsum; 1LMZ; -.
DR   PDBsum; 1NKU; -.
DR   PDBsum; 1P7M; -.
PE   1: Evidence at protein level;
KW   3D-structure; Direct protein sequencing; DNA damage; DNA repair; Hydrolase;
KW   Metal-binding; Reference proteome; Zinc.
FT   CHAIN           1..187
FT                   /note="DNA-3-methyladenine glycosylase 1"
FT                   /id="PRO_0000194877"
FT   BINDING         4
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000269|PubMed:12654914,
FT                   ECO:0000269|PubMed:13129925, ECO:0007744|PDB:1NKU,
FT                   ECO:0007744|PDB:1P7M"
FT   BINDING         17
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000269|PubMed:12654914,
FT                   ECO:0000269|PubMed:13129925, ECO:0007744|PDB:1NKU,
FT                   ECO:0007744|PDB:1P7M"
FT   BINDING         175
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000269|PubMed:12654914,
FT                   ECO:0000269|PubMed:13129925, ECO:0007744|PDB:1NKU,
FT                   ECO:0007744|PDB:1P7M"
FT   BINDING         179
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000269|PubMed:12654914,
FT                   ECO:0000269|PubMed:13129925, ECO:0007744|PDB:1NKU,
FT                   ECO:0007744|PDB:1P7M"
FT   TURN            5..9
FT                   /evidence="ECO:0007829|PDB:1P7M"
FT   HELIX           12..19
FT                   /evidence="ECO:0007829|PDB:1LMZ"
FT   STRAND          20..23
FT                   /evidence="ECO:0007829|PDB:1LMZ"
FT   HELIX           25..27
FT                   /evidence="ECO:0007829|PDB:1P7M"
FT   HELIX           28..39
FT                   /evidence="ECO:0007829|PDB:1LMZ"
FT   TURN            40..43
FT                   /evidence="ECO:0007829|PDB:1LMZ"
FT   HELIX           46..56
FT                   /evidence="ECO:0007829|PDB:1LMZ"
FT   HELIX           57..61
FT                   /evidence="ECO:0007829|PDB:1LMZ"
FT   HELIX           62..70
FT                   /evidence="ECO:0007829|PDB:1LMZ"
FT   HELIX           73..81
FT                   /evidence="ECO:0007829|PDB:1LMZ"
FT   STRAND          82..85
FT                   /evidence="ECO:0007829|PDB:1LMZ"
FT   HELIX           90..107
FT                   /evidence="ECO:0007829|PDB:1LMZ"
FT   HELIX           112..118
FT                   /evidence="ECO:0007829|PDB:1LMZ"
FT   TURN            119..122
FT                   /evidence="ECO:0007829|PDB:1LMZ"
FT   TURN            132..134
FT                   /evidence="ECO:0007829|PDB:1LMZ"
FT   HELIX           140..152
FT                   /evidence="ECO:0007829|PDB:1LMZ"
FT   HELIX           159..169
FT                   /evidence="ECO:0007829|PDB:1LMZ"
FT   STRAND          171..173
FT                   /evidence="ECO:0007829|PDB:1LMZ"
FT   STRAND          175..177
FT                   /evidence="ECO:0007829|PDB:1P7M"
FT   STRAND          179..181
FT                   /evidence="ECO:0007829|PDB:1LMZ"
SQ   SEQUENCE   187 AA;  21100 MW;  5A305B5CA66A48FE CRC64;
     MERCGWVSQD PLYIAYHDNE WGVPETDSKK LFEMICLEGQ QAGLSWITVL KKRENYRACF
     HQFDPVKVAA MQEEDVERLV QDAGIIRHRG KIQAIIGNAR AYLQMEQNGE PFVDFVWSFV
     NHQPQVTQAT TLSEIPTSTS ASDALSKALK KRGFKFVGTT ICYSFMQACG LVNDHVVGCC
     CYPGNKP
//