3MG1_ECOLI
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 03-AUG-2022, entry version 174.
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; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC 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_SSZK01000068.1.
DR PDB; 1LMZ; NMR; -; A=1-187.
DR PDB; 1NKU; NMR; -; A=1-187.
DR PDB; 1P7M; NMR; -; A=1-187.
DR PDBsum; 1LMZ; -.
DR PDBsum; 1NKU; -.
DR PDBsum; 1P7M; -.
DR AlphaFoldDB; P05100; -.
DR BMRB; P05100; -.
DR SMR; P05100; -.
DR BioGRID; 4261555; 196.
DR BioGRID; 851471; 1.
DR DIP; DIP-10950N; -.
DR IntAct; P05100; 5.
DR STRING; 511145.b3549; -.
DR BindingDB; P05100; -.
DR ChEMBL; CHEMBL2295563; -.
DR DrugBank; DB04104; 3-Methyladenine.
DR jPOST; P05100; -.
DR PaxDb; P05100; -.
DR PRIDE; P05100; -.
DR EnsemblBacteria; AAC76573; AAC76573; b3549.
DR EnsemblBacteria; BAE77746; BAE77746; BAE77746.
DR GeneID; 947137; -.
DR KEGG; ecj:JW3518; -.
DR KEGG; eco:b3549; -.
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; YVAYHDT; -.
DR PhylomeDB; P05100; -.
DR BioCyc; EcoCyc:EG10986-MON; -.
DR BioCyc; MetaCyc:EG10986-MON; -.
DR BRENDA; 3.2.2.20; 2026.
DR EvolutionaryTrace; P05100; -.
DR PRO; PR:P05100; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0008725; F:DNA-3-methyladenine glycosylase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006284; P:base-excision repair; IEA:InterPro.
DR GO; GO:0006307; P:DNA dealkylation involved in DNA repair; IBA:GO_Central.
DR InterPro; IPR005019; Adenine_glyco.
DR InterPro; IPR011257; DNA_glycosylase.
DR InterPro; IPR004597; Tag.
DR Pfam; PF03352; Adenine_glyco; 1.
DR SUPFAM; SSF48150; SSF48150; 1.
DR TIGRFAMs; TIGR00624; tag; 1.
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 28..39
FT /evidence="ECO:0007829|PDB:1LMZ"
FT TURN 40..43
FT /evidence="ECO:0007829|PDB:1LMZ"
FT HELIX 46..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
