3MG2_ECOLI
ID 3MG2_ECOLI Reviewed; 282 AA.
AC P04395;
DT 20-MAR-1987, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-1987, sequence version 1.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=DNA-3-methyladenine glycosylase 2;
DE EC=3.2.2.21;
DE AltName: Full=3-methyladenine-DNA glycosylase II, inducible;
DE Short=TAG II;
DE AltName: Full=DNA-3-methyladenine glycosidase II;
DE AltName: Full=DNA-3-methyladenine glycosylase II;
GN Name=alkA; Synonyms=aidA; OrderedLocusNames=b2068, JW2053;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-12 AND 14-20.
RX PubMed=6094528; DOI=10.1016/s0021-9258(18)89806-4;
RA Nakabeppu Y., Miyata T., Kondo H., Iwanaga S., Sekiguchi M.;
RT "Structure and expression of the alkA gene of Escherichia coli involved in
RT adaptive response to alkylating agents.";
RL J. Biol. Chem. 259:13730-13736(1984).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9097040; DOI=10.1093/dnares/3.6.379;
RA Itoh T., Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K.,
RA Kasai H., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T.,
RA Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S., Nakamura Y.,
RA Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y.,
RA Sivasundaram S., Tagami H., Takeda J., Takemoto K., Wada C., Yamamoto Y.,
RA Horiuchi T.;
RT "A 460-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 40.1-50.0 min region on the linkage map.";
RL DNA Res. 3:379-392(1996).
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 CHARACTERIZATION.
RX PubMed=6389535; DOI=10.1016/s0021-9258(18)89805-2;
RA Nakabeppu Y., Kondo H., Sekiguchi M.;
RT "Cloning and characterization of the alkA gene of Escherichia coli that
RT encodes 3-methyladenine DNA glycosylase II.";
RL J. Biol. Chem. 259:13723-13729(1984).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-2.
RX PubMed=3529081; DOI=10.1073/pnas.83.17.6297;
RA Nakabeppu Y., Sekiguchi M.;
RT "Regulatory mechanisms for induction of synthesis of repair enzymes in
RT response to alkylating agents: ada protein acts as a transcriptional
RT regulator.";
RL Proc. Natl. Acad. Sci. U.S.A. 83:6297-6301(1986).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS), AND MUTAGENESIS.
RX PubMed=8706135; DOI=10.1016/s0092-8674(00)80102-6;
RA Yamagata Y., Kato M., Odawara K., Tokuno Y., Nakashima Y., Matsushima N.,
RA Yasumura K., Tomita K., Ihara K., Fujii Y., Nakabeppu Y., Sekiguchi M.,
RA Fujii S.;
RT "Three-dimensional structure of a DNA repair enzyme, 3-methyladenine DNA
RT glycosylase II, from Escherichia coli.";
RL Cell 86:311-319(1996).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
RX PubMed=8706136; DOI=10.1016/s0092-8674(00)80103-8;
RA Labahn J., Scharer O.D., Long A., Ezaz-Nikpay K., Verdine G.L.,
RA Ellenberger T.E.;
RT "Structural basis for the excision repair of alkylation-damaged DNA.";
RL Cell 86:321-329(1996).
CC -!- FUNCTION: Hydrolysis of the deoxyribose N-glycosidic bond to excise 3-
CC methyladenine, 3-methylguanine, 7-methylguanine, O2-methylthymine, and
CC O2-methylcytosine from the damaged DNA polymer formed by alkylation
CC lesions.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of alkylated DNA, releasing 3-methyladenine, 3-
CC methylguanine, 7-methylguanine and 7-methyladenine.; EC=3.2.2.21;
CC -!- SUBUNIT: Monomer.
CC -!- INTERACTION:
CC P04395; P06959: aceF; NbExp=2; IntAct=EBI-544077, EBI-542707;
CC -!- INDUCTION: Up-regulated by methylated Ada in response to the exposure
CC to alkylating agents.
CC -!- SIMILARITY: Belongs to the alkylbase DNA glycosidase AlkA family.
CC {ECO:0000305}.
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DR EMBL; K02498; AAA23430.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75129.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA15926.1; -; Genomic_DNA.
DR EMBL; M13827; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; A00904; DGECMA.
DR RefSeq; NP_416572.1; NC_000913.3.
DR RefSeq; WP_000288420.1; NZ_LN832404.1.
DR PDB; 1DIZ; X-ray; 2.50 A; A/B=1-282.
DR PDB; 1MPG; X-ray; 1.80 A; A/B=1-282.
DR PDB; 1PVS; X-ray; 2.40 A; A/B=1-282.
DR PDB; 3CVS; X-ray; 2.40 A; A/B/C/D=1-282.
DR PDB; 3CVT; X-ray; 2.50 A; A/B/C/D=1-282.
DR PDB; 3CW7; X-ray; 2.30 A; A/B/C/D=1-282.
DR PDB; 3CWA; X-ray; 2.40 A; A/B/C/D=1-282.
DR PDB; 3CWS; X-ray; 2.30 A; A/B/C/D=1-282.
DR PDB; 3CWT; X-ray; 2.30 A; A/B/C/D=1-282.
DR PDB; 3CWU; X-ray; 2.80 A; A/B/C/D=1-282.
DR PDB; 3D4V; X-ray; 2.90 A; A/B/C/D=1-282.
DR PDB; 3OGD; X-ray; 2.80 A; A=2-282.
DR PDB; 3OH6; X-ray; 2.89 A; A=2-282.
DR PDB; 3OH9; X-ray; 2.80 A; A=2-282.
DR PDBsum; 1DIZ; -.
DR PDBsum; 1MPG; -.
DR PDBsum; 1PVS; -.
DR PDBsum; 3CVS; -.
DR PDBsum; 3CVT; -.
DR PDBsum; 3CW7; -.
DR PDBsum; 3CWA; -.
DR PDBsum; 3CWS; -.
DR PDBsum; 3CWT; -.
DR PDBsum; 3CWU; -.
DR PDBsum; 3D4V; -.
DR PDBsum; 3OGD; -.
DR PDBsum; 3OH6; -.
DR PDBsum; 3OH9; -.
DR AlphaFoldDB; P04395; -.
DR SMR; P04395; -.
DR BioGRID; 4259681; 55.
DR DIP; DIP-9084N; -.
DR IntAct; P04395; 19.
DR STRING; 511145.b2068; -.
DR jPOST; P04395; -.
DR PaxDb; P04395; -.
DR PRIDE; P04395; -.
DR EnsemblBacteria; AAC75129; AAC75129; b2068.
DR EnsemblBacteria; BAA15926; BAA15926; BAA15926.
DR GeneID; 947371; -.
DR KEGG; ecj:JW2053; -.
DR KEGG; eco:b2068; -.
DR PATRIC; fig|1411691.4.peg.183; -.
DR EchoBASE; EB1204; -.
DR eggNOG; COG0122; Bacteria.
DR HOGENOM; CLU_000445_72_3_6; -.
DR InParanoid; P04395; -.
DR OMA; YLWRSIE; -.
DR PhylomeDB; P04395; -.
DR BioCyc; EcoCyc:EG11222-MON; -.
DR BioCyc; MetaCyc:EG11222-MON; -.
DR BRENDA; 3.2.2.21; 2026.
DR EvolutionaryTrace; P04395; -.
DR PRO; PR:P04395; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IDA:EcoliWiki.
DR GO; GO:0032993; C:protein-DNA complex; IBA:GO_Central.
DR GO; GO:0032131; F:alkylated DNA binding; IBA:GO_Central.
DR GO; GO:0003905; F:alkylbase DNA N-glycosylase activity; IDA:EcoliWiki.
DR GO; GO:0008725; F:DNA-3-methyladenine glycosylase activity; IBA:GO_Central.
DR GO; GO:0052822; F:DNA-3-methylguanine glycosylase activity; IEA:UniProtKB-EC.
DR GO; GO:0052821; F:DNA-7-methyladenine glycosylase activity; IEA:UniProtKB-EC.
DR GO; GO:0043916; F:DNA-7-methylguanine glycosylase activity; IBA:GO_Central.
DR GO; GO:0006284; P:base-excision repair; IDA:EcoliWiki.
DR GO; GO:0006285; P:base-excision repair, AP site formation; IBA:GO_Central.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IMP:EcoliWiki.
DR GO; GO:0006307; P:DNA dealkylation involved in DNA repair; IMP:EcoliWiki.
DR GO; GO:0006281; P:DNA repair; IDA:EcoliWiki.
DR CDD; cd00056; ENDO3c; 1.
DR Gene3D; 1.10.1670.10; -; 1.
DR Gene3D; 3.30.310.20; -; 1.
DR InterPro; IPR010316; AlkA_N.
DR InterPro; IPR037046; AlkA_N_sf.
DR InterPro; IPR000035; Alkylbase_DNA_glycsylse_CS.
DR InterPro; IPR011257; DNA_glycosylase.
DR InterPro; IPR003265; HhH-GPD_domain.
DR InterPro; IPR023170; HhH_base_excis_C.
DR Pfam; PF06029; AlkA_N; 1.
DR Pfam; PF00730; HhH-GPD; 1.
DR SMART; SM01009; AlkA_N; 1.
DR SMART; SM00478; ENDO3c; 1.
DR SUPFAM; SSF48150; SSF48150; 1.
DR PROSITE; PS00516; ALKYLBASE_DNA_GLYCOS; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; DNA damage; DNA repair; Hydrolase;
KW Reference proteome.
FT CHAIN 1..282
FT /note="DNA-3-methyladenine glycosylase 2"
FT /id="PRO_0000194878"
FT ACT_SITE 238
FT /note="Proton acceptor"
FT SITE 218
FT /note="Determinant for substrate specificity and/or
FT activity"
FT MUTAGEN 124
FT /note="Q->A: Methylmethane sulfonate-resistant."
FT /evidence="ECO:0000269|PubMed:8706135"
FT MUTAGEN 218
FT /note="W->A: No catalytic activity, methylmethane
FT sulfonate-sensitive."
FT /evidence="ECO:0000269|PubMed:8706135"
FT MUTAGEN 237
FT /note="D->N: More than 30% catalytic activity,
FT methylmethane sulfonate-resistant."
FT /evidence="ECO:0000269|PubMed:8706135"
FT MUTAGEN 238
FT /note="D->N: No catalytic activity, methylmethane
FT sulfonate-sensitive."
FT /evidence="ECO:0000269|PubMed:8706135"
FT STRAND 2..5
FT /evidence="ECO:0007829|PDB:1MPG"
FT HELIX 12..22
FT /evidence="ECO:0007829|PDB:1MPG"
FT TURN 25..27
FT /evidence="ECO:0007829|PDB:1MPG"
FT STRAND 28..30
FT /evidence="ECO:0007829|PDB:1MPG"
FT STRAND 35..41
FT /evidence="ECO:0007829|PDB:1MPG"
FT STRAND 44..53
FT /evidence="ECO:0007829|PDB:1MPG"
FT TURN 54..57
FT /evidence="ECO:0007829|PDB:1MPG"
FT STRAND 58..63
FT /evidence="ECO:0007829|PDB:1MPG"
FT HELIX 65..70
FT /evidence="ECO:0007829|PDB:1MPG"
FT HELIX 71..82
FT /evidence="ECO:0007829|PDB:1MPG"
FT TURN 83..85
FT /evidence="ECO:0007829|PDB:1MPG"
FT HELIX 88..95
FT /evidence="ECO:0007829|PDB:1MPG"
FT HELIX 96..99
FT /evidence="ECO:0007829|PDB:1MPG"
FT HELIX 113..122
FT /evidence="ECO:0007829|PDB:1MPG"
FT TURN 123..125
FT /evidence="ECO:0007829|PDB:1MPG"
FT HELIX 128..142
FT /evidence="ECO:0007829|PDB:1MPG"
FT STRAND 149..153
FT /evidence="ECO:0007829|PDB:3CW7"
FT HELIX 158..162
FT /evidence="ECO:0007829|PDB:1MPG"
FT HELIX 166..171
FT /evidence="ECO:0007829|PDB:1MPG"
FT HELIX 176..190
FT /evidence="ECO:0007829|PDB:1MPG"
FT HELIX 202..209
FT /evidence="ECO:0007829|PDB:1MPG"
FT HELIX 217..227
FT /evidence="ECO:0007829|PDB:1MPG"
FT HELIX 239..244
FT /evidence="ECO:0007829|PDB:1MPG"
FT STRAND 245..247
FT /evidence="ECO:0007829|PDB:1PVS"
FT HELIX 250..257
FT /evidence="ECO:0007829|PDB:1MPG"
FT HELIX 258..260
FT /evidence="ECO:0007829|PDB:1MPG"
FT HELIX 264..272
FT /evidence="ECO:0007829|PDB:1MPG"
SQ SEQUENCE 282 AA; 31393 MW; B66BB5E23019899C CRC64;
MYTLNWQPPY DWSWMLGFLA ARAVSSVETV ADSYYARSLA VGEYRGVVTA IPDIARHTLH
INLSAGLEPV AAECLAKMSR LFDLQCNPQI VNGALGRLGA ARPGLRLPGC VDAFEQGVRA
ILGQLVSVAM AAKLTARVAQ LYGERLDDFP EYICFPTPQR LAAADPQALK ALGMPLKRAE
ALIHLANAAL EGTLPMTIPG DVEQAMKTLQ TFPGIGRWTA NYFALRGWQA KDVFLPDDYL
IKQRFPGMTP AQIRRYAERW KPWRSYALLH IWYTEGWQPD EA
