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Description:
DNA-3-methyladenine glycosylase II (EC 3.2.2.21) (3-methyladenine-DNAglycosylase II, inducible) (TAG II) (DNA-3-methyladenine glycosidaseII).
Molecular weight: 31393
View which proteins in this organism that is involved with DNA Repair;
classified after biological processes (using data from the GOA project):
DNA repair( GO:0006281 ) base-excision repair( GO:0006284 )
Important dates:
20-MAR-1987, integrated into UniProtKB/Swiss-Prot.
20-MAR-1987, sequence version 1.
07-MAR-2006, entry version 65.
Phylogenetic order:
Bacteria Proteobacteria Gammaproteobacteria Enterobacteriales Enterobacteriaceae Escherichia.
To calculate the pI (Isoelectric point - the pH where a protein has a neutral charge),
go to this page and enter the protein ID (e.g 3MG_ECOLI): http://us.expasy.org/tools/pi_tool.html
Links to references in other databases for protein 3MG2_ECOLI:
| Database | Pointer | Add. info#1 | Add. info#2 |
| EMBL | K02498 | AAA23430.1 | - |
| EMBL | U00096 | AAC75129.1 | - |
| EMBL | D90844 | BAA15921.1 | - |
| EMBL | D90845 | BAA15926.1 | - |
| EMBL | M13827 | NOT_ANNOTATED_CDS | |
| PIR | A00904 | DGECMA. | |
| PDB | 1DIZ | X-ray | A/B=1-282. |
| PDB | 1MPG | X-ray | A/B=1-282. |
| PDB | 1PVS | X-ray | A/B=1-282. |
| GenomeReviews | U00096_GR | b2068.1 | |
| EchoBASE | EB1204 | -.1 | |
| EcoGene | EG11222 | alkA. | |
| BioCyc | EcoCyc:EG11222-MONOMER | -.1 | |
| LinkHub | P04395 | -.1 | |
| GO | GO:0005515 | F:protein binding | IPI. |
| InterPro | IPR000035 | AlbDNA_glycsylse. | |
| InterPro | IPR010316 | AlkA_N. | |
| InterPro | IPR003265 | Endo_3c. | |
| InterPro | IPR012294 | TFIID_C/glycos_N. | |
| Pfam | PF06029 | AlkA_N | 1. |
| Pfam | PF00730 | HhH-GPD | 1. |
| SMART | SM00478 | ENDO3c | 1. |
| PROSITE | PS00516 | ALKYLBASE_DNA_GLYCOS | 1. |
Keywords:
3D-structure; Complete proteome; Direct protein sequencing; DNA damage; DNA repair; Hydrolase.
References:
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-12 AND
RP 14-20.
RX MEDLINE=85054800; PubMed=6094528;
RA Nakabeppu Y., Miyata T., Kondo H., Iwanaga S., Sekiguchi M.;
RT "Structure and expression of the alkA gene of Escherichia coli
RT involved in 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 / MG1655;
RX MEDLINE=97426617; 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.,
RA Mau B., Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1474(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12;
RX MEDLINE=97251358; 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.,
RA Yamamoto Y., Horiuchi T.;
RT "A 460-kb DNA sequence of the Escherichia coli K-12 genome
RT corresponding to the 40.1-50.0 min region on the linkage map.";
RL DNA Res. 3:379-392(1996).
RN [4]
RP CHARACTERIZATION.
RX MEDLINE=85054799; PubMed=6389535;
RA Nakabeppu Y., Kondo H., Sekiguchi M.;
RT "Cloning and characterization of the alkA gene of Escherichia coli
RT that encodes 3-methyladenine DNA glycosylase II.";
RL J. Biol. Chem. 259:13723-13729(1984).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-2.
RX MEDLINE=86313568; PubMed=3529081;
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 [6]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS), AND MUTAGENESIS.
RX MEDLINE=96319733; PubMed=8706135; DOI=10.1016/S0092-8674(00)80102-6;
RA Yamagata Y., Kato M., Odawara K., Tokuno Y., Nakashima Y.,
RA Matsushima N., Yasumura K., Tomita K., Ihara K., Fujii Y.,
RA Nakabeppu Y., Sekiguchi M., Fujii S.;
RT "Three-dimensional structure of a DNA repair enzyme, 3-methyladenine
RT DNA glycosylase II, from Escherichia coli.";
RL Cell 86:311-319(1996).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
RX MEDLINE=96319734; 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).
Feature:
CHAIN 1 282 DNA-3-methyladenine glycosylase II.
/FTId=PRO_0000194878.
ACT_SITE 238 238 Proton acceptor.
SITE 218 218 Determinant for substrate specificity
and/or activity.
MUTAGEN 124 124 Q->A: Methylmethane sulfonate-resistant.
MUTAGEN 218 218 W->A: No catalytic activity,
methylmethane sulfonate-sensitive.
MUTAGEN 237 237 D->N: More than 30% catalytic activity,
methylmethane sulfonate-resistant.
MUTAGEN 238 238 D->N: No catalytic activity,
methylmethane sulfonate-sensitive.
STRAND 2 5
STRAND 8 8
HELIX 12 22
TURN 25 27
STRAND 28 30
STRAND 32 33
STRAND 35 41
TURN 42 43
STRAND 44 53
TURN 54 57
STRAND 58 63
HELIX 65 82
TURN 83 85
HELIX 88 99
TURN 100 101
TURN 103 104
STRAND 111 111
HELIX 113 122
TURN 123 125
STRAND 126 126
HELIX 128 142
STRAND 145 145
STRAND 147 148
TURN 150 151
STRAND 153 153
HELIX 158 162
TURN 163 163
HELIX 166 171
TURN 172 173
STRAND 174 174
HELIX 176 190
TURN 191 192
STRAND 194 194
STRAND 196 197
STRAND 200 200
HELIX 202 209
TURN 210 211
STRAND 212 212
TURN 213 214
HELIX 217 227
STRAND 228 228
STRAND 231 232
TURN 236 237
HELIX 239 244
STRAND 245 245
TURN 246 247
HELIX 250 260
TURN 261 262
HELIX 264 272
TURN 273 273
TURN 275 276
Comments:
-!- FUNCTION: Hydrolysis of the deoxyribose N-glycosidic bond to
excise 3-methyladenine, 3-methylguanine, 7-methylguanine, O2-
methylthymine, and O2-methylcytosine from the damaged DNA polymer
formed by alkylation lesions.
-!- CATALYTIC ACTIVITY: Hydrolysis of alkylated DNA, releasing 3-
methyladenine, 3-methylguanine, 7-methylguanine and 7-
methyladenine.
-!- SUBUNIT: Monomer.
-!- INTERACTION:
P06959:aceF; NbExp=1; IntAct=EBI-544077, EBI-542707;
-!- INDUCTION: When E.coli cells are exposed to doses of DNA
alkylating agent. It is not inhibited by reaction products.
-!- SIMILARITY: Belongs to the alkylbase DNA glycosidase alkA family.
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Sequence length: 282
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