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Reviewed, UniProtKB/Swiss-Prot P04395 (3MG2_ECOLI)

Last modified November 3, 2009. Version 97. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    DNA-3-methyladenine glycosylase 2
    EC=3.2.2.21
Alternative name(s):
    DNA-3-methyladenine glycosylase II
    3-methyladenine-DNA glycosylase II, inducible
      Short name=TAG II
    DNA-3-methyladenine glycosidase II
Gene names
Name: alkA
Synonyms: aidA
Ordered Locus Names: b2068, JW2053
OrganismEscherichia coli (strain K12) [Complete proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length282 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (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 structure

Monomer.

Induction

When E.coli cells are exposed to doses of DNA alkylating agent. It is not inhibited by reaction products.

Sequence similarities

Belongs to the alkylbase DNA glycosidase alkA family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

aceFP069591EBI-544077,EBI-542707

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 282282DNA-3-methyladenine glycosylase 2
PRO_0000194878

Sites

Active site2381Proton acceptor
Site2181Determinant for substrate specificity and/or activity

Experimental info

Mutagenesis1241Q → A: Methylmethane sulfonate-resistant.
Mutagenesis2181W → A: No catalytic activity, methylmethane sulfonate-sensitive.
Mutagenesis2371D → N: More than 30% catalytic activity, methylmethane sulfonate-resistant.
Mutagenesis2381D → N: No catalytic activity, methylmethane sulfonate-sensitive.

Secondary structure

........................................... 282
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P04395-1 [UniParc].

Last modified March 20, 1987. Version 1.
Checksum: B66BB5E23019899C

FASTA28231,393
        10         20         30         40         50         60 
MYTLNWQPPY DWSWMLGFLA ARAVSSVETV ADSYYARSLA VGEYRGVVTA IPDIARHTLH 

        70         80         90        100        110        120 
INLSAGLEPV AAECLAKMSR LFDLQCNPQI VNGALGRLGA ARPGLRLPGC VDAFEQGVRA 

       130        140        150        160        170        180 
ILGQLVSVAM AAKLTARVAQ LYGERLDDFP EYICFPTPQR LAAADPQALK ALGMPLKRAE 

       190        200        210        220        230        240 
ALIHLANAAL EGTLPMTIPG DVEQAMKTLQ TFPGIGRWTA NYFALRGWQA KDVFLPDDYL 

       250        260        270        280 
IKQRFPGMTP AQIRRYAERW KPWRSYALLH IWYTEGWQPD EA 

« Hide

References

« Hide 'large scale' references
[1]"Structure and expression of the alkA gene of Escherichia coli involved in adaptive response to alkylating agents."
Nakabeppu Y., Miyata T., Kondo H., Iwanaga S., Sekiguchi M.
J. Biol. Chem. 259:13730-13736(1984) [PubMed: 6094528] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-12 AND 14-20.
[2]"A 460-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 40.1-50.0 min region on the linkage map."
Itoh T., Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Kasai H., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S. expand/collapse author list , Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Wada C., Yamamoto Y., Horiuchi T.
DNA Res. 3:379-392(1996) [PubMed: 9097040] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[3]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[4]"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
Mol. Syst. Biol. 2:E1-E5(2006) [PubMed: 16738553] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]"Cloning and characterization of the alkA gene of Escherichia coli that encodes 3-methyladenine DNA glycosylase II."
Nakabeppu Y., Kondo H., Sekiguchi M.
J. Biol. Chem. 259:13723-13729(1984) [PubMed: 6389535] [Abstract]
Cited for: CHARACTERIZATION.
[6]"Regulatory mechanisms for induction of synthesis of repair enzymes in response to alkylating agents: ada protein acts as a transcriptional regulator."
Nakabeppu Y., Sekiguchi M.
Proc. Natl. Acad. Sci. U.S.A. 83:6297-6301(1986) [PubMed: 3529081] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-2.
[7]"Three-dimensional structure of a DNA repair enzyme, 3-methyladenine DNA glycosylase II, from Escherichia coli."
Yamagata Y., Kato M., Odawara K., Tokuno Y., Nakashima Y., Matsushima N., Yasumura K., Tomita K., Ihara K., Fujii Y., Nakabeppu Y., Sekiguchi M., Fujii S.
Cell 86:311-319(1996) [PubMed: 8706135] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS), MUTAGENESIS.
[8]"Structural basis for the excision repair of alkylation-damaged DNA."
Labahn J., Scharer O.D., Long A., Ezaz-Nikpay K., Verdine G.L., Ellenberger T.E.
Cell 86:321-329(1996) [PubMed: 8706136] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

K02498 Genomic DNA. Translation: AAA23430.1.
U00096 Genomic DNA. Translation: AAC75129.1.
AP009048 Genomic DNA. Translation: BAA15926.1.
M13827 Genomic DNA. No translation available.
PIRDGECMA. A00904.
RefSeqAP_002668.1.
NP_416572.1.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1DIZX-ray2.50A/B1-282[»]
1MPGX-ray1.80A/B1-282[»]
1PVSX-ray2.40A/B1-282[»]
3CVSX-ray2.40A/B/C/D1-282[»]
3CVTX-ray2.50A/B/C/D1-282[»]
3CW7X-ray2.30A/B/C/D1-282[»]
3CWAX-ray2.40A/B/C/D1-282[»]
3CWSX-ray2.30A/B/C/D1-282[»]
3CWTX-ray2.30A/B/C/D1-282[»]
3CWUX-ray2.80A/B/C/D1-282[»]
3D4VX-ray2.90A/B/C/D1-282[»]
ModBaseSearch...

Protein-protein interaction databases

DIPDIP:9084N.
IntActP04395. 19 interactions.
STRINGP04395.

Genome annotation databases

GeneID947371.
GenomeReviewsGene locus JW2053 in contig AP009048_GR.
Gene locus b2068 in contig U00096_GR.
KEGGecj:JW2053.
eco:b2068.

Organism-specific databases

EchoBASEEB1204.
EcoGeneEG11222. alkA.
CMRSearch...

Phylogenomic databases

HOGENOMP04395.
OMAGLARDPW.

Enzyme and pathway databases

BioCycEcoCyc:EG11222-MON.

Gene expression databases

GenevestigatorP04395.

Family and domain databases

InterProIPR010316. AlkA_N.
IPR000035. Alkylbase_DNA_glycsylse_CS.
IPR003265. HhH-GPD_domain.
[Graphical view]
Gene3DG3DSA:3.30.310.20. AlkA_N. 1 hit.
PfamPF06029. AlkA_N. 1 hit.
PF00730. HhH-GPD. 1 hit.
[Graphical view]
SMARTSM00478. ENDO3c. 1 hit.
[Graphical view]
PROSITEPS00516. ALKYLBASE_DNA_GLYCOS. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry name3MG2_ECOLI
AccessionPrimary (citable) accession number: P04395
Entry history
Integrated into UniProtKB/Swiss-Prot: March 20, 1987
Last sequence update: March 20, 1987
Last modified: November 3, 2009
This is version 97 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents