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

Last modified May 14, 2014. Version 134. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
DNA-3-methyladenine glycosylase 2

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

Protein attributes

Sequence length282 AA.
Sequence statusComplete.
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

Up-regulated by methylated Ada in response to the exposure to alkylating agents.

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 [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] [Europe PMC] [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] [Europe PMC] [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 277:1453-1462(1997) [PubMed] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_416572.1. NC_000913.3.
YP_490310.1. NC_007779.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
3OGDX-ray2.80A2-282[»]
3OH6X-ray2.89A2-282[»]
3OH9X-ray2.80A2-282[»]
ProteinModelPortalP04395.
SMRP04395. Positions 1-282.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-9084N.
IntActP04395. 19 interactions.
MINTMINT-1227621.
STRING511145.b2068.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC75129; AAC75129; b2068.
BAA15926; BAA15926; BAA15926.
GeneID12930687.
947371.
KEGGecj:Y75_p2031.
eco:b2068.
PATRIC32119469. VBIEscCol129921_2145.

Organism-specific databases

EchoBASEEB1204.
EcoGeneEG11222. alkA.

Phylogenomic databases

eggNOGCOG0122.
HOGENOMHOG000221908.
KOK01247.
OMAQIKEKSM.
OrthoDBEOG61VZ6W.
PhylomeDBP04395.

Enzyme and pathway databases

BioCycEcoCyc:EG11222-MONOMER.
ECOL316407:JW2053-MONOMER.
MetaCyc:EG11222-MONOMER.

Gene expression databases

GenevestigatorP04395.

Family and domain databases

Gene3D1.10.1670.10. 1 hit.
1.10.340.30. 1 hit.
3.30.310.20. 1 hit.
InterProIPR010316. AlkA_N.
IPR000035. Alkylbase_DNA_glycsylse_CS.
IPR011257. DNA_glycosylase.
IPR003265. HhH-GPD_domain.
IPR023170. HTH_base_excis_C.
[Graphical view]
PfamPF06029. AlkA_N. 1 hit.
PF00730. HhH-GPD. 1 hit.
[Graphical view]
SMARTSM01009. AlkA_N. 1 hit.
SM00478. ENDO3c. 1 hit.
[Graphical view]
SUPFAMSSF48150. SSF48150. 1 hit.
PROSITEPS00516. ALKYLBASE_DNA_GLYCOS. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP04395.
PROP04395.

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: May 14, 2014
This is version 134 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Escherichia coli

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