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P04395

- 3MG2_ECOLI

UniProt

P04395 - 3MG2_ECOLI

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Protein
DNA-3-methyladenine glycosylase 2
Gene
alkA, aidA, b2068, JW2053
Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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 activityi

Hydrolysis of alkylated DNA, releasing 3-methyladenine, 3-methylguanine, 7-methylguanine and 7-methyladenine.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei218 – 2181Determinant for substrate specificity and/or activity
Active sitei238 – 2381Proton acceptor

GO - Molecular functioni

  1. DNA-3-methyladenine glycosylase activity Source: UniProtKB-EC
  2. DNA-3-methylguanine glycosylase activity Source: UniProtKB-EC
  3. DNA-7-methyladenine glycosylase activity Source: UniProtKB-EC
  4. DNA-7-methylguanine glycosylase activity Source: UniProtKB-EC
  5. alkylbase DNA N-glycosylase activity Source: EcoliWiki
Complete GO annotation...

GO - Biological processi

  1. DNA dealkylation involved in DNA repair Source: EcoliWiki
  2. DNA repair Source: EcoliWiki
  3. base-excision repair Source: EcoliWiki
  4. cellular response to DNA damage stimulus Source: EcoliWiki
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

DNA damage, DNA repair

Enzyme and pathway databases

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

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:alkA
Synonyms:aidA
Ordered Locus Names:b2068, JW2053
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG11222. alkA.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: EcoliWiki
Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi124 – 1241Q → A: Methylmethane sulfonate-resistant.
Mutagenesisi218 – 2181W → A: No catalytic activity, methylmethane sulfonate-sensitive.
Mutagenesisi237 – 2371D → N: More than 30% catalytic activity, methylmethane sulfonate-resistant.
Mutagenesisi238 – 2381D → N: No catalytic activity, methylmethane sulfonate-sensitive.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 282282DNA-3-methyladenine glycosylase 2
PRO_0000194878Add
BLAST

Expressioni

Inductioni

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

Gene expression databases

GenevestigatoriP04395.

Interactioni

Subunit structurei

Monomer.

Binary interactionsi

WithEntry#Exp.IntActNotes
aceFP069591EBI-544077,EBI-542707

Protein-protein interaction databases

DIPiDIP-9084N.
IntActiP04395. 19 interactions.
MINTiMINT-1227621.
STRINGi511145.b2068.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 54
Helixi12 – 2211
Turni25 – 273
Beta strandi28 – 303
Beta strandi35 – 417
Beta strandi44 – 5310
Turni54 – 574
Beta strandi58 – 636
Helixi65 – 706
Helixi71 – 8212
Turni83 – 853
Helixi88 – 958
Helixi96 – 994
Helixi113 – 12210
Turni123 – 1253
Helixi128 – 14215
Beta strandi149 – 1535
Helixi158 – 1625
Helixi166 – 1716
Helixi176 – 19015
Helixi202 – 2098
Helixi217 – 22711
Helixi239 – 2446
Beta strandi245 – 2473
Helixi250 – 2578
Helixi258 – 2603
Helixi264 – 2729

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
ProteinModelPortaliP04395.
SMRiP04395. Positions 1-282.

Miscellaneous databases

EvolutionaryTraceiP04395.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0122.
HOGENOMiHOG000221908.
KOiK01247.
OMAiQIKEKSM.
OrthoDBiEOG61VZ6W.
PhylomeDBiP04395.

Family and domain databases

Gene3Di1.10.1670.10. 1 hit.
1.10.340.30. 1 hit.
3.30.310.20. 1 hit.
InterProiIPR010316. AlkA_N.
IPR000035. Alkylbase_DNA_glycsylse_CS.
IPR011257. DNA_glycosylase.
IPR003265. HhH-GPD_domain.
IPR023170. HTH_base_excis_C.
[Graphical view]
PfamiPF06029. AlkA_N. 1 hit.
PF00730. HhH-GPD. 1 hit.
[Graphical view]
SMARTiSM01009. AlkA_N. 1 hit.
SM00478. ENDO3c. 1 hit.
[Graphical view]
SUPFAMiSSF48150. SSF48150. 1 hit.
PROSITEiPS00516. ALKYLBASE_DNA_GLYCOS. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P04395-1 [UniParc]FASTAAdd to Basket

« Hide

MYTLNWQPPY DWSWMLGFLA ARAVSSVETV ADSYYARSLA VGEYRGVVTA    50
IPDIARHTLH INLSAGLEPV AAECLAKMSR LFDLQCNPQI VNGALGRLGA 100
ARPGLRLPGC VDAFEQGVRA ILGQLVSVAM AAKLTARVAQ LYGERLDDFP 150
EYICFPTPQR LAAADPQALK ALGMPLKRAE ALIHLANAAL EGTLPMTIPG 200
DVEQAMKTLQ TFPGIGRWTA NYFALRGWQA KDVFLPDDYL IKQRFPGMTP 250
AQIRRYAERW KPWRSYALLH IWYTEGWQPD EA 282
Length:282
Mass (Da):31,393
Last modified:March 20, 1987 - v1
Checksum:iB66BB5E23019899C
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
K02498 Genomic DNA. Translation: AAA23430.1.
U00096 Genomic DNA. Translation: AAC75129.1.
AP009048 Genomic DNA. Translation: BAA15926.1.
M13827 Genomic DNA. No translation available.
PIRiA00904. DGECMA.
RefSeqiNP_416572.1. NC_000913.3.
YP_490310.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC75129; AAC75129; b2068.
BAA15926; BAA15926; BAA15926.
GeneIDi12930687.
947371.
KEGGiecj:Y75_p2031.
eco:b2068.
PATRICi32119469. VBIEscCol129921_2145.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
K02498 Genomic DNA. Translation: AAA23430.1 .
U00096 Genomic DNA. Translation: AAC75129.1 .
AP009048 Genomic DNA. Translation: BAA15926.1 .
M13827 Genomic DNA. No translation available.
PIRi A00904. DGECMA.
RefSeqi NP_416572.1. NC_000913.3.
YP_490310.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1DIZ X-ray 2.50 A/B 1-282 [» ]
1MPG X-ray 1.80 A/B 1-282 [» ]
1PVS X-ray 2.40 A/B 1-282 [» ]
3CVS X-ray 2.40 A/B/C/D 1-282 [» ]
3CVT X-ray 2.50 A/B/C/D 1-282 [» ]
3CW7 X-ray 2.30 A/B/C/D 1-282 [» ]
3CWA X-ray 2.40 A/B/C/D 1-282 [» ]
3CWS X-ray 2.30 A/B/C/D 1-282 [» ]
3CWT X-ray 2.30 A/B/C/D 1-282 [» ]
3CWU X-ray 2.80 A/B/C/D 1-282 [» ]
3D4V X-ray 2.90 A/B/C/D 1-282 [» ]
3OGD X-ray 2.80 A 2-282 [» ]
3OH6 X-ray 2.89 A 2-282 [» ]
3OH9 X-ray 2.80 A 2-282 [» ]
ProteinModelPortali P04395.
SMRi P04395. Positions 1-282.
ModBasei Search...

Protein-protein interaction databases

DIPi DIP-9084N.
IntActi P04395. 19 interactions.
MINTi MINT-1227621.
STRINGi 511145.b2068.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC75129 ; AAC75129 ; b2068 .
BAA15926 ; BAA15926 ; BAA15926 .
GeneIDi 12930687.
947371.
KEGGi ecj:Y75_p2031.
eco:b2068.
PATRICi 32119469. VBIEscCol129921_2145.

Organism-specific databases

EchoBASEi EB1204.
EcoGenei EG11222. alkA.

Phylogenomic databases

eggNOGi COG0122.
HOGENOMi HOG000221908.
KOi K01247.
OMAi QIKEKSM.
OrthoDBi EOG61VZ6W.
PhylomeDBi P04395.

Enzyme and pathway databases

BioCyci EcoCyc:EG11222-MONOMER.
ECOL316407:JW2053-MONOMER.
MetaCyc:EG11222-MONOMER.

Miscellaneous databases

EvolutionaryTracei P04395.
PROi P04395.

Gene expression databases

Genevestigatori P04395.

Family and domain databases

Gene3Di 1.10.1670.10. 1 hit.
1.10.340.30. 1 hit.
3.30.310.20. 1 hit.
InterProi IPR010316. AlkA_N.
IPR000035. Alkylbase_DNA_glycsylse_CS.
IPR011257. DNA_glycosylase.
IPR003265. HhH-GPD_domain.
IPR023170. HTH_base_excis_C.
[Graphical view ]
Pfami PF06029. AlkA_N. 1 hit.
PF00730. HhH-GPD. 1 hit.
[Graphical view ]
SMARTi SM01009. AlkA_N. 1 hit.
SM00478. ENDO3c. 1 hit.
[Graphical view ]
SUPFAMi SSF48150. SSF48150. 1 hit.
PROSITEi PS00516. ALKYLBASE_DNA_GLYCOS. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  3. 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).

Entry informationi

Entry namei3MG2_ECOLI
AccessioniPrimary (citable) accession number: P04395
Entry historyi
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 statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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