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Reviewed, UniProtKB/Swiss-Prot P05050 (ALKB_ECOLI)

Last modified June 16, 2009. Version 78. 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 · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Alpha-ketoglutarate-dependent dioxygenase alkB
    EC=1.14.11.-
Alternative name(s):
    Alkylated DNA repair protein alkB
Gene names
Name: alkB
Synonyms: aidD
Ordered Locus Names: b2212, JW2200
OrganismEscherichia coli (strain K12) [Complete proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length216 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Dioxygenase that repairs alkylated DNA and RNA containing 1-methyladenine and 3-methylcytosine by oxidative demethylation. Accepts double-stranded and single-stranded substrates. Requires molecular oxygen, alpha-ketoglutarate and iron. Provides extensive resistance to alkylating agents such as MMS and DMS (SN2 agents), but not to MMNG and MNU (SN1 agents). Ref.8

Cofactor

Binds 1 Fe2+ ion per subunit.

Sequence similarities

Belongs to the alkB family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 216216Alpha-ketoglutarate-dependent dioxygenase alkB
PRO_0000066665

Regions

Region76 – 783Substrate binding
Region204 – 2107Alpha-ketoglutarate binding

Sites

Metal binding1311Iron; catalytic
Metal binding1331Iron; catalytic
Metal binding1871Iron; catalytic
Binding site691Substrate
Binding site1201Alpha-ketoglutarate
Binding site1221Alpha-ketoglutarate
Binding site1351Substrate

Secondary structure

.................................. 216
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P05050-1 [UniParc].

Last modified August 13, 1987. Version 1.
Checksum: 494FE1E70EABD278

FASTA21624,076
        10         20         30         40         50         60 
MLDLFADAEP WQEPLAAGAV ILRRFAFNAA EQLIRDINDV ASQSPFRQMV TPGGYTMSVA 

        70         80         90        100        110        120 
MTNCGHLGWT THRQGYLYSP IDPQTNKPWP AMPQSFHNLC QRAATAAGYP DFQPDACLIN 

       130        140        150        160        170        180 
RYAPGAKLSL HQDKDEPDLR APIVSVSLGL PAIFQFGGLK RNDPLKRLLL EHGDVVVWGG 

       190        200        210 
ESRLFYHGIQ PLKAGFHPLT IDCRYNLTFR QAGKKE 

« Hide

References

« Hide 'large scale' references
[1]"Structure and expression of the alkB gene of Escherichia coli related to the repair of alkylated DNA."
Kondo H., Nakabeppu Y., Kataoka H., Kuhara S., Kawabata S., Sekiguchi M.
J. Biol. Chem. 261:15772-15777(1986) [PubMed: 3536913] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-30.
[2]"Automated multiplex sequencing of the E.coli genome."
Richterich P., Lakey N., Gryan G., Jaehn L., Mintz L., Robison K., Church G.M.
Submitted (OCT-1993) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / BHB2600.
[3]"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.
[4]"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.
[5]"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.
[6]"Active site and complete sequence of the suicidal methyltransferase that counters alkylation mutagenesis."
Demple B., Sedgwick B., Robins P., Totty N., Waterfield M.D., Lindahl T.
Proc. Natl. Acad. Sci. U.S.A. 82:2688-2692(1985) [PubMed: 3887409] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-53.
Strain: B.
[7]"The Escherichia coli AlkB protein protects human cells against alkylation-induced toxicity."
Chen B.J., Carroll P., Samson L.
J. Bacteriol. 176:6255-6261(1994) [PubMed: 7928996] [Abstract]
Cited for: CHARACTERIZATION.
[8]"Human and bacterial oxidative demethylases repair alkylation damage in both RNA and DNA."
Aas P.A., Otterlei M., Falnes P.O., Vaagboe C.B., Skorpen F., Akbari M., Sundheim O., Bjoeraas M., Slupphaug G., Seeberg E., Krokan H.E.
Nature 421:859-863(2003) [PubMed: 12594517] [Abstract]
Cited for: FUNCTION.
[9]"Crystal structures of catalytic complexes of the oxidative DNA/RNA repair enzyme AlkB."
Yu B., Edstrom W.C., Benach J., Hamuro Y., Weber P.C., Gibney B.R., Hunt J.F.
Nature 439:879-884(2006) [PubMed: 16482161] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 12-216 IN COMPLEX WITH SUBSTRATE; ALPHA-KETOGLUTARATE AND IRON.
+Additional computationally mapped references.

Cross-references

Sequence databases

J02607 Genomic DNA. Translation: AAA23416.1.
U00008 Genomic DNA. Translation: AAA16409.1.
U00096 Genomic DNA. Translation: AAC75272.1.
AP009048 Genomic DNA. Translation: BAA15995.1.
M10315 Genomic DNA. Translation: AAA23414.1.
PIRBVECKB. A24605.
RefSeqAP_002808.1.
NP_416716.1.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
2FD8X-ray2.30A12-216[»]
2FDFX-ray2.10A12-216[»]
2FDGX-ray2.20A12-216[»]
2FDHX-ray2.10A12-216[»]
2FDIX-ray1.80A12-216[»]
2FDJX-ray2.10A12-216[»]
2FDKX-ray2.30A12-216[»]
3BI3X-ray1.90A13-213[»]
3BIEX-ray1.68A13-214[»]
3BKZX-ray1.65A14-214[»]
ModBaseSearch...

Protein-protein interaction databases

DIPDIP:9085N.

Genome annotation databases

GeneID946708.
GenomeReviewsGene locus JW2200 in contig AP009048_GR.
Gene locus b2212 in contig U00096_GR.
KEGGecj:JW2200.
eco:b2212.

Organism-specific databases

EchoBASEEB0036.
EcoGeneEG10037. alkB.
CMRSearch...

Phylogenomic databases

HOGENOMP05050.
OMAP05050. MVTPGGF.

Enzyme and pathway databases

BioCycEcoCyc:EG10037-MON.
MetaCyc:EG10037-MON.

Family and domain databases

InterProIPR004574. Alkb.
IPR005123. Oxoglutarate/Fe-dep_Oase.
[Graphical view]
PfamPF03171. 2OG-FeII_Oxy. 1 hit.
[Graphical view]
TIGRFAMsTIGR00568. alkb. 1 hit.
ProtoNetSearch...

Entry information

Entry nameALKB_ECOLI
AccessionPrimary (citable) accession number: P05050
Entry history
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: August 13, 1987
Last modified: June 16, 2009
This is version 78 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 · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents