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Reviewed, UniProtKB/Swiss-Prot P37685 (ALDB_ECOLI)

Last modified June 16, 2009. Version 66. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:
    Aldehyde dehydrogenase B
    EC=1.2.1.-
Gene names
Name: aldB
Synonyms: yiaX
Ordered Locus Names: b3588, JW3561
OrganismEscherichia coli (strain K12) [Complete proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length512 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Catalyzes the NADP-dependent oxidation of diverse aldehydes such as chloroacetaldehyde, acetaldehyde, propionaldehyde, benzaldehyde, mafosfamide, 4-hydroperoxycyclophosphamide. Its preferred substrates are acetaldehyde and chloroacetaldehyde.

Cofactor

Magnesium.

Enzyme regulation

Negatively regulated by fis. Positively regulated by rpoS and crp. Induced by ethanol. Expression is maximally induced during the transition from exponential phase to stationary phase.

Subunit structure

Homotetramer.

Miscellaneous

Does not use either glyceraldehyde or glycolaldehyde as substrates.

Sequence similarities

Belongs to the aldehyde dehydrogenase family.

biophysicochemical properties

Kinetic parameters:

the highest catalytic efficiency was observed with acetaldehyde.

KM=2.5 µM for acetaldehyde

KM=3.6 µM for chloroacetaldehyde

KM=5.8 µM for propionaldehyde

KM=56.8 µM for benzaldehyde

KM=900 µM for 4-hydroperoxycyclophosphamide

Vmax=2 µmol/min/mg enzyme with acetaldehyde as substrate

Vmax=3.3 µmol/min/mg enzyme with chloroacetaldehyde as substrate

Vmax=1 µmol/min/mg enzyme with propionaldehyde as substrate

Vmax=0.6 µmol/min/mg enzyme with benzaldehyde as substrate

Vmax=0.2 µmol/min/mg enzyme with 4-hydroperoxycyclophosphamide

Mass spectrometry

Molecular mass is 56352 Da from positions 1 - 512. Determined by MALDI. Ref.5

Ontologies

Keywords
   LigandMagnesium
NADP
   Molecular functionOxidoreductase
   Technical termComplete proteome
Direct protein sequencing
Gene Ontology (GO)
   Biological processoxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionmagnesium ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

oxidoreductase activity

Inferred from electronic annotation. Source: UniProtKB-KW

protein binding

Inferred from physical interaction. Source: IntAct

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

dnaKP0A6Y81EBI-1132062,EBI-542092

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 512512Aldehyde dehydrogenase B
PRO_0000056565

Sites

Active site2681 By similarity
Active site3071 By similarity

Experimental info

Mutagenesis1971R → E: Less than 10% of wild-type acetaldehyde dehydrogenase activity. Ref.5

Sequences

Sequence LengthMass (Da)Tools
P37685-1 [UniParc].

Last modified November 1, 1995. Version 2.
Checksum: E673C34340DF68CD

FASTA51256,306
        10         20         30         40         50         60 
MTNNPPSAQI KPGEYGFPLK LKARYDNFIG GEWVAPADGE YYQNLTPVTG QLLCEVASSG 

        70         80         90        100        110        120 
KRDIDLALDA AHKVKDKWAH TSVQDRAAIL FKIADRMEQN LELLATAETW DNGKPIRETS 

       130        140        150        160        170        180 
AADVPLAIDH FRYFASCIRA QEGGISEVDS ETVAYHFHEP LGVVGQIIPW NFPLLMASWK 

       190        200        210        220        230        240 
MAPALAAGNC VVLKPARLTP LSVLLLMEIV GDLLPPGVVN VVNGAGGVIG EYLATSKRIA 

       250        260        270        280        290        300 
KVAFTGSTEV GQQIMQYATQ NIIPVTLELG GKSPNIFFAD VMDEEDAFFD KALEGFALFA 

       310        320        330        340        350        360 
FNQGEVCTCP SRALVQESIY ERFMERAIRR VESIRSGNPL DSVTQMGAQV SHGQLETILN 

       370        380        390        400        410        420 
YIDIGKKEGA DVLTGGRRKL LEGELKDGYY LEPTILFGQN NMRVFQEEIF GPVLAVTTFK 

       430        440        450        460        470        480 
TMEEALELAN DTQYGLGAGV WSRNGNLAYK MGRGIQAGRV WTNCYHAYPA HAAFGGYKQS 

       490        500        510 
GIGRETHKMM LEHYQQTKCL LVSYSDKPLG LF 

« Hide

References

« Hide 'large scale' references
[1]"aldB, an RpoS-dependent gene in Escherichia coli encoding an aldehyde dehydrogenase that is repressed by Fis and activated by Crp."
Xu J., Johnson R.C.
J. Bacteriol. 177:3166-3175(1995) [PubMed: 7768815] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], TRANSCRIPTION REGULATION.
Strain: K12 / MG1655 / ATCC 47076.
[2]"Analysis of the Escherichia coli genome. V. DNA sequence of the region from 76.0 to 81.5 minutes."
Sofia H.J., Burland V., Daniels D.L., Plunkett G. III, Blattner F.R.
Nucleic Acids Res. 22:2576-2586(1994) [PubMed: 8041620] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[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]"Isolation and characterization of an aldehyde dehydrogenase encoded by the aldB gene of Escherichia coli."
Ho K.K., Weiner H.
J. Bacteriol. 187:1067-1073(2005) [PubMed: 15659684] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-10, CHARACTERIZATION, MASS SPECTROMETRY, MUTAGENESIS OF ARG-197.
Strain: K12 / DH5-alpha.

Cross-references

Sequence databases

L40742 Genomic DNA. Translation: AAC36939.1.
U00039 Genomic DNA. Translation: AAB18565.1. Different initiation.
U00096 Genomic DNA. Translation: AAC76612.1. Different initiation.
AP009048 Genomic DNA. Translation: BAE77705.1.
PIRS47809.
RefSeqAP_004204.1.
NP_418045.4.

3D structure databases

HSSPHSSP built from PDB template 1O04 based on UniProtKB P05091.
ModBaseSearch...

Protein-protein interaction databases

IntActP37685. 2 interactions.

Genome annotation databases

GeneID948104.
GenomeReviewsGene locus JW3561 in contig AP009048_GR.
Gene locus b3588 in contig U00096_GR.
KEGGecj:JW3561.
eco:b3588.

Organism-specific databases

EchoBASEEB2200.
EcoGeneEG12292. aldB.
CMRSearch...

Phylogenomic databases

HOGENOMP37685.
OMAP37685. INGQPFC.

Enzyme and pathway databases

BioCycEcoCyc:ALDDEHYDROGB-MON.
MetaCyc:ALDDEHYDROGB-MON.

Family and domain databases

InterProIPR016160. Ald_DH_CS.
IPR016162. Ald_DH_N.
IPR015590. Aldehyde_DH.
[Graphical view]
Gene3DG3DSA:3.40.605.10. Aldehyde_dehydrogenase_N. 1 hit.
PANTHERPTHR11699. Aldehyde_dehyd. 1 hit.
PfamPF00171. Aldedh. 1 hit.
[Graphical view]
PROSITEPS00070. ALDEHYDE_DEHYDR_CYS. 1 hit.
PS00687. ALDEHYDE_DEHYDR_GLU. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameALDB_ECOLI
AccessionPrimary (citable) accession number: P37685
Secondary accession number(s): P78118, Q2M7Q1
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: November 1, 1995
Last modified: June 16, 2009
This is version 66 of the entry and version 2 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

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