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adhE fused acetaldehyde-CoA dehydrogenase and iron-dependent alcohol dehydrogenasealdehyde/alcohol dehydrogenase AdhE [ Escherichia coli str. K-12 substr. MG1655 ]

Gene ID: 945837, updated on 11-Apr-2024

Summary

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Gene symbol
adhE
Gene description
fused acetaldehyde-CoA dehydrogenase and iron-dependent alcohol dehydrogenasealdehyde/alcohol dehydrogenase AdhE
Primary source
ASAP:ABE-0004164
Locus tag
b1241
See related
ECOCYC:EG10031
Gene type
protein coding
RefSeq status
PROVISIONAL
Organism
Escherichia coli str. K-12 substr. MG1655 (strain: K-12, substrain: MG1655)
Lineage
Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia
Also known as
adhC; ana; ECK1235
Summary
The reported PFL deactivase activity of AdhE (Kessler, 1991, 1992) could not be reproduced (Nnyepi, 2007). [More information is available at EcoGene: EG10031]. A homopolymeric protein with three Fe++-dependent catalytic functions: alcohol dehydrogenase, acetaldehyde dehydrogenase and pyruvate formate-lyase deactivase. [More information is available at EcoCyc: EG10031].
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Genomic context

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Sequence:
NC_000913.3 (1295446..1298121, complement)

NC_000913.3Genomic Context describing neighboring genes Neighboring gene thymidine/deoxyuridine kinase Neighboring gene pseudo Neighboring gene protein YchT Neighboring gene MarC family putative inner membrane protein YchE

Genomic regions, transcripts, and products

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Genomic Sequence:
NC_000913.3

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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Related articles in PubMed

  1. Filamentation of the bacterial bi-functional alcohol/aldehyde dehydrogenase AdhE is essential for substrate channeling and enzymatic regulation. Pony P, et al. Nat Commun, 2020 Mar 18. PMID 32188856, Free PMC Article
  2. Aldehyde-alcohol dehydrogenase forms a high-order spirosome architecture critical for its activity. Kim G, et al. Nat Commun, 2019 Oct 4. PMID 31586059, Free PMC Article
  3. Inactivation of E. coli pyruvate formate-lyase: role of AdhE and small molecules. Nnyepi MR, et al. Arch Biochem Biophys, 2007 Mar 1. PMID 17280641, Free PMC Article
  4. Indole-3-acetic acid regulates the central metabolic pathways in Escherichia coli. Bianco C, et al. Microbiology (Reading), 2006 Aug. PMID 16849805
  5. Novel antioxidant role of alcohol dehydrogenase E from Escherichia coli. Echave P, et al. J Biol Chem, 2003 Aug 8. PMID 12783863

See all (63) citations in PubMed

GeneRIFs: Gene References Into Functions

What's a GeneRIF?
  1. AdhE filamentation is essential for its activity in vitro and function in vivo.
    Title: Filamentation of the bacterial bi-functional alcohol/aldehyde dehydrogenase AdhE is essential for substrate channeling and enzymatic regulation.
  2. Study presents the atomic resolution structure of AdhE from Escherichia coli K12 strain and suggests that the high-order helical structure regulates its enzymatic activity.
    Title: Aldehyde-alcohol dehydrogenase forms a high-order spirosome architecture critical for its activity.
  3. Deletion of the E. coli adhE gene (together with deletions of other ferementation disruption genes) increased production of succinate
    Title: Eliminating side products and increasing succinate yields in engineered strains of Escherichia coli C.
  4. N-terminus verified by Edman degradation on mature peptide
    Title: Cloning and sequence analysis of the fermentative alcohol-dehydrogenase-encoding gene of Escherichia coli.
  5. Our results demonstrate that AdhE is not a PFL deactivating enzyme.
    Title: Inactivation of E. coli pyruvate formate-lyase: role of AdhE and small molecules.
Submit: New GeneRIF Correction

Interactions

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Products Interactant Other Gene Complex Source Pubs Description

General gene information

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Gene Ontology Provided by EcoCyc

Function Evidence Code Pubs
enables acetaldehyde dehydrogenase (acetylating) activity IDA
Inferred from Direct Assay
more info
 PubMed 
enables acetaldehyde dehydrogenase (acetylating) activity IEA
Inferred from Electronic Annotation
more info
  
enables acetaldehyde dehydrogenase (acetylating) activity IMP
Inferred from Mutant Phenotype
more info
 PubMed 
enables alcohol dehydrogenase (NAD+) activity IBA
Inferred from Biological aspect of Ancestor
more info
  
enables alcohol dehydrogenase (NAD+) activity IEA
Inferred from Electronic Annotation
more info
  
enables alcohol dehydrogenase (NAD+) activity IMP
Inferred from Mutant Phenotype
more info
 PubMed 
enables alcohol dehydrogenase (NAD+) activity, iron-dependent IDA
Inferred from Direct Assay
more info
 PubMed 
enables alcohol dehydrogenase [NAD(P)+] activity IEA
Inferred from Electronic Annotation
more info
  
enables catalytic activity IEA
Inferred from Electronic Annotation
more info
  
enables ferrous iron binding IDA
Inferred from Direct Assay
more info
 PubMed 
enables identical protein binding IPI
Inferred from Physical Interaction
more info
 PubMed 
enables metal ion binding IEA
Inferred from Electronic Annotation
more info
  
enables oxidoreductase activity IEA
Inferred from Electronic Annotation
more info
  
enables oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor IEA
Inferred from Electronic Annotation
more info
  
enables oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor IEA
Inferred from Electronic Annotation
more info
  
enables protein binding IPI
Inferred from Physical Interaction
more info
 PubMed 
Process Evidence Code Pubs
involved_in alcohol metabolic process IEA
Inferred from Electronic Annotation
more info
  
involved_in carbon utilization IEA
Inferred from Electronic Annotation
more info
  
acts_upstream_of_or_within ethanol biosynthetic process IDA
Inferred from Direct Assay
more info
 PubMed 
involved_in metabolic process IEA
Inferred from Electronic Annotation
more info
  
acts_upstream_of_or_within mixed acid fermentation IMP
Inferred from Mutant Phenotype
more info
 PubMed 
acts_upstream_of_or_within protein homooligomerization IDA
Inferred from Direct Assay
more info
 PubMed 
acts_upstream_of_or_within response to oxidative stress IMP
Inferred from Mutant Phenotype
more info
 PubMed 
Component Evidence Code Pubs
located_in cytosol HDA PubMed 
located_in cytosol IDA
Inferred from Direct Assay
more info
 PubMed 
located_in membrane HDA PubMed 

General protein information

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Preferred Names
fused acetaldehyde-CoA dehydrogenase and iron-dependent alcohol dehydrogenasealdehyde/alcohol dehydrogenase AdhE
NP_415757.1

NCBI Reference Sequences (RefSeq)

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Genome Annotation

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference assembly

Genomic

  1. NC_000913.3 Reference assembly

    Range
    1295446..1298121 complement
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. NP_415757.1 fused acetaldehyde-CoA dehydrogenase and iron-dependent alcohol dehydrogenasealdehyde/alcohol dehydrogenase AdhE [Escherichia coli str. K-12 substr. MG1655]

    See identical proteins and their annotated locations for NP_415757.1

    Status: PROVISIONAL

    UniProtKB/TrEMBL
    A0A376X1B9, A0A418GRX9, A0A7A6R2I0, W1X0G4
    Conserved Domains (1) summary
    PRK13805
    Location:1 → 862
    PRK13805; bifunctional acetaldehyde-CoA/alcohol dehydrogenase; Provisional
Nucleotide Protein
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