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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 17-Dec-2024

    Summary

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    Official Symbol
    adhE
    Official Full Name
    fused acetaldehyde-CoA dehydrogenase and iron-dependent alcohol dehydrogenasealdehyde/alcohol dehydrogenase AdhE
    Primary source
    ECOCYC:EG10031
    Locus tag
    b1241
    See related
    ASAP:ABE-0004164
    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. Monoclonal antibodies to spirosin of Yersinia enterocolitica and analysis of the localization of spirosome by use of them. Yamato M, et al. Microbiol Immunol, 1994. PMID 7521508
    2. Novel antioxidant role of alcohol dehydrogenase E from Escherichia coli. Echave P, et al. J Biol Chem, 2003 Aug 8. PMID 12783863
    3. Aerobic activity of Escherichia coli alcohol dehydrogenase is determined by a single amino acid. Holland-Staley CA, et al. J Bacteriol, 2000 Nov. PMID 11029424, Free PMC Article
    4. Evolution of the adhE gene product of Escherichia coli from a functional reductase to a dehydrogenase. Genetic and biochemical studies of the mutant proteins. Membrillo-Hernandez J, et al. J Biol Chem, 2000 Oct 27. PMID 10922373
    5. Regulation of adhE (encoding ethanol oxidoreductase) by the Fis protein in Escherichia coli. Membrillo-Hernández J, et al. J Bacteriol, 1999 Dec. PMID 10572146, Free PMC Article

    See all (62) 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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    Homology

    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 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 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 
    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
    Heading Accession and Version

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