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    eutB ethanolamine ammonia-lyase subunit alpha [ Escherichia coli str. K-12 substr. MG1655 ]

    Gene ID: 946924, updated on 17-Dec-2024

    Summary

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    Official Symbol
    eutB
    Official Full Name
    ethanolamine ammonia-lyase subunit alpha
    Primary source
    ECOCYC:EG50006
    Locus tag
    b2441
    See related
    ASAP:ABE-0008046
    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
    ECK2436
    Summary
    EutBC deaminates amino-alcohols (ethanolamine) to oxo compounds (acetaldehyde) and ammonia. [More information is available at EcoGene: EG50006]. EutB codes for the larger subunit, which probably serves in a regulatory function. [More information is available at EcoCyc: EG50006].
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    Genomic context

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    Sequence:
    NC_000913.3 (2557318..2558679, complement)

    NC_000913.3Genomic Context describing neighboring genes Neighboring gene putative structural protein, ethanolamine utilization microcompartment Neighboring gene ethanolamine ammonia-lyase subunit beta Neighboring gene putative phage integrase IntZ Neighboring gene uncharacterized protein YffL

    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. Crystal structures of ethanolamine ammonia-lyase complexed with coenzyme B12 analogs and substrates. Shibata N, et al. J Biol Chem, 2010 Aug 20. PMID 20519496, Free PMC Article
    2. Microbial metabolism of amino alcohols. Purification and properties of coenzyme B12-dependent ethanolamine ammonia-lyase of Escherichia coli. Blackwell CM, et al. Biochem J, 1978 Nov 1. PMID 33657, Free PMC Article
    3. Direct Participation of a Peripheral Side Chain of a Corrin Ring in Coenzyme B(12) Catalysis. Shibata N, et al. Angew Chem Int Ed Engl, 2018 Jun 25. PMID 29797764
    4. Microbial metabolism of amino alcohols. Control of formation and stability of partially purified ethanolamine ammonia-lyase in Escherichia coli. Blackwell CM, et al. J Gen Microbiol, 1977 Jan. PMID 319195
    5. Microbial metabolism of amino alcohols. Formation of coenzyme B12-dependent ethanolamine ammonia-lyase and its concerted induction in Escherichia coli. Blackwell CM, et al. Biochem J, 1978 Dec 15. PMID 371614, Free PMC Article

    See all (21) citations in PubMed

    GeneRIFs: Gene References Into Functions

    What's a GeneRIF?
    1. The binary complex of the truncated enzyme with cyanocobalamin and the ternary complex with cyanocobalamin or adeninylpentylcobalamin and substrates were crystallized, and their x-ray structures were analyzed
      Title: Crystal structures of ethanolamine ammonia-lyase complexed with coenzyme B12 analogs and substrates.
    2. N-terminus verified by Edman degradation on complete protein
      Title: Cloning, sequencing, and expression of the genes encoding the adenosylcobalamin-dependent ethanolamine ammonia-lyase of Salmonella typhimurium.
    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 cobalamin binding IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables ethanolamine ammonia-lyase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables lyase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    Process Evidence Code Pubs
    involved_in amino acid metabolic process IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in ethanolamine catabolic process IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    involved_in ethanolamine catabolic process IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    involved_in ethanolamine catabolic process IEA
    Inferred from Electronic Annotation
    more info
    		  
    Component Evidence Code Pubs
    located_in bacterial microcompartment IEA
    Inferred from Electronic Annotation
    more info
    		  
    is_active_in cytosol IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    located_in cytosol IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    part_of ethanolamine ammonia-lyase complex IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    part_of ethanolamine ammonia-lyase complex IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    part_of ethanolamine ammonia-lyase complex IEA
    Inferred from Electronic Annotation
    more info
    		  
    part_of ethanolamine ammonia-lyase complex IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    part_of ethanolamine ammonia-lyase complex IPI
    Inferred from Physical Interaction
    more info
    		 PubMed 
    located_in ethanolamine degradation polyhedral organelle IEA
    Inferred from Electronic Annotation
    more info
    		  

    General protein information

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    Preferred Names
    ethanolamine ammonia-lyase subunit alpha
    NP_416936.4

    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
      2557318..2558679 complement
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NP_416936.4 ethanolamine ammonia-lyase subunit alpha [Escherichia coli str. K-12 substr. MG1655]

      See identical proteins and their annotated locations for NP_416936.4

      Status: PROVISIONAL

      UniProtKB/TrEMBL
      A0A3K0ZYS6
      Conserved Domains (1) summary
      COG4303
      Location:1 → 453
      EutB; Ethanolamine ammonia-lyase, large subunit [Amino acid transport and metabolism]
    Nucleotide Protein
    Heading Accession and Version

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