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    ebgC DUF386 domain-containing evolved beta-D-galactosidase subunit beta [ Escherichia coli str. K-12 substr. MG1655 ]

    Gene ID: 947581, updated on 3-Dec-2024

    Summary

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    Official Symbol
    ebgC
    Official Full Name
    DUF386 domain-containing evolved beta-D-galactosidase subunit beta
    Primary source
    ECOCYC:EG10253
    Locus tag
    b3077
    See related
    ASAP:ABE-0010106
    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
    ECK3067
    Summary
    EbgC is required for full activity: it has been suggested to be involved in the rate-limiting degalactosylation step and/or in electrophilic catalysis by the EbgA active site Mg(2+). [More information is available at EcoGene: EG10253]. The EbgA-EbgC complex represents the second -D-galactosidase enzyme in Escherichia coli. [More information is available at EcoCyc: EG10253].
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    Genomic context

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    Sequence:
    NC_000913.3 (3225722..3226171)

    NC_000913.3Genomic Context describing neighboring genes Neighboring gene putative tRNA-binding protein YgjH Neighboring gene DNA-binding transcriptional repressor EbgR Neighboring gene evolved beta-D-galactosidase subunit alpha Neighboring gene putative transporter YgjI Neighboring gene protein YgjJ

    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. Large changes of transition-state structure during experimental evolution of an enzyme. Srinivasan K, et al. Biochem J, 1993 Apr 1. PMID 8471034, Free PMC Article
    2. The catalytic consequences of experimental evolution. Studies on the subunit structure of the second (ebg) beta-galactosidase of Escherichia coli, and on catalysis by ebgab, an experimental evolvant containing two amino acid substitutions. Elliott AC, et al. Biochem J, 1992 Feb 15. PMID 1540130, Free PMC Article
    3. The catalytic consequences of experimental evolution. Transition-state structure during catalysis by the evolved beta-galactosidases of Escherichia coli (ebg enzymes) changed by a single mutational event. Li BF, et al. Biochem J, 1989 May 15. PMID 2505746, Free PMC Article
    4. Catalysis by the large subunit of the second beta-galactosidase of Escherichia coli in the absence of the small subunit. Calugaru SV, et al. Biochem J, 1995 Nov 15. PMID 7492325, Free PMC Article
    5. Evolutionary potential of the ebgA gene. Hall BG. Mol Biol Evol, 1995 May. PMID 7739392

    See all (18) citations in PubMed

    GeneRIFs: Gene References Into Functions

    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

    Process Evidence Code Pubs
    involved_in single-species biofilm formation IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    Component Evidence Code Pubs
    is_active_in cytosol IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  

    General protein information

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    Preferred Names
    DUF386 domain-containing evolved beta-D-galactosidase subunit beta

    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
      3225722..3226171
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NP_417548.1 DUF386 domain-containing evolved beta-D-galactosidase subunit beta [Escherichia coli str. K-12 substr. MG1655]

      See identical proteins and their annotated locations for NP_417548.1

      Status: PROVISIONAL

      UniProtKB/TrEMBL
      A0A6N0IM52
      Conserved Domains (1) summary
      PRK10202
      Location:1 → 149
      ebgC; beta-galactosidase subunit beta
    Nucleotide Protein
    Heading Accession and Version

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