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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
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