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    aceF pyruvate dehydrogenase, E2 subunit [ Escherichia coli str. K-12 substr. MG1655 ]

    Gene ID: 944794, updated on 4-Apr-2024

    Summary

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    Gene symbol
    aceF
    Gene description
    pyruvate dehydrogenase, E2 subunit
    Primary source
    ASAP:ABE-0000400
    Locus tag
    b0115
    See related
    ECOCYC:EG10025
    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
    ECK0114
    Summary
    Holoenzyme is AceE(24)+AceF(24)+Lpd(12). [More information is available at EcoGene: EG10025]. AceF, the "E2" or "core" component of the pyruvate dehydrogenase multienzyme complex, assembles into a 24-subunit cube . [More information is available at EcoCyc: EG10025].
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    Genomic context

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    Sequence:
    NC_000913.3 (125695..127587)

    NC_000913.3Genomic Context describing neighboring genes Neighboring gene DNA-binding transcriptional dual regulator PdhR Neighboring gene pyruvate dehydrogenase E1 component Neighboring gene lipoamide dehydrogenase Neighboring gene DUF3300 domain-containing protein YacH

    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. [Research progress of ERIC (IRU)]. Lin ZH, et al. Wei Sheng Wu Xue Bao, 2007 Apr. PMID 17552253
    2. Histidine 407, a phantom residue in the E1 subunit of the Escherichia coli pyruvate dehydrogenase complex, activates reductive acetylation of lipoamide on the E2 subunit. An explanation for conservation of active sites between the E1 subunit and transketolase. Nemeria N, et al. Biochemistry, 2002 Dec 31. PMID 12501174
    3. Identification of the E2-binding residues in the N-terminal domain of E1 of a prokaryotic pyruvate dehydrogenase complex. Hengeveld AF, et al. FEBS Lett, 2002 Jul 3. PMID 12095640
    4. Restricted motion of the lipoyl-lysine swinging arm in the pyruvate dehydrogenase complex of Escherichia coli. Jones DD, et al. Biochemistry, 2000 Jul 25. PMID 10913250
    5. Primary biliary cirrhosis: an orchestrated immune response against epithelial cells. Gershwin ME, et al. Immunol Rev, 2000 Apr. PMID 10807518

    See all (86) citations in PubMed

    GeneRIFs: Gene References Into Functions

    What's a GeneRIF?
    1. Dimerization of a 5-kDa domain defines the architecture of the 5-MDa gammaproteobacterial pyruvate dehydrogenase complex.
      Title: Dimerization of a 5-kDa domain defines the architecture of the 5-MDa gammaproteobacterial pyruvate dehydrogenase complex.
    2. The inclusion of each additional domain of E2p strengthened the interaction with E1p, and the interaction was strongest with intact E2p.
      Title: Structure and function of the catalytic domain of the dihydrolipoyl acetyltransferase component in Escherichia coli pyruvate dehydrogenase complex.
    3. The surface loop of E1o is important to the structural integrity of the protein and together with Thr42 plays an important role in specifying the interaction of the lipoyl domain with its partner E1o in the E. coli 2OGDH complex.
      Title: The role of loop and beta-turn residues as structural and functional determinants for the lipoyl domain from the Escherichia coli 2-oxoglutarate dehydrogenase complex.
    4. N-terminus verified by Edman degradation on mature peptide
      Title: Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12.
    5. the dynamic loop at the active center of the Escherichia coli pyruvate dehydrogenase complex E1 component modulates substrate utilization and chemical communication with the E2 component
      Title: A dynamic loop at the active center of the Escherichia coli pyruvate dehydrogenase complex E1 component modulates substrate utilization and chemical communication with the E2 component.
    6. Pyruvate dehydrogenase complex E2 (PDHc-E2)subunit protects N-terminal residues 1-55 of PDHc-E1 subunit selectively from trypsin digestion.
      Title: Amino-terminal residues 1-45 of the Escherichia coli pyruvate dehydrogenase complex E1 subunit interact with the E2 subunit and are required for activity of the complex but not for reductive acetylation of the E2 subunit.
    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 acetyltransferase activity IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    enables acyltransferase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables dihydrolipoyllysine-residue acetyltransferase activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables dihydrolipoyllysine-residue acetyltransferase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables lipoic acid binding IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    enables lipoic acid binding IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables protein binding IPI
    Inferred from Physical Interaction
    more info
    		 PubMed 
    contributes_to pyruvate dehydrogenase activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables transferase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    Process Evidence Code Pubs
    involved_in acetyl-CoA biosynthetic process from pyruvate IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    acts_upstream_of_or_within acetyl-CoA biosynthetic process from pyruvate IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    involved_in glycolytic process IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in pyruvate catabolic process NAS
    Non-traceable Author Statement
    more info
    		 PubMed 
    acts_upstream_of_or_within pyruvate metabolic process IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    Component Evidence Code Pubs
    located_in cytoplasm HDA PubMed 
    is_active_in cytoplasm IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    located_in cytoplasm IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    located_in cytoplasm IEA
    Inferred from Electronic Annotation
    more info
    		  
    part_of pyruvate dehydrogenase complex IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    part_of pyruvate dehydrogenase complex IEA
    Inferred from Electronic Annotation
    more info
    		  
    part_of pyruvate dehydrogenase complex IGI
    Inferred from Genetic Interaction
    more info
    		 PubMed 
    part_of pyruvate dehydrogenase complex NAS
    Non-traceable Author Statement
    more info
    		 PubMed 

    General protein information

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    Preferred Names
    pyruvate dehydrogenase, E2 subunit
    NP_414657.1

    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
      125695..127587
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NP_414657.1 pyruvate dehydrogenase, E2 subunit [Escherichia coli str. K-12 substr. MG1655]

      See identical proteins and their annotated locations for NP_414657.1

      Status: PROVISIONAL

      UniProtKB/TrEMBL
      A0A7M3TR39
      Conserved Domains (1) summary
      PRK11854
      Location:1 → 630
      aceF; pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
    Nucleotide Protein
    Heading Accession and Version

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