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    aceE pyruvate dehydrogenase E1 component [ Escherichia coli str. K-12 substr. MG1655 ]

    Gene ID: 944834, updated on 3-Dec-2024

    Summary

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    Official Symbol
    aceE
    Official Full Name
    pyruvate dehydrogenase E1 component
    Primary source
    ECOCYC:EG10024
    Locus tag
    b0114
    See related
    ASAP:ABE-0000397
    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
    ECK0113
    Summary
    Holoenzyme is AceE(24)+AceF(24)+Lpd(12). [More information is available at EcoGene: EG10024]. It is sometimes confusing that this component and the multi-enzyme complex both carry the same name. [More information is available at EcoCyc: EG10024].
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    Genomic context

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    Sequence:
    NC_000913.3 (123017..125680)

    NC_000913.3Genomic Context describing neighboring genes Neighboring gene aromatic amino acid:H(+) symporter AroP Neighboring gene DNA-binding transcriptional dual regulator PdhR Neighboring gene pyruvate dehydrogenase, E2 subunit Neighboring gene lipoamide dehydrogenase

    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. Communication between thiamin cofactors in the Escherichia coli pyruvate dehydrogenase complex E1 component active centers: evidence for a "direct pathway" between the 4'-aminopyrimidine N1' atoms. Nemeria NS, et al. J Biol Chem, 2010 Apr 9. PMID 20106967, Free PMC Article
    2. Conformational ensemble modulates cooperativity in the rate-determining catalytic step in the E1 component of the Escherichia coli pyruvate dehydrogenase multienzyme complex. Kale S, et al. J Biol Chem, 2009 Nov 27. PMID 19801660, Free PMC Article
    3. Structural determinants of enzyme binding affinity: the E1 component of pyruvate dehydrogenase from Escherichia coli in complex with the inhibitor thiamin thiazolone diphosphate. Arjunan P, et al. Biochemistry, 2004 Mar 9. PMID 14992577
    4. Efficient coupling of catalysis and dynamics in the E1 component of Escherichia coli pyruvate dehydrogenase multienzyme complex. Kale S, et al. Proc Natl Acad Sci U S A, 2008 Jan 29. PMID 18216265, Free PMC Article
    5. C2-alpha-lactylthiamin diphosphate is an intermediate on the pathway of thiamin diphosphate-dependent pyruvate decarboxylation. Evidence on enzymes and models. Zhang S, et al. J Biol Chem, 2004 Dec 24. PMID 15501823

    See all (61) 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. thiamin cofactor communication in the Escherichia coli pyruvate dehydrogenase complex E1 component active centers is a "direct pathway" between the 4'-aminopyrimidine N1' atoms
      Title: Communication between thiamin cofactors in the Escherichia coli pyruvate dehydrogenase complex E1 component active centers: evidence for a "direct pathway" between the 4'-aminopyrimidine N1' atoms.
    4. Observations suggest a mode of cooperativity in the E1 component that is consistent with the dynamical hypothesis shown to satisfactorily explain cooperativity in many well studied enzymes.
      Title: Conformational ensemble modulates cooperativity in the rate-determining catalytic step in the E1 component of the Escherichia coli pyruvate dehydrogenase multienzyme complex.
    5. Loop dynamics correlates with catalysis in the pyruvate dehydrogenase decarboxylase E1 component and represents the rate-limiting step for catalysis; overall dynamics of E1 creates a regulatory switch to streamline the catalytic steps in the complex.
      Title: Efficient coupling of catalysis and dynamics in the E1 component of Escherichia coli pyruvate dehydrogenase multienzyme complex.
    6. 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.
    7. 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.
    8. Evidence is presented for the N-terminal region of pyruvate dehydrogenase complex E1 (PDHc-E1) subunit from E. coli playing a major role in the interaction with the PDHc-E2 subunit.
      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.
    9. crystal structure
      Title: A thiamin-bound, pre-decarboxylation reaction intermediate analogue in the pyruvate dehydrogenase E1 subunit induces large scale disorder-to-order transformations in the enzyme and reveals novel structural features in the covalently bound adduct.
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    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 identical protein binding IPI
    Inferred from Physical Interaction
    more info
    		 PubMed 
    enables magnesium ion binding IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables metal ion binding IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables molecular adaptor activity EXP
    Inferred from Experiment
    more info
    		 PubMed 
    enables oxidoreductase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables protein binding IPI
    Inferred from Physical Interaction
    more info
    		 PubMed 
    enables protein homodimerization activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables pyruvate dehydrogenase (acetyl-transferring) activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables pyruvate dehydrogenase activity IGI
    Inferred from Genetic Interaction
    more info
    		 PubMed 
    enables small molecule binding EXP
    Inferred from Experiment
    more info
    		 PubMed 
    enables thiamine pyrophosphate binding IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    Process Evidence Code Pubs
    involved_in pyruvate catabolic process NAS
    Non-traceable Author Statement
    more info
    		 PubMed 
    Component Evidence Code Pubs
    located_in cytosol HDA PubMed 
    located_in membrane HDA 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 E1 component
    NP_414656.1

    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
      123017..125680
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NP_414656.1 pyruvate dehydrogenase E1 component [Escherichia coli str. K-12 substr. MG1655]

      See identical proteins and their annotated locations for NP_414656.1

      Status: PROVISIONAL

      UniProtKB/TrEMBL
      A0A6C9QDU8, A0A6M9WYP8, A0A7D7KHN0
      Conserved Domains (1) summary
      PRK09405
      Location:1 → 887
      aceE; pyruvate dehydrogenase subunit E1; Reviewed
    Nucleotide Protein
    Heading Accession and Version

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