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

Gene ID: 944834, updated on 11-Jun-2025
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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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 Sequence:
NC_000913.3

Go to nucleotide: Graphics FASTA GenBank

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 (60) 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.
Submit: New GeneRIF Correction
Products Interactant Other Gene Complex Source Pubs Description

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 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 
Preferred Names
pyruvate dehydrogenase E1 component
NP_414656.1

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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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