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fadH 2,4-dienoyl-CoA reductase [ Escherichia coli str. K-12 substr. MG1655 ]

Gene ID: 947594, updated on 30-Jul-2025
Official Symbol
fadH
Official Full Name
2,4-dienoyl-CoA reductase
Primary source
ECOCYC:G36
Locus tag
b3081
See related
ASAP:ABE-0010124
Gene type
protein coding
RefSeq status
REVIEWED
Organism
Escherichia coli str. K-12 substr. MG1655 (strain: K-12, substrain: MG1655)
Lineage
Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia
Also known as
ECK3071; ygjL
Summary
FadH contains FMN, FAD, and a 4Fe-4S cluster. [More information is available at EcoGene: EG12723].
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Sequence:
NC_000913.3 (3231665..3233683)

NC_000913.3Genomic Context describing neighboring genes Neighboring gene protein YgjJ Neighboring gene glycoside hydrolase Neighboring gene antitoxin/DNA-binding transcriptional repressor HigA Neighboring gene ribosome-dependent mRNA interferase toxin HigB Neighboring gene 23S rRNA m(2)G1835 methyltransferase

Genomic Sequence:
NC_000913.3

Go to nucleotide: Graphics FASTA GenBank

Related articles in PubMed

  1. Degradation of unsaturated fatty acids. Identification of intermediates in the degradation of cis-4-decenoly-CoA by extracts of beef-liver mitochondria. Kunau WH, et al. Eur J Biochem, 1978 Nov 15. PMID 729581
  2. Evidence for the essential function of 2,4-dienoyl-coenzyme A reductase in the beta-oxidation of unsaturated fatty acids in vivo. Isolation and characterization of an Escherichia coli mutant with a defective 2,4-dienoyl-coenzyme A reductase. You SY, et al. J Biol Chem, 1989 Oct 5. PMID 2506179
  3. 2,4-Dienoyl coenzyme A reductases from bovine liver and Escherichia coli. Comparison of properties. Dommes V, et al. J Biol Chem, 1984 Feb 10. PMID 6363415
  4. Cloning and expression of the fadH gene and characterization of the gene product 2,4-dienoyl coenzyme A reductase from Escherichia coli. He XY, et al. Eur J Biochem, 1997 Sep 1. PMID 9346310
  5. Overlapping repressor binding sites result in additive regulation of Escherichia coli FadH by FadR and ArcA. Feng Y, et al. J Bacteriol, 2010 Sep. PMID 20622065, Free PMC Article

See all (17) citations in PubMed

GeneRIFs: Gene References Into Functions

What's a GeneRIF?
  1. We report mapping of the fadH promoter and document its complex regulation by three independent regulators, the fatty acid degradation FadR repressor, the oxygen-responsive ArcA-ArcB two-component system, and the cyclic AMP receptor protein-cyclic AMP.
    Title: Overlapping repressor binding sites result in additive regulation of Escherichia coli FadH by FadR and ArcA.
  2. supports a mechanism that has Tyr166 with the assistance of His252 acting as proton donor in the wild-type enzyme to produce 2-enoyl-CoA
    Title: Two distinct proton donors at the active site of Escherichia coli 2,4-dienoyl-CoA reductase are responsible for the formation of different products.
  3. N-terminus verified by Edman degradation on mature peptide
    Title: Cloning and expression of the fadH gene and characterization of the gene product 2,4-dienoyl coenzyme A reductase from Escherichia coli.
Submit: New GeneRIF Correction
Products Interactant Other Gene Complex Source Pubs Description

Homology

Gene Ontology Provided by EcoCyc

Function Evidence Code Pubs
enables 2,4-dienoyl-CoA reductase (NADPH) activity IBA
Inferred from Biological aspect of Ancestor
more info
  
enables 2,4-dienoyl-CoA reductase (NADPH) activity IDA
Inferred from Direct Assay
more info
 PubMed 
enables 2,4-dienoyl-CoA reductase (NADPH) activity IEA
Inferred from Electronic Annotation
more info
  
enables 2,4-dienoyl-CoA reductase (NADPH) activity IMP
Inferred from Mutant Phenotype
more info
 PubMed 
enables 4 iron, 4 sulfur cluster binding IDA
Inferred from Direct Assay
more info
 PubMed 
enables 4 iron, 4 sulfur cluster binding IEA
Inferred from Electronic Annotation
more info
  
enables FAD binding IDA
Inferred from Direct Assay
more info
 PubMed 
enables FMN binding IDA
Inferred from Direct Assay
more info
 PubMed 
enables FMN binding IEA
Inferred from Electronic Annotation
more info
  
enables iron-sulfur cluster binding IEA
Inferred from Electronic Annotation
more info
  
enables metal ion binding IEA
Inferred from Electronic Annotation
more info
  
enables oxidoreductase activity IEA
Inferred from Electronic Annotation
more info
  
enables protein binding IPI
Inferred from Physical Interaction
more info
 PubMed 
Process Evidence Code Pubs
involved_in fatty acid beta-oxidation IEA
Inferred from Electronic Annotation
more info
  
involved_in fatty acid beta-oxidation, unsaturated, even number, reductase/isomerase pathway IBA
Inferred from Biological aspect of Ancestor
more info
  
acts_upstream_of_or_within fatty acid beta-oxidation, unsaturated, even number, reductase/isomerase pathway IMP
Inferred from Mutant Phenotype
more info
 PubMed 
Preferred Names
2,4-dienoyl-CoA reductase
NP_417552.1

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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
    3231665..3233683
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. NP_417552.1 2,4-dienoyl-CoA reductase

    See identical proteins and their annotated locations for NP_417552.1

    Status: REVIEWED

    UniProtKB/TrEMBL
    A0A8T6PU12
    Conserved Domains (2) summary
    COG0446
    Location:355 → 665
    FadH2; NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase [Lipid transport and metabolism]
    cd02930
    Location:6 → 358
    DCR_FMN; 2,4-dienoyl-CoA reductase (DCR) FMN-binding domain. DCR in E. coli is an iron-sulfur flavoenzyme which contains FMN, FAD, and a 4Fe-4S cluster. It is also a monomer, unlike that of its eukaryotic counterparts which form homotetramers and lack the ...
Nucleotide Protein
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