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fadA 3-ketoacyl-CoA thiolase [ Escherichia coli str. K-12 substr. MG1655 ]

Gene ID: 948324, updated on 2-May-2024

Summary

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Gene symbol
fadA
Gene description
3-ketoacyl-CoA thiolase
Primary source
ASAP:ABE-0012562
Locus tag
b3845
See related
ECOCYC:EG10278
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
ECK3837; oldA
Summary
FadR regulon. [More information is available at EcoGene: EG10278]. The beta subunit has one enzymatic activity associated with it and is part of a multienzyme complex. [More information is available at EcoCyc: EG10278].
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Genomic context

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Sequence:
NC_000913.3 (4027609..4028772, complement)

NC_000913.3Genomic Context describing neighboring genes Neighboring gene 3-octaprenyl-4-hydroxybenzoate decarboxylase Neighboring gene NAD(P)H-flavin reductase Neighboring gene multifunctional enoyl-CoA hydratase, 3-hydroxyacyl-CoA epimerase, Delta(3)-cis- Delta(2)-trans-enoyl-CoA isomerase, L-3-hydroxyacyl-CoA dehydrogenase Neighboring gene Xaa-Pro dipeptidase Neighboring gene IMPACT family member YigZ

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. Crystal structure of a thiolase from Escherichia coli at 1.8 Å resolution. Ithayaraja M, et al. Acta Crystallogr F Struct Biol Commun, 2016 Jul. PMID 27380370, Free PMC Article
  2. Purification and some properties of thiolase from Escherichia coli. Mazzei Y, et al. Biochim Biophys Acta, 1970 Oct 14. PMID 4919548
  3. The induction of the enzymes of fatty acid degradation in Escherichia coli. Overath P, et al. Biochem Biophys Res Commun, 1967 Oct 11. PMID 4861587
  4. Nucleotide sequence of the fadA gene. Primary structure of 3-ketoacyl-coenzyme A thiolase from Escherichia coli and the structural organization of the fadAB operon. Yang SY, et al. J Biol Chem, 1991 Aug 25. PMID 1678742
  5. Association of both enoyl coenzyme A hydratase and 3-hydroxyacyl coenzyme A epimerase with an active site in the amino-terminal domain of the multifunctional fatty acid oxidation protein from Escherichia coli. Yang SY, et al. J Biol Chem, 1993 Mar 25. PMID 8454629

See all (27) citations in PubMed

GeneRIFs: Gene References Into Functions

What's a GeneRIF?
  1. Crystal structure of a thiolase from Escherichia coli at 1.8 A resolution has been reported.
    Title: Crystal structure of a thiolase from Escherichia coli at 1.8 Å resolution.
  2. N-terminus verified by Edman degradation on complete protein
    Title: Nucleotide sequence of the fadA gene. Primary structure of 3-ketoacyl-coenzyme A thiolase from Escherichia coli and the structural organization of the fadAB operon.
Submit: New GeneRIF Correction

Pathways from PubChem

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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 acetyl-CoA C-acyltransferase activity IBA
Inferred from Biological aspect of Ancestor
more info
  
enables acetyl-CoA C-acyltransferase activity IDA
Inferred from Direct Assay
more info
 PubMed 
enables acetyl-CoA C-acyltransferase activity IEA
Inferred from Electronic Annotation
more info
  
enables acetyl-CoA C-acyltransferase activity IMP
Inferred from Mutant Phenotype
more info
 PubMed 
enables acyltransferase activity IEA
Inferred from Electronic Annotation
more info
  
enables acyltransferase activity, transferring groups other than amino-acyl groups 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 IBA
Inferred from Biological aspect of Ancestor
more info
  
involved_in fatty acid beta-oxidation IDA
Inferred from Direct Assay
more info
 PubMed 
involved_in fatty acid beta-oxidation IEA
Inferred from Electronic Annotation
more info
  
acts_upstream_of_or_within fatty acid beta-oxidation IMP
Inferred from Mutant Phenotype
more info
 PubMed 
acts_upstream_of_or_within fatty acid catabolic process IMP
Inferred from Mutant Phenotype
more info
 PubMed 
involved_in fatty acid metabolic process IEA
Inferred from Electronic Annotation
more info
  
involved_in lipid catabolic process IEA
Inferred from Electronic Annotation
more info
  
involved_in phenylacetate catabolic process IBA
Inferred from Biological aspect of Ancestor
more info
  
involved_in small molecule metabolic process IEA
Inferred from Electronic Annotation
more info
  
Component Evidence Code Pubs
located_in cytoplasm IDA
Inferred from Direct Assay
more info
 PubMed 
located_in cytoplasm IEA
Inferred from Electronic Annotation
more info
  
part_of fatty acid beta-oxidation multienzyme complex IDA
Inferred from Direct Assay
more info
 PubMed 
part_of fatty acid beta-oxidation multienzyme complex IPI
Inferred from Physical Interaction
more info
 PubMed 

General protein information

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Preferred Names
3-ketoacyl-CoA thiolase
YP_026272.1

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
    4027609..4028772 complement
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. YP_026272.1 3-ketoacyl-CoA thiolase [Escherichia coli str. K-12 substr. MG1655]

    See identical proteins and their annotated locations for YP_026272.1

    Status: PROVISIONAL

    UniProtKB/TrEMBL
    A0A827XSN5
    Conserved Domains (1) summary
    PRK08947
    Location:1 → 387
    fadA; 3-ketoacyl-CoA thiolase; Reviewed
Nucleotide Protein
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