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fadM long-chain acyl-CoA thioesterase FadM [ Escherichia coli str. K-12 substr. MG1655 ]

Gene ID: 945812, updated on 30-Jul-2025
Official Symbol
fadM
Official Full Name
long-chain acyl-CoA thioesterase FadM
Primary source
ECOCYC:G6244
Locus tag
b0443
See related
ASAP:ABE-0001537
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
ECK0437; tesC; ybaW
Summary
3,5-tetradecadienoyl-CoA is the preferred substrate for thioesterase III, which is induced by fatty acids, suggesting a role in beta-oxidation of fatty acids (Nie, 2008). [More information is available at EcoGene: EG13251]. Thioesterase III is a long-chain acyl-CoA thioesterase that is involved in the -oxidation of oleic acid. [More information is available at EcoCyc: G6244].
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Sequence:
NC_000913.3 (464402..464800)

NC_000913.3Genomic Context describing neighboring genes Neighboring gene periplasmic folding chaperone Neighboring gene helix-hairpin-helix 3 family protein Neighboring gene 7-cyano-7-deazaguanine synthase Neighboring gene uncharacterized protein YbaE

Genomic Sequence:
NC_000913.3

Go to nucleotide: Graphics FASTA GenBank

Related articles in PubMed

  1. An alternative pathway of oleate beta-oxidation in Escherichia coli involving the hydrolysis of a dead end intermediate by a thioesterase. Ren Y, et al. J Biol Chem, 2004 Mar 19. PMID 14707139
  2. A novel paradigm of fatty acid beta-oxidation exemplified by the thioesterase-dependent partial degradation of conjugated linoleic acid that fully supports growth of Escherichia coli. Nie L, et al. Biochemistry, 2008 Sep 9. PMID 18702504
  3. Analysis of proteins with the 'hot dog' fold: prediction of function and identification of catalytic residues of hypothetical proteins. Pidugu LS, et al. BMC Struct Biol, 2009 May 28. PMID 19473548, Free PMC Article
  4. Identification and characterization of Escherichia coli thioesterase III that functions in fatty acid beta-oxidation. Nie L, et al. Biochemistry, 2008 Jul 22. PMID 18576672
  5. A new member of the Escherichia coli fad regulon: transcriptional regulation of fadM (ybaW). Feng Y, et al. J Bacteriol, 2009 Oct. PMID 19684132, Free PMC Article

See all (10) citations in PubMed

GeneRIFs: Gene References Into Functions

Homology

Gene Ontology Provided by EcoCyc

Function Evidence Code Pubs
enables fatty acyl-CoA hydrolase activity IBA
Inferred from Biological aspect of Ancestor
more info
  
enables fatty acyl-CoA hydrolase activity IDA
Inferred from Direct Assay
more info
 PubMed 
enables hydrolase activity IEA
Inferred from Electronic Annotation
more info
  
Process Evidence Code Pubs
acts_upstream_of_or_within fatty acid beta-oxidation IEP
Inferred from Expression Pattern
more info
 PubMed 
Preferred Names
long-chain acyl-CoA thioesterase FadM

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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
    464402..464800
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. NP_414977.1 long-chain acyl-CoA thioesterase FadM

    See identical proteins and their annotated locations for NP_414977.1

    Status: REVIEWED

    UniProtKB/TrEMBL
    A0A2H4TPI9, A0A895NSL2
    Conserved Domains (1) summary
    TIGR00051
    Location:5 → 120
    TIGR00051; acyl-CoA thioester hydrolase, YbgC/YbaW family
Nucleotide Protein
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