Difference between revisions of "FadE"

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=References=
'''Additional publications:''' {{PubMed|23033921,21398533}}
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<pubmed>17189250,12817086 ,18763711</pubmed>
 
  
 
[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Revision as of 11:19, 4 June 2013

  • Description: acyl-CoA dehydrogenase

Gene name fadE
Synonyms yusJ
Essential no
Product acyl-CoA dehydrogenase
Function fatty acid degradation
Gene expression levels in SubtiExpress: fadE
Metabolic function and regulation of this protein in SubtiPathways:
Fatty acid degradation
MW, pI 65 kDa, 5.146
Gene length, protein length 1782 bp, 594 aa
Immediate neighbours yusI, fadA
Sequences Protein DNA DNA_with_flanks
Genetic context
YusJ context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
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Categories containing this gene/protein

utilization of lipids, membrane proteins

This gene is a member of the following regulons

CcpA regulon, FadR regulon, SdpR regulon

The gene

Basic information

  • Locus tag: BSU32820

Phenotypes of a mutant

Database entries

  • DBTBS entry: [1]
  • SubtiList entry: [2]

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: Acyl-CoA + ETF = 2,3-dehydroacyl-CoA + reduced ETF (according to Swiss-Prot)
  • Protein family: acyl-CoA dehydrogenase family (according to Swiss-Prot)

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification:
  • Cofactor(s):
  • Effectors of protein activity:

Database entries

  • Structure: 2Z1Q (from Thermus thermophilus hb8, 52% identity, 68% similarity)
  • KEGG entry: [3]
  • E.C. number:

Additional information

Expression and regulation

  • Additional information:

Biological materials

  • Mutant:
  • Expression vector:
  • lacZ fusion:
  • GFP fusion:
  • two-hybrid system:
  • Antibody:

Labs working on this gene/protein

Your additional remarks

References

Imke G de Jong, Jan-Willem Veening, Oscar P Kuipers
Single cell analysis of gene expression patterns during carbon starvation in Bacillus subtilis reveals large phenotypic variation.
Environ Microbiol: 2012, 14(12);3110-21
[PubMed:23033921] [WorldCat.org] [DOI] (I p)

Shigeo Tojo, Takenori Satomura, Hiroshi Matsuoka, Kazutake Hirooka, Yasutaro Fujita
Catabolite repression of the Bacillus subtilis FadR regulon, which is involved in fatty acid catabolism.
J Bacteriol: 2011, 193(10);2388-95
[PubMed:21398533] [WorldCat.org] [DOI] (I p)

Hannes Hahne, Susanne Wolff, Michael Hecker, Dörte Becher
From complementarity to comprehensiveness--targeting the membrane proteome of growing Bacillus subtilis by divergent approaches.
Proteomics: 2008, 8(19);4123-36
[PubMed:18763711] [WorldCat.org] [DOI] (I p)

Hiroshi Matsuoka, Kazutake Hirooka, Yasutaro Fujita
Organization and function of the YsiA regulon of Bacillus subtilis involved in fatty acid degradation.
J Biol Chem: 2007, 282(8);5180-94
[PubMed:17189250] [WorldCat.org] [DOI] (P p)

José E González-Pastor, Errett C Hobbs, Richard Losick
Cannibalism by sporulating bacteria.
Science: 2003, 301(5632);510-3
[PubMed:12817086] [WorldCat.org] [DOI] (I p)