FadB

• Description: 3-hydroxyacyl-CoA dehydratase
  
  

Gene name	fadB
Synonyms	ysiB
Essential	no
Product	3-hydroxyacyl-CoA dehydratase
Function	fatty acid degradation
Gene expression levels in SubtiExpress: fadB
Metabolic function and regulation of this protein in SubtiPathways: fadB
MW, pI	27 kDa, 4.951
Gene length, protein length	774 bp, 258 aa
Immediate neighbours	etfB, fadR
Sequences	Protein DNA DNA_with_flanks
Genetic context This image was kindly provided by SubtiList
Expression at a glance   PubMed

Categories containing this gene/protein

utilization of lipids, phosphoproteins

This gene is a member of the following regulons

CcpA regulon, FadR regulon

The gene

Basic information

• Locus tag: BSU28540

Database entries

• BsubCyc: BSU28540

• DBTBS entry: [1]

• SubtiList entry: [2]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity: (3S)-3-hydroxyacyl-CoA = trans-2(or 3)-enoyl-CoA + H₂O (according to Swiss-Prot)

• Protein family: enoyl-CoA hydratase/isomerase family (according to Swiss-Prot)

• Paralogous protein(s):

Extended information on the protein

• Kinetic information:

• Domains:

• Modification:
  • phosphorylated on Arg-230 PubMed

• Cofactor(s):

• Effectors of protein activity:

• Interactions:

• Localization:

Database entries

• BsubCyc: BSU28540

• Structure: 3PEA (from B. anthracis, 49% identity, 66% similarity)

• UniProt: P94549

• KEGG entry: [3]

• E.C. number: 4.2.1.17

Expression and regulation

• Operon:
  • lcfA-fadR-fadB-etfB-etfA PubMed
  • fadR-fadB-etfB-etfA PubMed

• Expression browser: fadB PubMed

• Sigma factor:
  • lcfA: SigA PubMed
  • fadR: SigA PubMed

• Regulation:
  • induced by long-chain fatty acids (FadR) PubMed
  • subject to carbon catabolite repression (3.8-fold) (CcpA-HPr(Ser-P) PubMed

• Regulatory mechanism:
  • FadR: transcription repression PubMed
  • CcpA-HPr(Ser-P): transcription repression PubMed

• Additional information:
  • number of protein molecules per cell (minimal medium with glucose and ammonium): 165 PubMed
  • number of protein molecules per cell (complex medium with amino acids, without glucose): 665 PubMed

Biological materials

• Mutant:
  • 1A854 ( fadB::cat), PubMed, available at BGSC

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

References

Additional publications: PubMed

Alexander K W Elsholz, Kürsad Turgay, Stephan Michalik, Bernd Hessling, Katrin Gronau, Dan Oertel, Ulrike Mäder, Jörg Bernhardt, Dörte Becher, Michael Hecker, Ulf Gerth
Global impact of protein arginine phosphorylation on the physiology of Bacillus subtilis.
Proc Natl Acad Sci U S A: 2012, 109(19);7451-6
[PubMed:22517742] [WorldCat.org] [DOI] (I p)

Yasutaro Fujita, Hiroshi Matsuoka, Kazutake Hirooka
Regulation of fatty acid metabolism in bacteria.
Mol Microbiol: 2007, 66(4);829-39
[PubMed:17919287] [WorldCat.org] [DOI] (P 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)

Hans-Matti Blencke, Georg Homuth, Holger Ludwig, Ulrike Mäder, Michael Hecker, Jörg Stülke
Transcriptional profiling of gene expression in response to glucose in Bacillus subtilis: regulation of the central metabolic pathways.
Metab Eng: 2003, 5(2);133-49
[PubMed:12850135] [WorldCat.org] [DOI] (P p)