FabHA

• Description: beta-ketoacyl-acyl carrier protein synthase III, principal condensing enzyme responsible for the initiation of fatty acid synthesis in non-stressed B. subtilis cells
  
  

Gene name	fabHA
Synonyms	yjaX , fabH1
Essential	no
Product	beta-ketoacyl-acyl carrier protein synthase III
Function	fatty acid biosynthesis
Gene expression levels in SubtiExpress: fabHA
Metabolic function and regulation of this protein in SubtiPathways: fabHA
MW, pI	33 kDa, 5.045
Gene length, protein length	936 bp, 312 aa
Immediate neighbours	yjzB, fabF
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

biosynthesis of lipids

This gene is a member of the following regulons

FapR regulon

The gene

Basic information

• Locus tag: BSU11330

Phenotypes of a mutant

• significant increase in the proportion of straight-chain fatty acids with a concomitant increase in 31:0-carbon phosphatidylethanolamine species PubMed

Database entries

• BsubCyc: BSU11330

• DBTBS entry: [1]

• SubtiList entry: [2]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity: Acetyl-CoA + malonyl-[acyl-carrier-protein] = acetoacyl-[acyl-carrier-protein] + CoA + CO₂ (according to Swiss-Prot)

• Protein family: fabH family (according to Swiss-Prot)

• Paralogous protein(s): FabHB, one of the two proteins has to be present for viability PubMed

Extended information on the protein

• Kinetic information:

• Domains:

• Modification:

• Cofactors:

• Effectors of protein activity:

• Interactions:

• Localization:
  • cytoplasm (according to Swiss-Prot)

Database entries

• BsubCyc: BSU11330

• Structure: 1EBL (FabH from E. coli) PubMed

• UniProt: O34746

• KEGG entry: [3]

• E.C. number: 2.3.1.180, 2.3.1.41

Additional information

• affinity for butyryl-CoA, but prefers acetyl-CoA in fatty acid biosynthesis PubMed

Expression and regulation

• Operon: fabHA-fabF PubMed

• Expression browser: fabHA PubMed

• Sigma factor: SigA PubMed

• Regulation:
  • expressed when the cells experience a lack of malonyl-CoA (FapR) PubMed
  • inhibited by cerulenin PubMed
  • induced upon fatty acid biosynthesis inhibition PubMed
  • expression is reduced when SigW is activated (by alkaline shock, polymyxin B, vancomycin, cephalosporin C, D-cycloserine, and triton X-100) PubMed

• Regulatory mechanism:
  • FapR: transcription repression PubMed

• Additional information:
  • number of protein molecules per cell (minimal medium with glucose and ammonium): 897 PubMed
  • number of protein molecules per cell (complex medium with amino acids, without glucose): 1078 PubMed
  • number of protein molecules per cell (minimal medium with glucose and ammonium, exponential phase): 2129 PubMed
  • number of protein molecules per cell (minimal medium with glucose and ammonium, early stationary phase after glucose exhaustion): 1833 PubMed
  • number of protein molecules per cell (minimal medium with glucose and ammonium, late stationary phase after glucose exhaustion): 2586 PubMed

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

References

Reviews

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)

Stephen W White, Jie Zheng, Yong-Mei Zhang, Rock
The structural biology of type II fatty acid biosynthesis.
Annu Rev Biochem: 2005, 74;791-831
[PubMed:15952903] [WorldCat.org] [DOI] (P p)