Difference between revisions of "FabHA"

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* '''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 <br/><br/>
 
 
 
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Revision as of 11:14, 9 August 2012

  • 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:
Lipid synthesis
MW, pI 33 kDa, 5.045
Gene length, protein length 936 bp, 312 aa
Immediate neighbours yjzB, fabF
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
FabHA context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
FabHA expression.png




























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

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

Additional information

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:
  • Cofactor(s):
  • Effectors of protein activity:

Database entries

  • KEGG entry: [3]

Additional information

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

Expression and regulation

  • 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:
  • 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

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)

Original Publications

Additional publications: PubMed

Michaela Wenzel, Malay Patra, Dirk Albrecht, David Y-K Chen, K C Nicolaou, Nils Metzler-Nolte, Julia E Bandow
Proteomic signature of fatty acid biosynthesis inhibition available for in vivo mechanism-of-action studies.
Antimicrob Agents Chemother: 2011, 55(6);2590-6
[PubMed:21383089] [WorldCat.org] [DOI] (I p)

Natalia Martin, Esteban Lombardía, Silvia G Altabe, Diego de Mendoza, María C Mansilla
A lipA (yutB) mutant, encoding lipoic acid synthase, provides insight into the interplay between branched-chain and unsaturated fatty acid biosynthesis in Bacillus subtilis.
J Bacteriol: 2009, 191(24);7447-55
[PubMed:19820084] [WorldCat.org] [DOI] (I p)

Helena B Thomaides, Ella J Davison, Lisa Burston, Hazel Johnson, David R Brown, Alison C Hunt, Jeffery Errington, Lloyd Czaplewski
Essential bacterial functions encoded by gene pairs.
J Bacteriol: 2007, 189(2);591-602
[PubMed:17114254] [WorldCat.org] [DOI] (P p)

Gustavo E Schujman, Luciana Paoletti, Alan D Grossman, Diego de Mendoza
FapR, a bacterial transcription factor involved in global regulation of membrane lipid biosynthesis.
Dev Cell: 2003, 4(5);663-72
[PubMed:12737802] [WorldCat.org] [DOI] (P p)

C Davies, R J Heath, S W White, C O Rock
The 1.8 A crystal structure and active-site architecture of beta-ketoacyl-acyl carrier protein synthase III (FabH) from escherichia coli.
Structure: 2000, 8(2);185-95
[PubMed:10673437] [WorldCat.org] [DOI] (P p)

K H Choi, R J Heath, C O Rock
beta-ketoacyl-acyl carrier protein synthase III (FabH) is a determining factor in branched-chain fatty acid biosynthesis.
J Bacteriol: 2000, 182(2);365-70
[PubMed:10629181] [WorldCat.org] [DOI] (P p)