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

• 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:

• Cofactor(s):

• Effectors of protein activity:

• Interactions:

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

Database entries

• 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:

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)

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)