FabHB

Gene name	fabHB
Synonyms	yhfB , fabH2
Essential	no
Product	beta-ketoacyl-acyl carrier protein synthase III
Function	fatty acid biosynthesis
Gene expression levels in SubtiExpress: fabHB
Metabolic function and regulation of this protein in SubtiPathways: Lipid synthesis
MW, pI	35 kDa, 5.684
Gene length, protein length	975 bp, 325 aa
Immediate neighbours	yhgE, yhfC
Get the DNA and protein sequences (Barbe et al., 2009)
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: BSU10170

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): FabHA, 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: O07600

• 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: fabHB PubMed

• Expression browser: fabHB PubMed

• Sigma factor:

• Regulation:
  • induced if the cells experience a lack of malonyl-CoA (FapR) PubMed
  • induced upon fatty acid biosynthesis inhibition 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

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)