FabG

• Description: beta-ketoacyl-acyl carrier protein reductase
  
  

Gene name	fabG
Synonyms	ylpF
Essential	yes PubMed
Product	beta-ketoacyl-acyl carrier protein reductase
Function	fatty acid biosynthesis
Metabolic function and regulation of this protein in SubtiPathways: Lipid synthesis
MW, pI	26 kDa, 8.091
Gene length, protein length	738 bp, 246 aa
Immediate neighbours	fabD, acpA
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, essential genes

This gene is a member of the following regulons

ComA regulon, FapR regulon

The gene

Basic information

• Locus tag: BSU15910

Phenotypes of a mutant

essential PubMed

Database entries

• DBTBS entry: [1]

• SubtiList entry: [2]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity: (3R)-3-hydroxyacyl-[acyl-carrier-protein] + NADP⁺ = 3-oxoacyl-[acyl-carrier-protein] + NADPH (according to Swiss-Prot)

• Protein family: short-chain dehydrogenases/reductases (SDR) family (according to Swiss-Prot)

• Paralogous protein(s):

Extended information on the protein

• Kinetic information:

• Domains:

• Modification:

• Cofactor(s):

• Effectors of protein activity:

• Interactions:

• Localization:

Database entries

• Structure: 1I01 (the enzyme from E. coli) PubMed

• UniProt: P51831

• KEGG entry: [3]

• E.C. number: 1.1.1.100

Expression and regulation

• Operon: fapR-plsX-fabD-fabG-acpA PubMed

• Expression browser: fabG PubMed

• Sigma factor: SigA PubMed

• Regulation:
  • induced if the cells experience an accumulation of malonyl-CoA (FapR) PubMed
  • expressed at high cell density (ComA) PubMed

• Regulatory mechanism:
  • ComA: transcription activation (ComA) PubMed
  • 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

Mariano A Martinez, Diego de Mendoza, Gustavo E Schujman
Transcriptional and functional characterization of the gene encoding acyl carrier protein in Bacillus subtilis.
Microbiology (Reading): 2010, 156(Pt 2);484-495
[PubMed:19850612] [WorldCat.org] [DOI] (I p)

Gustavo E Schujman, Marcelo Guerin, Alejandro Buschiazzo, Francis Schaeffer, Leticia I Llarrull, Georgina Reh, Alejandro J Vila, Pedro M Alzari, Diego de Mendoza
Structural basis of lipid biosynthesis regulation in Gram-positive bacteria.
EMBO J: 2006, 25(17);4074-83
[PubMed:16932747] [WorldCat.org] [DOI] (P p)

Natalia Comella, Alan D Grossman
Conservation of genes and processes controlled by the quorum response in bacteria: characterization of genes controlled by the quorum-sensing transcription factor ComA in Bacillus subtilis.
Mol Microbiol: 2005, 57(4);1159-74
[PubMed:16091051] [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)

A C Price, Y M Zhang, C O Rock, S W White
Structure of beta-ketoacyl-[acyl carrier protein] reductase from Escherichia coli: negative cooperativity and its structural basis.
Biochemistry: 2001, 40(43);12772-81
[PubMed:11669613] [WorldCat.org] [DOI] (P p)