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
Gene expression levels in SubtiExpress: fabG
Metabolic function and regulation of this protein in SubtiPathways: fabG
MW, pI	26 kDa, 8.091
Gene length, protein length	738 bp, 246 aa
Immediate neighbours	fabD, acpA
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, 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)