FabI

• Description: enoyl-acyl carrier protein reductase
  
  

Gene name	fabI
Synonyms	yjbW
Essential	no
Product	enoyl-acyl carrier protein reductase
Function	fatty acid biosynthesis
Metabolic function and regulation of this protein in SubtiPathways: Lipid synthesis
MW, pI	27 kDa, 5.605
Gene length, protein length	774 bp, 258 aa
Immediate neighbours	thiD, cotO
Get the DNA and protein sequences (Barbe et al., 2009)
Genetic context This image was kindly provided by SubtiList

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: BSU11720

Database entries

• DBTBS entry: [1]

• SubtiList entry: [2]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity: Acyl-[acyl-carrier-protein] + NAD⁺ = trans-2,3-dehydroacyl-[acyl-carrier-protein] + NADH (according to Swiss-Prot)

• Protein family: FabI subfamily (according to Swiss-Prot)

• Paralogous protein(s): FabL, 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:
  • inhibited by triclosan PubMed

• Interactions:

• Localization:

Database entries

• Structure: 3OIF (complex with NAD and inhibitor triclosan) PubMed

• UniProt: P54616

• KEGG entry: [3]

• E.C. number: 1.3.1.9

Expression and regulation

• Operon: fabI PubMed

• Sigma factor:

• Regulation:
  • expressed when 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)

Kook-Han Kim, Byung Hak Ha, Su Jin Kim, Seung Kon Hong, Kwang Yeon Hwang, Eunice Eunkyeong Kim
Crystal structures of Enoyl-ACP reductases I (FabI) and III (FabL) from B. subtilis.
J Mol Biol: 2011, 406(3);403-15
[PubMed:21185310] [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)

R J Heath, N Su, C K Murphy, C O Rock
The enoyl-[acyl-carrier-protein] reductases FabI and FabL from Bacillus subtilis.
J Biol Chem: 2000, 275(51);40128-33
[PubMed:11007778] [WorldCat.org] [DOI] (P p)

C Baldock, J B Rafferty, S E Sedelnikova, P J Baker, A R Stuitje, A R Slabas, T R Hawkes, D W Rice
A mechanism of drug action revealed by structural studies of enoyl reductase.
Science: 1996, 274(5295);2107-10
[PubMed:8953047] [WorldCat.org] [DOI] (P p)