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: Fatty acid and phospholipid biosynthesis
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

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: 1DFI (the enzyme from E. coli in complex with NAD) 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

• Regulatory mechanism:
  • FapR: transcription repression PubMed

• Additional information:

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

References

Original Publications

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 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)