Difference between revisions of "FabI"

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|style="background:#ABCDEF;" align="center"|'''Function''' || fatty acid biosynthesis  
|style="background:#ABCDEF;" align="center"|'''Function''' || fatty acid biosynthesis  
|colspan="2" style="background:#FAF8CC;" align="center"| '''Metabolic function and regulation of this protein in [[SubtiPathways|''Subti''Pathways]]: <br/>[http://subtiwiki.uni-goettingen.de/pathways/fatty_acid_syn.html Lipid synthesis]'''
|colspan="2" style="background:#FAF8CC;" align="center"| '''Metabolic function and regulation of this protein in [[SubtiPathways|''Subti''Pathways]]: <br/>[http://subtiwiki.uni-goettingen.de/pathways/fatty_acid_synthesis.html Lipid synthesis]'''
|style="background:#ABCDEF;" align="center"| '''MW, pI''' || 27 kDa, 5.605   
|style="background:#ABCDEF;" align="center"| '''MW, pI''' || 27 kDa, 5.605   

Revision as of 14:12, 7 March 2010

  • 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
FabI context.gif
This image was kindly provided by SubtiList

The gene

Basic information

  • Locus tag: BSU11720

Phenotypes of a mutant

Database entries

  • DBTBS entry: [1]
  • SubtiList entry: [2]

Additional information

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
  • KEGG entry: [3]

Additional information

Expression and regulation

  • Regulation:
    • expressed when the cells experience a lack of malonyl-CoA (FapR) PubMed
  • Regulatory mechanism:
  • Additional information:

Biological materials

  • Mutant:
  • Expression vector:
  • lacZ fusion:
  • GFP fusion:
  • two-hybrid system:
  • Antibody:

Labs working on this gene/protein

Your additional remarks



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

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)