Difference between revisions of "FabI"

From SubtiWiki
Jump to: navigation, search
(Original Publications)
Line 105: Line 105:
 
* '''Regulation:'''  
 
* '''Regulation:'''  
 
** expressed when the cells experience a lack of malonyl-CoA ([[FapR]]) {{PubMed|12737802}}
 
** expressed when the cells experience a lack of malonyl-CoA ([[FapR]]) {{PubMed|12737802}}
 +
** induced upon fatty acid biosynthesis inhibition {{PubMed|21383089}}
  
 
* '''Regulatory mechanism:'''  
 
* '''Regulatory mechanism:'''  
Line 133: Line 134:
 
<pubmed> 15952903 17919287</pubmed>
 
<pubmed> 15952903 17919287</pubmed>
 
==Original Publications==
 
==Original Publications==
<pubmed>12737802,17114254, 8953047 11007778 21185310</pubmed>
+
<pubmed>12737802,17114254, 8953047 11007778 21185310 21383089</pubmed>
 
[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Revision as of 15:40, 9 March 2011

  • 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







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

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: 3OIF (complex with NAD and inhibitor triclosan) PubMed
  • KEGG entry: [3]

Additional information

Expression and regulation

  • Regulation:
    • expressed when the cells experience a lack of malonyl-CoA (FapR) PubMed
    • induced upon fatty acid biosynthesis inhibition 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

References

Reviews

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)