Difference between revisions of "FabHB"

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(References)
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=== Database entries ===
 
=== Database entries ===
  
* '''Structure:'''
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* '''Structure:''' [http://www.rcsb.org/pdb/explore/explore.do?structureId=1EBL 1EBL] (FabH from ''E. coli'') {{PubMed|10673437}}
  
 
* '''UniProt:''' [http://www.uniprot.org/uniprot/O07600 O07600]
 
* '''UniProt:''' [http://www.uniprot.org/uniprot/O07600 O07600]
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<pubmed> 15952903 17919287</pubmed>
 
<pubmed> 15952903 17919287</pubmed>
 
==Original Publications==
 
==Original Publications==
<pubmed>12737802,17114254,10629181, </pubmed>
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<pubmed>12737802,17114254,10629181, 10673437 </pubmed>
  
 
[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Revision as of 18:02, 6 January 2010

  • Description: beta-ketoacyl-acyl carrier protein synthase III

Gene name fabHB
Synonyms yhfB
Essential no
Product beta-ketoacyl-acyl carrier protein synthase III
Function fatty acid biosynthesis
MW, pI 35 kDa, 5.684
Gene length, protein length 975 bp, 325 aa
Immediate neighbours yhgE, yhfC
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
FabHB context.gif
This image was kindly provided by SubtiList



The gene

Basic information

  • Locus tag: BSU10170

Phenotypes of a mutant

Database entries

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

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: Acetyl-CoA + malonyl-[acyl-carrier-protein] = acetoacyl-[acyl-carrier-protein] + CoA + CO2 (according to Swiss-Prot)
  • Protein family: fabH family (according to Swiss-Prot)
  • Paralogous protein(s): FabHA, 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:
  • Interactions:
  • Localization: cytoplasm (according to Swiss-Prot)

Database entries

  • KEGG entry: [3]

Additional information

Expression and regulation

  • Regulation:
    • repressed unless 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

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

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 Davies, R J Heath, S W White, C O Rock
The 1.8 A crystal structure and active-site architecture of beta-ketoacyl-acyl carrier protein synthase III (FabH) from escherichia coli.
Structure: 2000, 8(2);185-95
[PubMed:10673437] [WorldCat.org] [DOI] (P p)

K H Choi, R J Heath, C O Rock
beta-ketoacyl-acyl carrier protein synthase III (FabH) is a determining factor in branched-chain fatty acid biosynthesis.
J Bacteriol: 2000, 182(2);365-70
[PubMed:10629181] [WorldCat.org] [DOI] (P p)