Difference between revisions of "AccC"

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= [[Categories]] containing this gene/protein =
 
= [[Categories]] containing this gene/protein =
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=== Additional information===
 
=== Additional information===
 
 
 
  
 
=The protein=
 
=The protein=
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* '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=accC_2530354_2531706_-1 accC] {{PubMed|22383849}}
 
* '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=accC_2530354_2531706_-1 accC] {{PubMed|22383849}}
  
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* '''Regulation:'''  
 
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=References=
 
=References=
 
==Reviews==
 
==Reviews==
<pubmed> 15952903 </pubmed>
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<pubmed> 15952903 12121720 </pubmed>
 
==Original Publications==
 
==Original Publications==
 
<pubmed> 7592499, 7915138, </pubmed>
 
<pubmed> 7592499, 7915138, </pubmed>
  
 
[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Revision as of 16:39, 5 June 2014

  • Description: acetyl-CoA carboxylase (biotin carboxylase subunit)

Gene name accC
Synonyms yqhX
Essential yes PubMed
Product acetyl-CoA carboxylase (biotin carboxylase subunit)
Function production of malonyl-CoA, the substrate for fatty acid biosynthesis
Gene expression levels in SubtiExpress: accC
Interactions involving this protein in SubtInteract: AccC
Metabolic function and regulation of this protein in SubtiPathways:
accC
MW, pI 49 kDa, 4.72
Gene length, protein length 1350 bp, 450 aa
Immediate neighbours yqhY, accB
Sequences Protein DNA DNA_with_flanks
Genetic context
AccC context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
AccC expression.png















Categories containing this gene/protein

biosynthesis of lipids, essential genes

This gene is a member of the following regulons

The gene

Basic information

  • Locus tag: BSU24340

Phenotypes of a mutant

essential PubMed

Database entries

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

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: ATP + biotin-carboxyl-carrier protein + CO2 = ADP + phosphate + carboxybiotin-carboxyl-carrier protein (according to Swiss-Prot)
  • Protein family:
  • Paralogous protein(s): YotE

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification:
  • Cofactor(s):
  • Effectors of protein activity:

Database entries

  • Structure: 1BNC (the protein from E. coli) PubMed
  • KEGG entry: [3]

Additional information

Expression and regulation

  • Regulation:
  • Regulatory mechanism:
  • Additional information:
    • number of protein molecules per cell (minimal medium with glucose and ammonium, exponential phase): 527 PubMed
    • number of protein molecules per cell (minimal medium with glucose and ammonium, early stationary phase after glucose exhaustion): 286 PubMed
    • number of protein molecules per cell (minimal medium with glucose and ammonium, late stationary phase after glucose exhaustion): 634 PubMed

Biological materials

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

Labs working on this gene/protein

Your additional remarks

References

Reviews

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)

John E Cronan, Grover L Waldrop
Multi-subunit acetyl-CoA carboxylases.
Prog Lipid Res: 2002, 41(5);407-35
[PubMed:12121720] [WorldCat.org] [DOI] (P p)

Original Publications

P Marini, S J Li, D Gardiol, J E Cronan, D de Mendoza
The genes encoding the biotin carboxyl carrier protein and biotin carboxylase subunits of Bacillus subtilis acetyl coenzyme A carboxylase, the first enzyme of fatty acid synthesis.
J Bacteriol: 1995, 177(23);7003-6
[PubMed:7592499] [WorldCat.org] [DOI] (P p)

G L Waldrop, I Rayment, H M Holden
Three-dimensional structure of the biotin carboxylase subunit of acetyl-CoA carboxylase.
Biochemistry: 1994, 33(34);10249-56
[PubMed:7915138] [WorldCat.org] [DOI] (P p)