Difference between revisions of "AccA"

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=== Basic information/ Evolution ===
 
=== Basic information/ Evolution ===
  
* '''Catalyzed reaction/ biological activity:'''  
+
* '''Catalyzed reaction/ biological activity:''' ATP + acetyl-CoA + HCO<sub>3</sub><sup>-</sup> = ADP + phosphate + malonyl-CoA (according to Swiss-Prot)
  
 
* '''Protein family:''' accA family (according to Swiss-Prot)
 
* '''Protein family:''' accA family (according to Swiss-Prot)

Revision as of 12:13, 24 May 2009

  • Description: acetyl-CoA carboxylase (alpha subunit)

Gene name accA
Synonyms
Essential yes PubMed
Product acetyl-CoA carboxylase (alpha subunit))
Function production of malonyl-CoA, the substrate for fatty acid biosynthesis
MW, pI 36 kDa, 6.087
Gene length, protein length 975 bp, 325 aa
Immediate neighbours pfkA, accD
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
AccA context.gif
This image was kindly provided by SubtiList



The gene

Basic information

  • Coordinates:

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 + acetyl-CoA + HCO3- = ADP + phosphate + malonyl-CoA (according to Swiss-Prot)
  • Protein family: accA family (according to Swiss-Prot)
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification:
  • Cofactor(s):
  • Effectors of protein activity:
  • Interactions:
  • Localization: cytoplasm (according to Swiss-Prot), Membrane-proximal (Spotty) PubMed

Database entries

  • Structure:

Additional information

Expression and regulation

  • Operon:
  • Regulation:
  • 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

  1. Meile et al. (2006) Systematic localisation of proteins fused to the green fluorescent protein in Bacillus subtilis: identification of new proteins at the DNA replication factory Proteomics 6: 2135-2146. PubMed
  2. Author1, Author2 & Author3 (year) Title Journal volume: page-page. PubMed