AccB

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

Gene name accB
Synonyms fabE, yqhW
Essential yes PubMed
Product acetyl-CoA carboxylase (biotin carboxyl carrier subunit)
Function production of malonyl-CoA, the substrate for fatty acid biosynthesis
Metabolic function and regulation of this protein in SubtiPathways:
Fatty acid and phospholipid biosynthesis
MW, pI 17 kDa, 4.394
Gene length, protein length 477 bp, 159 aa
Immediate neighbours accC, spoIIIAH
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
AccB context.gif
This image was kindly provided by SubtiList



The gene

Basic information

  • Locus tag: BSU24350

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:
  • Protein family:
  • Paralogous protein(s):

Extended information on the protein

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

Database entries

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

Additional information

AccB binds to StrepTactin, and may be co-purified when purifying Strep-tagged proteins by SPINE.

Expression and regulation

  • 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

Reviews

Original Publications

F K Athappilly, W A Hendrickson
Structure of the biotinyl domain of acetyl-coenzyme A carboxylase determined by MAD phasing.
Structure: 1995, 3(12);1407-19
[PubMed:8747466] [WorldCat.org] [DOI] (P p)

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)