AccB

• 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: Lipid synthesis
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 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]

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:

• Interactions: (AccA-AccD)-AccB-AccC (acetyl-CoA carboxylase complex)

• Localization:

Database entries

• Structure: 1BDO (the protein from E. coli) PubMed

• UniProt: P49786

• KEGG entry: [3]

• E.C. number: 6.4.1.2

Additional information

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

Expression and regulation

• Operon: accB-accC-yqhY PubMed

• Sigma factor:

• Regulation:

• Regulatory mechanism:

• Additional information:

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

References

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)