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
Gene expression levels in SubtiExpress: accB
Interactions involving this protein in SubtInteract: AccB
Metabolic function and regulation of this protein in SubtiPathways: accB
MW, pI	17 kDa, 4.394
Gene length, protein length	477 bp, 159 aa
Immediate neighbours	accC, spoIIIAH
Sequences	Protein DNA DNA_with_flanks
Genetic context This image was kindly provided by SubtiList
Expression at a glance   PubMed

Categories containing this gene/protein

biosynthesis of lipids, essential genes

The gene

Basic information

• Locus tag: BSU24350

Phenotypes of a mutant

essential PubMed

Database entries

• BsubCyc: BSU24350

• 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:

• Cofactors: biotin

• Effectors of protein activity:

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

• Localization:

Database entries

• BsubCyc: BSU24350

• 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

• Expression browser: accB PubMed

• Sigma factor:

• Regulation:

• Regulatory mechanism:

• Additional information:
  • number of protein molecules per cell (minimal medium with glucose and ammonium, exponential phase): 3355 PubMed
  • number of protein molecules per cell (minimal medium with glucose and ammonium, early stationary phase after glucose exhaustion): 889 PubMed
  • number of protein molecules per cell (minimal medium with glucose and ammonium, late stationary phase after glucose exhaustion): 28 PubMed

Biological materials

• Mutant:

• Expression vector:
  • GP1477 (chromosomal accB-Strep fusion, aphA3), purification from B. subtilis, for SPINE, available in Jörg Stülke's lab
  • pGP2649: IPTG inducible expression, purification in E. coli with N-terminal His-tag, in pWH844, available in Jörg Stülke's lab
  • pGP2650: IPTG inducible expression, purification in E. coli with N-terminal Strep-tag, in pGP172, available in Jörg Stülke's lab
  • pGP2652: IPTG inducible expression, purification in E. coli with C-terminal Strep-tag, in pGP574, available in Jörg Stülke's lab

• lacZ fusion:

• GFP fusion:

• two-hybrid system: B. pertussis adenylate cyclase-based bacterial two hybrid system (BACTH), available in Jörg Stülke's lab

• FLAG-tag construct:
  • GP1484 (mls, based on pGP1087), available in Jörg Stülke's lab

• Antibody:

References

Reviews

L Tong
Acetyl-coenzyme A carboxylase: crucial metabolic enzyme and attractive target for drug discovery.
Cell Mol Life Sci: 2005, 62(16);1784-803
[PubMed:15968460] [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)

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

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)