Catalyzes the rate-limiting reaction in the biogenesis of long-chain fatty acids. Carries out three functions: biotin carboxyl carrier protein, biotin carboxylase and carboxyltransferase.
Monomer, homodimer, and homotetramer. Can form filamentous polymers. Interacts in its inactive phosphorylated form with the BRCT domains of BRCA1 which prevents ACACA dephosphorylation and inhibits lipid synthesis. Interacts with MID1IP1; interaction with MID1IP1 promotes oligomerization and increases its activity.
Expressed in brain, placental, skeletal muscle, renal, pancreatic and adipose tissues; expressed at low level in pulmonary tissue; not detected in the liver.
Contains 1 ATP-grasp domain.
Contains 1 biotin carboxylation domain.
Contains 1 biotinyl-binding domain.
Contains 1 carboxyltransferase domain.
Involvement in disease
Defects in ACACA are a cause of acetyl-CoA carboxylase 1 deficiency (ACACAD) [MIM:200350]; also known as ACAC deficiency or ACC deficiency. An inborn error of de novo fatty acid synthesis associated with severe brain damage, persistent myopathy and poor growth.
Phosphorylation on Ser-1263 is required for interaction with BRCA1.
Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1.
By phosphorylation (By similarity). Activity is increased by oligomerization. Citrate and MID1IP1 promote oligomerization.