LMPD Database

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LMP012678

UniProt Annotations

Entry Information
Gene Nameacetyl-CoA carboxylase alpha
Protein EntryACACA_RAT
UniProt IDP11497
SpeciesRat
Comments
Comment typeDescription
Alternative ProductsEvent=Alternative splicing; Named isoforms=2; Name=1; IsoId=P11497-1; Sequence=Displayed; Name=2; IsoId=P11497-2; Sequence=VSP_011753;
Catalytic ActivityATP + acetyl-CoA + HCO(3)(-) = ADP + phosphate + malonyl-CoA.
Catalytic ActivityATP + biotin-[carboxyl-carrier-protein] + CO(2) = ADP + phosphate + carboxy-biotin-[carboxyl-carrier- protein].
CofactorName=biotin; Xref=ChEBI:CHEBI:57586; Note=Biotin.;
CofactorName=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence= ; Note=Binds 2 manganese ions per subunit. ;
Enzyme RegulationActivity is increased by oligomerization. Citrate and MID1IP1 promote oligomerization (By similarity). Activity is increased by phosphorylation
FunctionCatalyzes the rate-limiting reaction in the biogenesis of long-chain fatty acids. Carries out three functions: biotin carboxyl carrier protein, biotin carboxylase and carboxyltransferase.
PathwayLipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1.
PtmPhosphorylation at Ser-79 by AMPK inactivates enzyme activity. Phosphorylated in vitro at Ser-1200 and Ser-1215 by AMPK; the relevance of phosphorylation of these sites in vivo is however unclear. {ECO:0000269|PubMed:1346520, ECO:0000269|PubMed:1974251, ECO:0000269|PubMed:2900138, ECO:0000269|PubMed:9029219}.
PtmPhosphorylation on Ser-1262 is required for interaction with BRCA1
PtmThe N-terminus is blocked.
SimilarityContains 1 ATP-grasp domain. {ECO:0000255|PROSITE- ProRule:PRU00409}.
SimilarityContains 1 biotin carboxylation domain
SimilarityContains 1 biotinyl-binding domain
SimilarityContains 1 carboxyltransferase domain
Subcellular LocationCytoplasm.
SubunitMonomer, 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 (By similarity)