LMPD Database

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LMP005741

UniProt Annotations

Entry Information
Gene Nameacetyl-Coenzyme A carboxylase beta
Protein EntryE9Q4Z2_MOUSE
UniProt IDQ9ESZ3
SpeciesMouse
Comments
Comment typeDescription
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; Evidence= ; Note=Biotin. ;
CofactorName=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence= ; Note=Binds 2 manganese ions per subunit. {ECO:0000255|PROSITE- ProRule:PRU00409};
Disruption PhenotypeNormal morphology, fertility, growth rate and lifespan but higher than normal food consumption and fatty acid oxidation rate and decreased fat content in adipose tissue and liver (PubMed:11283375). A high-fat/high-carbohydrate diet results in maintenance of normal insulin and glucose levels with less weight gain and less fat accumulation than wild-type mice (PubMed:12920182). Elevated levels of Ucp2 in adipose tissue and heart but not in skeletal muscle or liver, and elevated levels of Ucp3 in skeletal muscle but not in heart or brown adipose tissue (PubMed:12920182). Significant decrease in body weight, weight of epidydimal fat pads and levels of hepatic triglycerides under a range of dietary conditions including normal chow diet, fasting and refeeding a fat-free high-carbohydrate diet, and a high- fat/high-carbohydrate diet (PubMed:22362781). Up-regulation of lipogenic enzymes under de novo lipogenic conditions but reduced fat accumulation in liver (PubMed:22362781). Primary cultured adipocytes show increased fatty acid and glucose oxidation rates and increased lipolysis (PubMed:15677334). Reduced heart size, reduced Mlycd and malonyl-CoA levels in mutant hearts, reduced myocardial triglyceride levels, higher myocardial oleate and glucose oxidation rates, reduced levels of Ppara and reduced activation of Mtor (PubMed:18487439, PubMed:22730442). However, it has also been reported that mutants show no differences in body weight, food intake, body composition or glucose homeostasis as compared with controls fed on chow or a high-fat diet (PubMed:20368432). {ECO:0000269|PubMed:11283375, ECO:0000269|PubMed:12920182, ECO:0000269|PubMed:15677334, ECO:0000269|PubMed:18487439, ECO:0000269|PubMed:20368432, ECO:0000269|PubMed:22362781, ECO:0000269|PubMed:22730442}.
Enzyme RegulationActivity is increased by oligomerization. Activated by citrate. Citrate and MID1IP1 promote oligomerization. Inhibited by malonyl-CoA.
FunctionCatalyzes the ATP-dependent carboxylation of acetyl-CoA to malonyl-CoA (By similarity). Carries out three functions: biotin carboxyl carrier protein, biotin carboxylase and carboxyltransferase (By similarity). Involved in inhibition of fatty acid and glucose oxidation and enhancement of fat storage (PubMed:11283375, PubMed:12920182, PubMed:15677334, PubMed:18487439, PubMed:22362781). May play a role in regulation of mitochondrial fatty acid oxidation through malonyl-CoA- dependent inhibition of carnitine palmitoyltransferase 1 (PubMed:10677481). {ECO:0000250|UniProtKB:O00763, ECO:0000269|PubMed:11283375, ECO:0000269|PubMed:12920182, ECO:0000269|PubMed:15677334, ECO:0000269|PubMed:18487439, ECO:0000269|PubMed:22362781, ECO:0000303|PubMed:10677481}.
PathwayLipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1.
PtmPhosphorylated by AMPK, leading to inactivation of the enzyme. Required for the maintenance of skeletal muscle lipid and glucose homeostasis.
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 LocationMitochondrion . Nucleus . Endomembrane system . Note=May associate with membranes.
SubunitMonomer, homodimer, and homotetramer. Can form filamentous polymers. Interacts with MID1IP1; interaction with MID1IP1 promotes oligomerization and increases its activity.