ID:ACACB_HUMAN DESCRIPTION: RecName: Full=Acetyl-CoA carboxylase 2; EC=6.4.1.2; AltName: Full=ACC-beta; Includes: RecName: Full=Biotin carboxylase; EC=6.3.4.14; FUNCTION: ACC-beta may be involved in the provision of malonyl-CoA or in the regulation of fatty acid oxidation, rather than fatty acid biosynthesis. Carries out three functions: biotin carboxyl carrier protein, biotin carboxylase and carboxyltransferase. CATALYTIC ACTIVITY: ATP + acetyl-CoA + HCO(3)(-) = ADP + phosphate + malonyl-CoA. CATALYTIC ACTIVITY: ATP + biotin-[carboxyl-carrier-protein] + CO(2) = ADP + phosphate + carboxy-biotin-[carboxyl-carrier- protein]. COFACTOR: Biotin (By similarity). COFACTOR: Binds 2 manganese ions per subunit (By similarity). ENZYME REGULATION: Activity is increased by oligomerization. Activated by citrate. Citrate and MID1IP1 promote oligomerization. Inhibited by malonyl-CoA. BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=120 uM for ATP; KM=58 uM for Acetyl-CoA; KM=3.0 mM for NaHCO(3); PATHWAY: Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. SUBUNIT: Monomer, homodimer, and homotetramer. Can form filamentous polymers. Interacts with MID1IP1; interaction with MID1IP1 promotes oligomerization and increases its activity. SUBCELLULAR LOCATION: Endomembrane system. Note=May associate with membranes. TISSUE SPECIFICITY: Predominantly expressed in the heart, skeletal muscles and liver. PTM: Phosphorylated by AMPK, leading to inactivates enzyme activity (By similarity). SIMILARITY: Contains 1 ATP-grasp domain. SIMILARITY: Contains 1 biotin carboxylation domain. SIMILARITY: Contains 1 biotinyl-binding domain. SIMILARITY: Contains 1 carboxyltransferase domain. SEQUENCE CAUTION: Sequence=AAB58382.1; Type=Miscellaneous discrepancy; Note=Many Frameshifts and conflicts; Sequence=CAE01470.2; Type=Erroneous translation; Note=Wrong choice of CDS;
The RNAfold program from the Vienna RNA Package is used to perform the secondary structure predictions and folding calculations. The estimated folding energy is in kcal/mol. The more negative the energy, the more secondary structure the RNA is likely to have.
ModBase Predicted Comparative 3D Structure on O00763
Front
Top
Side
The pictures above may be empty if there is no ModBase structure for the protein. The ModBase structure frequently covers just a fragment of the protein. You may be asked to log onto ModBase the first time you click on the pictures. It is simplest after logging in to just click on the picture again to get to the specific info on that model.
Orthologous Genes in Other Species
Orthologies between human, mouse, and rat are computed by taking the best BLASTP hit, and filtering out non-syntenic hits. For more distant species reciprocal-best BLASTP hits are used. Note that the absence of an ortholog in the table below may reflect incomplete annotations in the other species rather than a true absence of the orthologous gene.
Biological Process: GO:0006084 acetyl-CoA metabolic process GO:0006629 lipid metabolic process GO:0006631 fatty acid metabolic process GO:0006633 fatty acid biosynthetic process GO:0006853 carnitine shuttle GO:0008152 metabolic process GO:0010629 negative regulation of gene expression GO:0010884 positive regulation of lipid storage GO:0010906 regulation of glucose metabolic process GO:0014070 response to organic cyclic compound GO:0031325 positive regulation of cellular metabolic process GO:0031667 response to nutrient levels GO:0031999 negative regulation of fatty acid beta-oxidation GO:0042493 response to drug GO:0043086 negative regulation of catalytic activity GO:0045540 regulation of cholesterol biosynthetic process GO:0046322 negative regulation of fatty acid oxidation GO:0050995 negative regulation of lipid catabolic process GO:0051289 protein homotetramerization GO:0060421 positive regulation of heart growth GO:0097009 energy homeostasis GO:2001295 malonyl-CoA biosynthetic process