CATH Classification

Domain Context

CATH Clusters

Superfamily ATP-grasp fold, B domain
Functional Family Acetyl-CoA carboxylase 1

Enzyme Information

6.4.1.2
Acetyl-CoA carboxylase.
based on mapping to UniProt O00763
ATP + acetyl-CoA + HCO(3)(-) = ADP + phosphate + malonyl-CoA.
-!- This enzyme is a multi-domain polypeptide that catalyzes three different activities - a biotin carboxyl-carrier protein (BCCP), a biotin carboxylase that catalyzes the transfer of a carboxyl group from hydrogencarbonate to the biotin molecule carried by the carrier protein, and the transfer of the carboxyl group from biotin to acetyl-CoA, forming malonyl-CoA. -!- In some organisms these activities are catalyzed by separate enzymes (see EC 6.3.4.14 and EC 2.1.3.15). -!- The carboxylation of the carrier protein requires ATP, while the transfer of the carboxyl group to acetyl-CoA does not.
6.3.4.14
Biotin carboxylase.
based on mapping to UniProt O00763
ATP + [biotin carboxyl-carrier protein]-biotin-N(6)-L-lysine + hydrogencarbonate- = ADP + phosphate + [biotin carboxyl-carrier protein]- carboxybiotin-N(6)-L-lysine.
-!- This enzyme, part of an acetyl-CoA carboxylase complex, acts on a biotin carboxyl-carrier protein (BCCP) that has been biotinylated by EC 6.3.4.15. -!- In some organisms the enzyme is part of a multi-domain polypeptide that also includes the carrier protein (e.g. mycobacteria). -!- Yet in other organisms (e.g. mammals) this activity is included in a single polypeptide that also catalyzes the transfer of the carboxyl group from biotin to acetyl-CoA (see EC 6.4.1.2).

UniProtKB Entries (1)

O00763
ACACB_HUMAN
Homo sapiens
Acetyl-CoA carboxylase 2

PDB Structure

PDB 2HJW
External Links
Method X-RAY DIFFRACTION
Organism Escherichia
Primary Citation
Crystal structure of the biotin carboxylase domain of human acetyl-CoA carboxylase 2.
Cho, Y.S., Lee, J.I., Shin, D., Kim, H.T., Cheon, Y.H., Seo, C.I., Kim, Y.E., Hyun, Y.L., Lee, Y.S., Sugiyama, K., Park, S.Y., Ro, S., Cho, J.M., Lee, T.G., Heo, Y.S.
Proteins