CATH Classification

Domain Context

CATH Clusters

Superfamily ATP-grasp fold, B domain
Functional Family Biotin carboxylase

Enzyme Information

6.4.1.2
Acetyl-CoA carboxylase.
based on mapping to UniProt P24182
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 P24182
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)

P24182
ACCC_ECOLI
Escherichia coli K-12
Biotin carboxylase

PDB Structure

PDB 2W6P
External Links
Method X-RAY DIFFRACTION
Organism
Primary Citation
Discovery of Antibacterial Biotin Carboxylase Inhibitors by Virtual Screening and Fragment-Based Approaches.
Mochalkin, I., Miller, J.R., Narasimhan, L.S., Thanabal, V., Erdman, P., Cox, P., Prasad, J.V., Lightle, S., Huband, M., Stover, K.
Acs Chem.Biol.