CATH Classification

Domain Context

CATH Clusters

Superfamily ATP-grasp fold, A domain
Functional Family

Enzyme Information

6.3.4.14
Biotin carboxylase.
based on mapping to UniProt P43873
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).
6.4.1.2
Acetyl-CoA carboxylase.
based on mapping to UniProt P43873
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.

UniProtKB Entries (1)

P43873
ACCC_HAEIN
Haemophilus influenzae Rd KW20
Biotin carboxylase

PDB Structure

PDB 4MV8
External Links
Method X-RAY DIFFRACTION
Organism
Primary Citation
Structural Analysis of Substrate, Reaction Intermediate, and Product Binding in Haemophilus influenzae Biotin Carboxylase.
Broussard, T.C., Pakhomova, S., Neau, D.B., Bonnot, R., Waldrop, G.L.
Biochemistry