CATH Domain 2v5aA02

CATH Classification

Level	CATH Code	Description
	3	Alpha Beta
	3.30	2-Layer Sandwich
	3.30.470	D-amino Acid Aminotransferase; Chain A, domain 1
	3.30.470.20	ATP-grasp fold, B domain

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	2V5A
External Links	PDBSum Proteopedia
Method	X-RAY DIFFRACTION
Organism
Primary Citation	A Class of Selective Antibacterials Derived from a Protein Kinase Inhibitor Pharmacophore. Miller, J.R., Dunham, S., Mochalkin, I., Banotai, C., Bowman, M., Buist, S., Dunkle, B., Hanna, D., Harwood, H.J., Huband, M.D., Karnovsky, A., Kuhn, M., Limberakis, C., Liu, J.Y., Mehrens, S., Mueller, W.T., Narasimhan, L., Ogden, A., Ohren, J., Prasad, J.V., Shelly, J.A., Skerlos, L., Sulavik, M., Thomas, V.H., Vanderroest, S., Wang, L., Wang, Z., Whitton, A., Zhu, T., Stover, C.K. Proc.Natl.Acad.Sci.USA