CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
2 | Mainly Beta |
|
2.40 | Beta Barrel |
|
2.40.460 | ClpP/crotonase fold |
|
2.40.460.10 | Biotin dependent carboxylase carboxyltransferase |
Domain Context
CATH Clusters
| Superfamily | Biotin dependent carboxylase carboxyltransferase |
| 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 | 3FF6 |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
The human ACC2 CT-domain C-terminus is required for full functionality and has a novel twist.
Acta Crystallogr.,Sect.D
|
