CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.90 | Alpha-Beta Complex |
|
3.90.226 | 2-enoyl-CoA Hydratase; Chain A, domain 1 |
|
3.90.226.10 | 2-enoyl-CoA Hydratase; Chain A, domain 1 |
Domain Context
CATH Clusters
| Superfamily | 2-enoyl-CoA Hydratase; Chain A, domain 1 |
| Functional Family |
Enzyme Information
| 2.1.3.15 |
Acetyl-CoA carboxytransferase.
based on mapping to UniProt Q2FG38
[Biotin carboxyl-carrier protein]-N(6)-carboxybiotinyl-L-lysine + acetyl- CoA = [biotin carboxyl-carrier protein]-N(6)-biotinyl-L-lysine + malonyl- CoA.
-!- The enzyme catalyzes the transfer of a carboxyl group carried on a biotinylated biotin carboxyl carrier protein (BCCP) to acetyl-CoA, forming malonyl-CoA. -!- In some organisms this activity is part of a multi-domain polypeptide that includes the carrier protein and EC 6.3.4.14 (see EC 6.4.1.2). -!- Some enzymes can also carboxylate propanonyl-CoA and butanoyl-CoA (Cf. EC 6.4.1.3).
|
UniProtKB Entries (2)
| Q5HF73 |
ACCD_STAAC
Staphylococcus aureus subsp. aureus COL
Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta
|
| Q2FG38 |
ACCA_STAA3
Staphylococcus aureus subsp. aureus USA300
Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha
|
PDB Structure
| PDB | 2F9I |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Escherichia |
| Primary Citation |
The structure of the carboxyltransferase component of acetyl-coA carboxylase reveals a zinc-binding motif unique to the bacterial enzyme.
Biochemistry
|
