CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.30 | 2-Layer Sandwich |
|
3.30.390 | Enolase-like; domain 1 |
|
3.30.390.50 | CO dehydrogenase flavoprotein, C-terminal domain |
Domain Context
CATH Clusters
| Superfamily | CO dehydrogenase flavoprotein, C-terminal domain |
| Functional Family | Lipoate-protein ligase A |
Enzyme Information
| 6.3.1.20 |
Lipoate--protein ligase.
based on mapping to UniProt P32099
ATP + (R)-lipoate + a [lipoyl-carrier protein]-L-lysine = a [lipoyl- carrier protein]-N(6)-(lipoyl)lysine + AMP + diphosphate.
-!- This enzyme participates in lipoate salvage, and is responsible for lipoylation in the presence of exogenous lipoic acid. -!- The enzyme attaches lipoic acid to the lipoyl domains of certain key enzymes involved in oxidative metabolism, including pyruvate dehydrogenase (E(2) domain), 2-oxoglutarate dehydrogenase (E(2) domain), the branched-chain 2-oxoacid dehydrogenases and the glycine cleavage system (H protein). -!- Lipoylation is essential for the function of these enzymes. -!- The enzyme can also use octanoate instead of lipoate. -!- Formerly EC 2.7.7.63.
|
UniProtKB Entries (1)
| P32099 |
LPLA_ECOLI
Escherichia coli K-12
Lipoate-protein ligase A
|
PDB Structure
| PDB | 1X2H |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Escherichia |
| Primary Citation |
Crystal structure of lipoate-protein ligase A from Escherichia coli: Determination of the lipoic acid-binding site
J.Biol.Chem.
|
