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.
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UniProtKB Entries (1)
P32099 |
LPLA_ECOLI
Escherichia coli K-12
Lipoate-protein ligase A
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PDB Structure
PDB | 4TVY |
External Links | |
Method | X-RAY DIFFRACTION |
Organism | |
Primary Citation |
Computational design of a red fluorophore ligase for site-specific protein labeling in living cells.
Proc.Natl.Acad.Sci.USA
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