CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.30 | 2-Layer Sandwich |
|
3.30.930 | BirA Bifunctional Protein; domain 2 |
|
3.30.930.10 | Bira Bifunctional Protein; Domain 2 |
Domain Context
CATH Clusters
| Superfamily | Bira Bifunctional Protein; Domain 2 |
| Functional Family | Putative lipoyltransferase 2, mitochondrial |
Enzyme Information
| 2.3.1.181 |
Lipoyl(octanoyl) transferase.
based on mapping to UniProt P9WK83
Octanoyl-[acyl-carrier-protein] + protein = protein N(6)-(octanoyl)lysine + [acyl-carrier-protein].
-!- The first committed step in the biosynthesis of lipoyl cofactor. -!- The lipoyl cofactor is essential for the function of several key enzymes involved in oxidative metabolism, as it converts apoprotein into the biologically active holoprotein. -!- Examples of such lipoylated proteins include pyruvate dehydrogenase (E(2) domain), 2-oxoglutarate dehydrogenase (E(2) domain), the branched-chain 2-oxoacid dehydrogenases and the glycine cleavage system (H protein). -!- Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the true substrate. -!- The other enzyme involved in the biosynthesis of lipoyl cofactor is EC 2.8.1.8. -!- An alternative lipoylation pathway involves EC 2.7.7.63, which can lipoylate apoproteins using exogenous lipoic acid (or its analogs).
|
UniProtKB Entries (1)
| P9WK83 |
LIPB_MYCTU
Mycobacterium tuberculosis H37Rv
Octanoyltransferase
|
PDB Structure
| PDB | 1W66 |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
The Mycobacterium Tuberculosis Lipb Enzyme Functions as a Cysteine/Lysine Dyad Acyltransferase.
Proc.Natl.Acad.Sci.USA
|