CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.90 | Alpha-Beta Complex |
|
3.90.470 | Ribosomal Protein L22; Chain A |
|
3.90.470.20 | 4'-phosphopantetheinyl transferase domain |
Domain Context
CATH Clusters
| Superfamily | 4'-phosphopantetheinyl transferase domain |
| Functional Family | Mitochondrial holo-[acyl-carrier-protein] synthase |
Enzyme Information
| 2.7.8.7 |
Holo-[acyl-carrier-protein] synthase.
based on mapping to UniProt Q7RB63
CoA-(4'-phosphopantetheine) + apo-[acyl-carrier-protein] = adenosine 3',5'-bisphosphate + holo-[acyl-carrier-protein].
-!- All polyketide synthases, fatty-acid synthases and non-ribosomal peptide synthases require post-translational modification of their constituent acyl-carrier-protein (ACP) domains to become catalytically active. -!- The inactive apo-proteins are converted into their active holo-forms by transfer of the 4'-phosphopantetheinyl moiety of CoA to the sidechain hydroxy group of a conserved serine residue in each ACP domain. -!- The enzyme from human can activate both the ACP domain of the human cytosolic multifunctional fatty acid synthase and that associated with human mitochondria as well as peptidyl-carrier and acyl-carrier- proteins from prokaryotes. -!- Removal of the 4-phosphopantetheinyl moiety from holo-ACP is carried out by EC 3.1.4.14.
|
UniProtKB Entries (1)
| Q7RB63 |
Q7RB63_PLAYO
Plasmodium yoelii yoelii
Uncharacterized protein
|
PDB Structure
| PDB | 2BDD |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Escherichia |
| Primary Citation |
Genome-scale protein expression and structural biology of Plasmodium falciparum and related Apicomplexan organisms.
Mol.Biochem.Parasitol.
|