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 |
Enzyme Information
| 2.7.8.7 |
Holo-[acyl-carrier-protein] synthase.
based on mapping to UniProt P96618
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 system (EC 2.3.1.85) 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)
| P96618 |
ACPS_BACSU
Bacillus subtilis subsp. subtilis str. 168
Holo-[acyl-carrier-protein] synthase
|
PDB Structure
| PDB | 1F7T |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Escherichia |
| Primary Citation |
Crystal structures of substrate binding to Bacillus subtilis holo-(acyl carrier protein) synthase reveal a novel trimeric arrangement of molecules resulting in three active sites.
Structure Fold.Des.
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