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 | Phosphopantetheinyl transferase |
Enzyme Information
| 2.7.8.7 |
Holo-[acyl-carrier-protein] synthase.
based on mapping to UniProt P39135
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.
|
| 2.7.8.- |
Transferases for other substituted phosphate groups.
based on mapping to UniProt P39135
|
UniProtKB Entries (1)
| P39135 |
SFP_BACSU
Bacillus subtilis subsp. subtilis str. 168
4'-phosphopantetheinyl transferase sfp
|
PDB Structure
| PDB | 1QR0 |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Bacillus |
| Primary Citation |
Crystal structure of the surfactin synthetase-activating enzyme sfp: a prototype of the 4'-phosphopantetheinyl transferase superfamily.
EMBO J.
|