CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
2 | Mainly Beta |
|
2.40 | Beta Barrel |
|
2.40.110 | Butyryl-CoA Dehydrogenase, subunit A; domain 2 |
|
2.40.110.10 | Butyryl-CoA Dehydrogenase, subunit A, domain 2 |
Domain Context
CATH Clusters
| Superfamily | Butyryl-CoA Dehydrogenase, subunit A, domain 2 |
| Functional Family | L-prolyl-[peptidyl-carrier protein] dehydrogenase |
Enzyme Information
| 1.3.8.14 |
L-prolyl-[peptidyl-carrier protein] dehydrogenase.
based on mapping to UniProt Q5W271
L-prolyl-[peptidyl-carrier protein] + 2 electron-transfer flavoprotein = 1H-pyrrole-2-carbonyl-[peptidyl-carrier protein] + 2 reduced electron- transfer flavoprotein.
-!- The enzyme participates in the biosynthesis of several pyrrole- containing compounds, such as undecylprodigiosin, prodigiosin, pyoluteorin, and coumermycin A1. -!- It is believed to catalyze the formation of a Delta(2)-pyrrolin-2- yl(carbonyl)-S-[peptidyl-carrier protein] intermediate, followed by a two-electron oxidation to 1H-pyrrol-2-carbonyl-[peptidyl-carrier protein].
|
UniProtKB Entries (1)
| Q5W271 |
PIGA_SERS3
Serratia sp. ATCC 39006
L-prolyl-[peptidyl-carrier protein] dehydrogenase
|
PDB Structure
| PDB | 6AF6 |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Crystal Structure of PigA: A Prolyl Thioester-Oxidizing Enzyme in Prodigiosin Biosynthesis.
Chembiochem
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