CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
1 | Mainly Alpha |
|
1.20 | Up-down Bundle |
|
1.20.5 | Single alpha-helices involved in coiled-coils or other helix-helix interfaces |
|
1.20.5.460 | Single helix bin |
Domain Context
CATH Clusters
| Superfamily | Single helix bin |
| Functional Family | Bifunctional protein PutA |
Enzyme Information
| 1.5.5.2 |
Proline dehydrogenase.
based on mapping to UniProt P09546
L-proline + a quinone = (S)-1-pyrroline-5-carboxylate + a quinol.
-!- The electrons from L-proline are transferred to the FAD cofactor, and from there to a quinone acceptor. -!- In many organisms, ranging from bacteria to mammals, proline is oxidized to glutamate in a two-step process involving this enzyme and EC 1.2.1.88. -!- Both activities are carried out by the same enzyme in enterobacteria. -!- Formerly EC 1.5.99.8.
|
| 1.2.1.88 |
L-glutamate gamma-semialdehyde dehydrogenase.
based on mapping to UniProt P09546
L-glutamate 5-semialdehyde + NAD(+) + H(2)O = L-glutamate + NADH.
-!- This enzyme catalyzes the irreversible oxidation of glutamate-gamma- semialdehyde to glutamate as part of the proline degradation pathway. -!- (S)-1-pyrroline-5-carboxylate, the product of the first enzyme of the pathway (EC 1.5.5.2) is in spontaneous equilibrium with its tautomer L-glutamate gamma-semialdehyde. -!- In many bacterial species, both activities are carried out by a single bifunctional enzyme. -!- The enzyme can also oxidize other 1-pyrrolines, e.g. 3-hydroxy-1- pyrroline-5-carboxylate is converted into 4-hydroxyglutamate and (R)- 1-pyrroline-5-carboxylate is converted into D-glutamate. -!- NADP(+) can also act as acceptor, but with lower activity. -!- Formerly EC 1.5.1.12.
|
UniProtKB Entries (1)
| P09546 |
PUTA_ECOLI
Escherichia coli K-12
Bifunctional protein PutA
|
PDB Structure
| PDB | 2FZN |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Escherichia |
| Primary Citation |
Hydrogen Bonding Interactions of the 2-OH Ribityl Group and the N(5) Position of the FAD Cofactor Regulate PutA-membrane Associations in Escherichia coli
To be Published
|
