CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.30 | 2-Layer Sandwich |
|
3.30.460 | Beta Polymerase; domain 2 |
|
3.30.460.30 | Glutamyl-tRNA reductase, N-terminal domain |
Domain Context
CATH Clusters
| Superfamily | Glutamyl-tRNA reductase, N-terminal domain |
| Functional Family | Glutamyl-tRNA reductase |
Enzyme Information
| 1.2.1.70 |
Glutamyl-tRNA reductase.
based on mapping to UniProt P42804
L-glutamate 1-semialdehyde + NADP(+) + tRNA(Glu) = L-glutamyl-tRNA(Glu) + NADPH.
-!- Forms part of the pathway for the biosynthesis of 5-aminolevulinate from glutamate, known as the C5 pathway, which is used in most eubacteria, and in all archaebacteria, algae and plants. -!- However, in the alpha-proteobacteria EC 2.3.1.37 is used in an alternative route to produce the product 5-aminolevulinate from succinyl-CoA and glycine. -!- This route is found in the mitochondria of fungi and animals, organelles that are considered to be derived from an endosymbiotic alpha-proteobacterium. -!- Although higher plants do not possess EC 2.3.1.37, the protistan Euglena gracilis possesses both the C5 pathway and EC 2.3.1.37.
|
UniProtKB Entries (1)
| Q940U6 |
FLU_ARATH
Arabidopsis thaliana
Protein FLUORESCENT IN BLUE LIGHT, chloroplastic
|
PDB Structure
| PDB | 5CHE |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
The Arabidopsis glutamyl-tRNA reductase (GluTR) forms a ternary complex with FLU and GluTR-binding protein
Sci Rep
|