CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.90 | Alpha-Beta Complex |
|
3.90.1150 | Aspartate Aminotransferase, domain 1 |
|
3.90.1150.180 |
Domain Context
CATH Clusters
| Superfamily | 3.90.1150.180 |
| Functional Family | L-seryl-tRNA(Sec) selenium transferase |
Enzyme Information
| 2.9.1.1 |
L-seryl-tRNA(Sec) selenium transferase.
based on mapping to UniProt O67140
L-seryl-tRNA(Sec) + selenophosphate = L-selenocysteinyl-tRNA(Sec) + phosphate.
-!- Recognizes specifically tRNA(Sec)-species. -!- Binding of tRNA(Sec) also occurs in the absence of the seryl group. -!- 2-aminoacryloyl-tRNA, bound to the enzyme as an imine with the pyridoxal phosphate, is an intermediate in the reaction. -!- Since the selenium atom replaces oxygen in serine, the product may also be referred to as L-selenoseryl-tRNA(Sel). -!- The abbreviation Sel has also been used for selenocysteine but Sec is preferred.
|
UniProtKB Entries (1)
| O67140 |
SELA_AQUAE
Aquifex aeolicus VF5
L-seryl-tRNA(Sec) selenium transferase
|
PDB Structure
| PDB | 3W1I |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Decameric SelA-tRNA(Sec) ring structure reveals mechanism of bacterial selenocysteine formation
Science
|
