CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.40 | 3-Layer(aba) Sandwich |
|
3.40.640 | Aspartate Aminotransferase; domain 2 |
|
3.40.640.10 | Type I PLP-dependent aspartate aminotransferase-like (Major domain) |
Domain Context
CATH Clusters
| Superfamily | Type I PLP-dependent aspartate aminotransferase-like (Major domain) |
| Functional Family |
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 | 3WCN |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Dimer-Dimer Interaction of the Bacterial Selenocysteine Synthase SelA Promotes Functional Active-Site Formation and Catalytic Specificity
J.Mol.Biol.
|
