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
| 2.9.1.2 |
O-phospho-L-seryl-tRNA(Sec):L-selenocysteinyl-tRNA synthase.
based on mapping to UniProt Q6P6M7
O-phospho-L-seryl-tRNA(Sec) + selenophosphate + H(2)O = L-selenocysteinyl-tRNA(Sec) + 2 phosphate.
-!- In archaea and eukarya selenocysteine formation is achieved by a two- step process: EC 2.7.1.164 phosphorylates the endogenous L-seryl- tRNA(Sec) to O-phospho-L-seryl-tRNA(Sec), and then this misacylated amino acid-tRNA species is converted to L-selenocysteinyl-tRNA(Sec) by Sep-tRNA:Sec-tRNA synthase. -!- Formerly EC 2.9.1.n1.
|
UniProtKB Entries (1)
| Q6P6M7 |
SPCS_MOUSE
Mus musculus
O-phosphoseryl-tRNA(Sec) selenium transferase
|
PDB Structure
| PDB | 3BC8 |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Escherichia |
| Primary Citation |
Structure and catalytic mechanism of eukaryotic selenocysteine synthase.
J.Biol.Chem.
|
