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 | O-phosphoseryl-tRNA(Sec) selenium transferase |
Enzyme Information
| 2.9.1.2 |
O-phospho-L-seryl-tRNA(Sec):L-selenocysteinyl-tRNA synthase.
based on mapping to UniProt Q9HD40
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)
| Q9HD40 |
SPCS_HUMAN
Homo sapiens
O-phosphoseryl-tRNA(Sec) selenium transferase
|
PDB Structure
| PDB | 4ZDO |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Structural basis for early-onset neurological disorders caused by mutations in human selenocysteine synthase.
Sci Rep
|
