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
| 4.1.1.81 |
Threonine-phosphate decarboxylase.
based on mapping to UniProt P97084
L-threonine O-3-phosphate = (R)-1-aminopropan-2-yl phosphate + CO(2).
-!- Unable to decarboxylate the D-isomer of threonine O-3-phosphate. -!- The product of this reaction, (R)-1-aminopropan-2-yl phosphate, is the substrate of EC 6.3.1.10, which converts adenosylcobyric acid into adenosylcobinamide phosphate in the anaerobic cobalamin biosynthesis pathway.
|
UniProtKB Entries (1)
| P97084 |
COBD_SALTY
Salmonella enterica subsp. enterica serovar Typhimurium str. LT2
Threonine-phosphate decarboxylase
|
PDB Structure
| PDB | 1LC5 |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Escherichia |
| Primary Citation |
Structural studies of the L-threonine-O-3-phosphate decarboxylase (CobD) enzyme from Salmonella enterica: the apo, substrate, and product-aldimine complexes.
Biochemistry
|
