Function and Biology Details
Reaction catalysed:
L-threonine O-3-phosphate = (R)-1-aminopropan-2-yl phosphate + CO(2)
Biochemical function:
Biological process:
Cellular component:
- not assigned
Sequence domains:
- Aminotransferases, class-I, pyridoxal-phosphate-binding site
- Pyridoxal phosphate-dependent transferase, major domain
- Pyridoxal phosphate-dependent transferase, small domain
- Aminotransferase, class I/classII, large domain
- L-threonine-O-3-phosphate decarboxylase
- Pyridoxal phosphate-dependent transferase
Structure domain:
Structure analysis Details
Assembly composition:
homo dimer (preferred)
Assembly name:
Threonine-phosphate decarboxylase (preferred)
PDBe Complex ID:
PDB-CPX-161271 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Threonine-phosphate decarboxylase
Molecule details ›
Chain: A
Length: 364 amino acids
Theoretical weight: 40.85 KDa
Source organism: Salmonella enterica
Expression system: Escherichia coli
UniProt:
Sequence domains: Aminotransferase class I and II
Structure domains:
Length: 364 amino acids
Theoretical weight: 40.85 KDa
Source organism: Salmonella enterica
Expression system: Escherichia coli
UniProt:
- Canonical:
P97084 (Residues: 1-364; Coverage: 100%)
Sequence domains: Aminotransferase class I and II
Structure domains:
