Function and Biology Details
Reactions catalysed:
L-alanine + glyoxylate = pyruvate + glycine
(1a) L-kynurenine + glyoxylate = 4-(2-aminophenyl)-2,4-dioxobutanoate + glycine
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
- Aminotransferase class-V, pyridoxal-phosphate binding site
- Aminotransferase class V domain
- Pyridoxal phosphate-dependent transferase, major domain
- Pyridoxal phosphate-dependent transferase, small domain
- Serine-pyruvate aminotransferase/2-aminoethylphosphonate-pyruvate transaminase
- Pyridoxal phosphate-dependent transferase
Structure domain:
Structure analysis Details
Assembly composition:
homo dimer (preferred)
Assembly name:
3-hydroxykynurenine transaminase (preferred)
PDBe Complex ID:
PDB-CPX-566032 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
3-hydroxykynurenine transaminase
Molecule details ›
Chains: A, B, C, D
Length: 396 amino acids
Theoretical weight: 44.35 KDa
Source organism: Anopheles gambiae
Expression system: Escherichia coli BL21(DE3)
UniProt:
Sequence domains: Aminotransferase class-V
Structure domains:
Length: 396 amino acids
Theoretical weight: 44.35 KDa
Source organism: Anopheles gambiae
Expression system: Escherichia coli BL21(DE3)
UniProt:
- Canonical:
Q7PRG3 (Residues: 1-396; Coverage: 100%)
Sequence domains: Aminotransferase class-V
Structure domains:
