Function and Biology Details
Reactions catalysed:
(1a) L-glutamine + H(2)O = L-glutamate + NH(3)
L-glutamine + H(2)O = L-glutamate + NH(3)
Biochemical function:
Biological process:
Cellular component:
Structure analysis Details
Assembly composition:
hetero 24-mer (preferred)
Assembly name:
Pyridoxal 5'-phosphate synthase (preferred)
PDBe Complex ID:
PDB-CPX-194548 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Pyridoxal 5'-phosphate synthase subunit PdxS
Molecule details ›
Chains: A, B, C
Length: 313 amino acids
Theoretical weight: 34.35 KDa
Source organism: Thermotoga maritima
Expression system: Escherichia coli
UniProt:
Sequence domains: SOR/SNZ family
Structure domains: Aldolase class I
Length: 313 amino acids
Theoretical weight: 34.35 KDa
Source organism: Thermotoga maritima
Expression system: Escherichia coli
UniProt:
- Canonical:
Q9WYU4 (Residues: 1-293; Coverage: 100%)
Sequence domains: SOR/SNZ family
Structure domains: Aldolase class I
Pyridoxal 5'-phosphate synthase subunit PdxT
Molecule details ›
Chains: D, E, F
Length: 208 amino acids
Theoretical weight: 23.38 KDa
Source organism: Thermotoga maritima
Expression system: Escherichia coli
UniProt:
Sequence domains: SNO glutamine amidotransferase family
Structure domains: Rossmann fold
Length: 208 amino acids
Theoretical weight: 23.38 KDa
Source organism: Thermotoga maritima
Expression system: Escherichia coli
UniProt:
- Canonical: Q9WYU3 (Residues: 1-188; Coverage: 100%)
Sequence domains: SNO glutamine amidotransferase family
Structure domains: Rossmann fold
