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-153421 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Pyridoxal 5'-phosphate synthase subunit PdxS
Molecule details ›
Chains: A, C, E, G, I, K, M, O, Q, S, U, W
Length: 294 amino acids
Theoretical weight: 31.65 KDa
Source organism: Bacillus subtilis
Expression system: Escherichia coli
UniProt:
Sequence domains: SOR/SNZ family
Structure domains: Aldolase class I
Length: 294 amino acids
Theoretical weight: 31.65 KDa
Source organism: Bacillus subtilis
Expression system: Escherichia coli
UniProt:
- Canonical:
P37527 (Residues: 1-294; Coverage: 100%)
Sequence domains: SOR/SNZ family
Structure domains: Aldolase class I
Pyridoxal 5'-phosphate synthase subunit PdxT
Molecule details ›
Chains: B, D, F, H, J, L, N, P, R, T, V, X
Length: 204 amino acids
Theoretical weight: 22.52 KDa
Source organism: Bacillus subtilis
Expression system: Escherichia coli
UniProt:
Sequence domains:
Structure domains: Rossmann fold
Length: 204 amino acids
Theoretical weight: 22.52 KDa
Source organism: Bacillus subtilis
Expression system: Escherichia coli
UniProt:
- Canonical: P37528 (Residues: 1-196; Coverage: 100%)
Sequence domains:
Structure domains: Rossmann fold
