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 dimer (preferred)
Assembly name:
Imidazole glycerol phosphate synthase (preferred)
PDBe Complex ID:
PDB-CPX-194693 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Imidazole glycerol phosphate synthase subunit HisF
Molecule details ›
Chains: A, C, E
Length: 253 amino acids
Theoretical weight: 27.75 KDa
Source organism: Thermotoga maritima
Expression system: Escherichia coli
UniProt:
Sequence domains: Histidine biosynthesis protein
Structure domains: Aldolase class I
Length: 253 amino acids
Theoretical weight: 27.75 KDa
Source organism: Thermotoga maritima
Expression system: Escherichia coli
UniProt:
- Canonical:
Q9X0C6 (Residues: 1-253; Coverage: 100%)
Sequence domains: Histidine biosynthesis protein
Structure domains: Aldolase class I
Imidazole glycerol phosphate synthase subunit HisH
Molecule details ›
Chains: B, D, F
Length: 201 amino acids
Theoretical weight: 23.13 KDa
Source organism: Thermotoga maritima
Expression system: Escherichia coli
UniProt:
Sequence domains:
Structure domains: Rossmann fold
Length: 201 amino acids
Theoretical weight: 23.13 KDa
Source organism: Thermotoga maritima
Expression system: Escherichia coli
UniProt:
- Canonical: Q9X0C8 (Residues: 1-201; Coverage: 100%)
Sequence domains:
Structure domains: Rossmann fold
