Function and Biology Details
Reaction catalysed:
L-glutamine + D-fructose 6-phosphate = L-glutamate + D-glucosamine 6-phosphate
Biochemical function:
Biological process:
Cellular component:
- not assigned
Sequence domains:
- SIS domain
- Nucleophile aminohydrolases, N-terminal
- GlmS/FrlB, SIS domain 2
- GlmS/AgaS, SIS domain 1
- SIS domain superfamily
- Glucosamine-fructose-6-phosphate aminotransferase, isomerising
- Glucosamine-fructose-6-phosphate aminotransferase, isomerising, N-terminal domain
- Glutamine amidotransferase type 2 domain
Structure analysis Details
Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-170306 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Glutamine--fructose-6-phosphate aminotransferase [isomerizing] 1
Molecule details ›
Chain: A
Length: 687 amino acids
Theoretical weight: 77.82 KDa
Source organism: Homo sapiens
Expression system: Spodoptera frugiperda
UniProt:
Sequence domains:
Length: 687 amino acids
Theoretical weight: 77.82 KDa
Source organism: Homo sapiens
Expression system: Spodoptera frugiperda
UniProt:
- Canonical:
Q06210 (Residues: 1-317, 318-699; Coverage: 97%)
Sequence domains:
Glutamine--fructose-6-phosphate aminotransferase [isomerizing] 1
Molecule details ›
Chain: B
Length: 687 amino acids
Theoretical weight: 77.74 KDa
Source organism: Homo sapiens
Expression system: Spodoptera frugiperda
UniProt:
Sequence domains:
Length: 687 amino acids
Theoretical weight: 77.74 KDa
Source organism: Homo sapiens
Expression system: Spodoptera frugiperda
UniProt:
- Canonical: Q06210 (Residues: 1-317, 318-699; Coverage: 97%)
Sequence domains:
