Function and Biology Details
Reaction catalysed:
(1a) L-glutamine + H(2)O = L-glutamate + NH(4)(+)
Biochemical function:
Biological process:
Cellular component:
- not assigned
Structure analysis Details
Assembly composition:
monomeric (preferred)
Assembly name:
GMP synthase [glutamine-hydrolyzing] subunit A (preferred)
PDBe Complex ID:
PDB-CPX-176719 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
GMP synthase [glutamine-hydrolyzing] subunit A
Molecule details ›
Chain: A
Length: 188 amino acids
Theoretical weight: 21.05 KDa
Source organism: Methanocaldococcus jannaschii DSM 2661
Expression system: Escherichia coli
UniProt:
Sequence domains: Glutamine amidotransferase class-I
Structure domains: Rossmann fold
Length: 188 amino acids
Theoretical weight: 21.05 KDa
Source organism: Methanocaldococcus jannaschii DSM 2661
Expression system: Escherichia coli
UniProt:
- Canonical:
Q58970 (Residues: 1-188; Coverage: 100%)
Sequence domains: Glutamine amidotransferase class-I
Structure domains: Rossmann fold
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
Chemical shift assignment:
56%
Refinement method:
na
Expression system: Escherichia coli
