Function and Biology Details
Reactions catalysed:
L-glutamine + H(2)O = L-glutamate + NH(3)
(1a) L-glutamine + H(2)O = L-glutamate + NH(3)
Biochemical function:
Biological process:
Cellular component:
- not assigned
Sequence domains:
- Mur-like, catalytic domain superfamily
- Class I glutamine amidotransferase-like
- Lipid II isoglutaminyl synthase (glutamine-hydrolyzing) subunit MurT, C-terminal
- Mur ligase, central
- Lipid II isoglutaminyl synthase (glutamine-hydrolyzing) subunit MurT
- Cobyric acid synthase, glutamine amidotransferase type 1
- CobB/CobQ-like glutamine amidotransferase
- Lipid II isoglutaminyl synthase (glutamine-hydrolyzing) subunit GatD
Structure analysis Details
Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-101916 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Lipid II isoglutaminyl synthase (glutamine-hydrolyzing) subunit GatD
Molecule details ›
Chains: A, C
Length: 251 amino acids
Theoretical weight: 28.54 KDa
Source organism: Staphylococcus aureus subsp. aureus N315
Expression system: Escherichia coli
UniProt:
Sequence domains: CobB/CobQ-like glutamine amidotransferase domain
Length: 251 amino acids
Theoretical weight: 28.54 KDa
Source organism: Staphylococcus aureus subsp. aureus N315
Expression system: Escherichia coli
UniProt:
- Canonical:
A0A0H3JN63 (Residues: 1-243; Coverage: 100%)
Sequence domains: CobB/CobQ-like glutamine amidotransferase domain
Lipid II isoglutaminyl synthase (glutamine-hydrolyzing) subunit MurT
Molecule details ›
Chains: B, D
Length: 437 amino acids
Theoretical weight: 49.25 KDa
Source organism: Staphylococcus aureus
Expression system: Escherichia coli
UniProt:
Sequence domains:
Length: 437 amino acids
Theoretical weight: 49.25 KDa
Source organism: Staphylococcus aureus
Expression system: Escherichia coli
UniProt:
- Canonical: A0A0H3JUU7 (Residues: 1-437; Coverage: 100%)
Sequence domains:
