Function and Biology Details
Reaction catalysed:
ATP + N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide + L-glutamine + H(2)O = ADP + phosphate + 2-(formamido)-N(1)-(5-phospho-D-ribosyl)acetamidine + L-glutamate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
- PurM-like, N-terminal domain superfamily
- PurM-like, C-terminal domain superfamily
- Phosphoribosylformylglycinamidine subunit PurL
- PurM-like, N-terminal domain
- PurL, C-terminal domain superfamily
- Phosphoribosylformylglycinamidine subunit PurL, C-terminal
- PurM-like, C-terminal domain
- Phosphoribosylformylglycinamidine synthase, linker domain
Structure domains:
Structure analysis Details
Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-194752 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Phosphoribosylformylglycinamidine synthase subunit PurL
Molecule details ›
Chain: A
Length: 615 amino acids
Theoretical weight: 68.3 KDa
Source organism: Thermotoga maritima
Expression system: Escherichia coli
UniProt:
Sequence domains:
Length: 615 amino acids
Theoretical weight: 68.3 KDa
Source organism: Thermotoga maritima
Expression system: Escherichia coli
UniProt:
- Canonical:
Q9X0X3 (Residues: 1-603; Coverage: 100%)
Sequence domains:
- Formylglycinamide ribonucleotide amidotransferase linker domain
- AIR synthase related protein, N-terminal domain
- AIR synthase related protein, C-terminal domain
- Phosphoribosylformylglycinamidine synthase II C-terminus
