Function and Biology Details
Reaction catalysed:
(1a) L-glutamate + NH(3) = L-glutamine + H(2)O
Biochemical function:
Biological process:
Cellular component:
- not assigned
Sequence domains:
- FAD/NAD(P)-binding domain superfamily
- Ferredoxin-NADP reductase (FNR), nucleotide-binding domain
- FAD/NAD(P)-binding domain
- Dihydroprymidine dehydrogenase domain II
- Sulfide dehydrogenase subunit alpha-like
- Alpha-helical ferredoxin
- Dihydroorotate dehydrogenase, electron transfer subunit, iron-sulphur cluster binding domain
- Oxidoreductase FAD/NAD(P)-binding
4 more domains
Structure analysis Details
Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-194849 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Dihydroorotate dehydrogenase B (NAD(+)), electron transfer subunit homolog
Molecule details ›
Chains: A, C
Length: 276 amino acids
Theoretical weight: 30.56 KDa
Source organism: Thermotoga maritima MSB8
Expression system: Escherichia coli BL21(DE3)
UniProt:
Sequence domains:
Length: 276 amino acids
Theoretical weight: 30.56 KDa
Source organism: Thermotoga maritima MSB8
Expression system: Escherichia coli BL21(DE3)
UniProt:
- Canonical:
Q9X1X4 (Residues: 1-276; Coverage: 98%)
Sequence domains:
Glutamate synthase, beta subunit
Molecule details ›
Chains: B, D
Length: 468 amino acids
Theoretical weight: 51.68 KDa
Source organism: Thermotoga maritima MSB8
Expression system: Escherichia coli BL21(DE3)
UniProt:
Sequence domains:
Length: 468 amino acids
Theoretical weight: 51.68 KDa
Source organism: Thermotoga maritima MSB8
Expression system: Escherichia coli BL21(DE3)
UniProt:
- Canonical: Q9X1X5 (Residues: 1-468; Coverage: 100%)
Sequence domains:
