_EC 1.4.7.1 Glutamate synthase (ferredoxin). 5 PDB entries  
EC 1.-.-.- Oxidoreductases. [8,010 PDB entries]
EC 1.4.-.- Acting on the CH-NH(2) group of donors. [338 PDB entries]
EC 1.4.7.- With an iron-sulfur protein as acceptor. [5 PDB entries]
EC 1.4.7.1 Glutamate synthase (ferredoxin). [5 PDB entries]    
1llw

Reaction: 2 L-glutamate + 2 oxidized ferredoxin = L-glutamine + 2-oxoglutarate + 2 reduced ferredoxin + 2 H(+).
 


2 × L-glutamate
+ 2 × oxidized ferredoxin
=
L-glutamine
+
2-oxoglutarate
+ 2 × reduced ferredoxin
+ 2 × H(+)
Molecule diagrams generated from .mol files obtained from the KEGG ftp site.

Other name(s): Ferredoxin-dependent glutamate synthase.
Cofactor(s): FAD; FMN; Iron-sulfur.
 

FAD

FMN

Iron-sulfur
Molecule diagrams generated from .mol files obtained from the KEGG ftp site.
Comments: The protein is composed of two domains, one hydrolyzing L-glutamine to NH(3) and L-glutamate (cf. Ec 3.5.1.2), the other combining the produced NH(3) with 2-oxoglutarate to produce a second molecule of L-glutamate. The NH(3) is channeled through a 24 A channel in the active protein. No hydrolysis of glutamine takes place without ferredoxin and 2-oxoglutarate being bound to the protein.
Links:   [IntEnz]   [ExPASy]   [KEGG]  

There are 5 PDB entries in enzyme class E.C.1.4.7.1

  PDB code Protein
1llw
Structural studies on the synchronization of catalytic cente glutamate synthase: complex with 2-oxoglutarate
Source: Synechocystis sp. Pcc 6803. Organism_taxid: 1148. Strain: pcc6803. Expressed in: escherichia coli. Expression_system_taxid: 562
Chain: A (1475 residues) CATH domains: 3.60.20.10 3.20.20.70 3.20.20.70 2.160.20.60
Bound ligand:   Het Group AKG corresponds to enzyme product L-glutamate
1llz
Structural studies on the synchronization of catalytic cente glutamate synthase: reduced enzyme
Source: Synechocystis sp. Pcc 6803. Organism_taxid: 1148. Strain: pcc6803. Expressed in: escherichia coli. Expression_system_taxid: 562
Chain: A (1475 residues) CATH domains: 3.60.20.10 3.20.20.70 3.20.20.70 2.160.20.60
1lm1
Structural studies on the synchronization of catalytic cente glutamate synthase: native enzyme
Source: Synechocystis sp. Pcc 6803. Organism_taxid: 1148. Strain: pcc6803. Expressed in: escherichia coli. Expression_system_taxid: 562
Chain: A (1475 residues) CATH domains: 3.60.20.10 3.20.20.70 3.20.20.70 2.160.20.60
Bound ligand:   Het Group ACT is 40.00% similar to enzyme reactant L-glutamate
1ofd
Glutamate synthase from synechocystis sp in complex with 2-oxoglutarate at 2.0 angstrom resolution
Source: Synechocystis sp.. Organism_taxid: 1148. Strain: pcc6803. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B (1491 residues) CATH domains: 3.60.20.10 3.20.20.70 3.20.20.70 2.160.20.60
Bound ligand:   Het Group AKG corresponds to enzyme product L-glutamate
1ofe
Glutamate synthase from synechocystis sp in complex with 2-oxoglutarate and l-don at 2.45 angstrom resolution
Source: Synechocystis sp.. Organism_taxid: 1148. Strain: pcc6803. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B (1485 residues) CATH domains: 3.60.20.10 3.20.20.70 3.20.20.70 2.160.20.60
Bound ligands:   Het Group ONL is 81.82% similar to enzyme product L-glutamate
  Het Group AKG corresponds to enzyme product