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7MFT

Glutamate synthase, glutamate dehydrogenase counter-enzyme complex (GudB6-GltA6-GltB6)

Functional Information from GO Data
ChainGOidnamespacecontents
A0004352molecular_functionglutamate dehydrogenase (NAD+) activity
A0006520biological_processamino acid metabolic process
A0006538biological_processL-glutamate catabolic process
A0016491molecular_functionoxidoreductase activity
A0016639molecular_functionoxidoreductase activity, acting on the CH-NH2 group of donors, NAD or NADP as acceptor
A0055114biological_processobsolete oxidation-reduction process
G0004355molecular_functionglutamate synthase (NADPH) activity
G0006537biological_processglutamate biosynthetic process
G0008652biological_processamino acid biosynthetic process
G0015930molecular_functionglutamate synthase activity
G0016491molecular_functionoxidoreductase activity
G0016638molecular_functionoxidoreductase activity, acting on the CH-NH2 group of donors
G0019676biological_processammonia assimilation cycle
G0046872molecular_functionmetal ion binding
G0051536molecular_functioniron-sulfur cluster binding
G0051538molecular_function3 iron, 4 sulfur cluster binding
G0097054biological_processL-glutamate biosynthetic process
I0004355molecular_functionglutamate synthase (NADPH) activity
I0006537biological_processglutamate biosynthetic process
I0008652biological_processamino acid biosynthetic process
I0016491molecular_functionoxidoreductase activity
I0016639molecular_functionoxidoreductase activity, acting on the CH-NH2 group of donors, NAD or NADP as acceptor
I0051536molecular_functioniron-sulfur cluster binding
I0097054biological_processL-glutamate biosynthetic process
Functional Information from PROSITE/UniProt
site_idPS00074
Number of Residues14
DetailsGLFV_DEHYDROGENASE Glu / Leu / Phe / Val dehydrogenases active site. LpyGGGKgGivcDP
ChainResidueDetails
ALEU110-PRO123

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI2
Number of Residues1
DetailsActive site: {"description":"Proton donor","evidences":[{"source":"PROSITE-ProRule","id":"PRU10011","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues60
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsSite: {"description":"Important for catalysis","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues393
DetailsDomain: {"description":"Glutamine amidotransferase type-2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00609","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues23
DetailsRegion: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues13
DetailsCompositional bias: {"description":"Basic and acidic residues","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues1
DetailsActive site: {"description":"For GATase activity","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues14
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

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PDB entries from 2025-12-03

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