1.4.7.1: glutamate synthase (ferredoxin)
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For detailed information about glutamate synthase (ferredoxin), go to the full flat file.
Word Map on EC 1.4.7.1
Reaction
2 L-glutamate
+
Synonyms
abc1, At5g04140, ES7, Fd-dependent glutamate synthase, Fd-GOGAT, Fd-GOGAT1, FdGOGAT, ferredoxin-dependent GltS, ferredoxin-dependent glutamate synthase, ferredoxin-dependent glutamate synthase1, ferredoxin-dependent glutamine 2-oxoglutarate aminotransferase, ferredoxin-dependent GOGAT, ferredoxin-glutamate synthase, ferredoxin-GOGAT, gltB, GltS, Glu1, glutamate synthase, glutamate synthase (ferredoxin-dependent), glutamine 2-oxoglutarate amidotransferase, glutamine:2-oxoglutarate amidotransferase, glutamine:oxoglutarate amidotransferase, GOGAT, lc7
ECTree
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Engineering on EC 1.4.7.1 - glutamate synthase (ferredoxin)
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
L1270F
retains wild type activity, in vivo: reduced mitochondrial serine hydroxymethyltransferase activity
H1144Q
ratio between the ferredoxin-dependent and the methyl viologen-dependent GOGAT activities is decreased by 18.7fold
N1147A
ratio between the ferredoxin-dependent and the methyl viologen-dependent GOGAT activities is decreased by 47.4fold
Q467A
ratio between the ferredoxin-dependent and the methyl viologen-dependent GOGAT activities is decreased by 5.5fold
R1162A
ratio between the ferredoxin-dependent and the methyl viologen-dependent GOGAT activities is decreased by 4.7fold
W676A
ratio between the ferredoxin-dependent and the methyl viologen-dependent GOGAT activities is decreased by 6.7fold
W676F
ratio between the ferredoxin-dependent and the methyl viologen-dependent GOGAT activities is decreased by 7.9fold
additional information
additional information
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C6410T was found in a photorespiratory mutant, retains wild type activity, in vivo: reduced mitochondrial serine hydroxymethyltransferase activity
additional information
C6410T was found in a photorespiratory mutant, retains wild type activity, in vivo: reduced mitochondrial serine hydroxymethyltransferase activity
additional information
knockout mutant glu1-2, with a T-DNA insertion in the Fd-GOGAT1, lacks expression of Fd-GOGAT1, transcriptional profiling of glu1-2 showing activation of multiple stress responses, mimicking cold, heat, drought and oxidative stress, overview. NMR analysis of glu1-2 mutant leaves and roots reveal differences in amino acid contents compared to the wild-type, overview
additional information
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knockout mutant glu1-2, with a T-DNA insertion in the Fd-GOGAT1, lacks expression of Fd-GOGAT1, transcriptional profiling of glu1-2 showing activation of multiple stress responses, mimicking cold, heat, drought and oxidative stress, overview. NMR analysis of glu1-2 mutant leaves and roots reveal differences in amino acid contents compared to the wild-type, overview
additional information
residues Gln467, His1144, Asn1147, Arg1162, and Trp676 constitute key binding residues in the interface of a glutamate synthase:ferredoxin complex. All interfacial mutants studied are able to form a complex under low ionic strength, but show significantly less ferredoxin-dependent activities, while still retaining enzymatic activity
additional information
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residues Gln467, His1144, Asn1147, Arg1162, and Trp676 constitute key binding residues in the interface of a glutamate synthase:ferredoxin complex. All interfacial mutants studied are able to form a complex under low ionic strength, but show significantly less ferredoxin-dependent activities, while still retaining enzymatic activity
