1.4.7.1	E1013A	dramatically lowered activity	687217	
1.4.7.1	E1013D	dramatically lowered activity	687217	
1.4.7.1	E1013N	dramatically lowered activity	687217	
1.4.7.1	H1144Q	ratio between the ferredoxin-dependent and the methyl viologen-dependent GOGAT activities is decreased by 18.7fold	763549	
1.4.7.1	L1270F	retains wild type activity, in vivo: reduced mitochondrial serine hydroxymethyltransferase activity	700740	
1.4.7.1	M1K	targeted to the mitochondrion	700740	
1.4.7.1	M3I	targeted to the chloroplast	700740	
1.4.7.1	additional information	C6410T was found in a photorespiratory mutant, retains wild type activity, in vivo: reduced mitochondrial serine hydroxymethyltransferase activity	700740	
1.4.7.1	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	711597	
1.4.7.1	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	763549	
1.4.7.1	N1147A	ratio between the ferredoxin-dependent and the methyl viologen-dependent GOGAT activities is decreased by 47.4fold	763549	
1.4.7.1	Q467A	ratio between the ferredoxin-dependent and the methyl viologen-dependent GOGAT activities is decreased by 5.5fold	763549	
1.4.7.1	R1162A	ratio between the ferredoxin-dependent and the methyl viologen-dependent GOGAT activities is decreased by 4.7fold	763549	
1.4.7.1	W676A	ratio between the ferredoxin-dependent and the methyl viologen-dependent GOGAT activities is decreased by 6.7fold	763549	
1.4.7.1	W676F	ratio between the ferredoxin-dependent and the methyl viologen-dependent GOGAT activities is decreased by 7.9fold	763549