1.4.1.13: glutamate synthase (NADPH)
This is an abbreviated version!
For detailed information about glutamate synthase (NADPH), go to the full flat file.
Word Map on EC 1.4.1.13
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1.4.1.13
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nitrate
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ammonia
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seedling
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no3
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ferredoxin-dependent
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chlorophyll
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shoot
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ferredoxin
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6.3.1.2
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iron-sulfur
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nadh-dependent
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azaserine
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nitrogenase
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1.4.7.1
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azospirillum
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assimilatory
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alpha-ketoglutarate
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brasilense
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amidotransferase
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glutaminase
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hydroponic
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photorespiratory
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photorespiration
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15n-labeled
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n2-fixing
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molecular biology
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nadp-glutamate
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heterocysts
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glutamine-dependent
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ureides
- 1.4.1.13
- nitrate
- ammonia
- seedling
- no3
-
ferredoxin-dependent
- chlorophyll
- shoot
- ferredoxin
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6.3.1.2
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iron-sulfur
-
nadh-dependent
- azaserine
- nitrogenase
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1.4.7.1
- azospirillum
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assimilatory
- alpha-ketoglutarate
- brasilense
-
amidotransferase
- glutaminase
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hydroponic
-
photorespiratory
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photorespiration
-
15n-labeled
-
n2-fixing
- molecular biology
-
nadp-glutamate
- heterocysts
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glutamine-dependent
-
ureides
Reaction
2 L-glutamate
+
Synonyms
EC 2.6.1.53, EhNO1, EhNO2, gltA, gltB, GltB1, GltB2, gltD, GltS, glutamate synthetase (NADP), glutamine amide-2-oxoglutarate aminotransferase (oxidoreductase, NADP), glutamine-ketoglutaric aminotransferase, GOGAT, L-glutamate synthase, L-glutamate synthetase, L-glutamine:2-oxoglutarate aminotransferase, NADPH oxidizing, NADPH-dependent glutamate synthase, NADPH-GltS, NADPH-glutamate synthase, NADPH-GOGAT, NADPH-linked glutamate synthase, pGLTY1, pGLTY2, pGLTZ, PH0876, PH1873, synthase, glutamate (reduced nicotinamide adenine dinucleotide phosphate)
ECTree
1.4.1.13 glutamate synthase (NADPH)Advanced search results
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results (Cofactor
Cofactor on EC 1.4.1.13 - glutamate synthase (NADPH)
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COFACTOR 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
IMAGE
[4Fe-4S]-center
the [4Fe-4S]+1,+2 cluster A displays three Cys and one Glu ligands for the Fe atoms. Residues Cys105 and Cys60 are linked to Fe1 and Fe2, respectively and the Fe3 atom shows bidentate coordination to Glu125 carboxylate, Fe4 is coordinated to Cys99, whose Calpha atom falls 5 A from FAD dimethyl-benzene ring C8 methyl. All Cys ligands to the [4Fe-4S]+1,+2 cluster B (Cys48, Cys51, Cys56, Cys109) are comprised in small subunit GltD loops at the interface with GltB
FAD
the isoalloxazine ring is almost solvent inaccessible, neighboring residues are Ile98, Pro100, Leu186, Ile191, Lys195, Leu266, Asp300, Thr301, Asp304, Leu450 and Val451, together with backbone atoms of the surrounding regions
flavin
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0.86 mol FAD per mol of mutant beta subunit, 0.83 mol FAD per mol of the wild type species
flavin
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the alpha subunit contains FMN as flavin cofactor, 0.94 FMN bound per alpha subunit
flavin
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the beta subunit contains the binding site for FAD, 0.83 mol FAD per mol beta subunit
NADPH
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the C-terminal potential ADP-binding fold of the beta subunit is the NADPH-binding site of the enzyme
NADPH
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the beta subunit contains the NADPH binding site of the enzyme
additional information
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the enzyme contains three distinct ion-sulfur centers per alphabeta protomer
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additional information
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the enzyme contains 8.1 acid-labile sulfur atoms per 220000-dalton dimer
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additional information
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the enzyme contains three different iron-sulfur clusters, one 3Fe-4S center on the alpha subunit and two 4Fe-4S clusters of unknown location, 11.7 mol sulfur per mol alphabeta protomer
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additional information
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purified enzyme contains 30.4 mol of labile sulfide per 800,000 g of protein
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additional information
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the alpha subunit contains the [3Fe-4S] cluster of the enzyme
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additional information
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midpoint potential value of the FMN cofactor: approximately -240 mV, midpoint potential value of the 3Fe-4S cluster: approximately -270 mV, midpoint potential value of the FAD cofactor: approximately -340 mV for the beta subunit and -300 mV for the holoenzyme
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additional information
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the FMN and FAD prosthetic groups are demonstrated to be nonequivalent with respect to their reactivities with sulfite, sulfite reacts with only one of the two flavins forming an N(5)-sulfite adduct
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additional information
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thio-NADPH and acetylpyridine-NADPH can be used as electron donors but are less efficient than NADPH
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additional information
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the enzyme contains 7.9 sulfur atoms per protomer with a molecular weight of 185000
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additional information
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the enzyme contains 7.2 mol of acid-labile sulfur per 200,000 g of protein
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