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Information on EC 1.4.7.1 - glutamate synthase (ferredoxin) and Organism(s) Arabidopsis thaliana and UniProt Accession Q9ZNZ7
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1.4.7.1 glutamate synthase (ferredoxin)IUBMB Comments
Binds a [3Fe-4S] cluster as well as FAD and FMN. The protein is composed of two domains, one hydrolysing L-glutamine to NH3 and L-glutamate (cf. EC 3.5.1.2, glutaminase), the other combining the produced NH3 with 2-oxoglutarate to produce a second molecule of L-glutamate. The NH3 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 [5,6].
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The taxonomic range for the selected organisms is: Arabidopsis thaliana
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Reaction Schemes
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Synonyms
fd-gogat, ferredoxin-dependent glutamate synthase, fd-dependent glutamate synthase, ferredoxin-glutamate synthase, ferredoxin-gogat, ferredoxin-dependent gogat, fd-gogat1, ferredoxin-dependent glts, fdgogat, ferredoxin-dependent glutamate synthase1, 
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topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Fd-GOGAT
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-
-
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ferredoxin-dependent glutamate synthase
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-
-
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ferredoxin-glutamate synthase
glutamate synthase (ferredoxin-dependent)
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-
-
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ferredoxin-glutamate synthase
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-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
redox reaction
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-
-
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oxidation
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-
-
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reduction
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-
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transamination
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-
-
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PATHWAY SOURCE
PATHWAYS
KEGG
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-, -, -, -
SYSTEMATIC NAME
IUBMB Comments
L-glutamate:ferredoxin oxidoreductase (transaminating)
Binds a [3Fe-4S] cluster as well as FAD and FMN. The protein is composed of two domains, one hydrolysing L-glutamine to NH3 and L-glutamate (cf. EC 3.5.1.2, glutaminase), the other combining the produced NH3 with 2-oxoglutarate to produce a second molecule of L-glutamate. The NH3 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 [5,6].
CAS REGISTRY NUMBER
COMMENTARY
62213-56-3
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2 L-glutamate + 2 oxidized ferredoxin
L-glutamine + 2-oxoglutarate + 2 reduced ferredoxin + 2 H+
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-
-
?
L-glutamine + 2-oxoglutarate + 2 reduced methyl viologen
2 L-glutamate + 2 oxidized methyl viologen
reductant: Na2S2O4
-
-
?
L-glutamine + 2-oxoglutarate + reduced methyl viologen + H+
L-glutamate + oxidized methyl viologen
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-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2 L-glutamate + 2 oxidized ferredoxin
L-glutamine + 2-oxoglutarate + 2 reduced ferredoxin + 2 H+
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-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
glu1 mainly expressed in the leaves, at significantly higher level than glu2
additional information
glu1 mainly expressed in the leaves, at significantly higher level than glu2
additional information
Fd-GOGAT1 is more highly expressed in leaves than in roots
additional information
-
Fd-GOGAT1 is more highly expressed in leaves than in roots
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
Glu1 is involved in the primary nitrogen assimilation, primary nitrogen assimilation and glutamate metabolism overview. Metabolic profiling and gene expression profiling in glu1-2 knockout mutant, most significantly affected pathways in the Glu1 knockout mutant glu1-2, photosynthesis, photorespiratory cycle and chlorophyll biosynthesis show an overall downregulation in glu1-2 leaves in accordance with their slight chlorotic phenotype, numerous other responsive genes linked to a number of different stresses/stimuli are induced in glu1-2 leaves, very detailed overview
physiological function
GLU1 is involved in iron homeostasis through affecting glutamate synthesis under iron deficiency conditions in Arabidopsis. Lesion of GLU1 results in reduced transcription of many iron-deficiency responsive genes in roots and shoots. The mutant plants reveal a decreased iron concentration in the shoots, and display severe leaf chlorosis under the condition of iron limitation, compared to wild-type. The product of GLU1, glutamate, can chelate iron in vivo and promote iron transportation
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). GLTB1_ARATH
1622
0
176752
Swiss-Prot
Chloroplast (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
L1270F
retains wild type activity, in vivo: reduced mitochondrial serine hydroxymethyltransferase activity
additional information
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
-
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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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
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene glu1 or gls1, genome wide microarray analysis of the transcriptional reprogramming, overview
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
expression of GLU1 is strongly induced by iron deficiency condition
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Ishizaki, T.; Ohsumi, C.; Totsuka, K.; Igarashi, D.
Analysis of glutamate homeostasis by overexpression of Fd-GOGAT gene in Arabidopsis thaliana
Amino Acids
38
943-950
2009
Arabidopsis thaliana (Q9ZNZ7), Arabidopsis thaliana
Potel, F.; Valadier, M.H.; Ferrario-Mery, S.; Grandjean, O.; Morin, H.; Gaufichon, L.; Boutet-Mercey, S.; Lothier, J.; Rothstein, S.J.; Hirose, N.; Suzuki, A.
Assimilation of excess ammonium into amino acids and nitrogen translocation in Arabidopsis thaliana - roles of glutamate synthases and carbamoylphosphate synthetase in leaves
FEBS J.
276
4061-4076
2009
Arabidopsis thaliana (Q9T0P4), Arabidopsis thaliana (Q9ZNZ7)
Jamai, A.; Salome, P.A.; Schilling, S.H.; Weber, A.P.; McClung, C.R.
Arabidopsis photorespiratory serine hydroxymethyltransferase activity requires the mitochondrial accumulation of ferredoxin-dependent glutamate synthase
Plant Cell
21
595-606
2009
Arabidopsis thaliana, Arabidopsis thaliana (Q9ZNZ7)
Kissen, R.; Winge, P.; Tran, D.H.; Joerstad, T.S.; Stoerseth, T.R.; Christensen, T.; Bones, A.M.
Transcriptional profiling of an Fd-GOGAT1/GLU1 mutant in Arabidopsis thaliana reveals a multiple stress response and extensive reprogramming of the transcriptome
BMC Genomics
11
190
2010
Arabidopsis thaliana (Q9ZNZ7), Arabidopsis thaliana
Takabayashi, A.; Niwata, A.; Tanaka, A.
Direct interaction with ACR11 is necessary for post-transcriptional control of GLU1-encoded ferredoxin-dependent glutamate synthase in leaves
Sci. Rep.
6
29668
2016
Arabidopsis thaliana (Q9ZNZ7)
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