Information on EC 1.4.7.1 - glutamate synthase (ferredoxin)

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea

EC NUMBER
COMMENTARY hide
1.4.7.1
-
RECOMMENDED NAME
GeneOntology No.
glutamate synthase (ferredoxin)
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
2 L-glutamate + 2 oxidized ferredoxin = L-glutamine + 2-oxoglutarate + 2 reduced ferredoxin + 2 H+
show the reaction diagram
L-glutamate + 2 oxidized ferredoxin + H2O = NH3 + 2-oxoglutarate + 2 reduced ferredoxin + 2 H+
show the reaction diagram
1b
-
-
-
L-glutamate + NH3 = L-glutamine + H2O
show the reaction diagram
1a
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
transamination
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
ammonia assimilation cycle II
-
-
glutamate and glutamine metabolism
-
-
Glyoxylate and dicarboxylate metabolism
-
-
L-glutamate biosynthesis V
-
-
L-glutamine biosynthesis III
-
-
Microbial metabolism in diverse environments
-
-
Nitrogen metabolism
-
-
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 hide
62213-56-3
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
induced biosynthesis during nodule development
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
cv Desiree
-
-
Manually annotated by BRENDA team
-
Uniprot
Manually annotated by BRENDA team
bean
-
-
Manually annotated by BRENDA team
grapevine
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
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
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2 L-glutamate + 2 oxidized ferredoxin
L-glutamine + 2-oxoglutarate + 2 reduced ferredoxin + 2 H+
show the reaction diagram
L-glutamate + oxidized iodonitrotetrazolium
2-oxoglutarate + NH3 + reduced iodonitrotetrazolium
show the reaction diagram
-
enzyme exhibits L-glutamate:iodonitrotetrazolium oxidoreductase activity at pH 7.5-9.5
-
?
L-glutamine + 2-oxoglutarate + 2 reduced ferredoxin + 2 H+
2 L-glutamate + 2 oxidized ferredoxin
show the reaction diagram
L-glutamine + 2-oxoglutarate + 2 reduced methyl viologen
2 L-glutamate + 2 oxidized methyl viologen
show the reaction diagram
reductant: Na2S2O4
-
-
?
L-glutamine + 2-oxoglutarate + reduced bacterial ferredoxin 1
L-glutamate + oxidized bacterial ferredoxin 1
show the reaction diagram
L-glutamine + 2-oxoglutarate + reduced bacterial ferredoxin 2
L-glutamate + oxidized bacterial ferredoxin 2
show the reaction diagram
L-glutamine + 2-oxoglutarate + reduced ferredoxin
L-glutamate + oxidized ferredoxin
show the reaction diagram
L-glutamine + 2-oxoglutarate + reduced methylviologen
L-glutamate + oxidized methylviologen
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
2 L-glutamate + 2 oxidized ferredoxin
L-glutamine + 2-oxoglutarate + 2 reduced ferredoxin + 2 H+
show the reaction diagram
L-glutamine + 2-oxoglutarate + reduced ferredoxin
L-glutamate + oxidized ferredoxin
show the reaction diagram
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Ferredoxin
flavin
-
enzyme may contain a flavin prosthetic group
iron-sulfur centre
[3Fe-4S]-center
-
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
-
1 mM, 6% activation
NaCl
maximal activity at salt concentrations from 3 to 4 M NaCl
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-oxoglutarate
-
at high concentrations
3-(3,4-dichlorophenyl)-1,1-dimethylurea
-
-
3-phosphoglycerate
-
-
3-phosphoserine
-
competitive inhibition
5-oxo-L-norleucine
covalent
6-diazo-5-oxo-L-norleucine
-
6-diazo-5-oxo-norleucine
aspartate
-
competitive inhibition
Atebrin
-
1 mM, 45% inhibition
azaserine
Bromocresol green
-
1 mM, 89% inhibition
Cd2+
-
5 mM, 69% inhibition
Co2+
-
5 mM, 65% inhibition
cycloheximide
-
complete disappearance of enzyme in roots and 90% decrease in leaves after 24 h
glycine
glycolate
-
20 mM, more than 60% inhibition
glyoxylate
-
20 mM, more than 60% inhibition
iodoacetamide
-
90% inactivation after 15 h, L-glutamine protects from inactivation
L-arginine
-
-
L-methionine
-
-
L-ornithine
-
-
L-serine
L-threonine
-
-
Mn2+
-
5 mM, 45% inhibition
N-ethylmaleimide
Ni2+
-
5 mM, 73% inhibition
p-chloromercuribenzoate
-
0.1 mM, complete inhibition
p-Chloromercuriphenylsulfonate
-
0.1 mM, complete inhibition
p-hydroxymercuribenzoate
additional information
-
not inhibitory: chloramphenicol
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
citrate
up to 50% increase in activity
malate
up to 50% increase in activity
oxaloacetate
up to 50% increase in activity
succinate
up to 50% increase in activity
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.062 - 31
2-oxoglutarate
0.0002 - 0.02
Ferredoxin
0.1
iodonitrotetrazolium
-
L-glutamate:iodonitrotetrazolium oxidoreductase activity at pH 9.5
0.044
L-glutamate
-
L-glutamate:iodonitrotetrazolium oxidoreductase activity at pH 9.5
0.182 - 2.5
L-glutamine
0.133 - 4.7
methyl viologen
0.005
reduced bacterial ferredoxin 1
in 20 mM NaPO4 (pH 7.2), at 70C
-
0.018
reduced ferredoxin
pH 7.5, 40C, 3 M NaCl
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3.67
L-glutamate
Synechocystis sp.
-
L-glutamate:iodonitrotetrazolium oxidoreductase activity at pH 9.5
137
L-glutamine
Oryza sativa
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-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.1
aspartate
-
-
4.9
phosphoserine
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-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.0045
-
activity in young leaves
0.0078
crude extract, at 70C
0.018
-
activity in root crude extracts
0.077
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enzyme separated from NADH-dependent activity on Sephadex G-200
0.084
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activity in leaf crude extracts
0.091
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activity in roots under airobic conditiones, approx. value
0.125
-
activity in roots after anaerobic treatment for 24 h, approx. value
1.5
after 191fold purification, at 70C
3.1
-
activity in first leaf after 5 d development
4.2
-
activity in 30 d old plants in the fourth leaf, activity declines in older leaves
7
-
ferredoxin affinity chromatographyie purified enzyme
35.88
-
-
36.6
-
recombinant enzyme
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5 - 8.5
-
-
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 10
pH 5.0: about 45% of maximal activity, pH 10.0: about 55% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30 - 80
30C: about 75% of maximal activity, 80C: about 55% of maximal activity
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
in etiolated seedling, enzyme activity doubles within 1 h upon exposure to light, and a further 4fold increase in comparison with dark value is reached within 5 h
Manually annotated by BRENDA team
additional information
-
Fd-GOGAT1 is more highly expressed in leaves than in roots
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
UNIPROT
Synechocystis sp. (strain PCC 6803 / Kazusa)
Synechocystis sp. (strain PCC 6803 / Kazusa)
Synechocystis sp. (strain PCC 6803 / Kazusa)
Synechocystis sp. (strain PCC 6803 / Kazusa)
Synechocystis sp. (strain PCC 6803 / Kazusa)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
16000
-
gel filtration
140000
-
gel filtration
141000
-
gel filtration
144000
-
sucrose density gradient centrifugation
145900
-
amino acid composition
163000
-
gel filtration
165000
-
gel filtration
168000
calculated from amino acid sequence
171000
-
gel filtration
175000
-
recombinant enzyme, gel filtration
178000
-
native enzyme, gel filtration
180000
-
gel filtration
198000
gel filtration
224000
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
-
2 * 115000, SDS-PAGE
monomer
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method, using 22-23% (w/v) PEG 3350, 170 mM sodium acetate trihydrate pH 7.0, 85 mM Tris-HCl pH 8.2, 15% (v/v) glycerol
-
hanging-drop vapor diffusion method, crystal structure of the enzyme with the substrate 2-oxoglutarate and the covalent inhibitor 5-oxo-L-norleucine
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50
-
full activity after 10 min, 50% activity remains after heating at 55C for 10 min, complete loss of activity at 60C
55
-
50% activity remains after 20 min, recombinant enzyme
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, 5 mM dithiothreitol, 20 days, 54% loss of activity
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
affinity chromatography on ferredoxin Sepharose
ammonium sulfate precipitation, hydroxyapatite column chromatography, butyl-Toyopearl column chromatography, MonoQ column chromatography, and DEAE-Toyopearl column chromatography
ammonium sulfate, DEAE cellulose, glutamate agarose
-
ammonium sulfate, DEAE-cellulose, DEAE-Sephacel, Phenyl-Sepharose
-
ferredoxin-immobilized Sepharose column chromatography
-
partially purified
-
protamine sulfate, DEAE-Sephacel, hydroxylapatite, ferredoxin-Sepharose
-
recombinant enzyme
-
recombinant enzyme expressed in Escherichia coli
recombinant enzyme, affinity chromatography on ferredoxin-Sepharose, native enzyme, partially purified
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
cDNA insert coding for 550 C-terminal amino acids, expression in Escherichia coli
-
expressed in Escherichia coli JM105 cells
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expression in Escherichia coli
gene glu1 or gls1, genome wide microarray analysis of the transcriptional reprogramming, overview
-
glu1, overexpressed
in vitro translation in reticulocyte lysate
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
expression is induced under conditions of ammonium restriction
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
L1270F
-
retains wild type activity, in vivo: reduced mitochondrial serine hydroxymethyltransferase activity
M1K
-
targeted to the mitochondrion; targeted to the mitochondrion
M3I
-
targeted to the chloroplast
E1013A
dramatically lowered activity
E1013D
dramatically lowered activity
E1013N
dramatically lowered activity
additional information
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