Information on EC 1.4.7.1 - glutamate synthase (ferredoxin)

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

EC NUMBER
COMMENTARY
1.4.7.1
-
RECOMMENDED NAME
GeneOntology No.
glutamate synthase (ferredoxin)
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
2 L-glutamate + 2 oxidized ferredoxin = L-glutamine + 2-oxoglutarate + 2 reduced ferredoxin + 2 H+
show the reaction diagram
overall reaction
-
-
-
2 L-glutamate + 2 oxidized ferredoxin = L-glutamine + 2-oxoglutarate + 2 reduced ferredoxin + 2 H+
show the reaction diagram
proposed electron-transfer pathway
-
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 ACCESSION NO.
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
transamination
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
ammonia assimilation cycle II
-
glutamate biosynthesis V
-
glutamine biosynthesis III
-
Glyoxylate and dicarboxylate metabolism
-
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].
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Fd-dependent glutamate synthase
Q9ZNZ7
-
Fd-GOGAT
-
-
-
-
Fd-GOGAT
Q9ZNZ7
-
Fd-GOGAT
A1IJT7
-
-
Fd-GOGAT
-
-
Fd-GOGAT
-
-
Fd-GOGAT
-
-
Fd-GOGAT1
Q9ZNZ7
-
ferredoxin-dependent GltS
-
-
ferredoxin-dependent glutamate synthase
-
-
-
-
ferredoxin-dependent glutamate synthase
Q9ZNZ7
-
ferredoxin-dependent glutamate synthase
A1IJT7
exhibits also glutaminase activity and does not react with a plant-type ferredoxin (Fd3) containing a [2Fe-2S] cluster, but does react with bacterial ferredoxins (Fd1 and Fd2) containing [4Fe-4S] clusters
ferredoxin-dependent glutamate synthase
A1IJT7
exhibits also glutaminase activity and does not react with a plant-type ferredoxin (Fd3) containing a [2Fe-2S] cluster, but does react with bacterial ferredoxins (Fd1 and Fd2) containing [4Fe-4S] clusters
-
ferredoxin-dependent glutamate synthase
-
-
ferredoxin-dependent glutamate synthase
-
-
ferredoxin-dependent glutamate synthase
-
-
ferredoxin-dependent glutamate synthase
-
-
ferredoxin-dependent glutamate synthase1
-, Q9ZNZ7
-
ferredoxin-dependent glutamine 2-oxoglutarate aminotransferase
Q9ZNZ7
-
ferredoxin-dependent GOGAT
-
-
ferredoxin-dependent GOGAT
Solanum lycopersicum Moneymaker
-
-
-
ferredoxin-glutamate synthase
-
-
-
-
ferredoxin-glutamate synthase
Q9T0P4, Q9ZNZ7
-
ferredoxin-GOGAT
-
-
glutamate synthase
-
-
glutamate synthase (ferredoxin-dependent)
-
-
-
-
glutamine 2-oxoglutarate amidotransferase
-
-
glutamine:2-oxoglutarate amidotransferase
A1IJT7
-
glutamine:2-oxoglutarate amidotransferase
A1IJT7
-
-
CAS REGISTRY NUMBER
COMMENTARY
62213-56-3
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
enzyme Glu1
UniProt
Manually annotated by BRENDA team
isoenzyme GLU1
UniProt
Manually annotated by BRENDA team
isoenzyme GLU2
UniProt
Manually annotated by BRENDA team
L. cv. maris mink, barley
-
-
Manually annotated by BRENDA team
induced biosynthesis during nodule development
-
-
Manually annotated by BRENDA team
L. cv. xanthi
-
-
Manually annotated by BRENDA team
L. cv. Sasanishiki
-
-
Manually annotated by BRENDA team
cv Desiree
-
-
Manually annotated by BRENDA team
PCC 6803
Uniprot
Manually annotated by BRENDA team
PCC 6803, cyanobacterium
-
-
Manually annotated by BRENDA team
Synechocystis sp. PCC 6008
-
Uniprot
Manually annotated by BRENDA team
bean
-
-
Manually annotated by BRENDA team
grapevine
-
-
Manually annotated by BRENDA team
-
Uniprot
Manually annotated by BRENDA team
maize
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
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
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
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
P55038
-
-
-
?
L-glutamine + 2-oxoglutarate + 2 reduced methyl viologen
2 L-glutamate + 2 oxidized methyl viologen
show the reaction diagram
Q9ZNZ7
reductant: Na2S2O4
-
-
?
L-glutamine + 2-oxoglutarate + reduced bacterial ferredoxin 1
L-glutamate + oxidized bacterial ferredoxin 1
show the reaction diagram
A1IJT7, -
-
-
-
?
L-glutamine + 2-oxoglutarate + reduced bacterial ferredoxin 1
L-glutamate + oxidized bacterial ferredoxin 1
show the reaction diagram
A1IJT7, -
-
-
-
?
L-glutamine + 2-oxoglutarate + reduced bacterial ferredoxin 2
L-glutamate + oxidized bacterial ferredoxin 2
show the reaction diagram
A1IJT7, -
-
-
-
?
L-glutamine + 2-oxoglutarate + reduced bacterial ferredoxin 2
L-glutamate + oxidized bacterial ferredoxin 2
show the reaction diagram
A1IJT7, -
-
-
-
?
L-glutamine + 2-oxoglutarate + reduced ferredoxin
L-glutamate + oxidized ferredoxin
show the reaction diagram
-
-
-
?
L-glutamine + 2-oxoglutarate + reduced ferredoxin
L-glutamate + oxidized ferredoxin
show the reaction diagram
-
-
-
?
L-glutamine + 2-oxoglutarate + reduced ferredoxin
L-glutamate + oxidized ferredoxin
show the reaction diagram
-
-
-
?
L-glutamine + 2-oxoglutarate + reduced ferredoxin
L-glutamate + oxidized ferredoxin
show the reaction diagram
-
-
-
?
L-glutamine + 2-oxoglutarate + reduced ferredoxin
L-glutamate + oxidized ferredoxin
show the reaction diagram
-
-
-
?
L-glutamine + 2-oxoglutarate + reduced ferredoxin
L-glutamate + oxidized ferredoxin
show the reaction diagram
-
-
-
?
L-glutamine + 2-oxoglutarate + reduced ferredoxin
L-glutamate + oxidized ferredoxin
show the reaction diagram
-
-
-
?
L-glutamine + 2-oxoglutarate + reduced ferredoxin
L-glutamate + oxidized ferredoxin
show the reaction diagram
-
-
-
?
L-glutamine + 2-oxoglutarate + reduced ferredoxin
L-glutamate + oxidized ferredoxin
show the reaction diagram
-
-
-
?
L-glutamine + 2-oxoglutarate + reduced ferredoxin
L-glutamate + oxidized ferredoxin
show the reaction diagram
-
-
-
?
L-glutamine + 2-oxoglutarate + reduced ferredoxin
L-glutamate + oxidized ferredoxin
show the reaction diagram
-
-
-
?
L-glutamine + 2-oxoglutarate + reduced ferredoxin
L-glutamate + oxidized ferredoxin
show the reaction diagram
-
-
-
?
L-glutamine + 2-oxoglutarate + reduced ferredoxin
L-glutamate + oxidized ferredoxin
show the reaction diagram
-
-
-
?
L-glutamine + 2-oxoglutarate + reduced ferredoxin
L-glutamate + oxidized ferredoxin
show the reaction diagram
P23225, -
-
-
-
?
L-glutamine + 2-oxoglutarate + reduced ferredoxin
L-glutamate + oxidized ferredoxin
show the reaction diagram
-
-
-
?
L-glutamine + 2-oxoglutarate + reduced ferredoxin
L-glutamate + oxidized ferredoxin
show the reaction diagram
-
-
-
?
L-glutamine + 2-oxoglutarate + reduced ferredoxin
L-glutamate + oxidized ferredoxin
show the reaction diagram
-
-
-
?
L-glutamine + 2-oxoglutarate + reduced ferredoxin
L-glutamate + oxidized ferredoxin
show the reaction diagram
-
-
-
?
L-glutamine + 2-oxoglutarate + reduced ferredoxin
L-glutamate + oxidized ferredoxin
show the reaction diagram
-
-
-
?
L-glutamine + 2-oxoglutarate + reduced ferredoxin
L-glutamate + oxidized ferredoxin
show the reaction diagram
-
-
-
?
L-glutamine + 2-oxoglutarate + reduced ferredoxin
L-glutamate + oxidized ferredoxin
show the reaction diagram
-
-
-
?
L-glutamine + 2-oxoglutarate + reduced ferredoxin
L-glutamate + oxidized ferredoxin
show the reaction diagram
-
-
-
?
L-glutamine + 2-oxoglutarate + reduced ferredoxin
L-glutamate + oxidized ferredoxin
show the reaction diagram
-
-
-
?
L-glutamine + 2-oxoglutarate + reduced ferredoxin
L-glutamate + oxidized ferredoxin
show the reaction diagram
-
-
-
-
?
L-glutamine + 2-oxoglutarate + reduced ferredoxin
L-glutamate + oxidized ferredoxin
show the reaction diagram
-
-
-
?
L-glutamine + 2-oxoglutarate + reduced ferredoxin
L-glutamate + oxidized ferredoxin
show the reaction diagram
-
-
-
?
L-glutamine + 2-oxoglutarate + reduced ferredoxin
L-glutamate + oxidized ferredoxin
show the reaction diagram
-
highly specific for glutamine and 2-oxoglutarate
-
?
L-glutamine + 2-oxoglutarate + reduced ferredoxin
L-glutamate + oxidized ferredoxin
show the reaction diagram
-
about 35% of activity with methylviologen
-
?
L-glutamine + 2-oxoglutarate + reduced ferredoxin
L-glutamate + oxidized ferredoxin
show the reaction diagram
-
enzyme may be linked to light driven electron transport
-
?
L-glutamine + 2-oxoglutarate + reduced ferredoxin
L-glutamate + oxidized ferredoxin
show the reaction diagram
Chlamydomonas reinhardtii CCAP
-
-
-
?
L-glutamine + 2-oxoglutarate + reduced methylviologen
L-glutamate + oxidized methylviologen
show the reaction diagram
-
-
-
-
?
L-glutamine + 2-oxoglutarate + reduced methylviologen
L-glutamate + oxidized methylviologen
show the reaction diagram
-
-
-
-
?
L-glutamine + 2-oxoglutarate + reduced methylviologen
L-glutamate + oxidized methylviologen
show the reaction diagram
-
-
-
?
L-glutamine + 2-oxoglutarate + reduced methylviologen
L-glutamate + oxidized methylviologen
show the reaction diagram
A1IJT7, -
-
-
-
?
L-glutamine + 2-oxoglutarate + reduced methylviologen
L-glutamate + oxidized methylviologen
show the reaction diagram
-
similar activity as with ferredoxin
-
?
L-glutamine + 2-oxoglutarate + reduced methylviologen
L-glutamate + oxidized methylviologen
show the reaction diagram
-
artificial elctron donor
-
?
L-glutamine + 2-oxoglutarate + reduced methylviologen
L-glutamate + oxidized methylviologen
show the reaction diagram
-
artificial elctron donor
-
?
L-glutamine + 2-oxoglutarate + reduced methylviologen
L-glutamate + oxidized methylviologen
show the reaction diagram
-
artificial elctron donor
-
?
L-glutamine + 2-oxoglutarate + reduced methylviologen
L-glutamate + oxidized methylviologen
show the reaction diagram
-
artificial elctron donor
-
?
L-glutamine + 2-oxoglutarate + reduced methylviologen
L-glutamate + oxidized methylviologen
show the reaction diagram
-
artificial elctron donor
-
?
L-glutamine + 2-oxoglutarate + reduced methylviologen
L-glutamate + oxidized methylviologen
show the reaction diagram
-
artificial elctron donor
-
?
L-glutamine + 2-oxoglutarate + reduced methylviologen
L-glutamate + oxidized methylviologen
show the reaction diagram
-
artificial elctron donor
-
?
L-glutamine + 2-oxoglutarate + reduced methylviologen
L-glutamate + oxidized methylviologen
show the reaction diagram
-
artificial elctron donor
-
?
L-glutamine + 2-oxoglutarate + reduced methylviologen
L-glutamate + oxidized methylviologen
show the reaction diagram
-
artificial elctron donor
-
?
L-glutamine + 2-oxoglutarate + reduced methylviologen
L-glutamate + oxidized methylviologen
show the reaction diagram
-
artificial elctron donor
-
?
L-glutamine + 2-oxoglutarate + reduced methylviologen
L-glutamate + oxidized methylviologen
show the reaction diagram
-
artificial elctron donor
-
?
L-glutamine + 2-oxoglutarate + reduced methylviologen
L-glutamate + oxidized methylviologen
show the reaction diagram
-
artificial elctron donor
-
-
?
L-glutamine + 2-oxoglutarate + reduced methylviologen
L-glutamate + oxidized methylviologen
show the reaction diagram
-
artificial elctron donor
-
?
L-glutamine + 2-oxoglutarate + reduced methylviologen
L-glutamate + oxidized methylviologen
show the reaction diagram
-
artificial elctron donor
-
?
L-glutamine + 2-oxoglutarate + reduced methylviologen
L-glutamate + oxidized methylviologen
show the reaction diagram
-
artificial elctron donor
-
?
L-glutamine + 2-oxoglutarate + reduced methylviologen
L-glutamate + oxidized methylviologen
show the reaction diagram
-
significantly higher activity with ferredoxin than with methyl viologen
-
-
L-glutamine + 2-oxoglutarate + reduced methylviologen
L-glutamate + oxidized methylviologen
show the reaction diagram
-
60% of ferredoxin activity
-
?
L-glutamine + 2-oxoglutarate + reduced methylviologen
L-glutamate + oxidized methylviologen
show the reaction diagram
-
only in the presence of ferredoxin
-
-
?
L-glutamine + 2-oxoglutarate + reduced methylviologen
L-glutamate + oxidized methylviologen
show the reaction diagram
A1IJT7, -
-
-
-
?
L-glutamine + 2-oxoglutarate + reduced methylviologen
L-glutamate + oxidized methylviologen
show the reaction diagram
Chlamydomonas reinhardtii CCAP
-
artificial elctron donor
-
?
additional information
?
-
-
existence of the enzyme in the companion cells, which are adjacent to the sieve elements, of the central cylinder in rice roots is advantageous for the access and efficient utilization of glutamine and carbohydrate transported through the sieve elements under anaerobic conditions
-
-
-
additional information
?
-
-
key enzyme of N-assimilation and biosynthesis of amino acids, decreases in leaves in response to salt stress
-
-
-
additional information
?
-
-
levels of Fd-GOGAT are coordinated by light, nitrate is necessary for the light regulation. Single or repeated red light pulses induce the activity of the enzymes and this effect is reverted by subsequent far-red light
-
-
-
additional information
?
-
-
the GS2/Fd-GOGAT cycle is the major pathway for ammonium assimilation in higher plants. Alternative metabolic pathways may be transiently activated during a day/night cycle in plants with low Fd-GOGAT activity
-
-
-
additional information
?
-
-
enzyme provides amino acids for nitrogen translocation
-
-
-
additional information
?
-
-
role of enzyme in supplying L-glutamate for the synthesis and transport of amino acids
-
-
-
additional information
?
-
A1IJT7, -
does not react with plant ferredoxin 3
-
-
-
additional information
?
-
A1IJT7, -
does not react with plant ferredoxin 3
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
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
-
-
-
?
L-glutamine + 2-oxoglutarate + reduced ferredoxin
L-glutamate + oxidized ferredoxin
show the reaction diagram
-
-
-
?
L-glutamine + 2-oxoglutarate + reduced ferredoxin
L-glutamate + oxidized ferredoxin
show the reaction diagram
-
-
-
?
L-glutamine + 2-oxoglutarate + reduced ferredoxin
L-glutamate + oxidized ferredoxin
show the reaction diagram
-
-
-
?
L-glutamine + 2-oxoglutarate + reduced ferredoxin
L-glutamate + oxidized ferredoxin
show the reaction diagram
-
-
-
?
L-glutamine + 2-oxoglutarate + reduced ferredoxin
L-glutamate + oxidized ferredoxin
show the reaction diagram
-
-
-
?
L-glutamine + 2-oxoglutarate + reduced ferredoxin
L-glutamate + oxidized ferredoxin
show the reaction diagram
-
-
-
?
L-glutamine + 2-oxoglutarate + reduced ferredoxin
L-glutamate + oxidized ferredoxin
show the reaction diagram
-
-
-
?
L-glutamine + 2-oxoglutarate + reduced ferredoxin
L-glutamate + oxidized ferredoxin
show the reaction diagram
-
-
-
?
L-glutamine + 2-oxoglutarate + reduced ferredoxin
L-glutamate + oxidized ferredoxin
show the reaction diagram
-
-
-
?
L-glutamine + 2-oxoglutarate + reduced ferredoxin
L-glutamate + oxidized ferredoxin
show the reaction diagram
-
-
-
?
L-glutamine + 2-oxoglutarate + reduced ferredoxin
L-glutamate + oxidized ferredoxin
show the reaction diagram
-
-
-
?
L-glutamine + 2-oxoglutarate + reduced ferredoxin
L-glutamate + oxidized ferredoxin
show the reaction diagram
-
-
-
?
L-glutamine + 2-oxoglutarate + reduced ferredoxin
L-glutamate + oxidized ferredoxin
show the reaction diagram
-
-
-
?
L-glutamine + 2-oxoglutarate + reduced ferredoxin
L-glutamate + oxidized ferredoxin
show the reaction diagram
-
-
-
?
L-glutamine + 2-oxoglutarate + reduced ferredoxin
L-glutamate + oxidized ferredoxin
show the reaction diagram
-
-
-
?
L-glutamine + 2-oxoglutarate + reduced ferredoxin
L-glutamate + oxidized ferredoxin
show the reaction diagram
-
-
-
?
L-glutamine + 2-oxoglutarate + reduced ferredoxin
L-glutamate + oxidized ferredoxin
show the reaction diagram
-
-
-
?
L-glutamine + 2-oxoglutarate + reduced ferredoxin
L-glutamate + oxidized ferredoxin
show the reaction diagram
-
-
-
?
L-glutamine + 2-oxoglutarate + reduced ferredoxin
L-glutamate + oxidized ferredoxin
show the reaction diagram
-
-
-
?
L-glutamine + 2-oxoglutarate + reduced ferredoxin
L-glutamate + oxidized ferredoxin
show the reaction diagram
-
-
-
?
L-glutamine + 2-oxoglutarate + reduced ferredoxin
L-glutamate + oxidized ferredoxin
show the reaction diagram
-
-
-
-
?
L-glutamine + 2-oxoglutarate + reduced ferredoxin
L-glutamate + oxidized ferredoxin
show the reaction diagram
-
-
-
?
L-glutamine + 2-oxoglutarate + reduced ferredoxin
L-glutamate + oxidized ferredoxin
show the reaction diagram
-
-
-
?
L-glutamine + 2-oxoglutarate + reduced ferredoxin
L-glutamate + oxidized ferredoxin
show the reaction diagram
-
highly specific for glutamine and 2-oxoglutarate
-
?
L-glutamine + 2-oxoglutarate + reduced ferredoxin
L-glutamate + oxidized ferredoxin
show the reaction diagram
-
enzyme may be linked to light driven electron transport
-
?
L-glutamine + 2-oxoglutarate + reduced ferredoxin
L-glutamate + oxidized ferredoxin
show the reaction diagram
Chlamydomonas reinhardtii CCAP
-
-
-
?
additional information
?
-
-
existence of the enzyme in the companion cells, which are adjacent to the sieve elements, of the central cylinder in rice roots is advantageous for the access and efficient utilization of glutamine and carbohydrate transported through the sieve elements under anaerobic conditions
-
-
-
additional information
?
-
-
key enzyme of N-assimilation and biosynthesis of amino acids, decreases in leaves in response to salt stress
-
-
-
additional information
?
-
-
levels of Fd-GOGAT are coordinated by light, nitrate is necessary for the light regulation. Single or repeated red light pulses induce the activity of the enzymes and this effect is reverted by subsequent far-red light
-
-
-
additional information
?
-
-
the GS2/Fd-GOGAT cycle is the major pathway for ammonium assimilation in higher plants. Alternative metabolic pathways may be transiently activated during a day/night cycle in plants with low Fd-GOGAT activity
-
-
-
additional information
?
-
-
enzyme provides amino acids for nitrogen translocation
-
-
-
additional information
?
-
-
role of enzyme in supplying L-glutamate for the synthesis and transport of amino acids
-
-
-
COFACTOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
Ferredoxin
-
enzyme forms an electrostatically stabilized complex with ferredoxin
-
Ferredoxin
-
-
-
Ferredoxin
A1IJT7, -
enzyme does not react with plant-type ferredoxin but with a bacterial-type ferredoxin containing [4Fe-4S] clusters
-
Ferredoxin
P23225, -
-
-
Ferredoxin
-
-
-
flavin
-
enzyme may contain a flavin prosthetic group
FMN
-
in contrast to earlier conclusions the enzyme contains 1 mol of FMN per mol enzyme but no FAD
FMN
-
one FMN per enzyme molecule
FMN
Q43155
the FMN-binding domain of FdGOGAT is essential for specific binding of the protein to UDP-sulfoquinovose synthase
FMN
A1IJT7, -
0.9 mol per mol of protein
FMN
Q9T0P4, Q9ZNZ7
;
iron-sulfur centre
P55038
-
iron-sulfur centre
Q9T0P4, Q9ZNZ7
;
[3Fe-4S]-center
-
-
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Ca2+
-
1 mM, 6% activation
Fe2+
P55038
iron-sulfur centre
Fe2+
Q9T0P4, Q9ZNZ7
iron-sulfur centre; iron-sulfur centre
Iron
-
enzyme may contain two [2Fe-2S] clusters rather than a single [4Fe-4S] cluster
Iron
-
enzyme contains an iron-sulfur-center
Iron
-
enzyme contains a [3Fe-4S] cluster
Iron
-
enzyme contains a single [3Fe-4S] cluster
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
2-oxoglutarate
-
at high concentrations
3-(3,4-Dichlorophenyl)-1,1-dimethylurea
-
-
3-phosphoglycerate
-
-
3-phosphoserine
-
competitive inhibition
5-oxo-L-norleucine
P55038
covalent
6-diazo-5-oxo-L-norleucine
P55038
-
6-Diazo-5-oxo-norleucine
-
reversible inactivator
6-Diazo-5-oxo-norleucine
-
5 mM, complete inhibition
6-Diazo-5-oxo-norleucine
-
0.05 mM, 99% inhibition
aspartate
-
competitive inhibition
Atebrin
-
1 mM, 45% inhibition
azaserine
-
0.5 mM, complete inhibition
azaserine
-
1 mM, complete inhibition
azaserine
-
-
azaserine
-
-
azaserine
-
0.05 mM, 62% inhibition
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
-
20 mM, 70% inhibition
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-serine
-
20 mM, 70% inhibition
N-ethylmaleimide
-
15 mM, 93% inactivation after 15 h, L-glutamine protects from inactivation
N-ethylmaleimide
-
0.05 mM, 94% inhibition
Ni2+
-
5 mM, 73% inhibition
p-chloromercuribenzoate
-
0.1 mM, complete inhibition
p-Chloromercuriphenylsulfonate
-
0.1 mM, complete inhibition
p-hydroxymercuribenzoate
-
1 mM, complete inactivation after 1 h
p-hydroxymercuribenzoate
-
-
Mn2+
-
5 mM, 45% inhibition
additional information
-
not inhibitory: chloramphenicol
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
citrate
A1IJT7, -
up to 50% increase in activity
malate
A1IJT7, -
up to 50% increase in activity
oxaloacetate
A1IJT7, -
up to 50% increase in activity
succinate
A1IJT7, -
up to 50% increase in activity
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.062
-
2-oxoglutarate
-
-
0.089
-
2-oxoglutarate
-
-
0.17
-
2-oxoglutarate
-
-
0.2
-
2-oxoglutarate
-
-
0.28
-
2-oxoglutarate
A1IJT7, -
in 20 mM NaPO4 (pH 7.2), 10 mM L-glutamine, 5 mM methylviologen, 5 mM dithionite, at 70C; pH 8.0, 70C
0.33
-
2-oxoglutarate
-
-
0.5
-
2-oxoglutarate
-
native enzyme
0.6
-
2-oxoglutarate
-
recombinant enzyme
0.606
-
2-oxoglutarate
-
-
1
-
2-oxoglutarate
-
-
0.0002
-
Ferredoxin
-
-
-
0.0018
-
Ferredoxin
-
-
-
0.0019
-
Ferredoxin
-
-
-
0.002
-
Ferredoxin
-
-
-
0.0035
-
Ferredoxin
-
native enzyme
-
0.0045
-
Ferredoxin
-
recombinant enzyme
-
0.0048
-
Ferredoxin
-
in etiolated leaf tissue
-
0.005
-
Ferredoxin
-
approx. value
-
0.0055
-
Ferredoxin
-
in green leaf tissue
-
0.0055
-
Ferredoxin
-
-
-
0.015
-
Ferredoxin
-
-
-
0.02
-
Ferredoxin
-
in root tissue
-
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
-
L-glutamine
-
-
0.19
-
L-glutamine
-
-
0.5
-
L-glutamine
-
-
0.53
-
L-glutamine
-
-
0.556
-
L-glutamine
-
-
0.7
-
L-glutamine
-
-
1.1
-
L-glutamine
A1IJT7, -
in 20 mM NaPO4 (pH 7.2), 1 mM 2-oxoglutarate, 5 mM methylviologen, 5 mM dithionite, at 70C; pH 8.0, 70C
2.2
-
L-glutamine
-
recombinant enzyme
2.5
-
L-glutamine
-
native enzyme
0.133
-
methyl viologen
-
-
4.7
-
methyl viologen
-
-
0.005
-
reduced bacterial ferredoxin 1
A1IJT7, -
in 20 mM NaPO4 (pH 7.2), at 70C
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
3.67
-
L-glutamate
-
L-glutamate:iodonitrotetrazolium oxidoreductase activity at pH 9.5
137
-
L-glutamine
-
-
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.1
-
aspartate
-
-
4.9
-
phosphoserine
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.0045
-
-
activity in young leaves
0.0078
-
A1IJT7, -
crude extract, at 70C
0.018
-
-
activity in root crude extracts
0.077
-
-
enzyme separated from NADH-dependent activity on Sephadex G-200
0.084
-
-
activity in leaf crude extracts
0.091
-
-
activity in roots under airobic conditiones, approx. value
0.125
-
-
activity in roots after anaerobic treatment for 24 h, approx. value
0.6
-
A1IJT7, -
pH 8.0, 70C
1.5
-
A1IJT7, -
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
8.16
-
-
-
35.88
-
-
-
35.9
-
-
-
36.6
-
-
recombinant enzyme
additional information
-
-
16.3 nmol glutamate/min/g fresh weight, activity in green cells, assay with methyl viologen; 31.3 nmol glutamate/min/g fresh weight, activity in green cells, assay with ferredoxin
additional information
-
-
0.0009 mmol/min/shoot, activity in 17 d old shoots, activity increases during seedling development
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6.9
7.4
A1IJT7, -
at 70C
7.3
-
-
-
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
-
more abundant than in stems, barely detectable in roots
Manually annotated by BRENDA team
-
activity decreases in response to salt stress
Manually annotated by BRENDA team
-
enzyme represents the major isoform, activity increases under nitrogen feeding
Manually annotated by BRENDA team
-
ammonium assimilation occurs via glutamine synthetase EC 6.1.1.3 and enzyme, regardless of leaf age. L-glutamate is continuously synthesized and supplied to the phloem. Enzyme is localized to the phloem companion cells-sieve element complex in the leaf veins
Manually annotated by BRENDA team
-
enzyme is active both in light and dark. In transgenic leaf disks expressing antisense enzyme mRNA, low level of enzyme limits the synthesis of glutamate. In the dark, low level of enzyme in transgenic leaves is not the main limiting factor of ammonium assimilation
Manually annotated by BRENDA team
Q9T0P4, Q9ZNZ7
glu1 mainly expressed in the leaves, at significantly higher level than glu2; glu1 mainly expressed in the leaves, at significantly higher level than glu2
Manually annotated by BRENDA team
Solanum lycopersicum Moneymaker
-
-
-
Manually annotated by BRENDA team
-
expression is induced by NO3-
Manually annotated by BRENDA team
-
existence of the enzyme in the companion cells, which are adjacent to the sieve elements, of the central cylinder in rice roots is advantageous for the access and efficient utilization of glutamine and carbohydrate transported through the sieve elements under anaerobic conditions
Manually annotated by BRENDA team
-
NADH-dependent enzyme is the major isoform
Manually annotated by BRENDA team
Q9T0P4, Q9ZNZ7
;
Manually annotated by BRENDA team
-
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
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
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
16000
-
-
gel filtration
115000
-
A1IJT7, -
gel filtration
140000
-
-
gel filtration
141000
-
-
gel filtration
144000
-
-
sucrose density gradient centrifugation
145900
-
-
amino acid composition
151000
-
A1IJT7, -
SDS-PAGE
163000
-
-
gel filtration
165000
-
-
gel filtration
168000
-
A1IJT7, -
calculated from amino acid sequence
171000
-
-
gel filtration
175000
-
-
recombinant enzyme, gel filtration
178000
-
-
native enzyme, gel filtration
180000
-
-
gel filtration
224000
-
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 68200, SDS-PAGE
?
-
x * 153000, SDS-PAGE
?
-
x * 165000, SDS-PAGE
?
-
x * 180000, SDS-PAGE
?
-
x + 160000, SDS-PAGE, immunodetection
?
Q9T0P4, Q9ZNZ7
x * 165000; x * 165000
dimer
-
2 * 115000, SDS-PAGE
monomer
-
1 * 153000, SDS-PAGE
monomer
-
1 * 145000, immunoprecipitation, SDS-PAGE; 1 * 145000, SDS-PAGE
monomer
-
1 * 151000, SDS-PAGE
monomer
-
SDS-PAGE
monomer
-
1 * 170000, SDS-PAGE
monomer
-
SDS-PAGE
monomer
-
1 * 168000, SDS-PAGE
monomer
A1IJT7, -
1 * 151000, SDS-PAGE; 1 * 151000, SDS-PAGE
monomer
P55038
in solution
monomer
-
1 * 151000, SDS-PAGE; 1 * 151000, SDS-PAGE
-
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
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
P55038
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
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 ACCESSION NO.
LITERATURE
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-20C, 5 mM dithiothreitol, 20 days, 54% loss of activity
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
partially purified
-
protamine sulfate, DEAE-Sephacel, hydroxylapatite, ferredoxin-Sepharose
-
ammonium sulfate precipitation, hydroxyapatite column chromatography, butyl-Toyopearl column chromatography, MonoQ column chromatography, and DEAE-Toyopearl column chromatography
A1IJT7, -
ferredoxin-immobilized Sepharose column chromatography
-
affinity chromatography on ferredoxin Sepharose
-
ammonium sulfate, DEAE-cellulose, DEAE-Sephacel, Phenyl-Sepharose
-
ammonium sulfate, DEAE cellulose, glutamate agarose
-
affinity chromatography on ferredoxin Sepharose
-
recombinant enzyme expressed in Escherichia coli
P55038
recombinant enzyme, affinity chromatography on ferredoxin-Sepharose, native enzyme, partially purified
-
affinity chromatography on ferredoxin Sepharose
-
recombinant enzyme
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
gene glu1 or gls1, genome wide microarray analysis of the transcriptional reprogramming, overview
-
glu1, overexpressed
Q9ZNZ7
expressed in Escherichia coli JM105 cells
-
cDNA insert coding for 550 C-terminal amino acids, expression in Escherichia coli
-
expression in Escherichia coli
-
expression in Escherichia coli
-
in vitro translation in reticulocyte lysate
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
L1270F
-
retains wild type activity, in vivo: reduced mitochondrial serine hydroxymethyltransferase activity
M1K
-
targeted to the mitochondrion; targeted to the mitochondrion
E1013A
P55038
dramatically lowered activity
E1013D
P55038
dramatically lowered activity
E1013N
P55038
dramatically lowered activity
M3I
-
targeted to the chloroplast
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