Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 1.4.7.1 - glutamate synthase (ferredoxin) and Organism(s) Zea mays and UniProt Accession P23225

for references in articles please use BRENDA:EC1.4.7.1
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
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].
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Zea mays
UNIPROT: P23225
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
hide
The taxonomic range for the selected organisms is: Zea mays
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Reaction Schemes
hide(Overall reactions are displayed. Show all >>)
2
L-glutamate
+
oxidized ferredoxin
=
L-glutamine
+
2-oxoglutarate
+
reduced ferredoxin
+
2
H+
2
+
=
+
+
+
2
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, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Fd-GOGAT
-
ferredoxin-GOGAT
-
Fd-GOGAT
ferredoxin-dependent glutamate synthase
ferredoxin-glutamate synthase
-
-
-
-
glutamate synthase (ferredoxin-dependent)
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
-
-
-
-
oxidation
-
-
-
-
reduction
-
-
-
-
transamination
-
-
-
-
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
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
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 + NADPH + H+
L-glutamate + oxidized ferredoxin + NADP+
show the reaction diagram
-
-
-
-
?
L-glutamine + 2-oxoglutarate + reduced methylviologen
L-glutamate + oxidized methylviologen
show the reaction diagram
L-glutamine + H2O
L-glutamate + NH3
show the reaction diagram
-
-
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
L-glutamine + 2-oxoglutarate + reduced ferredoxin
L-glutamate + oxidized ferredoxin
show the reaction diagram
L-glutamine + 2-oxoglutarate + reduced ferredoxin + NADPH + H+
L-glutamate + oxidized ferredoxin + NADP+
show the reaction diagram
-
-
-
-
?
L-glutamine + H2O
L-glutamate + NH3
show the reaction diagram
-
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Ferredoxin
-
-
Ferredoxin
-
-
-
NADPH
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.077
-
enzyme separated from NADH-dependent activity on Sephadex G-200
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
Uniprot
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
-
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
GLTB_MAIZE
1616
0
175173
Swiss-Prot
Chloroplast (Reliability: 3)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
145000
171000
-
gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
-
in vitro translation in reticulocyte lysate
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Commere, B.; Vidal, J.; Suzuki, A.; Gadal, P.; Caboche, M.
Detection of the messenger RNA encoding for the ferredoxin-dependent glutamate synthase in maize leaf
Plant Physiol.
80
859-862
1986
Zea mays
Manually annotated by BRENDA team
Misra, S.; Oaks, A.
Ferredoxin and pyridine nucleotide-dependent glutamate synthase activities in maize endosperm tissue
Plant Sci.
39
1-5
1985
Zea mays
-
Manually annotated by BRENDA team
Valadier, M.H.; Yoshida, A.; Grandjean, O.; Morin, H.; Kronenberger, J.; Boutet, S.; Raballand, A.; Hase, T.; Yoneyama, T.; Suzuki, A.
Implication of the glutamine synthetase/glutamate synthase pathway in conditioning the amino acid metabolism in bundle sheath and mesophyll cells of maize leaves
FEBS J.
275
3193-3206
2008
Zea mays (P23225), Zea mays
Manually annotated by BRENDA team
Yoneyama, T.; Fujimori, T.; Yanagisawa, S.; Hase, T.; Suzuki, A.
15N tracing studies on in vitro reactions of ferredoxin-dependent nitrite reductase and glutamate synthase using reconstituted electron donation systems
Plant Cell Physiol.
56
1154-1161
2015
Zea mays
Manually annotated by BRENDA team