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Information on EC 1.4.1.13 - glutamate synthase (NADPH) and Organism(s) Pseudomonas aeruginosa

for references in articles please use BRENDA:EC1.4.1.13
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EC Tree
IUBMB Comments
Binds FMN, FAD, 2 [4Fe-4S] clusters and 1 [3Fe-4S] cluster. The reaction takes place in the direction of L-glutamate production. The protein is composed of two subunits, alpha and beta. The alpha subunit 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 (cf. EC 1.4.1.4, glutamate dehydrogenase [NADP+]). The beta subunit transfers electrons from the cosubstrate. The NH3 is channeled within the alpha subunit through a 31 A channel. The chanelling is very efficient and in the intact alpha-beta complex ammonia is produced only within the complex. In the absence of the beta subunit, coupling between the two domains of the alpha subunit is compromised and some ammonium can leak.
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This record set is specific for:
Pseudomonas aeruginosa
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Word Map
The taxonomic range for the selected organisms is: Pseudomonas aeruginosa
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
hide(Overall reactions are displayed. Show all >>)
Synonyms
glutamate synthase, gogat, nadph-dependent glutamate synthase, nadph-gogat, l-glutamate synthase, ehno1, ehno2, glutamate synthase (nadph), gltb1, gltb2, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glutamate synthetase (NADP)
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-
-
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glutamine amide-2-oxoglutarate aminotransferase (oxidoreductase, NADP)
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-
-
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glutamine-ketoglutaric aminotransferase
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-
-
-
L-glutamate synthase
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-
-
-
L-glutamate synthetase
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-
-
-
L-glutamine:2-oxoglutarate aminotransferase, NADPH oxidizing
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-
-
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NADPH-dependent glutamate synthase
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-
-
-
NADPH-glutamate synthase
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-
-
-
NADPH-GOGAT
NADPH-linked glutamate synthase
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-
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synthase, glutamate (reduced nicotinamide adenine dinucleotide phosphate)
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-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
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reduction
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
L-glutamate:NADP+ oxidoreductase (transaminating)
Binds FMN, FAD, 2 [4Fe-4S] clusters and 1 [3Fe-4S] cluster. The reaction takes place in the direction of L-glutamate production. The protein is composed of two subunits, alpha and beta. The alpha subunit 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 (cf. EC 1.4.1.4, glutamate dehydrogenase [NADP+]). The beta subunit transfers electrons from the cosubstrate. The NH3 is channeled within the alpha subunit through a 31 A channel. The chanelling is very efficient and in the intact alpha-beta complex ammonia is produced only within the complex. In the absence of the beta subunit, coupling between the two domains of the alpha subunit is compromised and some ammonium can leak.
CAS REGISTRY NUMBER
COMMENTARY hide
37213-53-9
-
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 + NADPH + H+
L-glutamate + NADP+
show the reaction diagram
-
ammonia does not replace L-glutamine as amino donor
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADH
-
no activity with NADH
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2
2-oxoglutarate
-
-
1.7
L-glutamine
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-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
A0A8G7DG20_PSEAI
1481
0
161663
TrEMBL
-
A0A8G5J1R0_PSEAI
1481
0
161607
TrEMBL
-
A0A6B1YAJ9_PSEAI
1481
0
161626
TrEMBL
-
A0A8G6Y1J9_PSEAI
1481
0
161617
TrEMBL
-
P95457_PSEAI
477
0
52625
TrEMBL
-
A0A8F9P0J3_PSEAI
1481
0
161636
TrEMBL
-
A0A8G4AEU3_PSEAI
1481
0
161550
TrEMBL
-
A0A8G4LMU1_PSEAI
1481
0
161540
TrEMBL
-
A0A8G7P1I1_PSEAI
1481
0
161636
TrEMBL
-
A0A8G5I5Z0_PSEAI
1481
0
161523
TrEMBL
-
A0A485FX70_PSEAI
455
0
48920
TrEMBL
-
A0A6A9JQT8_PSEAI
1481
0
161564
TrEMBL
-
A0A8G2R479_PSEAI
1481
0
161536
TrEMBL
-
A0A8G2Z1N7_PSEAI
1481
0
161578
TrEMBL
-
A0A485I1X6_PSEAI
259
0
28033
TrEMBL
-
A0A643JD50_PSEAI
1481
0
161580
TrEMBL
-
A0A2X2BUL9_PSEAI
1481
0
161622
TrEMBL
-
A0A485GPC2_PSEAI
1481
0
161695
TrEMBL
-
A0A8G4AF43_PSEAI
1481
0
161606
TrEMBL
-
A0A5E5R0L4_PSEAI
477
0
52595
TrEMBL
-
A0A8G7IAB1_PSEAI
1481
0
161581
TrEMBL
-
A0A8G3KIT4_PSEAI
1481
0
161536
TrEMBL
-
A0A8B5BQL6_PSEAI
1481
0
161594
TrEMBL
-
A0A8G6H3G9_PSEAI
1481
0
161629
TrEMBL
-
A0A8G4BVM0_PSEAI
1481
0
161635
TrEMBL
-
A0A8G2TW58_PSEAI
1481
0
161598
TrEMBL
-
A0A0A8RJ93_PSEAI
1481
0
161605
TrEMBL
-
A0A8G3A7I1_PSEAI
1481
0
161634
TrEMBL
-
A0A8G2S0E4_PSEAI
1481
0
161564
TrEMBL
-
A0A8G5NRD0_PSEAI
1481
0
161524
TrEMBL
-
A0A0F7QUZ7_PSEAI
1481
0
161636
TrEMBL
-
A0A5F1BLS0_PSEAI
1481
0
161590
TrEMBL
-
A0A8G6LUU5_PSEAI
1481
0
161580
TrEMBL
-
A0A8G4I4J7_PSEAI
1481
0
161645
TrEMBL
-
A0A8G5QYT0_PSEAI
1481
0
161547
TrEMBL
-
A0A8G7M840_PSEAI
1481
0
161594
TrEMBL
-
A0A8G2NIX6_PSEAI
1481
0
161609
TrEMBL
-
A0A2R3IU05_PSEAI
477
0
52637
TrEMBL
-
A0A8G4G422_PSEAI
1481
0
161592
TrEMBL
-
A0A509JHU7_PSEAI
1481
0
161624
TrEMBL
-
A0A8G6G2F8_PSEAI
1481
0
161590
TrEMBL
-
A0A3S0IXP9_PSEAI
1481
0
161698
TrEMBL
-
A0A8G6DU49_PSEAI
1481
0
161666
TrEMBL
-
A0A8G7I192_PSEAI
1481
0
161652
TrEMBL
-
A0A8G3XIG0_PSEAI
1483
0
161914
TrEMBL
-
A0A8G6B4F1_PSEAI
1481
0
161576
TrEMBL
-
A0A0C7D5T0_PSEAI
1481
0
161608
TrEMBL
-
A0A8G6HCT3_PSEAI
1481
0
161636
TrEMBL
-
A0A8G7HZV9_PSEAI
1481
0
161526
TrEMBL
-
A0A367M6R9_PSEAI
722
0
80403
TrEMBL
-
A0A8G4DUW4_PSEAI
1481
0
161636
TrEMBL
-
A0A8G3WFM9_PSEAI
1481
0
161638
TrEMBL
-
A0A367MC59_PSEAI
803
0
86228
TrEMBL
-
A0A8G7DAI7_PSEAI
1481
0
161642
TrEMBL
-
P95456_PSEAI
1482
0
161706
TrEMBL
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
160000
-
gel filtration
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
partial purification using column chromatography on DEAE-cellulose
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Janssen, D.B.; op den Camp, H.J.M.; Leenen, P.J.M.; van der Drift, C.
The enzymes of the ammonia assimilation in Pseudomonas aeruginosa
Arch. Microbiol.
124
197-203
1980
Pseudomonas aeruginosa
Manually annotated by BRENDA team
Suzuki, A.; Knaff, D.B.
Glutamate synthase: structural, mechanistic and regulatory properties, and role in the amino acid metabolism
Photosynth. Res.
83
191-217
2005
Acidithiobacillus ferrooxidans (Q56266), Acidithiobacillus ferrooxidans (Q56267), Archaeoglobus fulgidus (O29309), Azospirillum brasilense (Q05755), Azospirillum brasilense (Q05756), Azospirillum brasilense (Q59084), Bacillus subtilis (P39812), Escherichia coli (P09831), Escherichia coli (P09832), Klebsiella aerogenes, Methanocaldococcus jannaschii (Q58746), Methanococcus thermoautotrophicum (O26308), no activity in Arabidopsis thaliana, Priestia megaterium, Pseudomonas aeruginosa (P95456), Pseudomonas aeruginosa (P95457), Pyrococcus sp., Pyrococcus sp. KOD1, Rhizobium etli (Q9ZFB8), Rhizobium etli (Q9ZFB9), Rhodospirillum rubrum, Salmonella enterica subsp. enterica serovar Typhimurium (Q8ZLR3), Salmonella enterica subsp. enterica serovar Typhimurium (Q8ZLR4)
Manually annotated by BRENDA team