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Information on EC 1.4.1.13 - glutamate synthase (NADPH) and Organism(s) Methanocaldococcus jannaschii and UniProt Accession Q58746

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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Methanocaldococcus jannaschii
UNIPROT: Q58746
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Word Map
The taxonomic range for the selected organisms is: Methanocaldococcus jannaschii
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
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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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glutamine amide-2-oxoglutarate aminotransferase (oxidoreductase, NADP)
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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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NADPH-dependent glutamate synthase
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NADPH-glutamate synthase
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NADPH-GOGAT
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NADPH-linked glutamate synthase
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synthase, glutamate (reduced nicotinamide adenine dinucleotide phosphate)
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
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oxidation
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reduction
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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
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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