B6QIC8 · B6QIC8_TALMQ
- Proteinglutamate synthase (NADH)
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids2124 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
Catalytic activity
- 2 L-glutamate + NAD+ = L-glutamine + 2-oxoglutarate + NADH + H+
Cofactor
Protein has several cofactor binding sites:
Note: Binds 1 [3Fe-4S] cluster.
Pathway
Amino-acid biosynthesis; L-glutamate biosynthesis via GLT pathway; L-glutamate from 2-oxoglutarate and L-glutamine (NAD+ route): step 1/1.
Energy metabolism; nitrogen metabolism.
Nitrogen metabolism.
Features
Showing features for active site, binding site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Active site | 52 | For GATase activity | |||
Binding site | 1183 | [3Fe-4S] cluster (UniProtKB | ChEBI) | |||
Binding site | 1189 | [3Fe-4S] cluster (UniProtKB | ChEBI) | |||
Binding site | 1194 | [3Fe-4S] cluster (UniProtKB | ChEBI) | |||
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | 3 iron, 4 sulfur cluster binding | |
Molecular Function | flavin adenine dinucleotide binding | |
Molecular Function | FMN binding | |
Molecular Function | glutamate synthase (NADH) activity | |
Molecular Function | iron ion binding | |
Molecular Function | oxidoreductase activity, acting on the CH-NH2 group of donors, NAD or NADP as acceptor | |
Biological Process | L-glutamate biosynthetic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameglutamate synthase (NADH)
- EC number
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Eurotiomycetes > Eurotiomycetidae > Eurotiales > Trichocomaceae > Talaromyces > Talaromyces sect. Talaromyces
Accessions
- Primary accessionB6QIC8
Proteomes
Organism-specific databases
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain, region, compositional bias.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Domain | 52-461 | Glutamine amidotransferase type-2 | |||
Region | 1565-1595 | Disordered | |||
Compositional bias | 1577-1592 | Basic and acidic residues | |||
Sequence similarities
Belongs to the glutamate synthase family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length2,124
- Mass (Da)233,641
- Last updated2008-12-16 v1
- MD5 ChecksumAAD4B414B0B49FD1AFA83744F5EBDB56
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Compositional bias | 1577-1592 | Basic and acidic residues | |||
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
DS995902 EMBL· GenBank· DDBJ | EEA23123.1 EMBL· GenBank· DDBJ | Genomic DNA |