A5DMF7 · A5DMF7_PICGU
- Proteinglutamate synthase (NADH)
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids2679 (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:
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.
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | 3 iron, 4 sulfur cluster binding | |
Molecular Function | endonuclease activity | |
Molecular Function | glutamate synthase activity | |
Molecular Function | metal ion binding | |
Molecular Function | oxidoreductase activity, acting on the CH-NH2 group of donors, NAD or NADP as acceptor | |
Biological Process | glutamine metabolic process | |
Biological Process | intein-mediated protein splicing | |
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 > Saccharomycotina > Saccharomycetes > Saccharomycetales > Debaryomycetaceae > Meyerozyma
Accessions
- Primary accessionA5DMF7
Proteomes
Organism-specific databases
PTM/Processing
Keywords
- PTM
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 45-457 | Glutamine amidotransferase type-2 | ||||
Sequence: CGVGFTCHIKGQASHKIVSDCRNLLCNMTHRGGELNPKDGDGAGLLSSLPHKFLVREFQYHCNVTLPPLGQYGTGNVFFKKDDVVFEKSKKTFENIAASLGLRVLGWRAVPHDSSILGPASLSREPLILQPLIVLAEAFGPGSAPQEDISTDDFEKKYQRSFEKNLFILRKQSSHTIGLHNWFYICSLSNRTIVYKGQLAPNQVYAYYHDLVNADFEAHFALVHSRFSTNTFPSWDRAQPLRWAAHNGEINTLRGNKNWMRAKEGVMASELFGDELDKLYPIIEEGGSDSAAFDNVLELLVINGVLSLPEAVMVMIPEAWQNDTHIDPKKKAFYEWAACLMEPWDGPALFTFADGRYCGANLDRNGLRPCRYYVTDDDRMICASEVGVIEIEPEKILQKGRLQPGRMLLVDTK | ||||||
Domain | 1489-1651 | DOD-type homing endonuclease | ||||
Sequence: FLGLWLGEGSSDSATISTTDREVVVWLQQYVERLNKDKPAEASPLRLTKINGFKPGQQMANGFVQKVTVPTYTITSGESFTGGNWNPVYNSLKSMGLLSNKSNGIPEAYKAADLQSRLALLAGLVDSDGCYVESYNSYRFMQKSELHKKIVYDLKEMATSCGI | ||||||
Region | 2140-2161 | Disordered | ||||
Sequence: KKGHVHRPSKASEPPVLDVEDT |
Sequence similarities
Belongs to the glutamate synthase family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length2,679
- Mass (Da)295,787
- Last updated2008-07-22 v2
- Checksum7932D10D624E20BB
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CH408159 EMBL· GenBank· DDBJ | EDK40360.2 EMBL· GenBank· DDBJ | Genomic DNA |