A6ZUD8 · A6ZUD8_YEAS7
- Proteinasparagine synthase (glutamine-hydrolyzing)
- GeneASN2
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids572 (go to sequence)
- Protein existencePredicted
- Annotation score2/5
Function
Catalytic activity
- L-aspartate + L-glutamine + ATP + H2O = L-asparagine + L-glutamate + AMP + diphosphate + H+
Pathway
Amino-acid biosynthesis.
Features
Showing features for active site, binding site, site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Active site | 2 | For GATase activity | |||
Binding site | 97 | L-glutamine (UniProtKB | ChEBI) | |||
Binding site | 233 | ATP (UniProtKB | ChEBI) | |||
Binding site | 291 | ATP (UniProtKB | ChEBI) | |||
Binding site | 365-366 | ATP (UniProtKB | ChEBI) | |||
Site | 367 | Important for beta-aspartyl-AMP intermediate formation | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Molecular Function | asparagine synthase (glutamine-hydrolyzing) activity | |
Molecular Function | ATP binding | |
Biological Process | asparagine biosynthetic process | |
Biological Process | glutamine metabolic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameasparagine synthase (glutamine-hydrolyzing)
- EC number
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Saccharomycotina > Saccharomycetes > Saccharomycetales > Saccharomycetaceae > Saccharomyces
Accessions
- Primary accessionA6ZUD8
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Structure
Sequence
- Sequence statusComplete
- Length572
- Mass (Da)64,621
- Last updated2007-09-11 v1
- MD5 Checksum33242E3ACF5505ADDFF6BBF30750E15E
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AAFW02000100 EMBL· GenBank· DDBJ | EDN61715.1 EMBL· GenBank· DDBJ | Genomic DNA |