A0A9C7Q3J3 · A0A9C7Q3J3_9RHOD
- Proteinasparagine synthase (glutamine-hydrolyzing)
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids559 (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 | 101 | L-glutamine (UniProtKB | ChEBI) | |||
Binding site | 351-352 | ATP (UniProtKB | ChEBI) | |||
Site | 353 | 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
- Organism
- Strain
- Taxonomic lineageEukaryota > Rhodophyta > Bangiophyceae > Galdieriales > Galdieriaceae > Galdieria
Accessions
- Primary accessionA0A9C7Q3J3
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Structure
Sequence
- Sequence statusComplete
- Length559
- Mass (Da)63,598
- Last updated2023-05-03 v1
- ChecksumCFCAA28A8020416D
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
BQMJ01000075 EMBL· GenBank· DDBJ | GJQ15828.1 EMBL· GenBank· DDBJ | Genomic DNA |