Q6BFY9 · Q6BFY9_PARTE
- Proteinasparagine synthase (glutamine-hydrolyzing)
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids588 (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 | 106 | L-glutamine (UniProtKB | ChEBI) | |||
Binding site | 278 | ATP (UniProtKB | ChEBI) | |||
Site | 354 | 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 > Sar > Alveolata > Ciliophora > Intramacronucleata > Oligohymenophorea > Peniculida > Parameciidae > Paramecium
Accessions
- Primary accessionQ6BFY9
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Interaction
Protein-protein interaction databases
Structure
Sequence
- Sequence statusComplete
- Length588
- Mass (Da)68,283
- Last updated2004-08-16 v1
- MD5 Checksum7D8B11796BB8BAA07F1F3D7E56E82989
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CR548612 EMBL· GenBank· DDBJ | CAH03431.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CT867985 EMBL· GenBank· DDBJ | CAK55849.1 EMBL· GenBank· DDBJ | Genomic DNA |