P0CX77 · ASP22_YEAST
- ProteinL-asparaginase 2-2
- GeneASP3-2
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids362 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
Miscellaneous
Yeast contains 2 L-asparaginase isoenzymes: cytoplasmic L-asparaginase I, and cell wall L-asparaginase II.
There are 4 copies for L-asparaginase 2 in yeast. The 4 identical copies ASP3-1, ASP3-2, ASP3-3 and ASP3-4 are arranged in tandem repeats located near a ribosomal DNA cluster.
Catalytic activity
- L-asparagine + H2O = L-aspartate + NH4+
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
0.27 mM | L-asparagine | |||||
0.27 mM | D-asparagine | |||||
0.27 mM | N-acetyl-L-asparagine | |||||
0.07 mM | N-carbamyl-L-asparagine | |||||
0.06 mM | N-isoleucyl-L-asparagine | |||||
0.06 mM | N-glycyl-L-asparagine | |||||
0.06 mM | N-valyl-L-asparagine | |||||
0.2 mM | N-methionyl-L-asparagine | |||||
0.4 mM | N-glycyl-D-asparagine |
Vmax | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|
42 μmol/min/mg | for L-asparagine | ||||
60 μmol/min/mg | for D-asparagine | ||||
167 μmol/min/mg | for N-acetyl-L-asparagine | ||||
79 μmol/min/mg | for N-carbamyl-L-asparagine | ||||
67 μmol/min/mg | for N-isoleucyl-L-asparagine | ||||
135 μmol/min/mg | for N-glycyl-L-asparagine | ||||
56 μmol/min/mg | for N-valyl-L-asparagine | ||||
92 μmol/min/mg | for N-methionyl-L-asparagine | ||||
8 μmol/min/mg | for N-glycyl-D-asparagine |
Does not act on isoasparagine, L-aspartate diamide, beta-alanine amide and L-glutamine.
pH Dependence
Optimum pH is 6.8. Active from pH 5.5 to pH 7.5. Stable from pH 3.5 to pH 10.5.
Features
Showing features for active site, binding site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Active site | 43 | O-isoaspartyl threonine intermediate | |||
Binding site | 89 | substrate | |||
Binding site | 122-123 | substrate | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cell wall-bounded periplasmic space | |
Cellular Component | extracellular region | |
Cellular Component | periplasmic space | |
Molecular Function | asparaginase activity | |
Biological Process | asparagine catabolic process | |
Biological Process | cellular response to nitrogen starvation |
Keywords
- Molecular function
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameL-asparaginase 2-2
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Saccharomycotina > Saccharomycetes > Saccharomycetales > Saccharomycetaceae > Saccharomyces
Accessions
- Primary accessionP0CX77
- Secondary accessions
Proteomes
Organism-specific databases
Phenotypes & Variants
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Natural variant | 26-55 | ||||
Variants
![](/variants.8e7f84.jpg)
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 1 variant from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for signal, chain, glycosylation.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Signal | 1-25 | ||||
Chain | PRO_0000410441 | 26-362 | L-asparaginase 2-2 | ||
Glycosylation | 29 | N-linked (GlcNAc...) asparagine | |||
Glycosylation | 93 | N-linked (GlcNAc...) asparagine | |||
Glycosylation | 239 | N-linked (GlcNAc...) asparagine | |||
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Induction
Subject to nitrogen catabolite repression (NCR). Not found in cells grown on rich nitrogen sources like ammonia, glutamine or glutamate, but is found in cells that have been subjected to nitrogen starvation or have been grown on a poor nitrogen source such as proline.
Gene expression databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Domain | 33-359 | Asparaginase/glutaminase | |||
Sequence similarities
Belongs to the asparaginase 1 family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length362
- Mass (Da)38,687
- Last updated2011-06-28 v1
- Checksum1DE5DC8692BF0461
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Sequence conflict | 243 | in Ref. 4; AAS56284 | |||
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
U51921 EMBL· GenBank· DDBJ | AAB67481.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY557958 EMBL· GenBank· DDBJ | AAS56284.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BK006945 EMBL· GenBank· DDBJ | DAA09472.1 EMBL· GenBank· DDBJ | Genomic DNA |