P0A962 · ASPG1_ECOLI
- ProteinL-asparaginase 1
- GeneansA
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids338 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
Miscellaneous
E.coli contains two L-asparaginase isoenzymes: L-asparaginase I, a low-affinity enzyme located in the cytoplasm, and L-asparaginase II, a high-affinity secreted enzyme.
Catalytic activity
- H2O + L-asparagine = L-aspartate + NH4+
Activity regulation
Shows cooperative activation. Allosterically activated by asparagine.
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
3.5 mM | L-asparagine |
Features
Showing features for active site, binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 14 | O-isoaspartyl threonine intermediate | ||||
Sequence: T | ||||||
Binding site | 59-61 | L-asparagine 1 (UniProtKB | ChEBI); substrate | ||||
Sequence: DSS | ||||||
Binding site | 91-92 | L-asparagine 1 (UniProtKB | ChEBI); substrate | ||||
Sequence: TD | ||||||
Binding site | 162 | L-asparagine 2 (UniProtKB | ChEBI); allosteric activator | ||||
Sequence: T | ||||||
Binding site | 240 | L-asparagine 2 (UniProtKB | ChEBI); allosteric activator | ||||
Sequence: R | ||||||
Binding site | 271-273 | L-asparagine 2 (UniProtKB | ChEBI); allosteric activator | ||||
Sequence: TQC |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | cytosol | |
Molecular Function | asparaginase activity | |
Molecular Function | identical protein binding | |
Biological Process | asparagine catabolic process via L-aspartate | |
Biological Process | protein homotetramerization |
Keywords
- Molecular function
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameL-asparaginase 1
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > Escherichia
Accessions
- Primary accessionP0A962
- Secondary accessions
Proteomes
Subcellular Location
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 14 | Loss of enzyme activity. | ||||
Sequence: T → A or V | ||||||
Mutagenesis | 61 | Loss of enzyme activity. | ||||
Sequence: S → Q | ||||||
Mutagenesis | 91 | Loss of enzyme activity. | ||||
Sequence: T → A or V | ||||||
Mutagenesis | 118 | Loss of enzyme activity. | ||||
Sequence: Q → D | ||||||
Mutagenesis | 162 | No effect on activity at saturating substrate concentration. Abolishes cooperativity. | ||||
Sequence: T → A | ||||||
Mutagenesis | 240 | No effect on activity at saturating substrate concentration. Reduced activity at lower substrate concentrations. | ||||
Sequence: R → A |
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000171079 | 1-338 | L-asparaginase 1 | |||
Sequence: MQKKSIYVAYTGGTIGMQRSEQGYIPVSGHLQRQLALMPEFHRPEMPDFTIHEYTPLMDSSDMTPEDWQHIAEDIKAHYDDYDGFVILHGTDTMAYTASALSFMLENLGKPVIVTGSQIPLAELRSDGQINLLNALYVAANYPINEVTLFFNNRLYRGNRTTKAHADGFDAFASPNLPPLLEAGIHIRRLNTPPAPHGEGELIVHPITPQPIGVVTIYPGISADVVRNFLRQPVKALILRSYGVGNAPQNKAFLQELQEASDRGIVVVNLTQCMSGKVNMGGYATGNALAHAGVIGGADMTVEATLTKLHYLLSQELDTETIRKAMSQNLRGELTPDD |
Proteomic databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 4-329 | Asparaginase/glutaminase | ||||
Sequence: KSIYVAYTGGTIGMQRSEQGYIPVSGHLQRQLALMPEFHRPEMPDFTIHEYTPLMDSSDMTPEDWQHIAEDIKAHYDDYDGFVILHGTDTMAYTASALSFMLENLGKPVIVTGSQIPLAELRSDGQINLLNALYVAANYPINEVTLFFNNRLYRGNRTTKAHADGFDAFASPNLPPLLEAGIHIRRLNTPPAPHGEGELIVHPITPQPIGVVTIYPGISADVVRNFLRQPVKALILRSYGVGNAPQNKAFLQELQEASDRGIVVVNLTQCMSGKVNMGGYATGNALAHAGVIGGADMTVEATLTKLHYLLSQELDTETIRKAMSQN |
Sequence similarities
Belongs to the asparaginase 1 family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length338
- Mass (Da)37,127
- Last updated2005-07-19 v1
- Checksum75D97E6D10E9F8DA
Sequence caution
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
M26934 EMBL· GenBank· DDBJ | AAA23446.1 EMBL· GenBank· DDBJ | Genomic DNA | Different initiation | |
U00096 EMBL· GenBank· DDBJ | AAC74837.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AP009048 EMBL· GenBank· DDBJ | BAA15558.1 EMBL· GenBank· DDBJ | Genomic DNA |