P30363 (ASPG_BACLI) Reviewed, UniProtKB/Swiss-Prot
Last modified
September 21, 2011.
Version 55.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: L-asparaginase Short name=L-ASNase EC=3.5.1.1 Alternative name(s): L-asparagine amidohydrolase | ||
| Gene names |
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| Organism | Bacillus licheniformis | ||
| Taxonomic identifier | 1402 [NCBI] | ||
| Taxonomic lineage | Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus |
Protein attributes
| Sequence length | 322 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Catalytic activity | L-asparagine + H2O = L-aspartate + NH3. |
| Subunit structure | Homotetramer By similarity. |
| Subcellular location | |
| Sequence similarities | Belongs to the asparaginase 1 family. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Cytoplasm |
| Molecular function | Hydrolase |
| Gene Ontology (GO) | |
| Biological process | cellular amino acid metabolic process Inferred from electronic annotation. Source: InterPro |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | asparaginase activity Inferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
Sequences
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References
| [1] | "Lack of specific hybridization between the lep genes of Salmonella typhimurium and Bacillus licheniformis." van Dijl J.M., de Jong A., Smith H., Bron S., Venema G. FEMS Microbiol. Lett. 65:345-351(1991) [PubMed: 1916233] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | Z11497 Genomic DNA. Translation: CAA77574.1. |
| PIR | S18999. |
3D structure databases | |
| ProteinModelPortal | P30363. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Family and domain databases | |
| InterPro | IPR006034. Asparaginase/glutaminase. IPR020827. Asparaginase/glutaminase_CS. [Graphical view] |
| PANTHER | PTHR11707. Asp/Glutamnse. 1 hit. |
| Pfam | PF00710. Asparaginase. 1 hit. [Graphical view] |
| PIRSF | PIRSF001220. L-ASNase_gatD. 1 hit. |
| PRINTS | PR00139. ASNGLNASE. |
| SMART | SM00870. Asparaginase. 1 hit. [Graphical view] |
| SUPFAM | SSF53774. Asp/Glutamnse. 1 hit. |
| PROSITE | PS00144. ASN_GLN_ASE_1. 1 hit. PS00917. ASN_GLN_ASE_2. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | ASPG_BACLI | ||||||||
| Accession | Primary (citable) accession number: P30363 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

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