O57971 (ASGX_PYRHO) Reviewed, UniProtKB/Swiss-Prot
Last modified
December 14, 2011.
Version 63.
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: Putative L-asparaginase EC=3.5.1.1 Alternative name(s): L-asparagine amidohydrolase Cleaved into the following 2 chains: | ||
| Gene names |
| ||
| Organism | Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3) [Complete proteome] [HAMAP] | ||
| Taxonomic identifier | 70601 [NCBI] | ||
| Taxonomic lineage | Archaea › Euryarchaeota › Thermococci › Thermococcales › Thermococcaceae › Pyrococcus |
Protein attributes
| Sequence length | 305 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Catalytic activity | L-asparagine + H2O = L-aspartate + NH3. |
| Post-translational modification | Autocleaved. Generates the alpha and beta subunits. The N-terminal residue of the beta subunit is thought to be responsible for the nucleophile hydrolase activity Potential. |
| Sequence similarities | Belongs to the Ntn-hydrolase family. |
Ontologies
| Keywords | |
|---|---|
| Molecular function | Hydrolase Protease |
| PTM | Autocatalytic cleavage |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | proteolysis Inferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | asparaginase activity Inferred from electronic annotation. Source: EC peptidase activityInferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 174 | 174 | Putative L-asparaginase subunit alpha | PRO_0000184581 | |||||
| Chain | 175 – 305 | 131 | Putative L-asparaginase subunit beta | PRO_0000329018 | |||||
Sites | |||||||||
| Active site | 175 | 1 | Nucleophile By similarity | ||||||
| Site | 174 – 175 | 2 | Cleavage; by autolysis Potential | ||||||
Sequences
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References
| [1] | "Complete sequence and gene organization of the genome of a hyper-thermophilic archaebacterium, Pyrococcus horikoshii OT3." Kawarabayasi Y., Sawada M., Horikawa H., Haikawa Y., Hino Y., Yamamoto S., Sekine M., Baba S., Kosugi H., Hosoyama A., Nagai Y., Sakai M., Ogura K., Otsuka R., Nakazawa H., Takamiya M., Ohfuku Y., Funahashi T. Kikuchi H.DNA Res. 5:55-76(1998) [PubMed: 9679194] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | BA000001 Genomic DNA. Translation: BAA29304.1. |
| PIR | A71247. |
| RefSeq | NP_142228.1. NC_000961.1. |
3D structure databases | |
| ProteinModelPortal | O57971. |
| ModBase | Search... |
Protein family/group databases | |
| MEROPS | T02.002. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | EBPYRT00000001542; EBPYRP00000001542; EBPYRG00000001542. |
| GeneID | 1444122. |
| GenomeReviews | Gene locus PH0232 in contig BA000001_GR. |
| KEGG | pho:PH0232. |
| NMPDR | fig|70601.1.peg.222. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| GeneTree | EBGT00050000022719. |
| HOGENOM | HBG735787. |
| OMA | WAVKWTS. |
| PhylomeDB | O57971. |
| ProtClustDB | CLSK253204. |
Enzyme and pathway databases | |
| BioCyc | PHOR70601:PH0232-MONOMER. |
Family and domain databases | |
| InterPro | IPR000246. Peptidase_T2. [Graphical view] |
| KO | K13051. |
| PANTHER | PTHR10188. Peptidase_T2. 1 hit. |
| Pfam | PF01112. Asparaginase_2. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | ASGX_PYRHO | ||||||||
| Accession | Primary (citable) accession number: O57971 | ||||||||
| 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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