Q8U4E6 (ASGX_PYRFU) Reviewed, UniProtKB/Swiss-Prot
Last modified
December 14, 2011.
Version 46.
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 furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1) | ||
| Taxonomic identifier | 186497 [NCBI] | ||
| Taxonomic lineage | Archaea › Euryarchaeota › Thermococci › Thermococcales › Thermococcaceae › Pyrococcus |
Protein attributes
| Sequence length | 306 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 Reference 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 – 175 | 175 | Putative L-asparaginase subunit alpha | PRO_0000184580 | |||||
| Chain | 176 – 306 | 131 | Putative L-asparaginase subunit beta | PRO_0000329017 | |||||
Sites | |||||||||
| Active site | 176 | 1 | Nucleophile By similarity | ||||||
| Site | 175 – 176 | 2 | Cleavage; by autolysis Potential | ||||||
Sequences
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References
| [1] | "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P. horikoshii inferred from complete genomic sequences." Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M., DiRuggiero J., Robb F.T. Genetics 152:1299-1305(1999) [PubMed: 10430560] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 43587 / DSM 3638 / JCM 8422 / Vc1. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AE009950 Genomic DNA. Translation: AAL80266.1. |
| RefSeq | NP_577871.1. NC_003413.1. |
3D structure databases | |
| ProteinModelPortal | Q8U4E6. |
| ModBase | Search... |
Protein family/group databases | |
| MEROPS | T02.002. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | EBPYRT00000004210; EBPYRP00000004071; EBPYRG00000004210. |
| GeneID | 1467974. |
| GenomeReviews | Gene locus PF0142 in contig AE009950_GR. |
| KEGG | pfu:PF0142. |
| NMPDR | fig|186497.1.peg.145. |
Phylogenomic databases | |
| GeneTree | EBGT00050000022719. |
| HOGENOM | HBG735787. |
| OMA | ATGHGEF. |
| PhylomeDB | Q8U4E6. |
| ProtClustDB | CLSK253204. |
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_PYRFU | ||||||||
| Accession | Primary (citable) accession number: Q8U4E6 | ||||||||
| 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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