P46547 (PIP_AERSO) Reviewed, UniProtKB/Swiss-Prot
Last modified
November 16, 2011.
Version 62.
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: Proline iminopeptidase Short name=PIP EC=3.4.11.5 Alternative name(s): Prolyl aminopeptidase Short name=PAP | ||||
| Gene names |
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| Organism | Aeromonas sobria | ||||
| Taxonomic identifier | 646 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Aeromonadales › Aeromonadaceae › Aeromonas |
Protein attributes
| Sequence length | 425 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | Higher activity toward long peptides. Acts on hydroxyproline beta-naphthylamide with almost as high an activity as on proline beta-naphthylamide. |
| Catalytic activity | Release of N-terminal proline from a peptide. |
| Subunit structure | Homotetramer. |
| Subcellular location | |
| Sequence similarities | Belongs to the peptidase S33 family. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Cytoplasm |
| Molecular function | Aminopeptidase Hydrolase Protease |
| Technical term | Direct protein sequencing |
| Gene Ontology (GO) | |
| Biological process | proteolysis Inferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | aminopeptidase activity Inferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Sequence annotation (Features)
Sequences
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References
| [1] | "Isolation and characterization of the prolyl aminopeptidase gene (pap) from Aeromonas sobria: comparison with the Bacillus coagulans enzyme." Kitazono A., Kitano A., Tsuru D., Yoshimoto T. J. Biochem. 116:818-825(1994) [PubMed: 7883756] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | D30714 Genomic DNA. Translation: BAA06380.1. |
| PIR | JC4184. |
3D structure databases | |
| ProteinModelPortal | P46547. |
| ModBase | Search... |
Protein family/group databases | |
| MEROPS | S33.008. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Family and domain databases | |
| InterPro | IPR000073. AB_hydrolase_1. IPR002410. Peptidase_S33. [Graphical view] |
| Pfam | PF00561. Abhydrolase_1. 1 hit. [Graphical view] |
| PRINTS | PR00793. PROAMNOPTASE. |
| ProtoNet | Search... |
Entry information
| Entry name | PIP_AERSO | ||||||||
| Accession | Primary (citable) accession number: P46547 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| Peptidase families Classification of peptidase families and list of entries |
| SIMILARITY comments Index of protein domains and families |

Clusters with