Q11010 (AMPN_STRLI) Reviewed, UniProtKB/Swiss-Prot
Last modified
November 16, 2011.
Version 72.
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: Aminopeptidase N EC=3.4.11.2 Alternative name(s): Alanine aminopeptidase Lysyl aminopeptidase Short name=Lys-AP | ||
| Gene names |
| ||
| Organism | Streptomyces lividans | ||
| Taxonomic identifier | 1916 [NCBI] | ||
| Taxonomic lineage | Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Streptomycineae › Streptomycetaceae › Streptomyces |
Protein attributes
| Sequence length | 857 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | Aminopeptidase with broad substrate specificity to several peptides. Shows strong preference for leucine but cleaves also next to Arg and lysine in peptide-bond-containing substrates. |
| Catalytic activity | Release of an N-terminal amino acid, Xaa-|-Yaa- from a peptide, amide or arylamide. Xaa is preferably Ala, but may be most amino acids including Pro (slow action). When a terminal hydrophobic residue is followed by a prolyl residue, the two may be released as an intact Xaa-Pro dipeptide. |
| Cofactor | Binds 1 zinc ion per subunit By similarity. |
| Subunit structure | Monomer. |
| Subcellular location | |
| Post-translational modification | The N-terminus is blocked. |
| Sequence similarities | Belongs to the peptidase M1 family. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Cytoplasm |
| Ligand | Metal-binding Zinc |
| Molecular function | Aminopeptidase Hydrolase Metalloprotease 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 metallopeptidase activityInferred from electronic annotation. Source: UniProtKB-KW zinc ion bindingInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 857 | 857 | Aminopeptidase N | PRO_0000095076 | |||||
Regions | |||||||||
| Region | 264 – 268 | 5 | Substrate binding By similarity | ||||||
Sites | |||||||||
| Active site | 299 | 1 | Proton acceptor By similarity | ||||||
| Metal binding | 298 | 1 | Zinc; catalytic By similarity | ||||||
| Metal binding | 302 | 1 | Zinc; catalytic By similarity | ||||||
| Metal binding | 321 | 1 | Zinc; catalytic By similarity | ||||||
| Binding site | 130 | 1 | Substrate By similarity | ||||||
| Site | 386 | 1 | Transition state stabilizer By similarity | ||||||
Sequences
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References
| [1] | "The aminopeptidase N-encoding pepN gene of Streptomyces lividans 66." Butler M.J., Aphale J.S., Binnie C., Dizonno M.A., Krygsman P., Soltes G.A., Walczyk E., Malek L.T. Gene 141:115-119(1994) [PubMed: 7909302] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 415-439. Strain: 66 / 1326. |
| [2] | "Intracellular aminopeptidases in Streptomyces lividans 66." Butler M.J., Aphale J.S., Dizonno M.A., Krygsman P., Walczyk E., Malek L.T. J. Ind. Microbiol. 13:24-29(1994) [PubMed: 7765336] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 66 / 1326. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | L23172 Genomic DNA. Translation: AAA26696.1. |
3D structure databases | |
| ProteinModelPortal | Q11010. |
| ModBase | Search... |
Protein family/group databases | |
| MEROPS | M01.009. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Family and domain databases | |
| InterPro | IPR012778. Pept_M1_aminopeptidase. IPR024571. Pept_M1_aminopeptidase_C. IPR001930. Peptidase_M1. IPR014782. Peptidase_M1_N. [Graphical view] |
| PANTHER | PTHR11533. Peptidase_M1. 1 hit. |
| Pfam | PF11838. DUF3358. 1 hit. PF01433. Peptidase_M1. 1 hit. [Graphical view] |
| PRINTS | PR00756. ALADIPTASE. |
| TIGRFAMs | TIGR02412. PepN_strep_liv. 1 hit. |
| PROSITE | PS00142. ZINC_PROTEASE. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | AMPN_STRLI | ||||||||
| Accession | Primary (citable) accession number: Q11010 | ||||||||
| 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 |

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