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P37896 (AMPN_LACDL) Reviewed, UniProtKB/Swiss-Prot

Last modified September 18, 2013. Version 78. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Aminopeptidase N

EC=3.4.11.2
Alternative name(s):
Alanine aminopeptidase
Lysyl aminopeptidase
Short name=Lys-AP
Gene names
Name:pepN
OrganismLactobacillus delbrueckii subsp. lactis
Taxonomic identifier29397 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliLactobacillalesLactobacillaceaeLactobacillus

Protein attributes

Sequence length843 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Aminopeptidase with broad substrate specificity to several peptides.

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 By similarity.

Subcellular location

Cytoplasm. Note: It may be secreted through an unknown mechanism.

Sequence similarities

Belongs to the peptidase M1 family.

Biophysicochemical properties

pH dependence:

Optimum pH is 6.5-7.0.

Temperature dependence:

Optimum temperature is 54-55 degrees Celsius.

Ontologies

Keywords
   Cellular componentCytoplasm
   LigandMetal-binding
Zinc
   Molecular functionAminopeptidase
Hydrolase
Metalloprotease
Protease
Gene Ontology (GO)
   Biological_processproteolysis

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionaminopeptidase activity

Inferred from electronic annotation. Source: UniProtKB-KW

metallopeptidase activity

Inferred from electronic annotation. Source: UniProtKB-KW

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 843842Aminopeptidase N
PRO_0000095071

Regions

Region252 – 2565Substrate binding By similarity

Sites

Active site2891Proton acceptor By similarity
Metal binding2881Zinc; catalytic By similarity
Metal binding2921Zinc; catalytic By similarity
Metal binding3111Zinc; catalytic By similarity
Binding site1201Substrate By similarity
Site3751Transition state stabilizer By similarity

Sequences

Sequence LengthMass (Da)Tools
P37896 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 08EF9F8CBD7AB1B0

FASTA84395,348
        10         20         30         40         50         60 
MAVKRFYETF HPDHYDLYID VDRAARSFSG TSTIHGEIQE ETVLVHQKYM TISKVTVDGK 

        70         80         90        100        110        120 
EVPFTFGDDF EGIKIEAGKT GEAVIAIDYS APLTDTMMGI YPSYYQVDGV KKELIGTQFE 

       130        140        150        160        170        180 
TTFAREAFPC VDEPEAKATF SLALKFDEHE GETVLANMPE DRVENGVHYF KETVRMSSYL 

       190        200        210        220        230        240 
VAFAFGEMRS LTTHTKSGVL IGVYSTQAHT EKELTFSLDI AKRAIEFYED FYQTPYPLPQ 

       250        260        270        280        290        300 
SLQLALPDFS AGAMENWGLV TYREAYLLLD PDNTTLEMKK LVATVVTHEL AHQWFGDLVT 

       310        320        330        340        350        360 
MEWWDNLWLN ESFANMMEYL SVDHLEPNWH IWEMFQTSEA AAALTRDATD GVQSVHVEVN 

       370        380        390        400        410        420 
DPAEIDALFD GAIVYAKGSR MLVMVRSLLG DEALRKGLKR YFDKHKFGNA AGDDLWDALS 

       430        440        450        460        470        480 
TATDLNIGEI MHTWLDQPGY PVVNAFVEDG HLKLTQKQFF IGEGKEVGRK WEIPLNANFK 

       490        500        510        520        530        540 
APKIMSDVEL DLGDYQALRA EAGHALRLNV GNNSHFIVKY DQTLMDDIMK EAKDLDPVSQ 

       550        560        570        580        590        600 
LQLLQDLRLL AEGKQASYAD VVPVLELFKN SESHIVNDAL YTTADKLRQF APAGSEADKN 

       610        620        630        640        650        660 
LRALYNDLSK DQVARLGWLP KAGESDEDIQ TRPYVLSASL YGRNADSEKQ AHEIYVEYAD 

       670        680        690        700        710        720 
KLAELSADIR PYVLINEVEN YGSSELTDKL IGLYQATSDP SFKMDLEAAI VKSKDEGELK 

       730        740        750        760        770        780 
KIVSWFKNAE IVKPQDLRGW FSGVLSNPAG EQLAWDWIRD EWAWLEKTVG GDMEFATFIT 

       790        800        810        820        830        840 
VISRVFKTKE RYDEYNAFFT DKESNMLLNR EIKMDRKVIA NRVDLIASEQ ADVNAAVAAA 


LQK 

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References

[1]"Cloning, DNA sequence analysis and partial characterization of pepN, a lysyl aminopeptidase from Lactobacillus delbruckii ssp. lactis DSM7290."
Klein J.R., Klein U., Schad M., Plapp R.
Eur. J. Biochem. 217:105-114(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: DSM 7290.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z21701 Genomic DNA. Translation: CAA79805.1.
PIRS38364.

3D structure databases

ProteinModelPortalP37896.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

MEROPSM01.002.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR024571. ERAP1-like_C_dom.
IPR001930. Peptidase_M1.
IPR014782. Peptidase_M1_N.
[Graphical view]
PANTHERPTHR11533. PTHR11533. 1 hit.
PfamPF11838. ERAP1_C. 1 hit.
PF01433. Peptidase_M1. 1 hit.
[Graphical view]
PRINTSPR00756. ALADIPTASE.
PROSITEPS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameAMPN_LACDL
AccessionPrimary (citable) accession number: P37896
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: January 23, 2007
Last modified: September 18, 2013
This is version 78 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries