Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q10736 (AMPN_ACEPA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 71. 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):
Alpha-aminoacylpeptide hydrolase
Gene names
Name:pepN
OrganismAcetobacter pasteurianus (Acetobacter turbidans)
Taxonomic identifier438 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhodospirillalesAcetobacteraceaeAcetobacter

Protein attributes

Sequence length355 AA.
Sequence statusFragment.
Protein existenceInferred from homology

General annotation (Comments)

Function

Aminopeptidase N is involved in the degradation of intracellular peptides generated by protein breakdown during normal growth as well as in response to nutrient starvation By similarity.

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.

Subcellular location

Cytoplasm By similarity.

Sequence similarities

Belongs to the peptidase M1 family.

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

Chain1 – ›355›355Aminopeptidase N
PRO_0000095067

Regions

Region290 – 2945Substrate binding By similarity

Sites

Active site3271Proton acceptor By similarity
Metal binding3261Zinc; catalytic By similarity
Metal binding3301Zinc; catalytic By similarity
Metal binding3491Zinc; catalytic By similarity
Binding site1561Substrate By similarity
Binding site3491Substrate By similarity

Experimental info

Non-terminal residue3551

Sequences

Sequence LengthMass (Da)Tools
Q10736 [UniParc].

Last modified November 1, 1997. Version 1.
Checksum: 8F214BDB2B368232

FASTA35538,820
        10         20         30         40         50         60 
MRRLLTLTTL LAGVPLAAPV CAEQVFSFQR AAGQLPKTVV PVSYGINIST DIDNLKLTGQ 

        70         80         90        100        110        120 
ETIQVDVRTP TEDVTLNQAG LHLAGAVLDN GVKATITQDD AAETATLHFP AKVSKGAHTL 

       130        140        150        160        170        180 
VITYSGPILK TPNGIYVDDY TAPSGETKRM LVTQFEVADA RRMFPGWDEP AFKATFQLNV 

       190        200        210        220        230        240 
TLPKEAVAVS NMPVTQSTPE GTSQKRVSFA TTPRMSTYLL ALVAGDMKSV QGQADGTPLA 

       250        260        270        280        290        300 
VYAPSGLEEQ GEYALHASEK ILPYYNNYFG VKYPLPQMDM VAIPGNYQAG AMENWGLLTY 

       310        320        330        340        350 
IDNVLLFDPP NSTPRTRELI YEVVAHEMAH QWSGDLVTMG WWDNIWLNEG FASWM 

« Hide

References

[1]"Cloning and DNA sequence analysis of the 5' end of aminopeptidase N (pepN) from Acetobacter turbidans ATCC9325."
Weber M.
Submitted (JAN-1996) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 9325 / NCTC 6249 / NRRL B-570.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X94692 Genomic DNA. Translation: CAA64355.1.

3D structure databases

ProteinModelPortalQ10736.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR001930. Peptidase_M1.
IPR014782. Peptidase_M1_N.
[Graphical view]
PANTHERPTHR11533. PTHR11533. 1 hit.
PfamPF01433. Peptidase_M1. 1 hit.
[Graphical view]
PRINTSPR00756. ALADIPTASE.
PROSITEPS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameAMPN_ACEPA
AccessionPrimary (citable) accession number: Q10736
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: May 1, 2013
This is version 71 of the entry and version 1 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