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Q10736

- AMPN_ACEPA

UniProt

Q10736 - AMPN_ACEPA

Protein

Aminopeptidase N

Gene

pepN

Organism
Acetobacter pasteurianus (Acetobacter turbidans)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 73 (01 Oct 2014)
      Sequence version 1 (01 Nov 1997)
      Previous versions | rss
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    Functioni

    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 activityi

    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.

    Cofactori

    Binds 1 zinc ion per subunit.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei156 – 1561SubstrateBy similarity
    Metal bindingi326 – 3261Zinc; catalyticPROSITE-ProRule annotation
    Active sitei327 – 3271Proton acceptorPROSITE-ProRule annotation
    Metal bindingi330 – 3301Zinc; catalyticPROSITE-ProRule annotation
    Metal bindingi349 – 3491Zinc; catalyticPROSITE-ProRule annotation
    Binding sitei349 – 3491SubstrateBy similarity

    GO - Molecular functioni

    1. aminopeptidase activity Source: UniProtKB-KW
    2. metallopeptidase activity Source: UniProtKB-KW
    3. zinc ion binding Source: InterPro

    Keywords - Molecular functioni

    Aminopeptidase, Hydrolase, Metalloprotease, Protease

    Keywords - Ligandi

    Metal-binding, Zinc

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Aminopeptidase N (EC:3.4.11.2)
    Alternative name(s):
    Alpha-aminoacylpeptide hydrolase
    Gene namesi
    Name:pepN
    OrganismiAcetobacter pasteurianus (Acetobacter turbidans)
    Taxonomic identifieri438 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhodospirillalesAcetobacteraceaeAcetobacter

    Subcellular locationi

    Cytoplasm By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – ›355›355Aminopeptidase NPRO_0000095067Add
    BLAST

    Structurei

    3D structure databases

    ProteinModelPortaliQ10736.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni290 – 2945Substrate bindingBy similarity

    Sequence similaritiesi

    Belongs to the peptidase M1 family.Curated

    Family and domain databases

    InterProiIPR001930. Peptidase_M1.
    IPR014782. Peptidase_M1_N.
    [Graphical view]
    PANTHERiPTHR11533. PTHR11533. 1 hit.
    PfamiPF01433. Peptidase_M1. 1 hit.
    [Graphical view]
    PRINTSiPR00756. ALADIPTASE.
    PROSITEiPS00142. ZINC_PROTEASE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Fragment.

    Q10736-1 [UniParc]FASTAAdd to Basket

    « Hide

    MRRLLTLTTL LAGVPLAAPV CAEQVFSFQR AAGQLPKTVV PVSYGINIST    50
    DIDNLKLTGQ ETIQVDVRTP TEDVTLNQAG LHLAGAVLDN GVKATITQDD 100
    AAETATLHFP AKVSKGAHTL VITYSGPILK TPNGIYVDDY TAPSGETKRM 150
    LVTQFEVADA RRMFPGWDEP AFKATFQLNV TLPKEAVAVS NMPVTQSTPE 200
    GTSQKRVSFA TTPRMSTYLL ALVAGDMKSV QGQADGTPLA VYAPSGLEEQ 250
    GEYALHASEK ILPYYNNYFG VKYPLPQMDM VAIPGNYQAG AMENWGLLTY 300
    IDNVLLFDPP NSTPRTRELI YEVVAHEMAH QWSGDLVTMG WWDNIWLNEG 350
    FASWM 355
    Length:355
    Mass (Da):38,820
    Last modified:November 1, 1997 - v1
    Checksum:i8F214BDB2B368232
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Non-terminal residuei355 – 3551

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X94692 Genomic DNA. Translation: CAA64355.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X94692 Genomic DNA. Translation: CAA64355.1 .

    3D structure databases

    ProteinModelPortali Q10736.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Family and domain databases

    InterProi IPR001930. Peptidase_M1.
    IPR014782. Peptidase_M1_N.
    [Graphical view ]
    PANTHERi PTHR11533. PTHR11533. 1 hit.
    Pfami PF01433. Peptidase_M1. 1 hit.
    [Graphical view ]
    PRINTSi PR00756. ALADIPTASE.
    PROSITEi PS00142. ZINC_PROTEASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.

    Entry informationi

    Entry nameiAMPN_ACEPA
    AccessioniPrimary (citable) accession number: Q10736
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: November 1, 1997
    Last modified: October 1, 2014
    This is version 73 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Documents

    1. Peptidase families
      Classification of peptidase families and list of entries
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3