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Q10736

- AMPN_ACEPA

UniProt

Q10736 - AMPN_ACEPA

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Protein

Aminopeptidase N

Gene

pepN

Organism
Acetobacter pasteurianus (Acetobacter turbidans)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi

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
Complete GO annotation...

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-KW
Complete GO annotation...

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

        10         20         30         40         50
MRRLLTLTTL LAGVPLAAPV CAEQVFSFQR AAGQLPKTVV PVSYGINIST
60 70 80 90 100
DIDNLKLTGQ ETIQVDVRTP TEDVTLNQAG LHLAGAVLDN GVKATITQDD
110 120 130 140 150
AAETATLHFP AKVSKGAHTL VITYSGPILK TPNGIYVDDY TAPSGETKRM
160 170 180 190 200
LVTQFEVADA RRMFPGWDEP AFKATFQLNV TLPKEAVAVS NMPVTQSTPE
210 220 230 240 250
GTSQKRVSFA TTPRMSTYLL ALVAGDMKSV QGQADGTPLA VYAPSGLEEQ
260 270 280 290 300
GEYALHASEK ILPYYNNYFG VKYPLPQMDM VAIPGNYQAG AMENWGLLTY
310 320 330 340 350
IDNVLLFDPP NSTPRTRELI YEVVAHEMAH QWSGDLVTMG WWDNIWLNEG

FASWM
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 29, 2014
This is version 74 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