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Q11010 (AMPN_STRLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 82. 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
OrganismStreptomyces lividans
Taxonomic identifier1916 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesStreptomycineaeStreptomycetaceaeStreptomyces

Protein attributes

Sequence length857 AA.
Sequence statusComplete.
Protein existenceEvidence 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

Cytoplasm.

Post-translational modification

The N-terminus is blocked.

Sequence similarities

Belongs to the peptidase M1 family.

Ontologies

Keywords
   Cellular componentCytoplasm
   LigandMetal-binding
Zinc
   Molecular functionAminopeptidase
Hydrolase
Metalloprotease
Protease
   Technical termDirect protein sequencing
Gene Ontology (GO)
   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 – 857857Aminopeptidase N
PRO_0000095076

Regions

Region264 – 2685Substrate binding By similarity

Sites

Active site2991Proton acceptor By similarity
Metal binding2981Zinc; catalytic By similarity
Metal binding3021Zinc; catalytic By similarity
Metal binding3211Zinc; catalytic By similarity
Binding site1301Substrate By similarity
Site3861Transition state stabilizer By similarity

Sequences

Sequence LengthMass (Da)Tools
Q11010 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: 40B749F78D201A7D

FASTA85794,424
        10         20         30         40         50         60 
MPGTNLTREE ARQRATLLTV DSYEIDLDLT GAQEGGTYRS VTTVRFDVAE GGGESFIDLV 

        70         80         90        100        110        120 
APTVHEVTLN GDALDTAEVF QDSRIALPGL LPGRNILRVV ADCAYTNTGE GLHRFVDPVD 

       130        140        150        160        170        180 
DQAYLYTQFE VPDARRVFAS FEQPDLKATF QFTVKAPEGW TVISNSPTPE PKDNVWEFEP 

       190        200        210        220        230        240 
TPRISSYVTA LIVGPYHSVH SVYEKDGQSV PLGIYCRPSL AEHLDADAIF EVTRQGFDWF 

       250        260        270        280        290        300 
QEKFDYAYPF KKYDQLFVPE FNAGAMENAG AVTIRDQYVF RSKVTDAAYE VRAATILHEL 

       310        320        330        340        350        360 
AHMWFGDLVT MEWWNDLWLN ESFATYAEAA CQAAAPGSKW PHSWTTFANQ MKTWAYRQDQ 

       370        380        390        400        410        420 
LPSTHPIMAD ISDLDDVLVN FDGITYAKGA SVLKQLVAYV GEEAFFKGVQ AYFKRHAFGN 

       430        440        450        460        470        480 
TRLSDLLGAL EETSGRDLKT WSKAWLETAG INVLRPEIET DADGVITSFA IRQEAPALPA 

       490        500        510        520        530        540 
GAKGEPTLRP HRIAIGAYDL DGAGKLVRGD RVELDVDGEL TAVPQLVGKA RPAVLLLNDD 

       550        560        570        580        590        600 
DLSYAKVRLD EQSLAVVTEH LGDFTESLPR ALCWASAWDM TRDAELATRD YLALVLSGIG 

       610        620        630        640        650        660 
KESDIGVVQS LHRQVKLAID QYAAPTAREA LLTRWTEATL AHLRAAEAGS DHQLAWARAF 

       670        680        690        700        710        720 
AATARTPEQL DLLDALLDGT QTIEGLAVDT ELRWAFVQRL AAVGRFGGSE IAAEYERDKT 

       730        740        750        760        770        780 
AAGERHAATA RAARPTEAAK AEAWESVVES DKLPNAVQEA VIAGFVQTDQ RELLAAYTER 

       790        800        810        820        830        840 
YFEALKDVWA SRSHEMAQQI AVGLYPAVQV SQDTLDRTDA WLASAEPNAA LRRLVSESRS 

       850 
GIERALRAQA ADAAAAE 

« Hide

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] [Europe PMC] [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] [Europe PMC] [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

ProteinModelPortalQ11010.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

MEROPSM01.009.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR024571. ERAP1-like_C_dom.
IPR012778. Pept_M1_aminopeptidase.
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.
TIGRFAMsTIGR02412. pepN_strep_liv. 1 hit.
PROSITEPS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameAMPN_STRLI
AccessionPrimary (citable) accession number: Q11010
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: May 14, 2014
This is version 82 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