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

A2RI32 (AMPN_LACLM) Reviewed, UniProtKB/Swiss-Prot

Last modified November 13, 2013. Version 48. 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
Synonyms:lap
Ordered Locus Names:llmg_0319
OrganismLactococcus lactis subsp. cremoris (strain MG1363) [Complete proteome] [HAMAP]
Taxonomic identifier416870 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeLactococcus

Protein attributes

Sequence length846 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. It has more affinity for oligopeptides than for dipeptides. It plays an essential role in the metabolism, it may be involved in nitrogen supply or protein turnover.

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

Sequence similarities

Belongs to the peptidase M1 family.

Ontologies

Keywords
   Cellular componentCytoplasm
   LigandMetal-binding
Zinc
   Molecular functionAminopeptidase
Hydrolase
Metalloprotease
Protease
   Technical termComplete proteome
Direct protein sequencing
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 Ref.1
Chain2 – 846845Aminopeptidase N
PRO_0000285237

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
A2RI32 [UniParc].

Last modified March 6, 2007. Version 1.
Checksum: 3288DB1A43DBDEF8

FASTA84695,369
        10         20         30         40         50         60 
MAVKRLIETF VPENYKIFLD IDRKTKKIKG QVAITGEAKD TVVSFHTKGL HFNKVRAFSV 

        70         80         90        100        110        120 
DTNFIENEED EEIVVKIGET GRVTVSFEYE AELTDNMMGI YPSYYEVNGE KKMLIGTQFE 

       130        140        150        160        170        180 
SHFARQAFPS IDEPEAKATF DLSVKFDEEE GDIIVSNMPE LLNINGIHVF ERTVKMSSYL 

       190        200        210        220        230        240 
LAFVFGELQY KKGKTKSGVE VGAFATKAHS QAALDFPLDI AIRSIEFYED YYQTPYPLPH 

       250        260        270        280        290        300 
SWHIALPDFS AGAMENWGCI TYREVCMLVD PENATIQSKQ YVATVIAHEL AHQWFGDLVT 

       310        320        330        340        350        360 
MQWWDDLWLN ESFANNMEYV CMDALEPSWN VWESFSISEA NMALNRDATD GVQSVHVEVT 

       370        380        390        400        410        420 
HPDEIGTLFD PAIVYAKGSR LMVMLRKWLG DEDFAAGLAL YFKRHQYGNT VGDNLWDALA 

       430        440        450        460        470        480 
EVSGKDVAAF MHSWVNQPGY PVVTAEVVDD TLILSQKQFF VGEGVDKGRL WNVPLNTNWT 

       490        500        510        520        530        540 
GLPDLLSSEK VEIPGFAALK TKNNGKALFL NDANMAHYII DYKGALLTDL LSEVESLENV 

       550        560        570        580        590        600 
TKFQILQDRK LLAKAGVISY ADVVNILPSF TNEESYLVNT GLSQLISELE LFVDEDSETE 

       610        620        630        640        650        660 
KAFQSLVGKL FAKNYARLGW DKVAGESAGD ESLRGIVLSK TLYSENADAK TKASQIFAAH 

       670        680        690        700        710        720 
KENLASIPAD IRPIVLNNEI KTTNSAELVK TYRETYIKTS LQEFKRELEG AVALIKDEKV 

       730        740        750        760        770        780 
IAELLESFKN ADIVKPQDIA FSWFYLLRND FSQDAAWAWE KANWAFLEEK LGGDMSYDKF 

       790        800        810        820        830        840 
VIYPGNTFKT ADKLAEYKAF FEPKLENQGL KRSIEMAIKQ ITARVALIDS QKAAVDKAIT 


DIAEKL 

« Hide

References

« Hide 'large scale' references
[1]"Characterization of the Lactococcus lactis pepN gene encoding an aminopeptidase homologous to mammalian aminopeptidase N."
Tan P.S.T., van Alen-Boerrigter I.J., Poolman B., Siezen R.J., de Vos W.M., Konings W.N.
FEBS Lett. 306:9-16(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-25.
[2]"The complete genome sequence of the lactic acid bacterial paradigm Lactococcus lactis subsp. cremoris MG1363."
Wegmann U., O'Connell-Motherway M., Zomer A., Buist G., Shearman C., Canchaya C., Ventura M., Goesmann A., Gasson M.J., Kuipers O.P., van Sinderen D., Kok J.
J. Bacteriol. 189:3256-3270(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: MG1363.
[3]"Characterization and overexpression of the Lactococcus lactis pepN gene and localization of its product, aminopeptidase N."
van Alen-Boerrigter I.J., Baankreis R., de Vos W.M.
Appl. Environ. Microbiol. 57:2555-2561(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-167, CHARACTERIZATION.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M87840 Genomic DNA. Translation: AAA25205.1.
S39955 Genomic DNA. Translation: AAB22460.1.
AM406671 Genomic DNA. Translation: CAL96925.1.
M65867 Genomic DNA. Translation: AAA25162.1.
PIRS23157.
RefSeqYP_001031673.1. NC_009004.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING416870.llmg_0319.

Protein family/group databases

MEROPSM01.002.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAL96925; CAL96925; llmg_0319.
GeneID4797345.
KEGGllm:llmg_0319.
PATRIC22281679. VBILacLac4574_0328.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0308.
HOGENOMHOG000235375.
KOK01256.
OMAYLDINRE.
OrthoDBEOG693GJ0.
ProtClustDBCLSK876725.

Enzyme and pathway databases

BioCycLLAC416870:GCDT-332-MONOMER.

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_LACLM
AccessionPrimary (citable) accession number: A2RI32
Secondary accession number(s): P37897
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 2007
Last sequence update: March 6, 2007
Last modified: November 13, 2013
This is version 48 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