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Q5NXM1 (AMPA_AROAE) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 50. 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:
Probable cytosol aminopeptidase

EC=3.4.11.1
Alternative name(s):
Leucine aminopeptidase
Short name=LAP
EC=3.4.11.10
Leucyl aminopeptidase
Gene names
Name:pepA
Ordered Locus Names:AZOSEA40680
ORF Names:ebA7174
OrganismAromatoleum aromaticum (strain EbN1) (Azoarcus sp. (strain EbN1)) [Complete proteome] [HAMAP]
Taxonomic identifier76114 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaRhodocyclalesRhodocyclaceaeAromatoleum

Protein attributes

Sequence length500 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Presumably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N-terminal amino acids from various peptides By similarity. HAMAP MF_00181

Catalytic activity

Release of an N-terminal amino acid, Xaa-|-Yaa-, in which Xaa is preferably Leu, but may be other amino acids including Pro although not Arg or Lys, and Yaa may be Pro. Amino acid amides and methyl esters are also readily hydrolyzed, but rates on arylamides are exceedingly low. HAMAP MF_00181

Release of an N-terminal amino acid, preferentially leucine, but not glutamic or aspartic acids.

Cofactor

Binds 2 manganese ions per subunit By similarity. HAMAP MF_00181

Subcellular location

Cytoplasm By similarity HAMAP MF_00181.

Sequence similarities

Belongs to the peptidase M17 family.

Ontologies

Keywords
   Cellular componentCytoplasm
   LigandManganese
Metal-binding
   Molecular functionAminopeptidase
Hydrolase
Protease
   Technical termComplete proteome
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

manganese ion binding

Inferred from electronic annotation. Source: InterPro

metalloexopeptidase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 500500Probable cytosol aminopeptidase HAMAP MF_00181
PRO_1000019880

Sites

Active site2801 Potential
Active site3541 Potential
Metal binding2681Manganese 2 By similarity
Metal binding2731Manganese 1 By similarity
Metal binding2731Manganese 2 By similarity
Metal binding2911Manganese 2 By similarity
Metal binding3501Manganese 1 By similarity
Metal binding3521Manganese 1 By similarity
Metal binding3521Manganese 2 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5NXM1 [UniParc].

Last modified January 4, 2005. Version 1.
Checksum: 332FA8DC26D73770

FASTA50052,362
        10         20         30         40         50         60 
MEFTIKTGTP EKLKTGSVVV GVFADGQLGD AAAALDKASK GKFAAILGRG DLEDKAGSLL 

        70         80         90        100        110        120 
AIHDLPGSAC ERVLAVSLGK RDEFGDKAWR DALVAIGKAL ASGAASDVAV CLTDTPVPGR 

       130        140        150        160        170        180 
DIDWVLQQLV RAIADGAYRF DATKSKDKGK DSKRRGAGKV VLLTREITAS MEAAIQRGQA 

       190        200        210        220        230        240 
IAEGMALAKD LGNLPGNFCT PSYLADTAVA LGKQYKLKVE VLDRDDMEKL GMGSLLSVAR 

       250        260        270        280        290        300 
GSHQPPRFIV MHYKGGKSKD KPVVLVGKGI TFDSGGISLK PGAEMDEMKF DMCGAASVLG 

       310        320        330        340        350        360 
TFKAIARMAL PINVVGLIPT TENMPGGGAT KPGDVVTSMS GQTIEILNTD AEGRLILCDA 

       370        380        390        400        410        420 
LTYAERFKPA CVVDIATLTG ACVVALGKIP SGLLANDDAL ARELLDCGTV SGDRAWQLPL 

       430        440        450        460        470        480 
WDEYQELLKS NFADMGNIGG RFAGTITAAC FLARFTKAYK WAHLDIAGTA WVSGDAKGAT 

       490        500 
GRPVPLLAEF LIARSQGAPG 

« Hide

References

[1]"The genome sequence of an anaerobic aromatic-degrading denitrifying bacterium, strain EbN1."
Rabus R., Kube M., Heider J., Beck A., Heitmann K., Widdel F., Reinhardt R.
Arch. Microbiol. 183:27-36(2005) [PubMed: 15551059] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: EbN1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CR555306 Genomic DNA. Translation: CAI10193.1.
RefSeqYP_161094.1. NC_006513.1.

3D structure databases

HSSPHSSP built from PDB template 1GYT based on UniProtKB P68767.
ProteinModelPortalQ5NXM1.
SMRQ5NXM1. Positions 1-495.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ5NXM1.

Protein family/group databases

MEROPSM17.003.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3181364.
GenomeReviewsGene locus AZOSEA40680 in contig CR555306_GR.
KEGGeba:ebA7174.
NMPDRfig|76114.4.peg.4083.
PATRIC20974385. VBIAroAro98752_4106.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0260.
HOGENOMHBG742580.
OMANSGLMST.
ProtClustDBPRK00913.

Enzyme and pathway databases

BioCycASP76114:EBA7174-MONOMER.

Family and domain databases

HAMAPMF_00181. Cytosol_peptidase_M17.
[Tree]
InterProIPR011356. Peptidase_M17.
IPR000819. Peptidase_M17_C.
IPR023042. Peptidase_M17_cytosol_amino.
IPR008283. Peptidase_M17_N.
[Graphical view]
KOK01255.
PfamPF00883. Peptidase_M17. 1 hit.
PF02789. Peptidase_M17_N. 1 hit.
[Graphical view]
PRINTSPR00481. LAMNOPPTDASE.
PROSITEPS00631. CYTOSOL_AP. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameAMPA_AROAE
AccessionPrimary (citable) accession number: Q5NXM1
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: January 4, 2005
Last modified: January 25, 2012
This is version 50 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families