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Protein

Cytosol aminopeptidase

Gene

pepA

Organism
Pseudomonas putida (Arthrobacter siderocapsulatus)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

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).By similarity

Catalytic activityi

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

Cofactori

Mn2+By similarityNote: Binds 2 manganese ions per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi267 – 2671Manganese 2By similarity
Metal bindingi272 – 2721Manganese 1By similarity
Metal bindingi272 – 2721Manganese 2By similarity
Active sitei279 – 2791Sequence analysis
Metal bindingi290 – 2901Manganese 2By similarity
Metal bindingi349 – 3491Manganese 1By similarity
Metal bindingi351 – 3511Manganese 1By similarity
Metal bindingi351 – 3511Manganese 2By similarity
Active sitei353 – 3531Sequence analysis

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Aminopeptidase, Hydrolase, Protease

Keywords - Ligandi

Manganese, Metal-binding

Enzyme and pathway databases

BRENDAi3.4.11.10. 5092.

Names & Taxonomyi

Protein namesi
Recommended name:
Cytosol aminopeptidase (EC:3.4.11.1)
Alternative name(s):
Leucine aminopeptidase (EC:3.4.11.10)
Short name:
LAP
Leucyl aminopeptidase
Gene namesi
Name:pepA
OrganismiPseudomonas putida (Arthrobacter siderocapsulatus)
Taxonomic identifieri303 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 497497Cytosol aminopeptidasePRO_0000165783Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi160488.PP_0980.

Structurei

Secondary structure

1
497
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 65Combined sources
Helixi10 – 123Combined sources
Beta strandi18 – 236Combined sources
Helixi24 – 263Combined sources
Helixi30 – 389Combined sources
Turni39 – 413Combined sources
Helixi42 – 487Combined sources
Beta strandi59 – 624Combined sources
Beta strandi69 – 713Combined sources
Beta strandi73 – 8210Combined sources
Helixi86 – 10217Combined sources
Beta strandi106 – 1105Combined sources
Turni122 – 1243Combined sources
Helixi125 – 13612Combined sources
Beta strandi156 – 1605Combined sources
Helixi163 – 1653Combined sources
Helixi166 – 19126Combined sources
Turni194 – 1963Combined sources
Helixi199 – 21214Combined sources
Beta strandi216 – 2216Combined sources
Helixi223 – 2286Combined sources
Helixi232 – 2387Combined sources
Beta strandi241 – 2433Combined sources
Beta strandi246 – 2538Combined sources
Beta strandi262 – 27211Combined sources
Helixi284 – 2896Combined sources
Helixi292 – 30716Combined sources
Beta strandi310 – 32213Combined sources
Beta strandi333 – 3364Combined sources
Beta strandi342 – 3465Combined sources
Helixi352 – 36312Combined sources
Helixi364 – 3663Combined sources
Beta strandi369 – 3757Combined sources
Helixi379 – 3857Combined sources
Turni386 – 3883Combined sources
Beta strandi389 – 3957Combined sources
Helixi397 – 41014Combined sources
Beta strandi414 – 4163Combined sources
Helixi421 – 4244Combined sources
Helixi425 – 4273Combined sources
Beta strandi430 – 4367Combined sources
Beta strandi440 – 4423Combined sources
Helixi443 – 45210Combined sources
Beta strandi460 – 4645Combined sources
Turni466 – 4683Combined sources
Beta strandi469 – 4713Combined sources
Helixi484 – 49512Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3H8EX-ray2.75A/B1-497[»]
3H8FX-ray2.20A/B/C/D/E/F1-497[»]
3H8GX-ray1.50A/B/C/D/E/F1-497[»]
ProteinModelPortaliO86436.
SMRiO86436. Positions 1-496.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO86436.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase M17 family.Curated

Phylogenomic databases

eggNOGiENOG4105BZ6. Bacteria.
COG0260. LUCA.

Family and domain databases

HAMAPiMF_00181. Cytosol_peptidase_M17.
InterProiIPR011356. Leucine_aapep/pepB.
IPR000819. Peptidase_M17_C.
IPR023042. Peptidase_M17_leu_NH2_pept.
IPR008283. Peptidase_M17_N.
[Graphical view]
PANTHERiPTHR11963. PTHR11963. 1 hit.
PfamiPF00883. Peptidase_M17. 1 hit.
PF02789. Peptidase_M17_N. 1 hit.
[Graphical view]
PRINTSiPR00481. LAMNOPPTDASE.
PROSITEiPS00631. CYTOSOL_AP. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O86436-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MELVVKSVAA ASVKTATLVI PVGENRKLGA VAKAVDLASE GAISAVLKRG
60 70 80 90 100
DLAGKPGQTL LLQNLQGLKA ERVLLVGSGK DEALGDRTWR KLVASVAGVL
110 120 130 140 150
KGLNGADAVL ALDDVAVNNR DAHYGKYRLL AETLLDGEYV FDRFKSQKVE
160 170 180 190 200
PRALKKVTLL ADKAGQAEVE RAVKHASAIA TGMAFTRDLG NLPPNLCHPS
210 220 230 240 250
FLAEQAKELG KAHKALKVEV LDEKKIKDLG MGAFYAVGQG SDQPPRLIVL
260 270 280 290 300
NYQGGKKADK PFVLVGKGIT FDTGGISLKP GAGMDEMKYD MCGAASVFGT
310 320 330 340 350
LRAVLELQLP VNLVCLLACA ENMPSGGATR PGDIVTTMSG QTVEILNTDA
360 370 380 390 400
EGRLVLCDTL TYAERFKPQA VIDIATLTGA CIVALGSHTT GLMGNNDDLV
410 420 430 440 450
GQLLDAGKRA DDRAWQLPLF DEYQEQLDSP FADMGNIGGP KAGTITAGCF
460 470 480 490
LSRFAKAYNW AHMDIAGTAW ISGGKDKGAT GRPVPLLTQY LLDRAGA
Length:497
Mass (Da):52,469
Last modified:November 1, 1998 - v1
Checksum:i69851EB412B7F81A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ010261 Genomic DNA. Translation: CAA09054.1.
RefSeqiWP_016501309.1. NZ_LWDW01000056.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ010261 Genomic DNA. Translation: CAA09054.1.
RefSeqiWP_016501309.1. NZ_LWDW01000056.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3H8EX-ray2.75A/B1-497[»]
3H8FX-ray2.20A/B/C/D/E/F1-497[»]
3H8GX-ray1.50A/B/C/D/E/F1-497[»]
ProteinModelPortaliO86436.
SMRiO86436. Positions 1-496.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi160488.PP_0980.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG4105BZ6. Bacteria.
COG0260. LUCA.

Enzyme and pathway databases

BRENDAi3.4.11.10. 5092.

Miscellaneous databases

EvolutionaryTraceiO86436.

Family and domain databases

HAMAPiMF_00181. Cytosol_peptidase_M17.
InterProiIPR011356. Leucine_aapep/pepB.
IPR000819. Peptidase_M17_C.
IPR023042. Peptidase_M17_leu_NH2_pept.
IPR008283. Peptidase_M17_N.
[Graphical view]
PANTHERiPTHR11963. PTHR11963. 1 hit.
PfamiPF00883. Peptidase_M17. 1 hit.
PF02789. Peptidase_M17_N. 1 hit.
[Graphical view]
PRINTSiPR00481. LAMNOPPTDASE.
PROSITEiPS00631. CYTOSOL_AP. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "New developments in the enzymatic preparation and use of enantiopure alpha-hydrogen and alpha,alpha-disubstituted alpha-amino acids."
    Sonke T., Kaptein B., Boesten W.H.J., Broxterman Q.B., Kamphuis J., Formaggio F., Toniolo C., Rutjes F.P.J.T., Schoemaker H.E.
    Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 12633 / DSM 291 / JCM 13063 / NCIMB 9494 / NCTC 10936 / VKM B-2187 / Stanier 90.

Entry informationi

Entry nameiAMPA_PSEPU
AccessioniPrimary (citable) accession number: O86436
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: November 1, 1998
Last modified: July 6, 2016
This is version 85 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.