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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)DescriptionActionsGraphical viewLength
Metal bindingi267Manganese 2By similarity1
Metal bindingi272Manganese 1By similarity1
Metal bindingi272Manganese 2By similarity1
Active sitei279Sequence analysis1
Metal bindingi290Manganese 2By similarity1
Metal bindingi349Manganese 1By similarity1
Metal bindingi351Manganese 1By similarity1
Metal bindingi351Manganese 2By similarity1
Active sitei353Sequence analysis1

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)DescriptionActionsGraphical viewLength
ChainiPRO_00001657831 – 497Cytosol aminopeptidaseAdd BLAST497

Interactioni

Protein-protein interaction databases

STRINGi160488.PP_0980.

Structurei

Secondary structure

1497
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi2 – 6Combined sources5
Helixi10 – 12Combined sources3
Beta strandi18 – 23Combined sources6
Helixi24 – 26Combined sources3
Helixi30 – 38Combined sources9
Turni39 – 41Combined sources3
Helixi42 – 48Combined sources7
Beta strandi59 – 62Combined sources4
Beta strandi69 – 71Combined sources3
Beta strandi73 – 82Combined sources10
Helixi86 – 102Combined sources17
Beta strandi106 – 110Combined sources5
Turni122 – 124Combined sources3
Helixi125 – 136Combined sources12
Beta strandi156 – 160Combined sources5
Helixi163 – 165Combined sources3
Helixi166 – 191Combined sources26
Turni194 – 196Combined sources3
Helixi199 – 212Combined sources14
Beta strandi216 – 221Combined sources6
Helixi223 – 228Combined sources6
Helixi232 – 238Combined sources7
Beta strandi241 – 243Combined sources3
Beta strandi246 – 253Combined sources8
Beta strandi262 – 272Combined sources11
Helixi284 – 289Combined sources6
Helixi292 – 307Combined sources16
Beta strandi310 – 322Combined sources13
Beta strandi333 – 336Combined sources4
Beta strandi342 – 346Combined sources5
Helixi352 – 363Combined sources12
Helixi364 – 366Combined sources3
Beta strandi369 – 375Combined sources7
Helixi379 – 385Combined sources7
Turni386 – 388Combined sources3
Beta strandi389 – 395Combined sources7
Helixi397 – 410Combined sources14
Beta strandi414 – 416Combined sources3
Helixi421 – 424Combined sources4
Helixi425 – 427Combined sources3
Beta strandi430 – 436Combined sources7
Beta strandi440 – 442Combined sources3
Helixi443 – 452Combined sources10
Beta strandi460 – 464Combined sources5
Turni466 – 468Combined sources3
Beta strandi469 – 471Combined sources3
Helixi484 – 495Combined sources12

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
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

CDDicd00433. Peptidase_M17. 1 hit.
HAMAPiMF_00181. Cytosol_peptidase_M17. 1 hit.
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
PDB 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.
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

CDDicd00433. Peptidase_M17. 1 hit.
HAMAPiMF_00181. Cytosol_peptidase_M17. 1 hit.
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...

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: November 2, 2016
This is version 88 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.