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Protein

Bacterial leucyl aminopeptidase

Gene
N/A
Organism
Vibrio proteolyticus (Aeromonas proteolytica)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Cofactori

Zn2+Note: Binds 2 Zn2+ ions per subunit.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi203 – 2031Zinc 1
Metal bindingi223 – 2231Zinc 1
Metal bindingi223 – 2231Zinc 2; catalytic
Metal bindingi258 – 2581Zinc 2; catalytic
Metal bindingi285 – 2851Zinc 1
Metal bindingi362 – 3621Zinc 2; catalytic

GO - Molecular functioni

  1. aminopeptidase activity Source: UniProtKB-KW
  2. metal ion binding Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Aminopeptidase, Hydrolase, Protease

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BRENDAi3.4.11.10. 167.
SABIO-RKQ01693.

Protein family/group databases

MEROPSiM28.002.

Names & Taxonomyi

Protein namesi
Recommended name:
Bacterial leucyl aminopeptidase (EC:3.4.11.10)
OrganismiVibrio proteolyticus (Aeromonas proteolytica)
Taxonomic identifieri671 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaVibrionalesVibrionaceaeVibrio

Subcellular locationi

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2121Sequence AnalysisAdd
BLAST
Propeptidei22 – 10685Sequence AnalysisPRO_0000026849Add
BLAST
Chaini107 – 405299Bacterial leucyl aminopeptidasePRO_0000026850Add
BLAST
Propeptidei406 – 50499Removed in mature formSequence AnalysisPRO_0000026851Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi329 ↔ 333

Keywords - PTMi

Disulfide bond, Zymogen

Miscellaneous databases

PMAP-CutDBQ01693.

Interactioni

Structurei

Secondary structure

1
504
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi113 – 1197Combined sources
Helixi120 – 1223Combined sources
Helixi125 – 13612Combined sources
Helixi146 – 16318Combined sources
Beta strandi164 – 1663Combined sources
Beta strandi169 – 1768Combined sources
Beta strandi179 – 18810Combined sources
Beta strandi191 – 20313Combined sources
Turni221 – 2244Combined sources
Helixi225 – 24016Combined sources
Beta strandi246 – 25510Combined sources
Helixi257 – 2593Combined sources
Helixi262 – 27312Combined sources
Beta strandi277 – 2837Combined sources
Beta strandi292 – 2998Combined sources
Beta strandi301 – 3033Combined sources
Helixi305 – 31814Combined sources
Beta strandi324 – 3274Combined sources
Helixi336 – 3416Combined sources
Beta strandi349 – 3524Combined sources
Helixi354 – 3563Combined sources
Turni359 – 3624Combined sources
Helixi368 – 3703Combined sources
Helixi376 – 39419Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AMPX-ray1.80A107-397[»]
1CP6X-ray1.90A107-397[»]
1FT7X-ray2.20A107-397[»]
1IGBX-ray2.30A107-397[»]
1LOKX-ray1.20A107-397[»]
1RTQX-ray0.95A107-405[»]
1TXRX-ray2.00A107-405[»]
1XRYX-ray2.10A107-405[»]
2ANPX-ray1.90A107-397[»]
2DEAX-ray1.24A107-405[»]
2IQ6X-ray2.00A107-397[»]
2NYQX-ray2.50A107-405[»]
2PRQX-ray2.15A107-397[»]
3B35X-ray1.10A107-397[»]
3B3CX-ray1.46A107-397[»]
3B3SX-ray1.18A107-397[»]
3B3TX-ray1.17A107-397[»]
3B3VX-ray1.22A107-397[»]
3B3WX-ray1.75A107-397[»]
3B7IX-ray1.75A107-397[»]
3FH4X-ray1.95A107-405[»]
3VH9X-ray1.29A107-405[»]
ProteinModelPortaliQ01693.
SMRiQ01693. Positions 107-397.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ01693.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase M28 family. M28E subfamily.Curated

Keywords - Domaini

Signal

Family and domain databases

InterProiIPR012189. Pept_M28E_Ap1.
IPR007280. Peptidase_C_arc/bac.
IPR007484. Peptidase_M28.
[Graphical view]
PfamiPF04389. Peptidase_M28. 1 hit.
PF04151. PPC. 1 hit.
[Graphical view]
PIRSFiPIRSF036685. BacLeuNPeptidase. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q01693-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKYTKTLLAM VLSATFCQAY AEDKVWISIG ADANQTVMKS GAESILPNSV
60 70 80 90 100
ASSGQVWVGQ VDVAQLAELS HNMHEEHNRC GGYMVHPSAQ SAMAASAMPT
110 120 130 140 150
TLASFVMPPI TQQATVTAWL PQVDASQITG TISSLESFTN RFYTTTSGAQ
160 170 180 190 200
ASDWIASEWQ ALSASLPNAS VKQVSHSGYN QKSVVMTITG SEAPDEWIVI
210 220 230 240 250
GGHLDSTIGS HTNEQSVAPG ADDDASGIAA VTEVIRVLSE NNFQPKRSIA
260 270 280 290 300
FMAYAAEEVG LRGSQDLANQ YKSEGKNVVS ALQLDMTNYK GSAQDVVFIT
310 320 330 340 350
DYTDSNFTQY LTQLMDEYLP SLTYGFDTCG YACSDHASWH NAGYPAAMPF
360 370 380 390 400
ESKFNDYNPR IHTTQDTLAN SDPTGSHAKK FTQLGLAYAI EMGSATGDTP
410 420 430 440 450
TPGNQLEDGV PVTDLSGSRG SNVWYTFELE TQKNLQITTS GGYGDLDLYV
460 470 480 490 500
KFGSKASKQN WDCRPYLSGN NEVCTFNNAS PGTYSVMLTG YSNYSGASLK

ASTF
Length:504
Mass (Da):54,232
Last modified:July 1, 1993 - v1
Checksum:i7B33317EF6153B48
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti303 – 3042TD → DT AA sequence (PubMed:1627651).Curated
Sequence conflicti306 – 3061N → D AA sequence (PubMed:1627651).Curated
Sequence conflicti312 – 3143TQL → QT AA sequence (PubMed:1627651).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z11993 Genomic DNA. Translation: CAA78039.1.
M85159 Genomic DNA. Translation: AAA21940.1.
PIRiS24314.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z11993 Genomic DNA. Translation: CAA78039.1.
M85159 Genomic DNA. Translation: AAA21940.1.
PIRiS24314.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AMPX-ray1.80A107-397[»]
1CP6X-ray1.90A107-397[»]
1FT7X-ray2.20A107-397[»]
1IGBX-ray2.30A107-397[»]
1LOKX-ray1.20A107-397[»]
1RTQX-ray0.95A107-405[»]
1TXRX-ray2.00A107-405[»]
1XRYX-ray2.10A107-405[»]
2ANPX-ray1.90A107-397[»]
2DEAX-ray1.24A107-405[»]
2IQ6X-ray2.00A107-397[»]
2NYQX-ray2.50A107-405[»]
2PRQX-ray2.15A107-397[»]
3B35X-ray1.10A107-397[»]
3B3CX-ray1.46A107-397[»]
3B3SX-ray1.18A107-397[»]
3B3TX-ray1.17A107-397[»]
3B3VX-ray1.22A107-397[»]
3B3WX-ray1.75A107-397[»]
3B7IX-ray1.75A107-397[»]
3FH4X-ray1.95A107-405[»]
3VH9X-ray1.29A107-405[»]
ProteinModelPortaliQ01693.
SMRiQ01693. Positions 107-397.
ModBaseiSearch...
MobiDBiSearch...

Chemistry

BindingDBiQ01693.
ChEMBLiCHEMBL3750.

Protein family/group databases

MEROPSiM28.002.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BRENDAi3.4.11.10. 167.
SABIO-RKQ01693.

Miscellaneous databases

EvolutionaryTraceiQ01693.
PMAP-CutDBQ01693.

Family and domain databases

InterProiIPR012189. Pept_M28E_Ap1.
IPR007280. Peptidase_C_arc/bac.
IPR007484. Peptidase_M28.
[Graphical view]
PfamiPF04389. Peptidase_M28. 1 hit.
PF04151. PPC. 1 hit.
[Graphical view]
PIRSFiPIRSF036685. BacLeuNPeptidase. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "Cloning and nucleotide sequence of the Vibrio proteolyticus aminopeptidase gene."
    van Heeke G., Denslow S., Watkins J., Wilson K., Wagner F.
    Biochim. Biophys. Acta 1131:337-340(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 107-136 AND 233-405.
    Strain: ATCC 15338 / DSM 30189 / JCM 21193 / LMG 3772 / NBRC 13287 / NCIMB 1326.
  2. "Isolation of the leucine aminopeptidase gene from Aeromonas proteolytica. Evidence for an enzyme precursor."
    Guenet C., Lepage P., Harris B.A.
    J. Biol. Chem. 267:8390-8395(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 73-504.
  3. "Rapid purification of the Aeromonas proteolytica aminopeptidase: crystallization and preliminary X-ray data."
    Schalk C., Remy J.M., Chevrier B., Moras D., Tarnus C.
    Arch. Biochem. Biophys. 294:91-97(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION, CRYSTALLIZATION.
  4. "Crystal structure of Aeromonas proteolytica aminopeptidase: a prototypical member of the co-catalytic zinc enzyme family."
    Chevrier B., Schalk C., D'Orchymont H., Rondeau J.-M., Moras D., Tarnus C.
    Structure 2:283-290(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 107-396.
  5. "The structure of the Aeromonas proteolytica aminopeptidase complexed with a hydroxamate inhibitor. Involvement in catalysis of Glu151 and two zinc ions of the co-catalytic unit."
    Chevrier B., D'Orchymont H., Schalk C., Tarnus C., Moras D.
    Eur. J. Biochem. 237:393-398(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH INHIBITOR.
  6. "1-butaneboronic acid binding to Aeromonas proteolytica aminopeptidase: a case of arrested development."
    De Paola C.C., Bennett B., Holz R.C., Ringe D., Petsko G.A.
    Biochemistry 38:9048-9053(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF INHIBITOR COMPLEX.
  7. "Inhibition of the aminopeptidase from Aeromonas proteolytica by L-leucinephosphonic acid. Spectroscopic and crystallographic characterization of the transition state of peptide hydrolysis."
    Stamper C., Bennett B., Edwards T., Holz R.C., Ringe D., Petsko G.A.
    Biochemistry 40:7035-7046(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF INHIBITOR COMPLEX.

Entry informationi

Entry nameiAMPX_VIBPR
AccessioniPrimary (citable) accession number: Q01693
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: July 1, 1993
Last modified: April 1, 2015
This is version 106 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, Direct protein sequencing

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

External Data

Dasty 3

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 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.