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Q01693

- AMPX_VIBPR

UniProt

Q01693 - AMPX_VIBPR

Protein

Bacterial leucyl aminopeptidase

Gene
N/A
Organism
Vibrio proteolyticus (Aeromonas proteolytica)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 102 (01 Oct 2014)
      Sequence version 1 (01 Jul 1993)
      Previous versions | rss
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    Functioni

    Catalytic activityi

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

    Cofactori

    Binds 2 zinc 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

    Keywords - Molecular functioni

    Aminopeptidase, Hydrolase, Protease

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    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

    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 – 1197
    Helixi120 – 1223
    Helixi125 – 13612
    Helixi146 – 16318
    Beta strandi164 – 1663
    Beta strandi169 – 1768
    Beta strandi179 – 18810
    Beta strandi191 – 20313
    Turni221 – 2244
    Helixi225 – 24016
    Beta strandi246 – 25510
    Helixi257 – 2593
    Helixi262 – 27312
    Beta strandi277 – 2837
    Beta strandi292 – 2998
    Beta strandi301 – 3033
    Helixi305 – 31814
    Beta strandi324 – 3274
    Helixi336 – 3416
    Beta strandi349 – 3524
    Helixi354 – 3563
    Turni359 – 3624
    Helixi368 – 3703
    Helixi376 – 39419

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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

    MKYTKTLLAM VLSATFCQAY AEDKVWISIG ADANQTVMKS GAESILPNSV    50
    ASSGQVWVGQ VDVAQLAELS HNMHEEHNRC GGYMVHPSAQ SAMAASAMPT 100
    TLASFVMPPI TQQATVTAWL PQVDASQITG TISSLESFTN RFYTTTSGAQ 150
    ASDWIASEWQ ALSASLPNAS VKQVSHSGYN QKSVVMTITG SEAPDEWIVI 200
    GGHLDSTIGS HTNEQSVAPG ADDDASGIAA VTEVIRVLSE NNFQPKRSIA 250
    FMAYAAEEVG LRGSQDLANQ YKSEGKNVVS ALQLDMTNYK GSAQDVVFIT 300
    DYTDSNFTQY LTQLMDEYLP SLTYGFDTCG YACSDHASWH NAGYPAAMPF 350
    ESKFNDYNPR IHTTQDTLAN SDPTGSHAKK FTQLGLAYAI EMGSATGDTP 400
    TPGNQLEDGV PVTDLSGSRG SNVWYTFELE TQKNLQITTS GGYGDLDLYV 450
    KFGSKASKQN WDCRPYLSGN NEVCTFNNAS PGTYSVMLTG YSNYSGASLK 500
    ASTF 504
    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:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z11993 Genomic DNA. Translation: CAA78039.1.
    M85159 Genomic DNA. Translation: AAA21940.1.
    PIRiS24314.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z11993 Genomic DNA. Translation: CAA78039.1 .
    M85159 Genomic DNA. Translation: AAA21940.1 .
    PIRi S24314.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1AMP X-ray 1.80 A 107-397 [» ]
    1CP6 X-ray 1.90 A 107-397 [» ]
    1FT7 X-ray 2.20 A 107-397 [» ]
    1IGB X-ray 2.30 A 107-397 [» ]
    1LOK X-ray 1.20 A 107-397 [» ]
    1RTQ X-ray 0.95 A 107-405 [» ]
    1TXR X-ray 2.00 A 107-405 [» ]
    1XRY X-ray 2.10 A 107-405 [» ]
    2ANP X-ray 1.90 A 107-397 [» ]
    2DEA X-ray 1.24 A 107-405 [» ]
    2IQ6 X-ray 2.00 A 107-397 [» ]
    2NYQ X-ray 2.50 A 107-405 [» ]
    2PRQ X-ray 2.15 A 107-397 [» ]
    3B35 X-ray 1.10 A 107-397 [» ]
    3B3C X-ray 1.46 A 107-397 [» ]
    3B3S X-ray 1.18 A 107-397 [» ]
    3B3T X-ray 1.17 A 107-397 [» ]
    3B3V X-ray 1.22 A 107-397 [» ]
    3B3W X-ray 1.75 A 107-397 [» ]
    3B7I X-ray 1.75 A 107-397 [» ]
    3FH4 X-ray 1.95 A 107-405 [» ]
    3VH9 X-ray 1.29 A 107-405 [» ]
    ProteinModelPortali Q01693.
    SMRi Q01693. Positions 107-397.
    ModBasei Search...
    MobiDBi Search...

    Chemistry

    BindingDBi Q01693.
    ChEMBLi CHEMBL3750.

    Protein family/group databases

    MEROPSi M28.002.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    SABIO-RK Q01693.

    Miscellaneous databases

    EvolutionaryTracei Q01693.
    PMAP-CutDB Q01693.

    Family and domain databases

    InterProi IPR012189. Pept_M28E_Ap1.
    IPR007280. Peptidase_C_arc/bac.
    IPR007484. Peptidase_M28.
    [Graphical view ]
    Pfami PF04389. Peptidase_M28. 1 hit.
    PF04151. PPC. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF036685. BacLeuNPeptidase. 1 hit.
    ProtoNeti Search...

    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(1992) [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(1992) [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(1992) [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(1994) [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(1996) [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(1999) [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(2001) [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: October 1, 2014
    This is version 102 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