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B3EWI9

- OXLA_BOTMT

UniProt

B3EWI9 - OXLA_BOTMT

Protein

L-amino-acid oxidase

Gene
N/A
Organism
Bothrops matogrossensis (Pitviper) (Bothrops neuwiedi matogrossensis)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
  1. Functioni

    Catalyzes an oxidative deamination of predominantly hydrophobic and aromatic L-amino acids, thus producing hydrogen peroxide that may contribute to the diverse toxic effects of this enzyme. Exhibits diverse biological activities, such as hemorrhage, hemolysis, edema, antibacterial and antiparasitic activities, as well as regulation of platelet aggregation. Its effect on platelets is controversial, since it either induces aggregation or inhibits agonist-induced aggregation. These different effects are probably due to different experimental conditions By similarity. Inhibits growth of B.subtilis strain ATCC 6633 (MIC=32 µM), E.faecalis strain ATCC 12953 (MIC=32 µM), S.aureus strain ATCC 29213 (MIC=32 µM), S.pyogenes strain ATCC 19615 (MIC=8 µM), E.coli strain ATCC 8739 (MIC=4 µM), K.pneumoniae strain ATCC 13885 (MIC=2 µM), P.mirabilis strain ATCC 25933 (MIC=2 µM), P.aeruginosa strain ATCC 15442 (MIC=8 µM) and S.typhimurium strain ATCC 14028 (MIC=8 µM).By similarity1 Publication

    Catalytic activityi

    An L-amino acid + H2O + O2 = a 2-oxo acid + NH3 + H2O2.1 Publication

    Cofactori

    FAD.By similarity

    GO - Molecular functioni

    1. L-amino-acid oxidase activity Source: UniProtKB-EC

    GO - Biological processi

    1. apoptotic process Source: UniProtKB-KW
    2. defense response to bacterium Source: UniProtKB-KW
    3. hemolysis in other organism Source: UniProtKB-KW

    Keywords - Molecular functioni

    Antibiotic, Antimicrobial, Hemostasis impairing toxin, Oxidoreductase, Toxin

    Keywords - Biological processi

    Apoptosis, Cytolysis, Hemolysis

    Keywords - Ligandi

    FAD, Flavoprotein

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    L-amino-acid oxidase1 Publication (EC:1.4.3.21 Publication)
    Short name:
    Bm-LAO1 Publication
    Short name:
    LAAOBy similarity
    Short name:
    LAOBy similarity
    OrganismiBothrops matogrossensis (Pitviper) (Bothrops neuwiedi matogrossensis)
    Taxonomic identifieri1171125 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiLepidosauriaSquamataBifurcataUnidentataEpisquamataToxicoferaSerpentesColubroideaViperidaeCrotalinaeBothrops

    Subcellular locationi

    Secreted 1 Publication

    GO - Cellular componenti

    1. extracellular region Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini‹1 – ›31›31L-amino-acid oxidasePRO_0000417918Add
    BLAST

    Post-translational modificationi

    N-glycosylated.By similarity

    Expressioni

    Tissue specificityi

    Expressed by the venom gland.1 Publication

    Interactioni

    Subunit structurei

    Homodimer; non-covalently linked.By similarity

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the flavin monoamine oxidase family. FIG1 subfamily.Sequence Analysis

    Sequencei

    Sequence statusi: Fragments.

    B3EWI9-1 [UniParc]FASTAAdd to Basket

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    IKFEPPLPPK KAHKKFWEDD GIYYPPNHNF P                       31
    Length:31
    Mass (Da):3,751
    Last modified:June 13, 2012 - v1
    Checksum:i778F60FA5F08EB99
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Non-terminal residuei1 – 111 Publication
    Non-adjacent residuesi13 – 1421 Publication
    Non-adjacent residuesi21 – 2221 Publication
    Non-terminal residuei31 – 3111 Publication

    Cross-referencesi

    3D structure databases

    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Family and domain databases

    ProtoNeti Search...

    Publicationsi

    1. "Evaluation of an antimicrobial L-amino acid oxidase and peptide derivatives from Bothropoides mattogrosensis pitviper venom."
      Okubo B.M., Silva O.N., Migliolo L., Gomes D.G., Porto W.F., Batista C.L., Ramos C.S., Holanda H.H., Dias S.C., Franco O.L., Moreno S.E.
      PLoS ONE 7:E33639-E33639(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION.
      Tissue: Venom1 Publication.

    Entry informationi

    Entry nameiOXLA_BOTMT
    AccessioniPrimary (citable) accession number: B3EWI9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 13, 2012
    Last sequence update: June 13, 2012
    Last modified: October 1, 2014
    This is version 9 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    Annotation programAnimal Toxin Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Direct protein sequencing

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3