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P0DI86

- OXLA_BOTAL

UniProt

P0DI86 - OXLA_BOTAL

Protein

L-amino-acid oxidase

Gene
N/A
Organism
Bothrops alternatus (Urutu) (Rhinocerophis alternatus)
Status
Reviewed - Annotation score: 4 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 slight hemorrhage, induction of platelet aggregation, edema in the mouse paw and bactericidal activity against both Gram-positive (S.aureus) and Gram-negative (E.coli) bacteria. May also induce hemolysis, apoptosis of vascular endothelial cells or tumor cell lines, and may have antiparasitic activities. Effects of snake L-amino oxidases on platelets are controversial, since they either induce aggregation or inhibit agonist-induced aggregation. These different effects are probably due to different experimental conditions.1 Publication

    Catalytic activityi

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

    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, Hemorrhagic toxin, Hemostasis impairing toxin, Oxidoreductase, Platelet aggregation activating toxin, Toxin

    Keywords - Biological processi

    Apoptosis, Cytolysis, Hemolysis

    Keywords - Ligandi

    FAD, Flavoprotein

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    L-amino-acid oxidase (EC:1.4.3.2)
    Short name:
    Balt-LAAO-I
    Short name:
    LAAO
    Short name:
    LAO
    OrganismiBothrops alternatus (Urutu) (Rhinocerophis alternatus)
    Taxonomic identifieri64174 [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
    Chaini1 – ›18›18L-amino-acid oxidasePRO_0000412593Add
    BLAST

    Post-translational modificationi

    Contains 2 disulfide bonds.By similarity
    N-glycosylated Probable. The enzymatic activity is not affected by deglycosylation.1 PublicationCurated

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Expressioni

    Tissue specificityi

    Expressed by the venom gland.1 Publication

    Interactioni

    Subunit structurei

    Homodimer; non-covalently linked.1 Publication

    Family & Domainsi

    Sequence similaritiesi

    Sequencei

    Sequence statusi: Fragment.

    P0DI86-1 [UniParc]FASTAAdd to Basket

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    ADVRNPLEEF RETDYEVL                                      18
    Length:18
    Mass (Da):2,195
    Last modified:September 21, 2011 - v1
    Checksum:iCA5F483463FD1ADC
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Non-terminal residuei18 – 181

    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. "Platelet aggregation and antibacterial effects of an L-amino acid oxidase purified from Bothrops alternatus snake venom."
      Stabeli R.G., Marcussi S., Carlos G.B., Pietro R.C., Selistre-de-Araujo H.S., Giglio J.R., Oliveira E.B., Soares A.M.
      Bioorg. Med. Chem. 12:2881-2886(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE, FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, GLYCOSYLATION.
      Tissue: Venom.

    Entry informationi

    Entry nameiOXLA_BOTAL
    AccessioniPrimary (citable) accession number: P0DI86
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 21, 2011
    Last sequence update: September 21, 2011
    Last modified: October 1, 2014
    This is version 13 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programAnimal Toxin Annotation Program
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Caution

    The existence of several isoforms has been reported that may be due to either different composition or different glycosylation or by the synthesis from different genes.1 Publication

    Keywords - Technical termi

    Direct protein sequencing

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3