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L-amino-acid oxidase

Bothrops alternatus (Urutu) (Rhinocerophis alternatus)
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli


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.


FADBy similarity

GO - Molecular functioni

GO - Biological processi


Molecular functionAntibiotic, Antimicrobial, Hemorrhagic toxin, Hemostasis impairing toxin, Oxidoreductase, Platelet aggregation activating toxin, Toxin
Biological processApoptosis, Cytolysis, Hemolysis
LigandFAD, Flavoprotein

Names & Taxonomyi

Protein namesi
Recommended name:
L-amino-acid oxidase (EC:
Short name:
Short name:
Short name:
OrganismiBothrops alternatus (Urutu) (Rhinocerophis alternatus)
Taxonomic identifieri64174 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiLepidosauriaSquamataBifurcataUnidentataEpisquamataToxicoferaSerpentesColubroideaViperidaeCrotalinaeBothrops

Subcellular locationi

GO - Cellular componenti

Keywords - Cellular componenti


PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004125931 – ›18L-amino-acid oxidaseAdd BLAST›18

Post-translational modificationi

Contains 2 disulfide bonds.By similarity
N-glycosylated (Probable). The enzymatic activity is not affected by deglycosylation.Curated1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein


Tissue specificityi

Expressed by the venom gland.1 Publication


Subunit structurei

Homodimer; non-covalently linked.1 Publication

Family & Domainsi

Sequence similaritiesi


Sequence statusi: Fragment.

P0DI86-1 [UniParc]FASTAAdd to basket

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Mass (Da):2,195
Last modified:September 21, 2011 - v1

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Non-terminal residuei181

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.

Entry informationi

Entry nameiOXLA_BOTAL
AccessioniPrimary (citable) accession number: P0DI86
Entry historyiIntegrated into UniProtKB/Swiss-Prot: September 21, 2011
Last sequence update: September 21, 2011
Last modified: January 7, 2015
This is version 16 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
Annotation programAnimal Toxin Annotation Program



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


  1. SIMILARITY comments
    Index of protein domains and families