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Protein

L-amino-acid oxidase

Gene
N/A
Organism
Bothrops pirajai (Piraja's lance head)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

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 edema, antibacterial (E.coli, and P.aeruginosa) and antiparasitic activities, as well as induction of platelet aggregation. 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. This protein may also have activities in hemorrhage, hemolysis, and apoptosis.1 Publication

Catalytic activityi

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

Cofactori

FADBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi42 – 432FADBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

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:
LAAO
Short name:
LAO
Alternative name(s):
BpirLAAO-I
OrganismiBothrops pirajai (Piraja's lance head)
Taxonomic identifieri113192 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiLepidosauriaSquamataBifurcataUnidentataEpisquamataToxicoferaSerpentesColubroideaViperidaeCrotalinaeBothrops

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – ›49›49L-amino-acid oxidasePRO_0000273566Add
BLAST

Post-translational modificationi

Contains 2 disulfide bonds.By similarity
N-glycosylated.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein

Expressioni

Tissue specificityi

Expressed by the venom gland.

Interactioni

Subunit structurei

Homodimer; non-covalently linked.1 Publication

Structurei

3D structure databases

ProteinModelPortaliP0C2D1.
SMRiP0C2D1. Positions 3-49.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Sequencei

Sequence statusi: Fragment.

P0C2D1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40 
ADDKNPLEEF RETNYEVFLE IAKNGLKATS NPKRVVIVGA GMAGLSAAY
Length:49
Mass (Da):5,299
Last modified:January 23, 2007 - v1
Checksum:i5D190816B54BACCA
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei49 – 491

Cross-referencesi

3D structure databases

ProteinModelPortaliP0C2D1.
SMRiP0C2D1. Positions 3-49.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

ProtoNetiSearch...

Publicationsi

  1. "Biochemical and functional characterization of an L-amino acid oxidase isolated from Bothrops pirajai snake venom."
    Izidoro L.F.M., Ribeiro M.C., Souza G.R.L., Sant'Ana C.D., Hamaguchi A., Homsi-Brandeburgo M.I., Goulart L.R., Beleboni R.O., Nomizo A., Sampaio S.V., Soares A.M., Rodrigues V.M.
    Bioorg. Med. Chem. 14:7034-7043(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE, FUNCTION, SUBUNIT, GLYCOSYLATION.
    Tissue: Venom.

Entry informationi

Entry nameiOXLA_BOTPI
AccessioniPrimary (citable) accession number: P0C2D1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 23, 2007
Last sequence update: January 23, 2007
Last modified: January 7, 2015
This is version 37 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

Miscellaneous

Has parasiticidal activities against leishmania, as a result of enzyme-catalyzed hydrogen peroxide production.1 Publication

Keywords - Technical termi

Direct protein sequencing

Documents

  1. 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.