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Protein

L-amino-acid oxidase

Gene
N/A
Organism
Agkistrodon contortrix laticinctus (Broad-banded copperhead) (Agkistrodon mokasen laticinctus)
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 (L-Ile followed by L-Phe, L-Met, L-Val, L-Arg, L-Leu), thus producing hydrogen peroxide that may contribute to the diverse toxic effects of this enzyme. Exhibits diverse biological activities, such as hemorrhage (minimum hemorrhagic dose of 10 µg), and apoptosis. May also induce hemolysis, edema, antibacterial and antiparasitic activities. May also regulate 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.1 Publication

Catalytic activityi

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

Cofactori

FMN1 Publication

GO - Molecular functioni

  • FMN binding Source: UniProtKB
  • L-amino-acid oxidase activity Source: UniProtKB
  • protein dimerization activity Source: UniProtKB

GO - Biological processi

  • apoptotic process Source: UniProtKB-KW
  • defense response to bacterium Source: UniProtKB-KW
  • hemolysis in other organism Source: UniProtKB-KW
  • killing of cells of other organism Source: UniProtKB
  • oxidation-reduction process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Antibiotic, Antimicrobial, Hemorrhagic toxin, Hemostasis impairing toxin, Oxidoreductase, Toxin

Keywords - Biological processi

Apoptosis, Cytolysis, Hemolysis

Keywords - Ligandi

Flavoprotein, FMN

Names & Taxonomyi

Protein namesi
Recommended name:
L-amino-acid oxidase (EC:1.4.3.2)
Short name:
ACL-LAO
Short name:
LAAO
Short name:
LAO
OrganismiAgkistrodon contortrix laticinctus (Broad-banded copperhead) (Agkistrodon mokasen laticinctus)
Taxonomic identifieri37195 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiLepidosauriaSquamataBifurcataUnidentataEpisquamataToxicoferaSerpentesColubroideaViperidaeCrotalinaeAgkistrodon

Subcellular locationi

GO - Cellular componenti

  • extracellular region Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – ›19›19L-amino-acid oxidasePRO_0000390926Add
BLAST

Post-translational modificationi

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

Keywords - PTMi

Disulfide bond, Glycoprotein

Expressioni

Tissue specificityi

Expressed by the venom gland.1 Publication

Interactioni

Subunit structurei

Homodimer; non-covalently linked.By similarity

Family & Domainsi

Sequence similaritiesi

Sequencei

Sequence statusi: Fragment.

P0CC16-1 [UniParc]FASTAAdd to basket

« Hide

        10 
ADSRNPLEEE FRETNYEEF
Length:19
Mass (Da):2,375
Last modified:January 19, 2010 - v1
Checksum:iC1D709886B68E7B5
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei19 – 191

Cross-referencesi

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

ProtoNetiSearch...

Publicationsi

  1. "Isolation and structural characterization of a cytotoxic L-amino acid oxidase from Agkistrodon contortrix laticinctus snake venom: preliminary crystallographic data."
    Souza D.H.F., Eugenio L.M., Fletcher J.E., Jiang M.-S., Garratt R.C., Oliva G., Selistre-de-Araujo H.S.
    Arch. Biochem. Biophys. 368:285-290(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    Tissue: Venom.

Entry informationi

Entry nameiOXLA_AGKCL
AccessioniPrimary (citable) accession number: P0CC16
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 19, 2010
Last sequence update: January 19, 2010
Last modified: November 26, 2014
This is version 21 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

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.