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P0CJ40 (OXLA_BOTMA) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 12. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
L-amino-acid oxidase

Short name=BmarLAAO
Short name=LAAO
Short name=LAO
EC=1.4.3.2
OrganismBothrops marajoensis (Marajo lancehead)
Taxonomic identifier157554 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiLepidosauriaSquamataBifurcataUnidentataEpisquamataToxicoferaSerpentesColubroideaViperidaeCrotalinaeBothrops

Protein attributes

Sequence length39 AA.
Sequence statusFragment.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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, apoptosis of vascular endothelial cells or tumor cell lines, and antiparasitic activities, as well as regulation 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 By similarity. In addition, this protein inhibits dose-dependently the growth of Gram-positive, Gram-negative bacteria and yeast, probably by the generation of hydrogen peroxide. Ref.1

Catalytic activity

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

Cofactor

FAD By similarity.

Subunit structure

Monomer. This is in contrast with most of its orthologs, that are non-covalently linked homodimers. Ref.1

Subcellular location

Secreted.

Tissue specificity

Expressed by the venom gland.

Post-translational modification

N-glycosylated By similarity.

Miscellaneous

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

Sequence similarities

Belongs to the flavin monoamine oxidase family. FIG1 subfamily.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – ›39›39L-amino-acid oxidase
PRO_0000412597

Amino acid modifications

Disulfide bond10 ↔ ?

Experimental info

Non-terminal residue391

Sequences

Sequence LengthMass (Da)Tools
P0CJ40 [UniParc].

Last modified September 21, 2011. Version 1.
Checksum: 5A9BBD388988C742

FASTA394,405
        10         20         30 
AHDGNPLEEC FREDDEEFFL EIAKNGLTAT SNPKRVVIV 

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References

[1]"Antibacterial and antiparasitic effects of Bothrops marajoensis venom and its fractions: phospholipase A2 and L-amino acid oxidase."
Costa Torres A.F., Dantas R.T., Toyama M.H., Diz Filho E., Zara F.J., Rodrigues de Queiroz M.G., Pinto Nogueira N.A., Rosa de Oliveira M., de Oliveira Toyama D., Monteiro H.S.A., Martins A.M.C.
Toxicon 55:795-804(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE, FUNCTION, SUBUNIT.
Tissue: Venom.

Cross-references

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

ProtoNetSearch...

Entry information

Entry nameOXLA_BOTMA
AccessionPrimary (citable) accession number: P0CJ40
Entry history
Integrated into UniProtKB/Swiss-Prot: September 21, 2011
Last sequence update: September 21, 2011
Last modified: February 19, 2014
This is version 12 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programAnimal Toxin Annotation Program
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families