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P0DI86 (OXLA_BOTAL) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 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=Balt-LAAO-I
Short name=LAAO
Short name=LAO
EC=1.4.3.2
OrganismBothrops alternatus (Urutu) (Rhinocerophis alternatus)
Taxonomic identifier64174 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiLepidosauriaSquamataBifurcataUnidentataEpisquamataToxicoferaSerpentesColubroideaViperidaeCrotalinaeBothrops

Protein attributes

Sequence length18 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 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. Ref.1

Catalytic activity

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

Cofactor

FAD By similarity.

Subunit structure

Homodimer; non-covalently linked. Ref.1

Subcellular location

Secreted Ref.1.

Tissue specificity

Expressed by the venom gland. Ref.1

Post-translational modification

Contains 2 disulfide bonds By similarity.

N-glycosylated Probable. The enzymatic activity is not affected by deglycosylation. Ref.1

Sequence similarities

Belongs to the flavin monoamine oxidase family. FIG1 subfamily.

Caution

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – ›18›18L-amino-acid oxidase
PRO_0000412593

Experimental info

Non-terminal residue181

Sequences

Sequence LengthMass (Da)Tools
P0DI86 [UniParc].

Last modified September 21, 2011. Version 1.
Checksum: CA5F483463FD1ADC

FASTA182,195
        10 
ADVRNPLEEF RETDYEVL 

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References

[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.

Cross-references

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

ProtoNetSearch...

Entry information

Entry nameOXLA_BOTAL
AccessionPrimary (citable) accession number: P0DI86
Entry history
Integrated into UniProtKB/Swiss-Prot: September 21, 2011
Last sequence update: September 21, 2011
Last modified: April 16, 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