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P0C2D1 (OXLA_BOTPI) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 33. 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=LAAO
Short name=LAO
EC=1.4.3.2
Alternative name(s):
BpirLAAO-I
OrganismBothrops pirajai (Piraja's lance head)
Taxonomic identifier113192 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiLepidosauriaSquamataBifurcataUnidentataEpisquamataToxicoferaSerpentesColubroideaViperidaeCrotalinaeBothrops

Protein attributes

Sequence length49 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 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. 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.

Tissue specificity

Expressed by the venom gland.

Post-translational modification

Contains 2 disulfide bonds By similarity.

N-glycosylated Probable. Ref.1

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 – ›49›49L-amino-acid oxidase
PRO_0000273566

Regions

Nucleotide binding42 – 432FAD By similarity

Experimental info

Non-terminal residue491

Sequences

Sequence LengthMass (Da)Tools
P0C2D1 [UniParc].

Last modified January 23, 2007. Version 1.
Checksum: 5D190816B54BACCA

FASTA495,299
        10         20         30         40 
ADDKNPLEEF RETNYEVFLE IAKNGLKATS NPKRVVIVGA GMAGLSAAY 

« Hide

References

[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.

Cross-references

3D structure databases

ProteinModelPortalP0C2D1.
SMRP0C2D1. Positions 3-49.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

ProtoNetSearch...

Entry information

Entry nameOXLA_BOTPI
AccessionPrimary (citable) accession number: P0C2D1
Entry history
Integrated into UniProtKB/Swiss-Prot: January 23, 2007
Last sequence update: January 23, 2007
Last modified: February 19, 2014
This is version 33 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
Annotation programAnimal Toxin Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families