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P0C2D6 (OXLA_PROMU) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 28. 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
Short name=TM-LAO
EC=1.4.3.2
OrganismProtobothrops mucrosquamatus (Taiwan habu) (Trimeresurus mucrosquamatus)
Taxonomic identifier103944 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiLepidosauriaSquamataBifurcataUnidentataEpisquamataToxicoferaSerpentesColubroideaViperidaeCrotalinaeProtobothrops

Protein attributes

Sequence length24 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, and antiparasitic activities By similarity. This protein has antibacterial activity (against E.coli, S.aureus, and B.dysenteriae), cytotoxic activity, as well as an ability to induce 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. 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

N-glycosylated By similarity.

Sequence similarities

Belongs to the flavin monoamine oxidase family. FIG1 subfamily.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – ›24›24L-amino-acid oxidase
PRO_0000273571

Amino acid modifications

Disulfide bond10 ↔ ? By similarity

Experimental info

Non-terminal residue241

Sequences

Sequence LengthMass (Da)Tools
P0C2D6 [UniParc].

Last modified January 23, 2007. Version 1.
Checksum: A1D8D75DE753FAA7

FASTA242,931
        10         20 
ADNKNPLEEC FRETNYEEFL EIAR 

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References

[1]"Purification, characterization and biological activity of an L-amino acid oxidase from Trimeresurus mucrosquamatus venom."
Wei J.-F., Wei Q., Lu Q.-M., Tai H., Jin Y., Wang W.-Y., Xiong Y.-L.
Sheng Wu Hua Xue Yu Sheng Wu Wu Li Xue Bao 35:219-224(2003) [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_PROMU
AccessionPrimary (citable) accession number: P0C2D6
Entry history
Integrated into UniProtKB/Swiss-Prot: January 23, 2007
Last sequence update: January 23, 2007
Last modified: February 19, 2014
This is version 28 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