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Reviewed, UniProtKB/Swiss-Prot P0C2D3 (OXLA_ERIMA)

Last modified June 16, 2009. Version 14. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    L-amino-acid oxidase
      Short name=LAAO
      Short name=LAO
    EC=1.4.3.2
OrganismEristocophis macmahoni (Leaf-nosed viper)
Taxonomic identifier8702 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiLepidosauriaSquamataScleroglossaSerpentesColubroideaViperidaeViperinaeEristocophis

Protein attributes

Sequence length27 AA.
Sequence statusFragment.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Catalyzes an oxidative deamination of predominantly hydrophobic and aromatic L-amino acids. Induces edema and platelet aggregation. Has a potent hemolytic activity. Has an ability to induce apoptosis. Unlike other snake venom L-amino acid oxidases, does not induce hemorrhage. May have an antibacterial activity. Ref.1

Catalytic activity

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

Cofactor

FAD By similarity.

Subunit structure

Homodimer. Ref.1

Subcellular location

Secreted.

Tissue specificity

Expressed by the venom gland.

Post-translational modification

Glycosylated By similarity.

Sequence similarities

Belongs to the flavin monoamine oxidase family. FIG1 subfamily.

Mass spectrometry

Molecular mass is 58734.0 Da from positions 1 - ?. Determined by MALDI. Ref.1

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – ›27›27L-amino-acid oxidase
PRO_0000273568

Experimental info

Non-terminal residue271

Sequences

Sequence LengthMass (Da)Tools
P0C2D3-1 [UniParc].

Last modified January 23, 2007. Version 1.
Checksum: 18DBFD66E0655CE7

FASTA273,097
        10         20 
ADDKNPLEEA FREADYEVFL EIAKNGL 

« Hide

References

[1]"Isolation, structural, and functional characterization of an apoptosis-inducing L-amino acid oxidase from leaf-nosed viper (Eristocophis macmahoni) snake venom."
Ali S.A., Stoeva S., Abbasi A., Alam J.M., Kayed R., Faigle M., Neumeister B., Voelter W.
Arch. Biochem. Biophys. 384:216-226(2000) [PubMed: 11368308] [Abstract]
Cited for: PROTEIN SEQUENCE, FUNCTION, SUBUNIT, MASS SPECTROMETRY.
Tissue: Venom.

Cross-references

3D structure databases

ModBaseSearch...

Phylogenomic databases

HOVERGENP0C2D3.

Enzyme and pathway databases

BRENDA1.4.3.2. 279510.

Family and domain databases

ProtoNetSearch...

Entry information

Entry nameOXLA_ERIMA
AccessionPrimary (citable) accession number: P0C2D3
Entry history
Integrated into UniProtKB/Swiss-Prot: January 23, 2007
Last sequence update: January 23, 2007
Last modified: June 16, 2009
This is version 14 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectTox-Prot (Toxin Annotation Project)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents