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Reviewed, UniProtKB/Swiss-Prot P0C2D1 (OXLA_BOTPI)

Last modified November 4, 2008. 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
    EC=1.4.3.2
Alternative name(s):
    BpirLAAO-I
      Short name=LAAO
      Short name=LAO
OrganismBothrops pirajai (Piraja's lance head)
Taxonomic identifier113192 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiLepidosauriaSquamataScleroglossaSerpentesColubroideaViperidaeCrotalinaeBothrops

Protein attributes

Sequence length49 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 platelet aggregation. Induces mouse paw edema. Has an antibacterial activity against E.coli, and P.aeruginosa. Has cytotoxic activity against Leishmania spp and tumor cells. May have an ability to induce apoptosis and hemorrhage.

Catalytic activity

An L-amino acid + H(2)O + O(2) = a 2-oxo acid + NH(3) + H(2)O(2).

Cofactor

FAD By similarity.

Subunit structure

Homodimer.

Subcellular location

Secreted.

Tissue specificity

Expressed by the venom gland.

Post-translational modification

Glycosylated.

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

Experimental info

Non-terminal residue491

Sequences

Sequence LengthMass (Da)Tools
P0C2D1-1 [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: 16809041] [Abstract]
Cited for: PROTEIN SEQUENCE, FUNCTION, SUBUNIT, GLYCOSYLATION.
Tissue: Venom.

Cross-references

3D structure databases

SMRP0C2D1. Positions 3-49.
ModBaseSearch...

Phylogenomic databases

HOVERGENP0C2D1.

Family and domain databases

InterProIPR006076. FAD-dep_OxRdtase.
[Graphical view]
PfamPF01266. DAO. 1 hit.
[Graphical view]
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: November 4, 2008
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