Reviewed,
UniProtKB/Swiss-Prot P0C2D4 (OXLA_NAJKA)
Last modified
November 4, 2008.
Version 10.
History...
Clusters with 100%,
90%,
50% identity |
Documents (1) |
Third-party data |
Customize display | text xml rdf/xml gff fasta |
Names and origin
| Protein names | Recommended name: L-amino-acid oxidase EC=1.4.3.2 Alternative name(s): K-LAO LAAO Short name=LAO |
| Organism | Naja kaouthia (Monocled cobra) (Naja siamensis) |
| Taxonomic identifier | 8649 [NCBI] |
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Lepidosauria › Squamata › Scleroglossa › Serpentes › Colubroidea › Elapidae › Elapinae › Naja |
Protein attributes
| Sequence length | 38 AA. |
| Sequence status | Fragment. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | Catalyzes an oxidative deamination of predominantly hydrophobic and aromatic L-amino acids. Is very active against L-Phe and L-Tyr, moderately active against L-Trp, L-Met, L-Leu, and L-Arg. Inhibits both agonist- and shear stress-induced platelet aggregation (SIPA) dose-dependently through the formation of hydrogen peroxide (H(2)O(2)). May induce apoptosis and hemorrhage. May have an antibacterial activity. |
| 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 | |
| Tissue specificity | Expressed by the venom gland. |
| Post-translational modification | Glycosylated By similarity. |
| Sequence similarities | Belongs to the flavin monoamine oxidase family. FIG1 subfamily. |
| Biophysicochemical properties | pH dependence: Optimum pH is 8.5, unlike many other venom L-amino acid oxidase, is also stable in alkaline medium. |
Ontologies
Keywords | |
|---|---|
| Biological process | Apoptosis Blood coagulation |
| Cellular component | Secreted |
| Ligand | FAD Flavoprotein |
| Molecular function | Antibiotic Antimicrobial Oxidoreductase Toxin |
| PTM | Glycoprotein |
| Technical term | Direct protein sequencing |
Gene Ontology (GO) | |
| Biological process | apoptosis Inferred from electronic annotation. Source: UniProtKB-KW blood coagulationInferred from electronic annotation. Source: UniProtKB-KW defense response to bacteriumInferred from electronic annotation. Source: UniProtKB-KW oxidation reductionInferred from electronic annotation. Source: UniProtKB-KW pathogenesisInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | extracellular region Inferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | L-amino-acid oxidase activity Inferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
Sequences
References
| [1] | "Inhibition of human platelet aggregation by L-amino acid oxidase purified from Naja naja kaouthia venom." Sakurai Y., Takatsuka H., Yoshioka A., Matsui T., Suzuki M., Titani K., Fujimura Y. Toxicon 39:1827-1833(2001) [PubMed: 11600144] [Abstract] Cited for: PROTEIN SEQUENCE. Tissue: Venom. |
| [2] | "Purification and properties of the L-amino acid oxidase from monocellate cobra (Naja naja kaouthia) venom." Tan N.-H., Swaminathan S. Int. J. Biochem. 24:967-973(1992) [PubMed: 1612186] [Abstract] Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT. Tissue: Venom. |
Cross-references
Entry information
| Entry name | OXLA_NAJKA | ||||||||
| Accession | Primary (citable) accession number: P0C2D4 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | Tox-Prot (Toxin Annotation Project) | ||||||||

Clusters with


