Reviewed,
UniProtKB/Swiss-Prot P0C2D2 (OXLA_CRODC)
Last modified
June 16, 2009.
Version 16.
History...
Clusters with 100%,
90%,
50% identity |
 Documents (1) |
 Third-party data |
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Names and origin
| Protein names | Recommended name: L-amino-acid oxidase Short name=LAAO Short name=LAO Short name=Casca LAO EC=1.4.3.2 |
| Organism | Crotalus durissus cascavella (Northeastern Brazilian rattlesnake) |
| Taxonomic identifier | 184540 [NCBI] |
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Lepidosauria › Squamata › Scleroglossa › Serpentes › Colubroidea › Viperidae › Crotalinae › Crotalus |
Protein attributes
| Sequence length | 61 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. Induces a dose-dependent platelet aggregation. Has an ability to induce apoptosis. Has an antibacterial activity against both Gram-negative and Gram-positive bacteria. Has high antileishmanic activity against the promastigote of Leishmania amazonensis in vitro. May have an ability to induce hemorrhage. Ref.1 |
| Catalytic activity | An L-amino acid + H2O + O2 = a 2-oxo acid + NH3 + H2O2. |
| Cofactor | FAD. |
| Subunit structure | Homodimer. Ref.1 |
| 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 | Kinetic parameters: KM=46.7 µM for L-Leu pH dependence: Optimum pH is 6.5. |
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-SubCell |
| Molecular function | L-amino-acid oxidase activity Inferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
Sequences
References
| [1] | "Isolation of a new L-amino acid oxidase from Crotalus durissus cascavella venom." Toyama M.H., Toyama Dde O., Passero L.F., Laurenti M.D., Corbett C.E., Tomokane T.Y., Fonseca F.V., Antunes E., Joazeiro P.P., Beriam L.O., Martins M.A., Monteiro H.S., Fonteles M.C. Toxicon 47:47-57(2006) [PubMed: 16307769] [Abstract] Cited for: PROTEIN SEQUENCE, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT. Tissue: Venom. |
Cross-references
3D structure databases | |
|---|---|
| SMR | P0C2D2. Positions 3-61. |
| ModBase | Search... |
Phylogenomic databases | |
| HOVERGEN | P0C2D2. |
Enzyme and pathway databases | |
| BRENDA | 1.4.3.2. 274610. |
Family and domain databases | |
| InterPro | IPR006076. FAD-dep_OxRdtase. [Graphical view] |
| Pfam | PF01266. DAO. 1 hit. [Graphical view] |
| ProDom | PD000139. FAD_pyr_redox. 1 hit. [Graphical view] [Entries sharing at least one domain] |
| ProtoNet | Search... |
Entry information
| Entry name | OXLA_CRODC | ||||||||
| Accession | Primary (citable) accession number: P0C2D2 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | Tox-Prot (Toxin Annotation Project) | ||||||||
