Reviewed,
UniProtKB/Swiss-Prot P0C2D1 (OXLA_BOTPI)
Last modified
September 22, 2009.
Version 18.
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 Short name=LAAO Short name=LAO EC=1.4.3.2 Alternative name(s): BpirLAAO-I |
| Organism | Bothrops pirajai (Piraja's lance head) |
| Taxonomic identifier | 113192 [NCBI] |
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Lepidosauria › Squamata › Scleroglossa › Serpentes › Colubroidea › Viperidae › Crotalinae › Bothrops |
Protein attributes
| Sequence length | 49 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 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. 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 | |
| Tissue specificity | Expressed by the venom gland. |
| Post-translational modification | Glycosylated. Ref.1 |
| Sequence similarities | Belongs to the flavin monoamine oxidase family. FIG1 subfamily. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Apoptosis Blood coagulation Cell cycle |
| 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 cell cycleInferred 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] | "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 | |
|---|---|
| SMR | P0C2D1. Positions 3-49. |
| ModBase | Search... |
Phylogenomic databases | |
| HOVERGEN | P0C2D1. |
Enzyme and pathway databases | |
| BRENDA | 1.4.3.2. 278409. |
Family and domain databases | |
| InterPro | IPR006076. FAD-dep_OxRdtase. [Graphical view] |
| Pfam | PF01266. DAO. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | OXLA_BOTPI | ||||||||
| Accession | Primary (citable) accession number: P0C2D1 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | Tox-Prot (Toxin Annotation Project) | ||||||||

Clusters with


