Reviewed,
UniProtKB/Swiss-Prot P0C2D7 (OXLA_VIPBB)
Last modified
June 16, 2009.
Version 11.
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 EC=1.4.3.2 |
| Organism | Vipera berus berus (Common viper) |
| Taxonomic identifier | 31156 [NCBI] |
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Lepidosauria › Squamata › Scleroglossa › Serpentes › Colubroidea › Viperidae › Viperinae › Vipera |
Protein attributes
| Sequence length | 88 AA. |
| Sequence status | Fragments. |
| 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 (the most specific substrate is L-Phe, followed by L-Met, L-Leu, L-Phe, L-Ile, L-Arg and L-His). Inhibits both ADP-induced platelet aggregation dose-dependently. Has an ability to induce apoptosis in cultured HeLa and K562 cells. May have an ability to 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 | |
| Tissue specificity | Expressed by the venom gland. |
| Post-translational modification | Glycosylated By similarity. |
| Sequence similarities | Belongs to the flavin monoamine oxidase family. FIG1 subfamily. |
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)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – ›88 | ›88 | L-amino-acid oxidase | PRO_0000273573 | |||||
Regions | |||||||||
| Nucleotide binding | 83 – 86 | 4 | FAD By similarity | ||||||
Sites | |||||||||
| Binding site | 74 | 1 | FAD By similarity | ||||||
Experimental info | |||||||||
| Non-adjacent residues | 37 – 38 | 2 | |||||||
| Non-adjacent residues | 44 – 45 | 2 | |||||||
| Non-adjacent residues | 52 – 53 | 2 | |||||||
| Non-adjacent residues | 61 – 62 | 2 | |||||||
| Non-adjacent residues | 68 – 69 | 2 | |||||||
| Non-terminal residue | 88 | 1 | |||||||
Sequences
References
| [1] | "Isolation and characterization of an apoptotic and platelet aggregation inhibiting L-amino acid oxidase from Vipera berus berus (common viper) venom." Samel M., Vija H., Ronnholm G., Siigur J., Kalkkinen N., Siigur E. Biochim. Biophys. Acta 1764:707-714(2006) [PubMed: 16574513] [Abstract] Cited for: PROTEIN SEQUENCE, FUNCTION, SUBUNIT. Tissue: Venom. |
Cross-references
Entry information
| Entry name | OXLA_VIPBB | ||||||||
| Accession | Primary (citable) accession number: P0C2D7 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | Tox-Prot (Toxin Annotation Project) | ||||||||

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