Reviewed,
UniProtKB/Swiss-Prot Q6TGQ9 (OXLA_BOTJR)
Last modified
June 16, 2009.
Version 31.
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 | Bothrops jararacussu (Jararacussu) |
| Taxonomic identifier | 8726 [NCBI] |
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Lepidosauria › Squamata › Scleroglossa › Serpentes › Colubroidea › Viperidae › Crotalinae › Bothrops |
Protein attributes
| Sequence length | 497 AA. |
| Sequence status | Fragment. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at transcript level. |
General annotation (Comments)
| Function | Catalyzes an oxidative deamination of predominantly hydrophobic and aromatic L-amino acids. Inhibits platelet aggregation. Has an ability to induce apoptosis and hemorrhage. Has an antibacterial activity By similarity. |
| Catalytic activity | An L-amino acid + H2O + O2 = a 2-oxo acid + NH3 + H2O2. |
| Cofactor | FAD By similarity. |
| Subunit structure | Homodimer By similarity. |
| Subcellular location | Secreted By similarity. |
| 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 |
| Domain | Signal |
| Ligand | FAD Flavoprotein |
| Molecular function | Antibiotic Antimicrobial Oxidoreductase Toxin |
| PTM | Disulfide bond Glycoprotein |
| 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 electron carrier activityInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||
Molecule processing | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – 13 | 13 | By similarity | ||||||||
| Chain | 14 – ›497 | ›484 | L-amino-acid oxidase | PRO_0000273564 | |||||||
Regions | |||||||||||
| Nucleotide binding | 102 – 103 | 2 | FAD By similarity | ||||||||
| Nucleotide binding | 479 – 482 | 4 | FAD By similarity | ||||||||
Sites | |||||||||||
| Binding site | 57 | 1 | FAD By similarity | ||||||||
| Binding site | 76 | 1 | FAD By similarity | ||||||||
| Binding site | 103 | 1 | Substrate By similarity | ||||||||
| Binding site | 236 | 1 | Substrate By similarity | ||||||||
| Binding site | 274 | 1 | FAD; via amide nitrogen and carbonyl oxygen By similarity | ||||||||
| Binding site | 385 | 1 | Substrate By similarity | ||||||||
| Binding site | 470 | 1 | FAD By similarity | ||||||||
Amino acid modifications | |||||||||||
| Glycosylation | 185 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Disulfide bond | 23 ↔ 186 | By similarity | |||||||||
| Disulfide bond | 344 ↔ 425 | By similarity | |||||||||
Experimental info | |||||||||||
| Non-terminal residue | 497 | 1 | |||||||||
Sequences
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References
| [1] | "Structural and functional characterization of L-amino acid oxidase from Bothrops jararacussu snake venom." Soares A.M., Kashima S., Roberto P.G., Astolfi-Filho S., Pereira J.O., Giglio J.R., Franca S.C. Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Venom gland. |
Cross-references
Sequence databases | |
|---|---|
| AY398691 mRNA. Translation: AAR31182.1. | |
3D structure databases | |
| SMR | Q6TGQ9. Positions 17-497. |
| ModBase | Search... |
Phylogenomic databases | |
| HOVERGEN | Q6TGQ9. |
Enzyme and pathway databases | |
| BRENDA | 1.4.3.2. 274601. |
Family and domain databases | |
| InterPro | IPR001613. Amineoxid_fl. IPR002937. Amino_oxidase. [Graphical view] |
| Pfam | PF01593. Amino_oxidase. 1 hit. [Graphical view] |
| PRINTS | PR00757. AMINEOXDASEF. |
| ProDom | PD000139. FAD_pyr_redox. 1 hit. [Graphical view] [Entries sharing at least one domain] |
| ProtoNet | Search... |
Entry information
| Entry name | OXLA_BOTJR | ||||||||
| Accession | Primary (citable) accession number: Q6TGQ9 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | Tox-Prot (Toxin Annotation Project) | ||||||||

Clusters with


