Reviewed,
UniProtKB/Swiss-Prot Q4JHE1 (OXLA_PSEAU)
Last modified
November 25, 2008.
Version 25.
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 |
| Organism | Pseudechis australis (Mulga snake) (King brown snake) |
| Taxonomic identifier | 8670 [NCBI] |
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Lepidosauria › Squamata › Scleroglossa › Serpentes › Colubroidea › Elapidae › Acanthophiinae › Pseudechis |
Protein attributes
| Sequence length | 517 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein 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 By similarity. Has 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. Ref.2 |
| 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 |
| Domain | Signal |
| Ligand | FAD Flavoprotein |
| Molecular function | Antibiotic Antimicrobial Oxidoreductase Toxin |
| PTM | 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-KW |
| 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 – 18 | 18 | By similarity | ||||||||
| Chain | 19 – 517 | 499 | L-amino-acid oxidase | PRO_5000140380 | |||||||
Regions | |||||||||||
| Nucleotide binding | 108 – 109 | 2 | FAD By similarity | ||||||||
| Nucleotide binding | 485 – 488 | 4 | FAD By similarity | ||||||||
Sites | |||||||||||
| Binding site | 82 | 1 | FAD By similarity | ||||||||
| Binding site | 90 | 1 | FAD By similarity | ||||||||
| Binding site | 109 | 1 | Substrate By similarity | ||||||||
| Binding site | 280 | 1 | FAD; via amide nitrogen and carbonyl oxygen By similarity | ||||||||
| Binding site | 391 | 1 | Substrate By similarity | ||||||||
| Binding site | 476 | 1 | FAD By similarity | ||||||||
Amino acid modifications | |||||||||||
| Glycosylation | 191 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Disulfide bond | 29 ↔ 192 | By similarity | |||||||||
| Disulfide bond | 350 ↔ 431 | By similarity | |||||||||
Sequences
| ||||||||||||||||||
References
| [1] | "Identification and analysis of venom gland-specific genes from the coastal taipan (Oxyuranus scutellatus) and related species." St Pierre L., Woods R., Earl S.T.H., Masci P.P., Lavin M.F. Cell. Mol. Life Sci. 62:2679-2693(2005) [PubMed: 16261251] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Venom gland. |
| [2] | "Antibacterial effects of different snake venoms: purification and characterization of antibacterial proteins from Pseudechis australis (Australian king brown or mulga snake) venom." Stiles B.G., Sexton F.W., Weinstein S.A. Toxicon 29:1129-1141(1991) [PubMed: 1796476] [Abstract] Cited for: FUNCTION, SUBUNIT. Tissue: Venom. |
Cross-references
Sequence databases | |
|---|---|
| DQ088992 mRNA. Translation: AAY89682.1. | |
3D structure databases | |
| SMR | Q4JHE1. Positions 23-504. |
| ModBase | Search... |
Phylogenomic databases | |
| HOVERGEN | Q4JHE1. |
Family and domain databases | |
| InterPro | IPR000759. Adrndx_reductase. IPR001613. Amineoxid_fl. IPR002937. Amino_oxidase. [Graphical view] |
| Pfam | PF01593. Amino_oxidase. 1 hit. [Graphical view] |
| PRINTS | PR00419. ADXRDTASE. PR00757. AMINEOXDASEF. |
| ProtoNet | Search... |
Entry information
| Entry name | OXLA_PSEAU | ||||||||
| Accession | Primary (citable) accession number: Q4JHE1 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | Tox-Prot (Toxin Annotation Project) | ||||||||

Clusters with


