Reviewed,
UniProtKB/Swiss-Prot Q6WP39 (OXLA_TRIST)
Last modified
November 25, 2008.
Version 27.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: L-amino-acid oxidase EC=1.4.3.2 Alternative name(s): TSV-LAO LAAO Short name=LAO |
| Organism | Trimeresurus stejnegeri (Chinese green tree viper) |
| Taxonomic identifier | 39682 [NCBI] |
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Lepidosauria › Squamata › Scleroglossa › Serpentes › Colubroidea › Viperidae › Crotalinae › Viridovipera |
Protein attributes
| Sequence length | 516 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. Has an antibacterial activity By similarity. Has cytotoxic activity. Displays dose-dependent inhibition on HIV-1 infection and replication. |
| 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. |
| Subcellular location | SecretedBy similarity. |
| Tissue specificity | Expressed by the venom gland. |
| Post-translational modification | Glycosylated. |
| Sequence similarities | Belongs to the flavin monoamine oxidase family. FIG1 subfamily. |
Ontologies
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||
Molecule processing | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – 18 | 18 | By similarity | ||||||||
| Chain | 19 – 516 | 498 | L-amino-acid oxidase | PRO_0000273572 | |||||||
Regions | |||||||||||
| Nucleotide binding | 107 – 108 | 2 | FAD By similarity | ||||||||
| Nucleotide binding | 484 – 487 | 4 | FAD By similarity | ||||||||
Sites | |||||||||||
| Binding site | 62 | 1 | FAD By similarity | ||||||||
| Binding site | 81 | 1 | FAD By similarity | ||||||||
| Binding site | 89 | 1 | FAD By similarity | ||||||||
| Binding site | 108 | 1 | Substrate By similarity | ||||||||
| Binding site | 241 | 1 | Substrate By similarity | ||||||||
| Binding site | 279 | 1 | FAD; via amide nitrogen and carbonyl oxygen By similarity | ||||||||
| Binding site | 390 | 1 | Substrate By similarity | ||||||||
| Binding site | 475 | 1 | FAD By similarity | ||||||||
Amino acid modifications | |||||||||||
| Glycosylation | 190 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 379 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Disulfide bond | 28 ↔ 191 | By similarity | |||||||||
| Disulfide bond | 349 ↔ 430 | By similarity | |||||||||
Experimental info | |||||||||||
| Sequence conflict | 16 | 1 | G → E in AAQ16182. Ref.2 | ||||||||
| Sequence conflict | 53 | 1 | H → R in AAQ16182. Ref.2 | ||||||||
| Sequence conflict | 73 | 1 | A → T in AAQ16182. Ref.2 | ||||||||
| Sequence conflict | 181 | 1 | K → E in AAQ16182. Ref.2 | ||||||||
| Sequence conflict | 294 | 1 | H → Q in AAQ16182. Ref.2 | ||||||||
| Sequence conflict | 315 | 1 | R → G in AAQ16182. Ref.2 | ||||||||
| Sequence conflict | 354 | 1 | R → W in AAQ16182. Ref.2 | ||||||||
| Sequence conflict | 514 | 1 | D → N in AAQ16182. Ref.2 | ||||||||
Sequences
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References
| [1] | "Molecular characterization of Trimeresurus stejnegeri venom L-amino acid oxidase with potential anti-HIV activity." Zhang Y.-J., Wang J.-H., Lee W.-H., Wang Q., Liu H., Zheng Y.-T., Zhang Y. Biochem. Biophys. Res. Commun. 309:598-604(2003) [PubMed: 12963032] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBUNIT, GLYCOSYLATION, MASS SPECTROMETRY. Tissue: Venom and Venom gland. |
| [2] | "Purification, cloning and characterization of the L-amino acid oxidase in snake Trimeresurus stejnegeri." Wang J., Huang Q., Teng M., Niu L. Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Venom gland. |
Cross-references
Sequence databases | |
|---|---|
| AY277739 mRNA. Translation: AAQ56232.1. AY338966 mRNA. Translation: AAQ16182.1. | |
3D structure databases | |
| HSSP | HSSP built from PDB template 1F8R based on UniProtKB P81382. |
| SMR | Q6WP39. Positions 22-504. |
| ModBase | Search... |
Phylogenomic databases | |
| HOVERGEN | Q6WP39. |
Family and domain databases | |
| InterPro | IPR000759. Adrndx_reductase. IPR001613. Amineoxid_fl. IPR002937. Amino_oxidase. IPR013027. FAD_pyr_nucl-diS_OxRdtase. [Graphical view] |
| Pfam | PF01593. Amino_oxidase. 1 hit. [Graphical view] |
| PRINTS | PR00419. ADXRDTASE. PR00757. AMINEOXDASEF. PR00368. FADPNR. |
| ProtoNet | Search... |
Entry information
| Entry name | OXLA_TRIST | ||||||||
| Accession | Primary (citable) accession number: Q6WP39 Secondary accession number(s): Q7T062 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | Tox-Prot (Toxin Annotation Project) | ||||||||
Relevant documents
| UniProtKB secondary accession numbers Index of UniProtKB secondary accession numbers |
| SIMILARITY comments Index of protein domains and families |

Clusters with


