Reviewed,
UniProtKB/Swiss-Prot Q4F867 (OXLA_DABRU)
Last modified
January 19, 2010.
Version 17.
History...
Clusters with 100%,
90%,
50% identity |
Documents (1) |
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Names and origin
| Protein names | Recommended name: L-amino-acid oxidase Short name=DRS-LAAO Short name=LAAO Short name=LAO EC=1.4.3.2 |
| Organism | Daboia russelli siamensis (Eastern Russell's viper) (Daboia russelli formensis) |
| Taxonomic identifier | 343250 [NCBI] |
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Lepidosauria › Squamata › Scleroglossa › Serpentes › Colubroidea › Viperidae › Viperinae › Daboia |
Protein attributes
| Sequence length | 407 AA. |
| Sequence status | Fragments. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | Catalyzes an oxidative deamination of predominantly hydrophobic and aromatic L-amino acids. Displays high specificity towards L-Leu followed by L-Phe and L-Ile, while five substrates L-Pro, L-Asn, L-Gly, L-Ser and L-Cys are not oxidized. Does not show hemorrhagic activity. Dose-dependently inhibits platelet aggregation induced by ADP and TMVA. Has antibacterial activity against S.aureus (ATCC 25923) (MIC=9.0 µg/ml), P.aeruginosa (ATCC 27853) (MIC=144.0 µg/ml) and E.coli (ATCC 25922) (MIC=288.0 µg/ml). The hydrogen peroxide produced by L-amino acid oxidation may be partly involved in platelet aggregation inhibition and antimicrobial activities. |
| Catalytic activity | An L-amino acid + H2O + O2 = a 2-oxo acid + NH3 + H2O2. |
| Cofactor | FAD By similarity. |
| Subunit structure | Homodimer; not disulfid-linked. |
| Subcellular location | |
| Tissue specificity | Expressed by the venom gland. |
| Post-translational modification | Glycosylated. |
| Sequence similarities | Belongs to the flavin monoamine oxidase family. FIG1 subfamily. |
| Biophysicochemical properties | pH dependence: Optimum pH is 8.8. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Blood coagulation |
| Cellular component | Secreted |
| Ligand | FAD Flavoprotein |
| Molecular function | Antibiotic Antimicrobial Oxidoreductase Toxin |
| PTM | Disulfide bond 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 bacterium Ref.1Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Ref.1Inferred from electronic annotation. Source: UniProtKB-KW pathogenesisInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | extracellular region Ref.1 Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | L-amino-acid oxidase activity Ref.1 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 – 407 | 407 | L-amino-acid oxidase | PRO_0000315372 | |||||||
Regions | |||||||||||
| Nucleotide binding | 378 – 390 | 13 | FAD By similarity | ||||||||
Sites | |||||||||||
| Binding site | 144 | 1 | Substrate By similarity | ||||||||
| Binding site | 182 | 1 | FAD; via amide nitrogen and carbonyl oxygen By similarity | ||||||||
| Binding site | 293 | 1 | Substrate By similarity | ||||||||
Amino acid modifications | |||||||||||
| Glycosylation | 93 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 282 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Disulfide bond | 10 ↔ 94 | By similarity | |||||||||
| Disulfide bond | 252 ↔ 333 | By similarity | |||||||||
Experimental info | |||||||||||
| Non-adjacent residues | 15 – 16 | 2 | |||||||||
| Non-terminal residue | 1 | 1 | |||||||||
Sequences
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References
| [1] | "Purification and characterization of a new L-amino acid oxidase from Daboia russellii siamensis venom." Zhong S.-R., Jin Y., Wu J.-B., Jia Y.-H., Xu G.-L., Wang G.-C., Xiong Y.-L., Lu Q.-M. Toxicon 54:763-771(2009) [PubMed: 19523971] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-15, NUCLEOTIDE SEQUENCE [MRNA] OF 16-407, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, GLYCOSYLATION, BIOPHYSICOCHEMICAL PROPERTIES. Tissue: Venom and Venom gland. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | DQ104365 mRNA. Translation: AAZ08620.1. |
3D structure databases | |
| SMR | Q4F867. Positions 1-391. |
| ModBase | Search... |
Phylogenomic databases | |
| HOVERGEN | Q4F867. |
Family and domain databases | |
| InterPro | IPR002937. Amino_oxidase. [Graphical view] |
| Pfam | PF01593. Amino_oxidase. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | OXLA_DABRU | ||||||||
| Accession | Primary (citable) accession number: Q4F867 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | Tox-Prot (Toxin Annotation Project) | ||||||||

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