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Q4F867 (OXLA_DABRU) Reviewed, UniProtKB/Swiss-Prot

Last modified October 19, 2011. Version 26. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
L-amino-acid oxidase
Short name=DRS-LAAO
Short name=LAAO
Short name=LAO
EC=1.4.3.2
OrganismDaboia russelli siamensis (Eastern Russell's viper) (Daboia russelli formensis)
Taxonomic identifier343250 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Lepidosauria › Squamata › Scleroglossa › Serpentes › Colubroidea › Viperidae › Viperinae › Daboia

Protein attributes

Sequence length407 AA.
Sequence statusFragments.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes an oxidative deamination of predominantly hydrophobic and aromatic L-amino acids (highly active against L-Leu followed by L-Phe and L-Ile and not active against L-Pro, L-Asn, L-Gly, L-Ser and L-Cys), thus producing hydrogen peroxide that may contribute to the diverse toxic effects of this enzyme. Exhibits diverse biological activities such as antibacterial activity (Minimal inhibitory concentrations (MIC) are 9.0 µg/ml against S.aureus, 144.0 µg/ml against P.aeruginosa and 288.0 µg/ml against E.coli) and inhibition of ADP- and TMVA-induced platelet aggregation. Effects of snake L-amino oxidases on platelets are controversial, since they either induce aggregation or inhibit agonist-induced aggregation. These different effects are probably due to different experimental conditions. Unlike other snake venom L-amino acid oxidases, does not induce hemorrhage. This protein may also induce hemolysis, edema, apoptosis and have antiparasitic activities. Ref.1

Catalytic activity

An L-amino acid + H2O + O2 = a 2-oxo acid + NH3 + H2O2. Ref.1

Cofactor

FAD By similarity.

Subunit structure

Homodimer; non-covalently linked. Ref.1

Subcellular location

Secreted Ref.1.

Tissue specificity

Expressed by the venom gland. Ref.1

Post-translational modification

N-glycosylated Probable. Ref.1

Sequence similarities

Belongs to the flavin monoamine oxidase family. FIG1 subfamily.

Biophysicochemical properties

pH dependence:

Optimum pH is 8.8. Ref.1

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain‹1 – 407›407L-amino-acid oxidase
PRO_0000315372

Regions

Nucleotide binding385 – 3906FAD By similarity
Nucleotide binding385 – 3862Substrate By similarity

Sites

Binding site1441Substrate By similarity
Binding site1821FAD; via amide nitrogen and carbonyl oxygen By similarity
Binding site2931Substrate By similarity
Binding site3781FAD By similarity

Amino acid modifications

Glycosylation931N-linked (GlcNAc...) Potential
Glycosylation2821N-linked (GlcNAc...) Potential
Disulfide bond10 ↔ 94 By similarity
Disulfide bond252 ↔ 333 By similarity

Experimental info

Non-adjacent residues15 – 162
Non-terminal residue11

Sequences

Sequence LengthMass (Da)Tools
Q4F867 [UniParc].

Last modified January 19, 2010. Version 2.
Checksum: 8B7B22226EF561B9

FASTA40746,372
        10         20         30         40         50         60 
ADDKNPLEEC FREDDHRIVR EYIRKFGLKL NEFVQETENG WYFIKNIRKR VGEVKKDPGL 

        70         80         90        100        110        120 
LKYPVKPSEA GKSAGQLYQE SLGKAVEELK RTNCSYILNK YDTYSTKEYL IKEGNLSPGA 

       130        140        150        160        170        180 
VDMIGDLLNE DSGYYVSFIE SLKHDDIFAY EKRFDEIVGG MDQLPTSMYR AIEESVRFKA 

       190        200        210        220        230        240 
RVIKIQQNAE KVTVTYQTTQ KNLLLETVDY VIVCTTSRAA RRITFKPPLP PKKAHALRSV 

       250        260        270        280        290        300 
HYRSGTKIFL TCTKKFWEDD GIQGGKSTTD LPSRFIYYPN HNFTTGVGVI IAYGIGDDAN 

       310        320        330        340        350        360 
FFQALNLNEC ADIVFNDLSS IHQLPKKDLQ TFCYPSIIQK WSLDKYAMGA ITTFTPYQFQ 

       370        380        390        400 
HFSEALTAPV GRIFFAGEYT ANAHGWIDST IKSGLTAARD VNRASEL

« Hide

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

ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

HOVERGENHBG005729.

Family and domain databases

InterProIPR002937. Amino_oxidase.
[Graphical view]
PfamPF01593. Amino_oxidase. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameOXLA_DABRU
AccessionPrimary (citable) accession number: Q4F867
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: January 19, 2010
Last modified: October 19, 2011
This is version 26 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programAnimal Toxin Annotation Program
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

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