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P0DI91 (OXLA_NAJOX) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 9. 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=LAAO
Short name=LAO
EC=1.4.3.2
OrganismNaja oxiana (Central Asian cobra) (Oxus cobra)
Taxonomic identifier8657 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiLepidosauriaSquamataBifurcataUnidentataEpisquamataToxicoferaSerpentesColubroideaElapidaeElapinaeNaja

Protein attributes

Sequence length95 AA.
Sequence statusFragments.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes an oxidative deamination of predominantly hydrophobic and aromatic L-amino acids, thus producing hydrogen peroxide that may contribute to the diverse toxic effects of this enzyme. Exhibits diverse biological activities, such as antibacterial activity against both Gram-positive (B.subtilis) and Gram-negative (E.coli) bacteria, and inhibition of ADP- or collagen-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. This protein may also induce hemorrhage, hemolysis, edema, apoptosis, and have antiparasitic activities. Ref.1

Catalytic activity

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

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.

Sequence similarities

Belongs to the flavin monoamine oxidase family. FIG1 subfamily.

Biophysicochemical properties

Kinetic parameters:

KM=0.885 mM for L-Met Ref.1

KM=0.051 mM for L-Phe

KM=0.147 mM for L-Trp

KM=0.75 mM for L-Leu

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – ›95›95L-amino-acid oxidase
PRO_0000412604

Amino acid modifications

Disulfide bond10 ↔ ? By similarity
Disulfide bond? ↔ 89 By similarity

Experimental info

Non-adjacent residues25 – 262
Non-adjacent residues34 – 352
Non-adjacent residues56 – 572
Non-adjacent residues69 – 702
Non-terminal residue951

Sequences

Sequence LengthMass (Da)Tools
P0DI91 [UniParc].

Last modified September 21, 2011. Version 1.
Checksum: EFD6FF44B5FFF34A

FASTA9511,216
        10         20         30         40         50         60 
DDRRSPLEEC FQQNDYEEFL EIARNSQLYQ ESLREDSSYH LSFIESLKSD ALFSYEKKFW 

        70         80         90 
EADGIHGGKV INDLSLIHDL PKREIQALCY PSIKK 

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References

[1]"L-Amino acid oxidase from Naja naja oxiana venom."
Samel M., Tonismagi K., Ronnholm G., Vija H., Siigur J., Kalkkinen N., Siigur E.
Comp. Biochem. Physiol. 149:572-580(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE, FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES.
Tissue: Venom.

Cross-references

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

ProtoNetSearch...

Entry information

Entry nameOXLA_NAJOX
AccessionPrimary (citable) accession number: P0DI91
Entry history
Integrated into UniProtKB/Swiss-Prot: September 21, 2011
Last sequence update: September 21, 2011
Last modified: February 19, 2014
This is version 9 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
Annotation programAnimal Toxin Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families