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A8QL58 (OXLA_NAJAT) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 21. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
L-amino-acid oxidase

Short name=LAAO
Short name=LAO
Short name=NA-LAAO
EC=1.4.3.2
OrganismNaja atra (Chinese cobra)
Taxonomic identifier8656 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiLepidosauriaSquamataBifurcataUnidentataEpisquamataToxicoferaSerpentesColubroideaElapidaeElapinaeNaja

Protein attributes

Sequence length449 AA.
Sequence statusFragment.
Sequence processingThe displayed sequence is further processed into a mature form.
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 hemorrhage, hemolysis, edema, apoptosis of vascular endothelial cells or tumor cell lines, antibacterial and antiparasitic activities By similarity. This protein induces platelet aggregation by both hydrogen peroxide production and binding to platelet membrane proteins (that would enhance the sensitivity of platelets to hydrogen peroxide). 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. Ref.2

Catalytic activity

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

Cofactor

FAD By similarity.

Subunit structure

Homodimer; non-covalently linked By similarity.

Subcellular location

Secreted.

Tissue specificity

Expressed by the venom gland.

Post-translational modification

N-glycosylated By similarity.

Sequence similarities

Belongs to the flavin monoamine oxidase family. FIG1 subfamily.

Biophysicochemical properties

Kinetic parameters:

Vmax=38.4 µmol/min/mg enzyme Ref.2

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919 Ref.2
Chain20 – ›449›430L-amino-acid oxidase
PRO_0000412603

Regions

Nucleotide binding62 – 632FAD By similarity
Nucleotide binding82 – 832FAD By similarity
Nucleotide binding106 – 1094FAD By similarity

Sites

Binding site901FAD By similarity
Binding site1091Substrate By similarity
Binding site2801FAD; via amide nitrogen and carbonyl oxygen By similarity
Binding site3891Substrate By similarity

Amino acid modifications

Glycosylation1911N-linked (GlcNAc...) Potential
Glycosylation3781N-linked (GlcNAc...) Potential
Disulfide bond29 ↔ 192 By similarity
Disulfide bond348 ↔ 429 By similarity

Experimental info

Non-terminal residue4491

Sequences

Sequence LengthMass (Da)Tools
A8QL58 [UniParc].

Last modified January 15, 2008. Version 1.
Checksum: 905AD5DFB3D08362

FASTA44951,439
        10         20         30         40         50         60 
MNVLFIFSLL FLAALESCAD DRRSPLEECF QQNDYEEILE IARNGLKKTS NPKHVVVVGA 

        70         80         90        100        110        120 
GMAGLSAAYV LAGAGHKVTL LEASERVGGR VITYHNDREG WYVNMGPMRL PERHRIVREY 

       130        140        150        160        170        180 
IRKFGLKLNE FFQENENAWY YINNIRKRVW EVKKDPSLLK YPVKPSEEGK SASQLYQEPL 

       190        200        210        220        230        240 
RKVIEELKRT NCSYILNKYD SYSTKEYLIK EGNLSRGAVD MIGDLLNEDS SYHLSFMESL 

       250        260        270        280        290        300 
KSDALFSYEK RFDEIVGGFD QLPISMYQAI AEMVHLNARV IKIQYDAEKV RVTYQTPAKT 

       310        320        330        340        350        360 
FVTADYVIVC STSRAARRIY FEPPLPPKKA HALRSIHYRS ATKIFLTCSK KFWEADGIHG 

       370        380        390        400        410        420 
GKSTTDLPSR FIHYPNHNFT SGIGVIMAYV LADDSDFFQA LDTKTCADIV INDLSLIHDL 

       430        440 
PKREIQALCY PSIKKWNLDK YTMGSITSF 

« Hide

References

[1]"Molecular characterization of L-amino acid oxidase from king cobra venom."
Jin Y., Lee W.-H., Zeng L., Zhang Y.
Toxicon 50:479-489(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Venom gland.
[2]"L-amino acid oxidase from Naja atra venom activates and binds to human platelets."
Li R., Zhu S., Wu J., Wang W., Lu Q., Clemetson K.J.
Acta Biochim. Biophys. Sin. 40:19-26(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 20-29, FUNCTION IN PLATELET AGGREGATION, BIOPHYSICOCHEMICAL PROPERTIES.
Tissue: Venom.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
EF080839 mRNA. Translation: ABN72546.1.

3D structure databases

ProteinModelPortalA8QL58.
ModBaseSearch...
MobiDBSearch...

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_NAJAT
AccessionPrimary (citable) accession number: A8QL58
Entry history
Integrated into UniProtKB/Swiss-Prot: September 21, 2011
Last sequence update: January 15, 2008
Last modified: February 19, 2014
This is version 21 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