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Q6TGQ9 (OXLA_BOTJR) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 50. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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=BjussuLAAO-I
Short name=LAAO
Short name=LAO
EC=1.4.3.2
OrganismBothrops jararacussu (Jararacussu)
Taxonomic identifier8726 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiLepidosauriaSquamataBifurcataUnidentataEpisquamataToxicoferaSerpentesColubroideaViperidaeCrotalinaeBothrops

Protein attributes

Sequence length497 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, as well as regulation of 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 By similarity.

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 By similarity Ref.1.

Tissue specificity

Expressed by the venom gland. Ref.1

Post-translational modification

N-glycosylated By similarity.

Miscellaneous

Has parasiticidal activities against both trypanosomes and leishmania, as a result of enzyme-catalyzed hydrogen peroxide production (Ref.1).

Sequence similarities

Belongs to the flavin monoamine oxidase family. FIG1 subfamily.

Ontologies

Keywords
   Biological processApoptosis
Cytolysis
Hemolysis
   Cellular componentSecreted
   DomainSignal
   LigandFAD
Flavoprotein
   Molecular functionAntibiotic
Antimicrobial
Hemostasis impairing toxin
Oxidoreductase
Toxin
   PTMDisulfide bond
Glycoprotein
   Technical term3D-structure
Gene Ontology (GO)
   Biological_processapoptotic process

Inferred from electronic annotation. Source: UniProtKB-KW

defense response to bacterium

Inferred from electronic annotation. Source: UniProtKB-KW

hemolysis in other organism

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionL-amino-acid oxidase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1313 By similarity
Chain14 – ›497›484L-amino-acid oxidase
PRO_0000273564

Regions

Nucleotide binding56 – 572FAD By similarity
Nucleotide binding76 – 772FAD By similarity
Nucleotide binding100 – 1034FAD By similarity
Nucleotide binding477 – 4826FAD By similarity
Nucleotide binding477 – 4782Substrate By similarity

Sites

Binding site1031Substrate By similarity
Binding site2361Substrate By similarity
Binding site2741FAD; via amide nitrogen and carbonyl oxygen By similarity
Binding site3851Substrate By similarity
Binding site4701FAD By similarity

Amino acid modifications

Glycosylation1851N-linked (GlcNAc...) Potential
Disulfide bond23 ↔ 186 By similarity
Disulfide bond344 ↔ 425 By similarity

Experimental info

Non-terminal residue4971

Secondary structure

.................................................................................................... 497
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q6TGQ9 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: 51AFCB28038399A1

FASTA49756,289
        10         20         30         40         50         60 
MNVFFMFSKP GKLADDRNPL EECFRETDYE EFLEIAKNGL STTSNPKRVV IVGAGMSGLS 

        70         80         90        100        110        120 
AAYVLANAGH QVTVLEASER AGGQVKTYRN EKEGWYANLG PMRLPEKHRI VREYIRKFGL 

       130        140        150        160        170        180 
QLNEFSQENE NAWYFIKNIR KRVGEVNKDP GVLDYPVKPS EVGKSAGQLY EESLQKAVEE 

       190        200        210        220        230        240 
LRRTNCSYML NKYDTYSTKE YLLKEGNLSP GAVDMIGDLL NEDSGYYVSF IESLKHDDIF 

       250        260        270        280        290        300 
AYEKRFDEIV GGMDKLPTSM YQAIQEKVHL NARVIKIQQD VKEVTVTYQT SEKETLSVTA 

       310        320        330        340        350        360 
DYVIVCTTSR AARRIKFEPP LPPKKAHALR SVHYRSGTKI FLTCTKKFWE DDGIHGGKST 

       370        380        390        400        410        420 
TDLPSRFIYY PNHNFPNGVG VIIAYGIGDD ANYFEALDFE DCGDIVINDL SLIHQLPKEE 

       430        440        450        460        470        480 
IQAICRPSMI QRWSLDKYAM GGITTFTPYQ FQHFSEALTA PVDRIYFAGE YTAQAHGWIA 

       490 
STIKSGPEGL DVNRASE 

« Hide

References

[1]"Molecular approaches for structural characterization of Bothrops L-amino acid oxidases with antiprotozoal activity: cDNA cloning, comparative sequence analysis, and molecular modeling."
Franca S.C., Kashima S., Roberto P.G., Marins M., Ticli F.K., Pereira J.O., Astolfi-Filho S., Stabeli R.G., Magro A.J., Fontes M.R., Sampaio S.V., Soares A.M.
Biochem. Biophys. Res. Commun. 355:302-306(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
Tissue: Venom and Venom gland.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY398691 mRNA. Translation: AAR31182.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4E0VX-ray3.10A/B1-497[»]
ProteinModelPortalQ6TGQ9.
SMRQ6TGQ9. Positions 16-497.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

HOVERGENHBG005729.

Family and domain databases

InterProIPR002937. Amino_oxidase.
IPR001613. Flavin_amine_oxidase.
[Graphical view]
PfamPF01593. Amino_oxidase. 1 hit.
[Graphical view]
PRINTSPR00757. AMINEOXDASEF.
ProtoNetSearch...

Entry information

Entry nameOXLA_BOTJR
AccessionPrimary (citable) accession number: Q6TGQ9
Entry history
Integrated into UniProtKB/Swiss-Prot: January 23, 2007
Last sequence update: July 5, 2004
Last modified: February 19, 2014
This is version 50 of the entry and version 1 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references