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B3EWI9 (OXLA_BOTMT) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 8. 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=Bm-LAO
Short name=LAAO
Short name=LAO
EC=1.4.3.2
OrganismBothrops matogrossensis (Pitviper) (Bothrops neuwiedi matogrossensis)
Taxonomic identifier1171125 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiLepidosauriaSquamataBifurcataUnidentataEpisquamataToxicoferaSerpentesColubroideaViperidaeCrotalinaeBothrops

Protein attributes

Sequence length31 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 hemorrhage, hemolysis, edema, antibacterial and antiparasitic activities, as well as regulation of platelet aggregation. Its effect on platelets is controversial, since it either induces aggregation or inhibits agonist-induced aggregation. These different effects are probably due to different experimental conditions By similarity. Inhibits growth of B.subtilis strain ATCC 6633 (MIC=32 µM), E.faecalis strain ATCC 12953 (MIC=32 µM), S.aureus strain ATCC 29213 (MIC=32 µM), S.pyogenes strain ATCC 19615 (MIC=8 µM), E.coli strain ATCC 8739 (MIC=4 µM), K.pneumoniae strain ATCC 13885 (MIC=2 µM), P.mirabilis strain ATCC 25933 (MIC=2 µM), P.aeruginosa strain ATCC 15442 (MIC=8 µM) and S.typhimurium strain ATCC 14028 (MIC=8 µM). Ref.1 UniProtKB Q6STF1

Catalytic activity

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

Cofactor

FAD By similarity. UniProtKB Q6STF1

Subunit structure

Homodimer; non-covalently linked By similarity. UniProtKB Q6STF1

Subcellular location

Secreted Ref.1.

Tissue specificity

Expressed by the venom gland. Ref.1

Post-translational modification

N-glycosylated By similarity. UniProtKB Q6STF1

Sequence similarities

Belongs to the flavin monoamine oxidase family. FIG1 subfamily.

Ontologies

Keywords
   Biological processApoptosis
Cytolysis
Hemolysis
   Cellular componentSecreted
   LigandFAD
Flavoprotein
   Molecular functionAntibiotic
Antimicrobial
Hemostasis impairing toxin
Oxidoreductase
Toxin
   Technical termDirect protein sequencing
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

Chain‹1 – ›31›31L-amino-acid oxidase
PRO_0000417918

Experimental info

Non-adjacent residues13 – 142
Non-adjacent residues21 – 222
Non-terminal residue11
Non-terminal residue311

Sequences

Sequence LengthMass (Da)Tools
B3EWI9 [UniParc].

Last modified June 13, 2012. Version 1.
Checksum: 778F60FA5F08EB99

FASTA313,751
        10         20         30 
IKFEPPLPPK KAHKKFWEDD GIYYPPNHNF P 

« Hide

References

[1]"Evaluation of an antimicrobial L-amino acid oxidase and peptide derivatives from Bothropoides mattogrosensis pitviper venom."
Okubo B.M., Silva O.N., Migliolo L., Gomes D.G., Porto W.F., Batista C.L., Ramos C.S., Holanda H.H., Dias S.C., Franco O.L., Moreno S.E.
PLoS ONE 7:E33639-E33639(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION.
Tissue: Venom.

Cross-references

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

ProtoNetSearch...

Entry information

Entry nameOXLA_BOTMT
AccessionPrimary (citable) accession number: B3EWI9
Entry history
Integrated into UniProtKB/Swiss-Prot: June 13, 2012
Last sequence update: June 13, 2012
Last modified: March 19, 2014
This is version 8 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