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B3EWI9 (OXLA_BOTMT) Reviewed, UniProtKB/Swiss-Prot

Last modified October 3, 2012. Version 4. 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=Bm-LAO
Short name=LAAO
Short name=LAO
EC=1.4.3.2
OrganismBothropoides matogrossensis (Pitviper) (Bothrops neuwiedi matogrossensis)
Taxonomic identifier1171125 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiLepidosauriaSquamataScleroglossaSerpentesColubroideaViperidaeCrotalinaeBothropoides

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.

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 

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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...

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: October 3, 2012
This is version 4 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