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P0CC17 (OXLA_BOTAT) Reviewed, UniProtKB/Swiss-Prot

Last modified October 31, 2012. Version 12. 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=BatroxLAAO
Short name=LAAO
Short name=LAO
EC=1.4.3.2
OrganismBothrops atrox (Barba amarilla) (Fer-de-lance)
Taxonomic identifier8725 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Lepidosauria › Squamata › Scleroglossa › Serpentes › Colubroidea › Viperidae › Crotalinae › Bothrops

Protein attributes

Sequence length119 AA.
Sequence statusFragments.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes an oxidative deamination of predominantly hydrophobic and aromatic L-amino acids (L-Met, followed by L-Leu, L-Phe, L-Trp, L-Tyr, L-Ile), thus producing hydrogen peroxide that may contribute to the diverse toxic effects of this enzyme. Exhibits diverse biological activities, such as apoptosis, cytotoxicity towards several cancer cell lines, induction of platelet aggregation, induction of moderate mouse paw edema, and antibacterial activities against both Gram-positive and Gram-negative bacteria. Unlike other snake venom L-amino acid oxidases, does not induce hemorrhage (with 50 µg of enzyme). May also act in hemolysis, and antiparasitic activities. 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.1 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 Ref.1.

Tissue specificity

Expressed by the venom gland. Ref.1

Post-translational modification

Contains 2 disulfide bonds By similarity.

N-glycosylated Probable. Ref.1

Miscellaneous

Has parasiticidal activities against both trypanosomes and leishmania, as a result of enzyme-catalyzed hydrogen peroxide production (Ref.2).

Sequence similarities

Belongs to the flavin monoamine oxidase family. FIG1 subfamily.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain‹1 – ›119›119L-amino-acid oxidase
PRO_0000390927

Regions

Nucleotide binding112 – 1176FAD By similarity
Nucleotide binding112 – 1132Substrate By similarity

Sites

Binding site701Substrate By similarity
Binding site1061FAD By similarity

Experimental info

Non-adjacent residues9 – 102
Non-adjacent residues32 – 332
Non-adjacent residues69 – 702
Non-adjacent residues78 – 792
Non-adjacent residues88 – 892
Non-adjacent residues100 – 1012
Non-terminal residue11
Non-terminal residue1191

Sequences

Sequence LengthMass (Da)Tools
P0CC17 [UniParc].

Last modified January 19, 2010. Version 1.
Checksum: 9006A71038ED323D

FASTA11913,700
        10         20         30         40         50         60 
ADDRNPLEER KFDLQLNRFS QENENAWYFI KNRVGEVNKD PGVLEYPVKP SEVGKSSAGQ 

        70         80         90        100        110 
LYEESLQKAH DDIFAYEKIK FEPPLPPKKF WEDDGIHGGK IYFAGETAQA HGWIDSTIK

« Hide

References

[1]"Evidence of caspase-mediated apoptosis induced by l-amino acid oxidase isolated from Bothrops atrox snake venom."
Alves R.M., Antonucci G.A., Paiva H.H., Cintra A.C., Franco J.J., Mendonca-Franqueiro E.P., Dorta D.J., Giglio J.R., Rosa J.C., Fuly A.L., Dias-Baruffi M., Soares A.M., Sampaio S.V.
Comp. Biochem. Physiol. 151:542-550(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE, FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, GLYCOSYLATION.
Tissue: Venom.
[2]"Cell cycle arrest evidence, parasiticidal and bactericidal properties induced by L-amino acid oxidase from Bothrops atrox snake venom."
de Melo Alves Paiva R., de Freitas Figueiredo R., Antonucci G.A., Paiva H.H., de Lourdes Pires Bianchi M., Rodrigues K.C., Lucarini R., Caetano R.C., Linhari Rodrigues Pietro R.C., Gomes Martins C.H., de Albuquerque S., Sampaio S.V.
Biochimie 93:941-947(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
Tissue: Venom.
[3]"A rational protocol for the successful crystallization of L-amino-acid oxidase from Bothrops atrox."
Alves R.M., Feliciano P.R., Sampaio S.V., Nonato M.C.
Acta Crystallogr. F 67:475-478(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: CRYSTALLIZATION.
Tissue: Venom.

Cross-references

3D structure databases

ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

ProtoNetSearch...

Entry information

Entry nameOXLA_BOTAT
AccessionPrimary (citable) accession number: P0CC17
Entry history
Integrated into UniProtKB/Swiss-Prot: January 19, 2010
Last sequence update: January 19, 2010
Last modified: October 31, 2012
This is version 12 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

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