P0CJ40 (OXLA_BOTMA) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names	Recommended name: L-amino-acid oxidase Short name=BmarLAAO Short name=LAAO Short name=LAO EC=1.4.3.2
Organism	Bothrops marajoensis (Marajo lancehead)
Taxonomic identifier	157554 [NCBI]
Taxonomic lineage	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Sauropsida › Sauria › Lepidosauria › Squamata › Scleroglossa › Serpentes › Colubroidea › Viperidae › Crotalinae › Bothrops

Protein attributes

Sequence length	39 AA.
Sequence status	Fragment.
Protein existence	Evidence 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, 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. In addition, this protein inhibits dose-dependently the growth of Gram-positive, Gram-negative bacteria and yeast, probably by the generation of hydrogen peroxide. Ref.1
Catalytic activity	An L-amino acid + H2O + O2 = a 2-oxo acid + NH3 + H2O2.
Cofactor	FAD By similarity.
Subunit structure	Monomer. Ref.1
Subcellular location	Secreted.
Tissue specificity	Expressed by the venom gland.
Post-translational modification	N-glycosylated By similarity.
Miscellaneous	Has parasiticidal activities against 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 process	Apoptosis Cytolysis Hemolysis
Cellular component	Secreted
Ligand	FAD Flavoprotein
Molecular function	Antibiotic Antimicrobial Fungicide Hemostasis impairing toxin Oxidoreductase Toxin
PTM	Disulfide bond Glycoprotein
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological_process	apoptotic process Inferred from electronic annotation. Source: UniProtKB-KW cytolysis Inferred from electronic annotation. Source: UniProtKB-KW defense response to bacterium Inferred from electronic annotation. Source: UniProtKB-KW defense response to fungus Inferred from electronic annotation. Source: UniProtKB-KW hemolysis in other organism Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	L-amino-acid oxidase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – ›39	›39	L-amino-acid oxidase		PRO_0000412597
Amino acid modifications
	Disulfide bond	10 ↔ ?
Experimental info
	Non-terminal residue	39	1

Sequences

	Sequence		Length	Mass (Da)
	P0CJ40 [UniParc]. Last modified September 21, 2011. Version 1. Checksum: 5A9BBD388988C742	FASTA	39	4,405
	10 20 30 AHDGNPLEEC FREDDEEFFL EIAKNGLTAT SNPKRVVIV

References

[1]

"Antibacterial and antiparasitic effects of Bothrops marajoensis venom and its fractions: phospholipase A2 and L-amino acid oxidase." Costa Torres A.F., Dantas R.T., Toyama M.H., Diz Filho E., Zara F.J., Rodrigues de Queiroz M.G., Pinto Nogueira N.A., Rosa de Oliveira M., de Oliveira Toyama D., Monteiro H.S.A., Martins A.M.C. Toxicon 55:795-804(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE, FUNCTION, SUBUNIT. Tissue: Venom.

Cross-references

3D structure databases
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Family and domain databases
ProtoNet	Search...

Entry information

Entry name

OXLA_BOTMA

Accession

Primary (citable) accession number: P0CJ40

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 21, 2011
Last sequence update:	September 21, 2011
Last modified:	November 28, 2012
This is version 8 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Annotation program

Animal Toxin Annotation Program