P0C2D1 (OXLA_BOTPI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names	Recommended name: L-amino-acid oxidase Short name=LAAO Short name=LAO EC=1.4.3.2 Alternative name(s): BpirLAAO-I
Organism	Bothrops pirajai (Piraja's lance head)
Taxonomic identifier	113192 [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	49 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 edema, antibacterial (E.coli, and P.aeruginosa) and antiparasitic activities, as well as induction 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. This protein may also have activities in hemorrhage, hemolysis, and apoptosis. Ref.1
Catalytic activity	An L-amino acid + H2O + O2 = a 2-oxo acid + NH3 + H2O2.
Cofactor	FAD By similarity.
Subunit structure	Homodimer; non-covalently linked. Ref.1
Subcellular location	Secreted.
Tissue specificity	Expressed by the venom gland.
Post-translational modification	Contains 2 disulfide bonds By similarity. N-glycosylated Probable. Ref.1
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 Hemorrhagic toxin Hemostasis impairing toxin Oxidoreductase Platelet aggregation activating toxin 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 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 – ›49	›49	L-amino-acid oxidase		PRO_0000273566
Regions
	Nucleotide binding	42 – 43	2	FAD By similarity
Experimental info
	Non-terminal residue	49	1

Sequences

	Sequence		Length	Mass (Da)
	P0C2D1 [UniParc]. Last modified January 23, 2007. Version 1. Checksum: 5D190816B54BACCA	FASTA	49	5,299
	10 20 30 40 ADDKNPLEEF RETNYEVFLE IAKNGLKATS NPKRVVIVGA GMAGLSAAY

References

[1]

"Biochemical and functional characterization of an L-amino acid oxidase isolated from Bothrops pirajai snake venom." Izidoro L.F.M., Ribeiro M.C., Souza G.R.L., Sant'Ana C.D., Hamaguchi A., Homsi-Brandeburgo M.I., Goulart L.R., Beleboni R.O., Nomizo A., Sampaio S.V., Soares A.M., Rodrigues V.M. Bioorg. Med. Chem. 14:7034-7043(2006) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE, FUNCTION, SUBUNIT, GLYCOSYLATION. Tissue: Venom.

Cross-references

3D structure databases
ProteinModelPortal	P0C2D1.
SMR	P0C2D1. Positions 3-49.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Family and domain databases
ProtoNet	Search...

Entry information

Entry name

OXLA_BOTPI

Accession

Primary (citable) accession number: P0C2D1

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 23, 2007
Last sequence update:	January 23, 2007
Last modified:	October 3, 2012
This is version 30 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Animal Toxin Annotation Program

Annotation program

Chordata Protein Annotation Program