Reviewed, UniProtKB/Swiss-Prot P0C2D1 (OXLA_BOTPI)

Names and origin

Protein names	Recommended name:     L-amino-acid oxidase     EC=1.4.3.2 Alternative name(s):     BpirLAAO-I       Short name=LAAO       Short name=LAO
Organism	Bothrops pirajai (Piraja's lance head)
Taxonomic identifier	113192 [NCBI]
Taxonomic lineage	Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Lepidosauria › Squamata › Scleroglossa › Serpentes › Colubroidea › Viperidae › Crotalinae › Bothrops

Protein attributes

Sequence length	49 AA.
Sequence status	Fragment.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Catalyzes an oxidative deamination of predominantly hydrophobic and aromatic L-amino acids. Induces platelet aggregation. Induces mouse paw edema. Has an antibacterial activity against E.coli, and P.aeruginosa. Has cytotoxic activity against Leishmania spp and tumor cells. May have an ability to induce apoptosis and hemorrhage.
Catalytic activity	An L-amino acid + H(2)O + O(2) = a 2-oxo acid + NH(3) + H(2)O(2).
Cofactor	FAD By similarity.
Subunit structure	Homodimer.
Subcellular location	Secreted.
Tissue specificity	Expressed by the venom gland.
Post-translational modification	Glycosylated.
Sequence similarities	Belongs to the flavin monoamine oxidase family. FIG1 subfamily.

Ontologies

Keywords
Biological process	Apoptosis Blood coagulation Cell cycle
Cellular component	Secreted
Ligand	FAD Flavoprotein
Molecular function	Anti-oncogene Antibiotic Antimicrobial Oxidoreductase Toxin
PTM	Glycoprotein
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	apoptosis Inferred from electronic annotation. Source: UniProtKB-KW blood coagulation Inferred from electronic annotation. Source: UniProtKB-KW defense response to bacterium Inferred from electronic annotation. Source: UniProtKB-KW negative regulation of cell cycle Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW pathogenesis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	extracellular region Inferred from electronic annotation. Source: UniProtKB-KW
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
Experimental info
	Non-terminal residue	49	1

Sequences

	Sequence		Length	Mass (Da)
	P0C2D1-1 [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: 16809041] [Abstract] Cited for: PROTEIN SEQUENCE, FUNCTION, SUBUNIT, GLYCOSYLATION. Tissue: Venom.

Cross-references

3D structure databases
SMR	P0C2D1. Positions 3-49.
ModBase	Search...
Phylogenomic databases
HOVERGEN	P0C2D1.
Family and domain databases
InterPro	IPR006076. FAD-dep_OxRdtase. [Graphical view]
Pfam	PF01266. DAO. 1 hit. [Graphical view]
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:	November 4, 2008
This is version 14 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Tox-Prot (Toxin Annotation Project)