P0C2D7 (OXLA_VIPBB) 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
Organism	Vipera berus berus (Common viper)
Taxonomic identifier	31156 [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 › Viperinae › Vipera › Vipera berus

Protein attributes

Sequence length	88 AA.
Sequence status	Fragments.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes an oxidative deamination of predominantly hydrophobic and aromatic L-amino acids (the most specific substrate is L-Phe, followed by L-Met, L-Leu, L-Phe, L-Ile, L-Arg and L-His), 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, antibacterial and antiparasitic activities By similarity. In addition, this protein has an ability to induce apoptosis in cultured HeLa and K562 cells, and inhibits ADP-induced platelet aggregation dose-dependently. 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
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	N-glycosylated By similarity.
Sequence similarities	Belongs to the flavin monoamine oxidase family. FIG1 subfamily.
Biophysicochemical properties	Kinetic parameters: KM=0.361 mM for L-Leu Ref.1 KM=0.286 mM for L-Met KM=0.058 mM for L-Phe

Ontologies

Keywords
Biological process	Apoptosis Cytolysis Hemolysis
Cellular component	Secreted
Ligand	FAD Flavoprotein
Molecular function	Antibiotic Antimicrobial Hemostasis impairing toxin Oxidoreductase Platelet aggregation inhibiting 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 – ›88	›88	L-amino-acid oxidase		PRO_0000273573
Regions
	Nucleotide binding	81 – 86	6	FAD By similarity
	Nucleotide binding	81 – 82	2	Substrate By similarity
Sites
	Binding site	74	1	FAD By similarity
Amino acid modifications
	Disulfide bond	10 ↔ ?		By similarity
Experimental info
	Non-adjacent residues	37 – 38	2
	Non-adjacent residues	44 – 45	2
	Non-adjacent residues	52 – 53	2
	Non-adjacent residues	61 – 62	2
	Non-adjacent residues	68 – 69	2
	Non-terminal residue	88	1

Sequences

	Sequence		Length	Mass (Da)
	P0C2D7 [UniParc]. Last modified January 23, 2007. Version 1. Checksum: D2A63168391A7965	FASTA	88	10,295
	10 20 30 40 50 60 ADDKNPLEEC FREDDYEEFL EIAKNGLKKT SNPKHIVYPV KPSEQLYEES LRDQLPTSMH 70 80 RYPSMIQKIF FAGEYTANAH GWIDSTIK

References

[1]

"Isolation and characterization of an apoptotic and platelet aggregation inhibiting L-amino acid oxidase from Vipera berus berus (common viper) venom." Samel M., Vija H., Ronnholm G., Siigur J., Kalkkinen N., Siigur E. Biochim. Biophys. Acta 1764:707-714(2006) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE, MASS SPECTROMETRY, FUNCTION, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES. Tissue: Venom.

Cross-references

3D structure databases
ProteinModelPortal	P0C2D7.
SMR	P0C2D7. Positions 3-37.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Family and domain databases
ProtoNet	Search...

Entry information

Entry name

OXLA_VIPBB

Accession

Primary (citable) accession number: P0C2D7

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 23, 2007
Last sequence update:	January 23, 2007
Last modified:	October 3, 2012
This is version 25 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