P0C2D4 (OXLA_NAJKA) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names	Recommended name: L-amino-acid oxidase Short name=K-LAO Short name=LAAO Short name=LAO EC=1.4.3.2
Organism	Naja kaouthia (Monocled cobra) (Naja siamensis)
Taxonomic identifier	8649 [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 › Elapidae › Elapinae › Naja

Protein attributes

Sequence length	38 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 (highly active against L-Phe and L-Tyr, and moderately active against L-Trp, L-Met, L-Leu, and L-Arg), 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. This protein inhibits both agonist- and shear stress-induced platelet aggregation (SIPA). 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.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. Ref.2
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=0.63 mM for L-Met Ref.2 Ref.3 KM=0.06 mM for L-Phe KM=0.66 mM for L-Leu KM=0.29 mM for L-Trp pH dependence: Optimum pH is 8.5, unlike many other venom L-amino acid oxidase, is also stable in alkaline medium.

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 – ›38	›38	L-amino-acid oxidase		PRO_0000273569
Amino acid modifications
	Disulfide bond	10 ↔ ?		By similarity
Experimental info
	Non-terminal residue	38	1

Sequences

	Sequence		Length	Mass (Da)
	P0C2D4 [UniParc]. Last modified January 23, 2007. Version 1. Checksum: D988B9FC32DDDE08	FASTA	38	4,514
	10 20 30 DDRRSPLEEC FQQNDYEEFL EIAKNGLKKT XNPKHVXV

References

[1]	"Inhibition of human platelet aggregation by L-amino acid oxidase purified from Naja naja kaouthia venom." Sakurai Y., Takatsuka H., Yoshioka A., Matsui T., Suzuki M., Titani K., Fujimura Y. Toxicon 39:1827-1833(2001) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE. Tissue: Venom.
[2]	"Purification and properties of the L-amino acid oxidase from monocellate cobra (Naja naja kaouthia) venom." Tan N.-H., Swaminathan S. Int. J. Biochem. 24:967-973(1992) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT. Tissue: Venom.
[3]	"L-Amino acid oxidase from Naja naja oxiana venom." Samel M., Tonismagi K., Ronnholm G., Vija H., Siigur J., Kalkkinen N., Siigur E. Comp. Biochem. Physiol. 149:572-580(2008) [PubMed] [Europe PMC] [Abstract] Cited for: BIOPHYSICOCHEMICAL PROPERTIES.

Cross-references

3D structure databases
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Enzyme and pathway databases
SABIO-RK	P0C2D4.
Family and domain databases
ProtoNet	Search...

Entry information

Entry name

OXLA_NAJKA

Accession

Primary (citable) accession number: P0C2D4

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 23, 2007
Last sequence update:	January 23, 2007
Last modified:	March 6, 2013
This is version 26 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