P0DI91 (OXLA_NAJOX) 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	Naja oxiana (Central Asian cobra) (Oxus cobra)
Taxonomic identifier	8657 [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	95 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, thus producing hydrogen peroxide that may contribute to the diverse toxic effects of this enzyme. Exhibits diverse biological activities, such as antibacterial activity against both Gram-positive (B.subtilis) and Gram-negative (E.coli) bacteria, and inhibition of ADP- or collagen-induced 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 induce hemorrhage, hemolysis, edema, apoptosis, and have antiparasitic activities. 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 Ref.1.
Tissue specificity	Expressed by the venom gland. Ref.1
Post-translational modification	N-glycosylated Probable.
Sequence similarities	Belongs to the flavin monoamine oxidase family. FIG1 subfamily.
Biophysicochemical properties	Kinetic parameters: KM=0.885 mM for L-Met Ref.1 KM=0.051 mM for L-Phe KM=0.147 mM for L-Trp KM=0.75 mM for L-Leu

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 – ›95	›95	L-amino-acid oxidase		PRO_0000412604
Amino acid modifications
	Disulfide bond	10 ↔ ?		By similarity
	Disulfide bond	? ↔ 89		By similarity
Experimental info
	Non-adjacent residues	25 – 26	2
	Non-adjacent residues	34 – 35	2
	Non-adjacent residues	56 – 57	2
	Non-adjacent residues	69 – 70	2
	Non-terminal residue	95	1

Sequences

	Sequence		Length	Mass (Da)
	P0DI91 [UniParc]. Last modified September 21, 2011. Version 1. Checksum: EFD6FF44B5FFF34A	FASTA	95	11,216
	10 20 30 40 50 60 DDRRSPLEEC FQQNDYEEFL EIARNSQLYQ ESLREDSSYH LSFIESLKSD ALFSYEKKFW 70 80 90 EADGIHGGKV INDLSLIHDL PKREIQALCY PSIKK

References

[1]

"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: PROTEIN SEQUENCE, FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES. 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_NAJOX

Accession

Primary (citable) accession number: P0DI91

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 21, 2011
Last sequence update:	September 21, 2011
Last modified:	October 3, 2012
This is version 6 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