Reviewed, UniProtKB/Swiss-Prot P81383 (OXLA_OPHHA)

Names and origin

Protein names	Recommended name:     L-amino-acid oxidase       Short name=LAAO       Short name=LAO     EC=1.4.3.2
Organism	Ophiophagus hannah (King cobra) (Naja hannah)
Taxonomic identifier	8665 [NCBI]
Taxonomic lineage	Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Lepidosauria › Squamata › Scleroglossa › Serpentes › Colubroidea › Elapidae › Elapinae › Ophiophagus

Protein attributes

Sequence length	19 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. Has an ability to induce apoptosis and hemorrhage. Has an antibacterial activity By similarity. Has cytotoxic activity. Induces platelet aggregation. Ref.2
Catalytic activity	An L-amino acid + H2O + O2 = a 2-oxo acid + NH3 + H2O2.
Cofactor	FAD. Ref.1
Subunit structure	Homodimer. Ref.2 Ref.1
Subcellular location	Secreted.
Tissue specificity	Expressed by the venom gland.
Post-translational modification	Glycosylated. Ref.2 Ref.1
Sequence similarities	Belongs to the flavin monoamine oxidase family. FIG1 subfamily.

Ontologies

Keywords
Biological process	Apoptosis Blood coagulation
Cellular component	Secreted
Ligand	FAD Flavoprotein
Molecular function	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 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-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 – ›19	›19	L-amino-acid oxidase		PRO_0000099871
Experimental info
	Sequence conflict	1	1	H → S AA sequence Ref.2
	Non-terminal residue	19	1

Sequences

	Sequence		Length	Mass (Da)
	P81383-1 [UniParc]. Last modified July 15, 1999. Version 2. Checksum: DD911A5B414F1427	FASTA	19	2,298
	10 HVINLEESFQ EPEYENHLA

References

[1]	"Purification and properties of the L-amino acid oxidase from Malayan pit viper (Calloselasma rhodostoma) venom." Ponnudurai G., Chung M.C.M., Tan N.-H. Arch. Biochem. Biophys. 313:373-378(1994) [PubMed: 8080286] [Abstract] Cited for: PROTEIN SEQUENCE, SUBUNIT, GLYCOSYLATION, COFACTOR. Tissue: Venom.
[2]	"Characterization and cytotoxicity of L-amino acid oxidase from the venom of king cobra (Ophiophagus hannah)." Ahn M.-Y., Lee B.M., Kim Y.S. Int. J. Biochem. Cell Biol. 29:911-919(1997) [PubMed: 9304806] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-15, FUNCTION, SUBUNIT, GLYCOSYLATION. Tissue: Venom.

Cross-references

3D structure databases
ModBase	Search...
Phylogenomic databases
HOVERGEN	P81383.
Enzyme and pathway databases
BRENDA	1.4.3.2. 19088.
Family and domain databases
ProtoNet	Search...

Entry information

Entry name

OXLA_OPHHA

Accession

Primary (citable) accession number: P81383

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 15, 1998
Last sequence update:	July 15, 1999
Last modified:	June 16, 2009
This is version 36 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Tox-Prot (Toxin Annotation Project)