Reviewed, UniProtKB/Swiss-Prot P0C2D3 (OXLA_ERIMA)

Names and origin

Protein names	Recommended name:     L-amino-acid oxidase       Short name=LAAO       Short name=LAO     EC=1.4.3.2
Organism	Eristocophis macmahoni (Leaf-nosed viper)
Taxonomic identifier	8702 [NCBI]
Taxonomic lineage	Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Lepidosauria › Squamata › Scleroglossa › Serpentes › Colubroidea › Viperidae › Viperinae › Eristocophis

Protein attributes

Sequence length	27 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 edema and platelet aggregation. Has a potent hemolytic activity. Has an ability to induce apoptosis. Unlike other snake venom L-amino acid oxidases, does not induce hemorrhage. May have an antibacterial activity. Ref.1
Catalytic activity	An L-amino acid + H2O + O2 = a 2-oxo acid + NH3 + H2O2.
Cofactor	FAD By similarity.
Subunit structure	Homodimer. Ref.1
Subcellular location	Secreted.
Tissue specificity	Expressed by the venom gland.
Post-translational modification	Glycosylated By similarity.
Sequence similarities	Belongs to the flavin monoamine oxidase family. FIG1 subfamily.
Mass spectrometry	Molecular mass is 58734.0 Da from positions 1 - ?. Determined by MALDI. Ref.1

Ontologies

Keywords
Biological process	Apoptosis Blood coagulation Cytolysis Hemolysis
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 cytolysis Inferred from electronic annotation. Source: UniProtKB-KW defense response to bacterium Inferred from electronic annotation. Source: UniProtKB-KW hemolysis by symbiont of host erythrocytes 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 – ›27	›27	L-amino-acid oxidase		PRO_0000273568
Experimental info
	Non-terminal residue	27	1

Sequences

	Sequence		Length	Mass (Da)
	P0C2D3-1 [UniParc]. Last modified January 23, 2007. Version 1. Checksum: 18DBFD66E0655CE7	FASTA	27	3,097
	10 20 ADDKNPLEEA FREADYEVFL EIAKNGL

References

[1]

"Isolation, structural, and functional characterization of an apoptosis-inducing L-amino acid oxidase from leaf-nosed viper (Eristocophis macmahoni) snake venom." Ali S.A., Stoeva S., Abbasi A., Alam J.M., Kayed R., Faigle M., Neumeister B., Voelter W. Arch. Biochem. Biophys. 384:216-226(2000) [PubMed: 11368308] [Abstract] Cited for: PROTEIN SEQUENCE, FUNCTION, SUBUNIT, MASS SPECTROMETRY. Tissue: Venom.

Cross-references

3D structure databases
ModBase	Search...
Phylogenomic databases
HOVERGEN	P0C2D3.
Enzyme and pathway databases
BRENDA	1.4.3.2. 279510.
Family and domain databases
ProtoNet	Search...

Entry information

Entry name

OXLA_ERIMA

Accession

Primary (citable) accession number: P0C2D3

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 23, 2007
Last sequence update:	January 23, 2007
Last modified:	June 16, 2009
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)