PROTEIN SEQUENCE, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
TISSUE=Venom;
DOI=10.1016/j.toxicon.2005.09.008; PubMed=16307769 [NCBI, ExPASy, EBI, Israel, Japan]
Toyama M.H., Toyama Dde O., Passero L.F., Laurenti M.D., Corbett C.E., Tomokane T.Y., Fonseca F.V., Antunes E., Joazeiro P.P., Beriam L.O., Martins M.A., Monteiro H.S., Fonteles M.C.;
"Isolation of a new L-amino acid oxidase from Crotalus durissus cascavella venom.";
Toxicon 47:47-57(2006).

Comments

FUNCTION: Catalyzes an oxidative deamination of predominantly hydrophobic and aromatic L-amino acids. Induces a dose-dependent platelet aggregation. Has an ability to induce apoptosis. Has an antibacterial activity against both Gram-negative and Gram-positive bacteria. Has high antileishmanic activity against the promastigote of Leishmania amazonensis in vitro. May have an ability to induce hemorrhage.
CATALYTIC ACTIVITY: An L-amino acid + H₂O + O₂ = a 2-oxo acid + NH₃ + H₂O₂.
COFACTOR: FAD.
BIOPHYSICOCHEMICAL PROPERTIES:

Kinetic parameters: K_M=46.7 µM for L-Leu;
pH dependence: Optimum pH is 6.5;
SUBUNIT: Homodimer.
SUBCELLULAR LOCATION: Secreted.
TISSUE SPECIFICITY: Expressed by the venom gland.
PTM: Glycosylated (By similarity).
SIMILARITY: Belongs to the flavin monoamine oxidase family. FIG1 subfamily.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

3D structure databases

SMR

P0C2D2; 3-61.

ModBase

P0C2D2.

Ontologies

GO:0005576;	Cellular component: extracellular region (inferred from electronic annotation from UniProtKB-KW).
GO:0001716;	Molecular function: L-amino-acid oxidase activity (inferred from electronic annotation from EC).
GO:0006915;	Biological process: apoptosis (inferred from electronic annotation from UniProtKB-KW).
GO:0007596;	Biological process: blood coagulation (inferred from electronic annotation from UniProtKB-KW).
GO:0042742;	Biological process: defense response to bacterium (inferred from electronic annotation from UniProtKB-KW).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
GO:0009405;	Biological process: pathogenesis (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR006076; FAD-dep_OxRdtase.
Graphical view of domain structure.

Pfam

PF01266; DAO; 1.
Pfam graphical view of domain structure.

ProDom

PD000139; FAD_pyr_redox; 1.
[Domain structure / List of seq. sharing at least 1 domain]

Phylogenomic databases

HOVERGEN

P0C2D2; -.

Other

ProtoNet

P0C2D2.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Antibiotic; Antimicrobial; Apoptosis; Blood coagulation; Direct protein sequencing; FAD; Flavoprotein; Glycoprotein; Oxidoreductase; Secreted; Toxin.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 >61`	`>61`	`L-amino-acid oxidase.`	`PRO_0000273567`
`NON_TER`	`61 61`

Sequence information

Length: 61 AA [This is the length of the partial sequence of the unprocessed precursor]

Molecular weight: 6561 Da [This is the MW of the partial sequence of the unprocessed precursor]

CRC64: 9D7F04E64267A122 [This is a checksum on the sequence]

        10         20         30         40         50         60 
ADDRNPLEQC FRETDYEEFL EIARNNLKAT SNPKHVVIVG AGMAGLSAAY VLSGGGHQVT 


V

P0C2D2 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools