ID   OXLA_ERIMA              Reviewed;          27 AA.
AC   P0C2D3;
DT   23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   16-JUN-2009, entry version 14.
DE   RecName: Full=L-amino-acid oxidase;
DE            Short=LAAO;
DE            Short=LAO;
DE            EC=1.4.3.2;
DE   Flags: Fragment;
OS   Eristocophis macmahoni (Leaf-nosed viper).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Scleroglossa; Serpentes; Colubroidea;
OC   Viperidae; Viperinae; Eristocophis.
OX   NCBI_TaxID=8702;
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, SUBUNIT, AND MASS SPECTROMETRY.
RC   TISSUE=Venom;
RX   PubMed=11368308; DOI=10.1006/abbi.2000.2130;
RA   Ali S.A., Stoeva S., Abbasi A., Alam J.M., Kayed R., Faigle M.,
RA   Neumeister B., Voelter W.;
RT   "Isolation, structural, and functional characterization of an
RT   apoptosis-inducing L-amino acid oxidase from leaf-nosed viper
RT   (Eristocophis macmahoni) snake venom.";
RL   Arch. Biochem. Biophys. 384:216-226(2000).
CC   -!- FUNCTION: Catalyzes an oxidative deamination of predominantly
CC       hydrophobic and aromatic L-amino acids. Induces edema and platelet
CC       aggregation. Has a potent hemolytic activity. Has an ability to
CC       induce apoptosis. Unlike other snake venom L-amino acid oxidases,
CC       does not induce hemorrhage. May have an antibacterial activity.
CC   -!- CATALYTIC ACTIVITY: An L-amino acid + H(2)O + O(2) = a 2-oxo acid
CC       + NH(3) + H(2)O(2).
CC   -!- COFACTOR: FAD (By similarity).
CC   -!- SUBUNIT: Homodimer.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- PTM: Glycosylated (By similarity).
CC   -!- MASS SPECTROMETRY: Mass=58734.0; Method=MALDI; Range=1-?;
CC       Source=PubMed:11368308;
CC   -!- SIMILARITY: Belongs to the flavin monoamine oxidase family. FIG1
CC       subfamily.
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DR   HOVERGEN; P0C2D3; -.
DR   BRENDA; 1.4.3.2; 279510.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0001716; F:L-amino-acid oxidase activity; IEA:EC.
DR   GO; GO:0006915; P:apoptosis; IEA:UniProtKB-KW.
DR   GO; GO:0007596; P:blood coagulation; IEA:UniProtKB-KW.
DR   GO; GO:0019835; P:cytolysis; IEA:UniProtKB-KW.
DR   GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR   GO; GO:0019836; P:hemolysis by symbiont of host erythrocytes; IEA:UniProtKB-KW.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   GO; GO:0009405; P:pathogenesis; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Antibiotic; Antimicrobial; Apoptosis; Blood coagulation; Cytolysis;
KW   Direct protein sequencing; FAD; Flavoprotein; Glycoprotein; Hemolysis;
KW   Oxidoreductase; Secreted; Toxin.
FT   CHAIN         1    >27       L-amino-acid oxidase.
FT                                /FTId=PRO_0000273568.
FT   NON_TER      27     27
SQ   SEQUENCE   27 AA;  3097 MW;  18DBFD66E0655CE7 CRC64;
     ADDKNPLEEA FREADYEVFL EIAKNGL
//