ID   OXLA_VIPBB              Reviewed;          88 AA.
AC   P0C2D7;
DT   23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   16-JUN-2009, entry version 11.
DE   RecName: Full=L-amino-acid oxidase;
DE            Short=LAAO;
DE            Short=LAO;
DE            EC=1.4.3.2;
DE   Flags: Fragments;
OS   Vipera berus berus (Common viper).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Scleroglossa; Serpentes; Colubroidea;
OC   Viperidae; Viperinae; Vipera.
OX   NCBI_TaxID=31156;
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, AND SUBUNIT.
RC   TISSUE=Venom;
RX   PubMed=16574513; DOI=10.1016/j.bbapap.2006.01.021;
RA   Samel M., Vija H., Ronnholm G., Siigur J., Kalkkinen N., Siigur E.;
RT   "Isolation and characterization of an apoptotic and platelet
RT   aggregation inhibiting L-amino acid oxidase from Vipera berus berus
RT   (common viper) venom.";
RL   Biochim. Biophys. Acta 1764:707-714(2006).
CC   -!- FUNCTION: Catalyzes an oxidative deamination of predominantly
CC       hydrophobic and aromatic L-amino acids (the most specific
CC       substrate is L-Phe, followed by L-Met, L-Leu, L-Phe, L-Ile, L-Arg
CC       and L-His). Inhibits both ADP-induced platelet aggregation dose-
CC       dependently. Has an ability to induce apoptosis in cultured HeLa
CC       and K562 cells. May have an ability to induce hemorrhage. May have
CC       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   -!- SIMILARITY: Belongs to the flavin monoamine oxidase family. FIG1
CC       subfamily.
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DR   HOVERGEN; P0C2D7; -.
DR   BRENDA; 1.4.3.2; 292016.
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:0042742; P:defense response to bacterium; 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;
KW   Direct protein sequencing; FAD; Flavoprotein; Glycoprotein;
KW   Oxidoreductase; Secreted; Toxin.
FT   CHAIN         1    >88       L-amino-acid oxidase.
FT                                /FTId=PRO_0000273573.
FT   NP_BIND      83     86       FAD (By similarity).
FT   BINDING      74     74       FAD (By similarity).
FT   NON_CONS     37     38
FT   NON_CONS     44     45
FT   NON_CONS     52     53
FT   NON_CONS     61     62
FT   NON_CONS     68     69
FT   NON_TER      88     88
SQ   SEQUENCE   88 AA;  10295 MW;  D2A63168391A7965 CRC64;
     ADDKNPLEEC FREDDYEEFL EIAKNGLKKT SNPKHIVYPV KPSEQLYEES LRDQLPTSMH
     RYPSMIQKIF FAGEYTANAH GWIDSTIK
//