ID   OXLA_BOTPI              Reviewed;          49 AA.
AC   P0C2D1;
DT   23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   16-JUN-2009, entry version 16.
DE   RecName: Full=L-amino-acid oxidase;
DE            Short=LAAO;
DE            Short=LAO;
DE            EC=1.4.3.2;
DE   AltName: Full=BpirLAAO-I;
DE   Flags: Fragment;
OS   Bothrops pirajai (Piraja's lance head).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Scleroglossa; Serpentes; Colubroidea;
OC   Viperidae; Crotalinae; Bothrops.
OX   NCBI_TaxID=113192;
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, SUBUNIT, AND GLYCOSYLATION.
RC   TISSUE=Venom;
RX   PubMed=16809041; DOI=10.1016/j.bmc.2006.06.025;
RA   Izidoro L.F.M., Ribeiro M.C., Souza G.R.L., Sant'Ana C.D.,
RA   Hamaguchi A., Homsi-Brandeburgo M.I., Goulart L.R., Beleboni R.O.,
RA   Nomizo A., Sampaio S.V., Soares A.M., Rodrigues V.M.;
RT   "Biochemical and functional characterization of an L-amino acid
RT   oxidase isolated from Bothrops pirajai snake venom.";
RL   Bioorg. Med. Chem. 14:7034-7043(2006).
CC   -!- FUNCTION: Catalyzes an oxidative deamination of predominantly
CC       hydrophobic and aromatic L-amino acids. Induces platelet
CC       aggregation. Induces mouse paw edema. Has an antibacterial
CC       activity against E.coli, and P.aeruginosa. Has cytotoxic activity
CC       against Leishmania spp and tumor cells. May have an ability to
CC       induce apoptosis and hemorrhage.
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.
CC   -!- SIMILARITY: Belongs to the flavin monoamine oxidase family. FIG1
CC       subfamily.
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DR   SMR; P0C2D1; 3-49.
DR   HOVERGEN; P0C2D1; -.
DR   BRENDA; 1.4.3.2; 278409.
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:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR   GO; GO:0045786; P:negative regulation of cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   GO; GO:0009405; P:pathogenesis; IEA:UniProtKB-KW.
DR   InterPro; IPR006076; FAD-dep_OxRdtase.
DR   Pfam; PF01266; DAO; 1.
PE   1: Evidence at protein level;
KW   Anti-oncogene; Antibiotic; Antimicrobial; Apoptosis;
KW   Blood coagulation; Cell cycle; Direct protein sequencing; FAD;
KW   Flavoprotein; Glycoprotein; Oxidoreductase; Secreted; Toxin.
FT   CHAIN         1    >49       L-amino-acid oxidase.
FT                                /FTId=PRO_0000273566.
FT   NON_TER      49     49
SQ   SEQUENCE   49 AA;  5299 MW;  5D190816B54BACCA CRC64;
     ADDKNPLEEF RETNYEVFLE IAKNGLKATS NPKRVVIVGA GMAGLSAAY
//