ID   OXLA_BOTIN              Reviewed;          49 AA.
AC   P0DI87;
DT   21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT   21-SEP-2011, sequence version 1.
DT   03-MAY-2023, entry version 31.
DE   RecName: Full=L-amino-acid oxidase;
DE            Short=BiLAO {ECO:0000303|PubMed:17983639};
DE            Short=LAAO;
DE            EC=1.4.3.2 {ECO:0000269|PubMed:17983639};
DE   Flags: Fragment;
OS   Bothrops insularis (Golden lancehead) (Lachesis insularis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Crotalinae; Bothrops.
OX   NCBI_TaxID=8723;
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, AND SUBCELLULAR LOCATION.
RC   TISSUE=Venom;
RX   PubMed=17983639; DOI=10.1016/j.toxicon.2007.09.003;
RA   Braga M.D., Martins A.M., Amora D.N., de Menezes D.B., Toyama M.H.,
RA   Toyama D.O., Marangoni S., Alves C.D., Barbosa P.S., de Sousa Alves R.,
RA   Fonteles M.C., Monteiro H.S.A.;
RT   "Purification and biological effects of L-amino acid oxidase isolated from
RT   Bothrops insularis venom.";
RL   Toxicon 51:199-207(2008).
CC   -!- FUNCTION: Catalyzes an oxidative deamination of predominantly
CC       hydrophobic and aromatic L-amino acids, thus producing hydrogen
CC       peroxide that may contribute to the diverse toxic effects of this
CC       enzyme (PubMed:17983639). Shows activity on L-Leu (PubMed:17983639).
CC       Exhibits diverse biological activities, such as hemorrhage, hemolysis,
CC       edema, antibacterial and antiparasitic activities, as well as
CC       regulation of platelet aggregation. Its effect on platelets is
CC       controversial, since it either induces aggregation or inhibits agonist-
CC       induced aggregation. These different effects are probably due to
CC       different experimental conditions (By similarity). In addition, this
CC       protein induces apoptosis and necrosis and has inhibitory effects on
CC       rat kidney function (decrease of blood flow and glomerular filtration).
CC       {ECO:0000250|UniProtKB:P0CC17, ECO:0000269|PubMed:17983639}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an L-alpha-amino acid + H2O + O2 = a 2-oxocarboxylate + H2O2 +
CC         NH4(+); Xref=Rhea:RHEA:13781, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:35179,
CC         ChEBI:CHEBI:59869; EC=1.4.3.2;
CC         Evidence={ECO:0000269|PubMed:17983639};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + L-leucine + O2 = 4-methyl-2-oxopentanoate + H2O2 +
CC         NH4(+); Xref=Rhea:RHEA:60996, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:16240, ChEBI:CHEBI:17865, ChEBI:CHEBI:28938,
CC         ChEBI:CHEBI:57427; Evidence={ECO:0000269|PubMed:17983639};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000250|UniProtKB:P81382};
CC   -!- SUBUNIT: Homodimer; non-covalently linked.
CC       {ECO:0000250|UniProtKB:P81382}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:17983639}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:17983639}.
CC   -!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:P81382}.
CC   -!- SIMILARITY: Belongs to the flavin monoamine oxidase family. FIG1
CC       subfamily. {ECO:0000305}.
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DR   AlphaFoldDB; P0DI87; -.
DR   SMR; P0DI87; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0001716; F:L-amino-acid oxidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR   GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR   GO; GO:0031640; P:killing of cells of another organism; IEA:UniProtKB-KW.
DR   Gene3D; 3.90.660.10; -; 1.
PE   1: Evidence at protein level;
KW   Antibiotic; Antimicrobial; Apoptosis; Cytolysis; Direct protein sequencing;
KW   Disulfide bond; FAD; Flavoprotein; Glycoprotein; Hemolysis;
KW   Hemostasis impairing toxin; Oxidoreductase; Secreted; Toxin.
FT   CHAIN           1..>49
FT                   /note="L-amino-acid oxidase"
FT                   /id="PRO_0000412594"
FT   BINDING         43..44
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P81382"
FT   DISULFID        10..?
FT                   /evidence="ECO:0000250|UniProtKB:P81382"
FT   NON_TER         49
FT                   /evidence="ECO:0000303|PubMed:17983639"
SQ   SEQUENCE   49 AA;  5293 MW;  29BAD2AFDCBE9D1F CRC64;
     ADDKNPLEEC FREDDYEGFL EIAKNGLSTT SNPKRVVIVG AGMSGLAAY
//