ID   OXLA_PROMU              Reviewed;          24 AA.
AC   P0C2D6;
DT   23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   03-MAY-2023, entry version 39.
DE   RecName: Full=L-amino-acid oxidase;
DE            Short=LAAO;
DE            Short=TM-LAO {ECO:0000303|PubMed:12621545};
DE            EC=1.4.3.2 {ECO:0000250|UniProtKB:P81382};
DE   Flags: Fragment;
OS   Protobothrops mucrosquamatus (Taiwan habu) (Trimeresurus mucrosquamatus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Crotalinae; Protobothrops.
OX   NCBI_TaxID=103944;
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
RC   TISSUE=Venom;
RX   PubMed=12621545;
RA   Wei J.-F., Wei Q., Lu Q.-M., Tai H., Jin Y., Wang W.-Y., Xiong Y.-L.;
RT   "Purification, characterization and biological activity of an L-amino acid
RT   oxidase from Trimeresurus mucrosquamatus venom.";
RL   Sheng Wu Hua Xue Yu Sheng Wu Wu Li Xue Bao 35:219-224(2003).
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 (By similarity). Exhibits diverse biological activities, such as
CC       hemorrhage, hemolysis, edema, apoptosis, and antiparasitic activities
CC       (By similarity). This protein has antibacterial activity (against
CC       E.coli, S.aureus, and B.dysenteriae), cytotoxic activity, as well as an
CC       ability to induce platelet aggregation (PubMed:12621545). Effects of
CC       snake L-amino oxidases on platelets are controversial, since they
CC       either induce aggregation or inhibit agonist-induced aggregation (By
CC       similarity). These different effects are probably due to different
CC       experimental conditions (By similarity). {ECO:0000250|UniProtKB:P81382,
CC       ECO:0000269|PubMed:12621545}.
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:0000250|UniProtKB:P81382};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000250|UniProtKB:P81382};
CC   -!- SUBUNIT: Homodimer; non-covalently linked.
CC       {ECO:0000269|PubMed:12621545}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:12621545}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:12621545}.
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; P0C2D6; -.
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.
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;
KW   Platelet aggregation activating toxin; Secreted; Toxin.
FT   CHAIN           1..>24
FT                   /note="L-amino-acid oxidase"
FT                   /id="PRO_0000273571"
FT   DISULFID        10..?
FT                   /evidence="ECO:0000250|UniProtKB:P81382"
FT   NON_TER         24
FT                   /evidence="ECO:0000303|PubMed:12621545"
SQ   SEQUENCE   24 AA;  2931 MW;  A1D8D75DE753FAA7 CRC64;
     ADNKNPLEEC FRETNYEEFL EIAR
//