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   03-MAY-2023, entry version 45.
DE   RecName: Full=L-amino-acid oxidase;
DE            Short=LAAO;
DE            Short=LNV-LAO {ECO:0000303|PubMed:11368308};
DE            EC=1.4.3.2 {ECO:0000269|PubMed:11368308};
DE   Flags: Fragment;
OS   Eristicophis macmahoni (Leaf-nosed viper).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Viperinae; Eristicophis.
OX   NCBI_TaxID=110227;
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, MASS SPECTROMETRY,
RP   AND SUBCELLULAR LOCATION.
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 apoptosis-
RT   inducing L-amino acid oxidase from leaf-nosed viper (Eristocophis
RT   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, thus producing hydrogen
CC       peroxide that may contribute to the diverse toxic effects of this
CC       enzyme (PubMed:11368308). Shows activity on L-Leu (PubMed:11368308).
CC       Exhibits diverse biological activities, such as hemolysis, edema,
CC       apoptosis, as well as induction of platelet aggregation
CC       (PubMed:11368308). Effects of snake L-amino oxidases on platelets are
CC       controversial, since they either induce aggregation or inhibit agonist-
CC       induced aggregation (By similarity). These different effects are
CC       probably due to different experimental conditions. Unlike other snake
CC       venom L-amino acid oxidases, does not induce hemorrhage
CC       (PubMed:11368308). This protein may also have antibacterial and
CC       antiparasitic activities (By similarity).
CC       {ECO:0000250|UniProtKB:P0CC17, ECO:0000269|PubMed:11368308}.
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:11368308};
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:11368308};
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:11368308}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:11368308}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:11368308}.
CC   -!- PTM: Contains 2 disulfide bonds. {ECO:0000250|UniProtKB:P81382}.
CC   -!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:P81382}.
CC   -!- MASS SPECTROMETRY: Mass=58734; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:11368308};
CC   -!- SIMILARITY: Belongs to the flavin monoamine oxidase family. FIG1
CC       subfamily. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   AlphaFoldDB; P0C2D3; -.
DR   SMR; P0C2D3; -.
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..>27
FT                   /note="L-amino-acid oxidase"
FT                   /id="PRO_0000273568"
FT   NON_TER         27
FT                   /evidence="ECO:0000303|PubMed:11368308"
SQ   SEQUENCE   27 AA;  3097 MW;  18DBFD66E0655CE7 CRC64;
     ADDKNPLEEA FREADYEVFL EIAKNGL
//