ID   OXLA_BITGA              Reviewed;          60 AA.
AC   Q6T627;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 53.
DE   RecName: Full=L-amino-acid oxidase;
DE            Short=LAAO;
DE            Short=LAO {ECO:0000303|PubMed:15276202};
DE            EC=1.4.3.2 {ECO:0000250|UniProtKB:P81382};
DE   Flags: Fragment;
OS   Bitis gabonica (Gaboon adder) (Gaboon viper).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Viperinae; Bitis.
OX   NCBI_TaxID=8694;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Venom gland;
RX   PubMed=15276202; DOI=10.1016/j.gene.2004.03.024;
RA   Francischetti I.M.B., My-Pham V., Harrison J., Garfield M.K.,
RA   Ribeiro J.M.C.;
RT   "Bitis gabonica (Gaboon viper) snake venom gland: toward a catalog for the
RT   full-length transcripts (cDNA) and proteins.";
RL   Gene 337:55-69(2004).
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. Exhibits diverse biological activities, such as hemorrhage,
CC       hemolysis, edema, apoptosis of vascular endothelial cells or tumor cell
CC       lines, antibacterial and antiparasitic activities, as well as
CC       regulation of platelet aggregation. Effects of snake L-amino oxidases
CC       on platelets are controversial, since they either induce aggregation or
CC       inhibit agonist-induced aggregation. These different effects are
CC       probably due to different experimental conditions.
CC       {ECO:0000250|UniProtKB:P0CC17}.
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:0000250|UniProtKB:P81382}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:15276202}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:15276202}.
CC   -!- PTM: Contains 2 disulfide bonds. {ECO:0000250|UniProtKB:P81382}.
CC   -!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:P81382}.
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   EMBL; AY434453; AAR07363.1; -; mRNA.
DR   AlphaFoldDB; Q6T627; -.
DR   SMR; Q6T627; -.
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:0044179; P:hemolysis in another organism; IEA:UniProtKB-KW.
PE   2: Evidence at transcript level;
KW   Antibiotic; Antimicrobial; Apoptosis; Cytolysis; Disulfide bond; FAD;
KW   Flavoprotein; Glycoprotein; Hemolysis; Hemostasis impairing toxin;
KW   Oxidoreductase; Secreted; Toxin.
FT   CHAIN           <1..>60
FT                   /note="L-amino-acid oxidase"
FT                   /id="PRO_0000315371"
FT   BINDING         1..4
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P81382"
FT   BINDING         4
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P81382"
FT   NON_TER         1
FT                   /evidence="ECO:0000303|PubMed:15276202"
FT   NON_TER         60
FT                   /evidence="ECO:0000303|PubMed:15276202"
SQ   SEQUENCE   60 AA;  7323 MW;  584937BED0A03B07 CRC64;
     GPMRIPEKHR IVREYIRKFG LQLNEFVQET ENAWYYIKNI RKKVHEVKKD PGLLKYPVKP