ID   OXLA_BOTMT              Reviewed;          31 AA.
AC   B3EWI9;
DT   13-JUN-2012, integrated into UniProtKB/Swiss-Prot.
DT   13-JUN-2012, sequence version 1.
DT   25-MAY-2022, entry version 20.
DE   RecName: Full=L-amino-acid oxidase {ECO:0000303|PubMed:22438972};
DE            Short=Bm-LAO {ECO:0000303|PubMed:22438972};
DE            Short=LAAO {ECO:0000250|UniProtKB:P81382};
DE            EC=1.4.3.2 {ECO:0000269|PubMed:22438972};
DE   Flags: Fragments;
OS   Bothrops matogrossensis (Pitviper) (Bothrops neuwiedi matogrossensis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Crotalinae; Bothrops.
OX   NCBI_TaxID=1171125;
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND
RP   SUBSTRATE SPECIFICITY.
RC   TISSUE=Venom;
RX   PubMed=22438972; DOI=10.1371/journal.pone.0033639;
RA   Okubo B.M., Silva O.N., Migliolo L., Gomes D.G., Porto W.F., Batista C.L.,
RA   Ramos C.S., Holanda H.H., Dias S.C., Franco O.L., Moreno S.E.;
RT   "Evaluation of an antimicrobial L-amino acid oxidase and peptide
RT   derivatives from Bothropoides mattogrosensis pitviper venom.";
RL   PLoS ONE 7:E33639-E33639(2012).
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:22438972). Is moderately active on L-Leu, L-His, and L-
CC       Phe, and very weakly active on L-Thr, and L-Cys (PubMed:22438972).
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). Inhibits growth of
CC       B.subtilis strain ATCC 6633 (MIC=32 uM), E.faecalis strain ATCC 12953
CC       (MIC=32 uM), S.aureus strain ATCC 29213 (MIC=32 uM), S.pyogenes strain
CC       ATCC 19615 (MIC=8 uM), E.coli strain ATCC 8739 (MIC=4 uM), K.pneumoniae
CC       strain ATCC 13885 (MIC=2 uM), P.mirabilis strain ATCC 25933 (MIC=2 uM),
CC       P.aeruginosa strain ATCC 15442 (MIC=8 uM) and S.typhimurium strain ATCC
CC       14028 (MIC=8 uM) (PubMed:22438972). {ECO:0000250|UniProtKB:P0CC17,
CC       ECO:0000269|PubMed:22438972}.
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:22438972};
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:22438972};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + L-phenylalanine + O2 = 3-phenylpyruvate + H2O2 + NH4(+);
CC         Xref=Rhea:RHEA:61240, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:16240, ChEBI:CHEBI:18005, ChEBI:CHEBI:28938,
CC         ChEBI:CHEBI:58095; Evidence={ECO:0000269|PubMed:22438972};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + L-histidine + O2 = 3-(imidazol-5-yl)pyruvate + H2O2 +
CC         NH4(+); Xref=Rhea:RHEA:61228, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:57595,
CC         ChEBI:CHEBI:58133; Evidence={ECO:0000269|PubMed:22438972};
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:22438972}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:22438972}.
CC   -!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:P81382}.
CC   -!- SIMILARITY: Belongs to the flavin monoamine oxidase family. FIG1
CC       subfamily. {ECO:0000255}.
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DR   AlphaFoldDB; B3EWI9; -.
DR   SMR; B3EWI9; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0106329; F:L-phenylalaine oxidase activity; IEA:RHEA.
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   1: Evidence at protein level;
KW   Antibiotic; Antimicrobial; Apoptosis; Cytolysis; Direct protein sequencing;
KW   FAD; Flavoprotein; Hemolysis; Hemostasis impairing toxin; Oxidoreductase;
KW   Secreted; Toxin.
FT   CHAIN           <1..>31
FT                   /note="L-amino-acid oxidase"
FT                   /id="PRO_0000417918"
FT   NON_CONS        13..14
FT                   /evidence="ECO:0000303|PubMed:22438972"
FT   NON_CONS        21..22
FT                   /evidence="ECO:0000303|PubMed:22438972"
FT   NON_TER         1
FT                   /evidence="ECO:0000303|PubMed:22438972"
FT   NON_TER         31
FT                   /evidence="ECO:0000303|PubMed:22438972"
SQ   SEQUENCE   31 AA;  3751 MW;  778F60FA5F08EB99 CRC64;
     IKFEPPLPPK KAHKKFWEDD GIYYPPNHNF P