ID   OXLA_BOTPI              Reviewed;          49 AA.
AC   P0C2D1;
DT   23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   03-MAY-2023, entry version 59.
DE   RecName: Full=L-amino-acid oxidase;
DE            Short=BpirLAAO-I {ECO:0000303|PubMed:16809041};
DE            Short=LAO;
DE            EC=1.4.3.2 {ECO:0000269|PubMed:16809041};
DE   Flags: Fragment;
OS   Bothrops pirajai (Piraja's lancehead).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Crotalinae; Bothrops.
OX   NCBI_TaxID=113192;
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, GLYCOSYLATION,
RP   SUBCELLULAR LOCATION, AND SUBSTRATE SPECIFICITY.
RC   TISSUE=Venom;
RX   PubMed=16809041; DOI=10.1016/j.bmc.2006.06.025;
RA   Izidoro L.F.M., Ribeiro M.C., Souza G.R.L., Sant'Ana C.D., Hamaguchi A.,
RA   Homsi-Brandeburgo M.I., Goulart L.R., Beleboni R.O., Nomizo A.,
RA   Sampaio S.V., Soares A.M., Rodrigues V.M.;
RT   "Biochemical and functional characterization of an L-amino acid oxidase
RT   isolated from Bothrops pirajai snake venom.";
RL   Bioorg. Med. Chem. 14:7034-7043(2006).
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:16809041). Is highly active on L-Phe, L-Tyr, L-Trp, L-
CC       Leu, L-Met, and L-Ile, is moderately active on L-Val, and L-His, and is
CC       no or weakly active on L-Ala, L-Arg, L-Pro, L-Thr, L-Ser, L-Glu, L-Gly,
CC       and L-Lys (PubMed:16809041). Exhibits diverse biological activities,
CC       such as edema, antibacterial (E.coli, and P.aeruginosa) and
CC       antiparasitic activities against leishmania (as a result of enzyme-
CC       catalyzed hydrogen peroxide production), induction of platelet
CC       aggregation as well as cytotoxicity on S180 tumor, human breast (SKBR-
CC       3), acute T cell leukemia (Jurkat) cancer, and Erlich ascitic tumor
CC       (EAT) cell lines (PubMed:16809041). 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. This protein may
CC       also have activities in hemorrhage, hemolysis, and apoptosis.
CC       {ECO:0000269|PubMed:16809041}.
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:16809041};
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:16809041};
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:16809041};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + L-tryptophan + O2 = H2O2 + indole-3-pyruvate + NH4(+);
CC         Xref=Rhea:RHEA:61244, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:16240, ChEBI:CHEBI:17640, ChEBI:CHEBI:28938,
CC         ChEBI:CHEBI:57912; Evidence={ECO:0000269|PubMed:16809041};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + L-methionine + O2 = 4-methylsulfanyl-2-oxobutanoate +
CC         H2O2 + NH4(+); Xref=Rhea:RHEA:61236, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:16723,
CC         ChEBI:CHEBI:28938, ChEBI:CHEBI:57844;
CC         Evidence={ECO:0000269|PubMed:16809041};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + L-isoleucine + O2 = (S)-3-methyl-2-oxopentanoate + H2O2
CC         + NH4(+); Xref=Rhea:RHEA:61232, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:35146,
CC         ChEBI:CHEBI:58045; Evidence={ECO:0000269|PubMed:16809041};
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:16809041};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + L-tyrosine + O2 = 3-(4-hydroxyphenyl)pyruvate + H2O2 +
CC         NH4(+); Xref=Rhea:RHEA:61248, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:36242,
CC         ChEBI:CHEBI:58315; Evidence={ECO:0000269|PubMed:16809041};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + L-valine + O2 = 3-methyl-2-oxobutanoate + H2O2 + NH4(+);
CC         Xref=Rhea:RHEA:61252, ChEBI:CHEBI:11851, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:28938,
CC         ChEBI:CHEBI:57762; Evidence={ECO:0000269|PubMed:16809041};
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:16809041}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:16809041}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:16809041}.
CC   -!- PTM: Contains 2 disulfide bonds. {ECO:0000250|UniProtKB:P81382}.
CC   -!- PTM: N-glycosylated. {ECO:0000305|PubMed:16809041}.
CC   -!- MISCELLANEOUS: Negative results: does not show cytotoxicity towards
CC       macrophages. {ECO:0000269|PubMed:16809041}.
CC   -!- SIMILARITY: Belongs to the flavin monoamine oxidase family. FIG1
CC       subfamily. {ECO:0000305}.
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DR   AlphaFoldDB; P0C2D1; -.
DR   SMR; P0C2D1; -.
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:0031640; P:killing of cells of another organism; IEA:UniProtKB-KW.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE   1: Evidence at protein level;
KW   Antibiotic; Antimicrobial; Apoptosis; Cytolysis; Direct protein sequencing;
KW   Disulfide bond; FAD; Flavoprotein; Glycoprotein; Hemolysis;
KW   Hemorrhagic toxin; Hemostasis impairing toxin; Oxidoreductase;
KW   Platelet aggregation activating toxin; Secreted; Toxin.
FT   CHAIN           1..>49
FT                   /note="L-amino-acid oxidase"
FT                   /id="PRO_0000273566"
FT   BINDING         42..43
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P81382"
FT   NON_TER         49
FT                   /evidence="ECO:0000303|PubMed:16809041"
SQ   SEQUENCE   49 AA;  5299 MW;  5D190816B54BACCA CRC64;
     ADDKNPLEEF RETNYEVFLE IAKNGLKATS NPKRVVIVGA GMAGLSAAY
//