OXLA_BOTPA
ID OXLA_BOTPA Reviewed; 503 AA.
AC B5AR80;
DT 21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 45.
DE RecName: Full=L-amino-acid oxidase;
DE Short=Bp-LAAO {ECO:0000303|PubMed:19135502};
DE Short=LAO;
DE EC=1.4.3.2 {ECO:0000269|PubMed:19135502};
DE Flags: Precursor; Fragment;
OS Bothrops pauloensis (Neuwied's lancehead) (Bothrops neuwiedi pauloensis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Bothrops.
OX NCBI_TaxID=1042543;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 19-68, FUNCTION, CATALYTIC
RP ACTIVITY, SUBUNIT, GLYCOSYLATION, SUBCELLULAR LOCATION, AND SUBSTRATE
RP SPECIFICITY.
RC TISSUE=Venom, and Venom gland;
RX PubMed=19135502; DOI=10.1016/j.biochi.2008.12.004;
RA Rodrigues R.S., da Silva J.F., Boldrini Franca J., Fonseca F.P.,
RA Otaviano A.R., Henrique Silva F., Hamaguchi A., Magro A.J., Braz A.S.,
RA dos Santos J.I., Homsi-Brandeburgo M.I., Fontes M.R., Fuly A.L.,
RA Soares A.M., Rodrigues V.M.;
RT "Structural and functional properties of Bp-LAAO, a new L-amino acid
RT oxidase isolated from Bothrops pauloensis snake venom.";
RL Biochimie 91:490-501(2009).
RN [2]
RP PROTEIN SEQUENCE OF 19-34, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Venom;
RX PubMed=22480909; DOI=10.1016/j.jprot.2012.03.028;
RA Rodrigues R.S., Boldrini-Franca J., Fonseca F.P., de la Torre P.,
RA Henrique-Silva F., Sanz L., Calvete J.J., Rodrigues V.M.;
RT "Combined snake venomics and venom gland transcriptomic analysis of
RT Bothropoides pauloensis.";
RL J. Proteomics 75:2707-2720(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:19135502). Is highly active on L-Met, L-Leu, L-Phe and
CC L-Ile (PubMed:19135502). Exhibits diverse biological activities, such
CC as antibacterial on both Gram-positive and Gram-negative bacteria and
CC antiparasitic activities, as well as induction of platelet aggregation
CC (PubMed:19135502). Effects of snake L-amino oxidases on platelets are
CC controversial, since they either induce aggregation or inhibit agonist-
CC induced aggregation. These different effects are probably due to
CC different experimental conditions. This protein may also have
CC activities in hemorrhage, hemolysis, edema, and apoptosis.
CC {ECO:0000250|UniProtKB:P0CC17, ECO:0000269|PubMed:19135502}.
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:19135502};
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:19135502};
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:19135502};
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:19135502};
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:19135502};
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:19135502}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:19135502}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000305|PubMed:19135502}.
CC -!- PTM: N-glycosylated (Probable). The enzymatic activity is not affected
CC by deglycosylation. {ECO:0000269|PubMed:19135502, ECO:0000305}.
CC -!- MISCELLANEOUS: Has parasiticidal activities against leishmania, as a
CC result of enzyme-catalyzed hydrogen peroxide production.
CC {ECO:0000305|PubMed:19135502}.
CC -!- SIMILARITY: Belongs to the flavin monoamine oxidase family. FIG1
CC subfamily. {ECO:0000305}.
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DR EMBL; EU870608; ACG55578.1; -; mRNA.
DR AlphaFoldDB; B5AR80; -.
DR SMR; B5AR80; -.
DR BRENDA; 1.4.3.2; 10579.
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.
DR Gene3D; 3.50.50.60; -; 1.
DR InterPro; IPR002937; Amino_oxidase.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR001613; Flavin_amine_oxidase.
DR Pfam; PF01593; Amino_oxidase; 1.
DR PRINTS; PR00757; AMINEOXDASEF.
DR SUPFAM; SSF51905; SSF51905; 1.
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; Signal; Toxin.
FT SIGNAL 1..18
FT /evidence="ECO:0000269|PubMed:19135502,
FT ECO:0000269|PubMed:22480909"
FT CHAIN 19..>503
FT /note="L-amino-acid oxidase"
FT /id="PRO_0000412598"
FT BINDING 61..62
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P81382"
FT BINDING 81..82
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P81382"
FT BINDING 89
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P81382"
FT BINDING 105..108
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P81382"
FT BINDING 108
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P81382"
FT BINDING 241
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P81382"
FT BINDING 279
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P81382"
FT BINDING 390
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P81382"
FT BINDING 475
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P81382"
FT BINDING 482..487
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P81382"
FT BINDING 482..483
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P81382"
FT CARBOHYD 190
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 28..191
FT /evidence="ECO:0000250|UniProtKB:P81382"
FT DISULFID 349..430
FT /evidence="ECO:0000250|UniProtKB:P81382"
FT NON_TER 503
FT /evidence="ECO:0000303|PubMed:19135502"
SQ SEQUENCE 503 AA; 56799 MW; 800568E8C2166CD0 CRC64;
MNVFFMFSLL FLAALGSCAD DGNPLEECFR ETDYEEFLEI AKNGLSATSN PKHVVIVGAG
MSGLSAAYVL ANAGHQVTVL EASKRAGGRV RTYRNDKEGW YANLGPMRLP EKHRIVREYI
RKFGLQLNEF SQENENAWYF IKNIRKRVGE VNKDPGVLEY PVKPSEVGKS AGQLYEESLQ
KAVEELRRTN CSYMLNKYDT YSTKEYLLKE GNLSPGAVDM IGDLLNEDSG YYVSFIESLK
HDDIFAYEKR FDEIVGGMDK LPTSMYQAIQ EKVRLNVRVI KIQQDVKEVT VTYQTSAKET
LSVTADYVIV CTTSRAARRI KFEPPLPPKK AHALRSVHYR SGTKIFLTCT KKFWEDDGIH
GGKSTTDLPS RFIYYPNHNF PSGVGVIIAY GIGDDANFFQ ALDFKDCGDI VINDLSLIHQ
LPKEEIQAFC RPSMIQRWSL DKYAMGGITT FTPYQFQHFS EALTAPVDRI YFAGEYTAQA
HGWIDSTIKS GLTAARDVNR ASE
