OXLA_DABSI
ID OXLA_DABSI Reviewed; 407 AA.
AC Q4F867;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 19-JAN-2010, sequence version 2.
DT 03-AUG-2022, entry version 58.
DE RecName: Full=L-amino-acid oxidase;
DE Short=DRS-LAAO {ECO:0000303|PubMed:19523971};
DE Short=LAO;
DE EC=1.4.3.2 {ECO:0000269|PubMed:19523971};
DE Flags: Fragments;
OS Daboia siamensis (Eastern Russel's viper) (Daboia russelii siamensis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Viperinae; Daboia.
OX NCBI_TaxID=343250;
RN [1]
RP PROTEIN SEQUENCE OF 1-15, NUCLEOTIDE SEQUENCE [MRNA] OF 16-407, FUNCTION,
RP CATALYTIC ACTIVITY, SUBUNIT, SUBCELLULAR LOCATION, GLYCOSYLATION,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND SUBSTRATE SPECIFICITY.
RC TISSUE=Venom, and Venom gland;
RX PubMed=19523971; DOI=10.1016/j.toxicon.2009.06.004;
RA Zhong S.-R., Jin Y., Wu J.-B., Jia Y.-H., Xu G.-L., Wang G.-C.,
RA Xiong Y.-L., Lu Q.-M.;
RT "Purification and characterization of a new L-amino acid oxidase from
RT Daboia russellii siamensis venom.";
RL Toxicon 54:763-771(2009).
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:19523971). Is highly active on L-Leu followed by L-Phe
CC and L-Ile, moderately active on L-Asp, L-Glu, and L-Lys, and not active
CC on L-Pro, L-Asn, L-Gly, L-Ser and L-Cys (PubMed:19523971). Exhibits
CC diverse biological activities such as antibacterial activity (Minimal
CC inhibitory concentrations (MIC) are 9.0 ug/ml against S.aureus, 144.0
CC ug/ml against P.aeruginosa and 288.0 ug/ml against E.coli) and
CC inhibition of ADP- and TMVA-induced platelet aggregation. Effects of
CC snake L-amino oxidases on platelets are controversial, since they
CC either induce aggregation or inhibit agonist-induced aggregation. These
CC different effects are probably due to different experimental
CC conditions. Unlike other snake venom L-amino acid oxidases, does not
CC induce hemorrhage. This protein may also induce hemolysis, edema,
CC apoptosis and have antiparasitic activities.
CC {ECO:0000269|PubMed:19523971}.
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:19523971};
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:19523971};
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:19523971};
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:19523971};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-aspartate + O2 = H2O2 + NH4(+) + oxaloacetate;
CC Xref=Rhea:RHEA:19025, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16240, ChEBI:CHEBI:16452, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:29991; Evidence={ECO:0000269|PubMed:19523971};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-lysine + O2 = 6-amino-2-oxohexanoate + H2O2 + NH4(+);
CC Xref=Rhea:RHEA:14437, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:32551,
CC ChEBI:CHEBI:58183; Evidence={ECO:0000269|PubMed:19523971};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-glutamate + O2 = 2-oxoglutarate + H2O2 + NH4(+);
CC Xref=Rhea:RHEA:20728, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16240, ChEBI:CHEBI:16810, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:29985; Evidence={ECO:0000269|PubMed:19523971};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000250|UniProtKB:P81382};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 8.8. {ECO:0000269|PubMed:19523971};
CC -!- SUBUNIT: Homodimer; non-covalently linked.
CC {ECO:0000269|PubMed:19523971}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:19523971}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000305|PubMed:19523971}.
CC -!- SIMILARITY: Belongs to the flavin monoamine oxidase family. FIG1
CC subfamily. {ECO:0000305}.
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DR EMBL; DQ104365; AAZ08620.1; -; mRNA.
DR AlphaFoldDB; Q4F867; -.
DR SMR; Q4F867; -.
DR BRENDA; 1.4.3.2; 6667.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR GO; GO:0001716; F:L-amino-acid oxidase activity; IDA:UniProtKB.
DR GO; GO:0050025; F:L-glutamate oxidase activity; IEA:RHEA.
DR GO; GO:0050029; F:L-lysine oxidase activity; IEA:RHEA.
DR GO; GO:0106329; F:L-phenylalaine oxidase activity; IEA:RHEA.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0090729; F:toxin activity; IDA:UniProtKB.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0042742; P:defense response to bacterium; IDA:UniProtKB.
DR GO; GO:0044179; P:hemolysis in another organism; IEA:UniProtKB-KW.
DR GO; GO:0035893; P:negative regulation of platelet aggregation in another organism; IDA:UniProtKB.
DR Gene3D; 3.50.50.60; -; 1.
DR InterPro; IPR002937; Amino_oxidase.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR Pfam; PF01593; Amino_oxidase; 1.
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 inhibiting toxin; Secreted; Toxin.
FT CHAIN <1..407
FT /note="L-amino-acid oxidase"
FT /id="PRO_0000315372"
FT BINDING 144
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P81382"
FT BINDING 182
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P81382"
FT BINDING 293
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P81382"
FT BINDING 378
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P81382"
FT BINDING 385..390
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P81382"
FT BINDING 385..386
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P81382"
FT CARBOHYD 93
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 282
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 10..94
FT /evidence="ECO:0000250|UniProtKB:P81382"
FT DISULFID 252..333
FT /evidence="ECO:0000250|UniProtKB:P81382"
FT NON_CONS 15..16
FT /evidence="ECO:0000303|PubMed:19523971"
FT NON_TER 1
FT /evidence="ECO:0000303|PubMed:19523971"
SQ SEQUENCE 407 AA; 46372 MW; 8B7B22226EF561B9 CRC64;
ADDKNPLEEC FREDDHRIVR EYIRKFGLKL NEFVQETENG WYFIKNIRKR VGEVKKDPGL
LKYPVKPSEA GKSAGQLYQE SLGKAVEELK RTNCSYILNK YDTYSTKEYL IKEGNLSPGA
VDMIGDLLNE DSGYYVSFIE SLKHDDIFAY EKRFDEIVGG MDQLPTSMYR AIEESVRFKA
RVIKIQQNAE KVTVTYQTTQ KNLLLETVDY VIVCTTSRAA RRITFKPPLP PKKAHALRSV
HYRSGTKIFL TCTKKFWEDD GIQGGKSTTD LPSRFIYYPN HNFTTGVGVI IAYGIGDDAN
FFQALNLNEC ADIVFNDLSS IHQLPKKDLQ TFCYPSIIQK WSLDKYAMGA ITTFTPYQFQ
HFSEALTAPV GRIFFAGEYT ANAHGWIDST IKSGLTAARD VNRASEL
