ID   OXLA_BUNFA              Reviewed;         517 AA.
AC   A8QL52;
DT   21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 1.
DT   03-MAY-2023, entry version 60.
DE   RecName: Full=L-amino-acid oxidase;
DE            Short=Bf-LAAO {ECO:0000303|PubMed:19393676};
DE            Short=LAO;
DE            EC=1.4.3.2 {ECO:0000269|PubMed:19393676};
DE   Flags: Precursor;
OS   Bungarus fasciatus (Banded krait) (Pseudoboa fasciata).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Elapidae; Bungarinae; Bungarus.
OX   NCBI_TaxID=8613;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Venom gland;
RX   PubMed=17543361; DOI=10.1016/j.toxicon.2007.04.013;
RA   Jin Y., Lee W.-H., Zeng L., Zhang Y.;
RT   "Molecular characterization of L-amino acid oxidase from king cobra
RT   venom.";
RL   Toxicon 50:479-489(2007).
RN   [2]
RP   PROTEIN SEQUENCE OF 20-36, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP   PROPERTIES, SUBUNIT, SUBCELLULAR LOCATION, AND SUBSTRATE SPECIFICITY.
RC   TISSUE=Venom;
RX   PubMed=19393676; DOI=10.1016/j.toxicon.2009.04.017;
RA   Wei J.-F., Yang H.-W., Wei X.-L., Qiao L.-Y., Wang W.-Y., He S.-H.;
RT   "Purification, characterization and biological activities of the L-amino
RT   acid oxidase from Bungarus fasciatus snake venom.";
RL   Toxicon 54:262-271(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:19393676). Is highly active against L-Tyr, L-Asp, L-Phe,
CC       L-Glu, L-Trp, L-His, L-Gln, L-Ile, L-Met, L-Leu and moderately active
CC       against L-Lys, L-Arg, L-Ala and L-Asn (PubMed:19393676). Exhibits
CC       diverse biological activities, such as edema, inflammatory cell
CC       infiltration, cytotoxicity and apoptosis, as well as induction of
CC       platelet aggregation (PubMed:19393676). Effects of snake L-amino
CC       oxidases on platelets are controversial, since they either induce
CC       aggregation or inhibit agonist-induced aggregation. These different
CC       effects are probably due to different experimental conditions. This
CC       protein may also induce hemorrhage, hemolysis, and have antibacterial
CC       and antiparasitic activities. {ECO:0000250|UniProtKB:P0CC17,
CC       ECO:0000269|PubMed:19393676}.
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:19393676};
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:19393676};
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:19393676};
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:19393676};
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:19393676};
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:19393676};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + L-arginine + O2 = 5-guanidino-2-oxopentanoate + H2O2 +
CC         NH4(+); Xref=Rhea:RHEA:51404, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:32682,
CC         ChEBI:CHEBI:58489; Evidence={ECO:0000269|PubMed:19393676};
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:19393676};
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:19393676};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + L-asparagine + O2 = 2-oxosuccinamate + H2O2 + NH4(+);
CC         Xref=Rhea:RHEA:61224, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:57735,
CC         ChEBI:CHEBI:58048; Evidence={ECO:0000269|PubMed:19393676};
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:19393676};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + L-glutamine + O2 = 2-oxoglutaramate + H2O2 + NH4(+);
CC         Xref=Rhea:RHEA:61260, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:16240, ChEBI:CHEBI:16769, ChEBI:CHEBI:28938,
CC         ChEBI:CHEBI:58359; Evidence={ECO:0000269|PubMed:19393676};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + L-alanine + O2 = H2O2 + NH4(+) + pyruvate;
CC         Xref=Rhea:RHEA:61264, ChEBI:CHEBI:15361, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:28938,
CC         ChEBI:CHEBI:57972; Evidence={ECO:0000269|PubMed:19393676};
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:19393676};
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:19393676};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000250|UniProtKB:P81382};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=28.28 mM for L-Ala {ECO:0000269|PubMed:19393676};
CC         KM=18.75 mM for L-Arg {ECO:0000269|PubMed:19393676};
CC         KM=0.04 mM for L-Asp {ECO:0000269|PubMed:19393676};
CC         KM=19.07 mM for L-Asn {ECO:0000269|PubMed:19393676};
CC         KM=5.88 mM for L-Gln {ECO:0000269|PubMed:19393676};
CC         KM=1.44 mM for L-Glu {ECO:0000269|PubMed:19393676};
CC         KM=4.84 mM for L-His {ECO:0000269|PubMed:19393676};
CC         KM=1.64 mM for L-Ile {ECO:0000269|PubMed:19393676};
CC         KM=60.69 mM for L-Leu {ECO:0000269|PubMed:19393676};
CC         KM=21.49 mM for L-Lys {ECO:0000269|PubMed:19393676};
CC         KM=15.03 mM for L-Met {ECO:0000269|PubMed:19393676};
CC         KM=0.13 mM for L-Phe {ECO:0000269|PubMed:19393676};
CC         KM=0.27 mM for L-Trp {ECO:0000269|PubMed:19393676};
CC         KM=0.05 mM for L-Tyr {ECO:0000269|PubMed:19393676};
CC   -!- SUBUNIT: Monomer. This is in contrast with most of its orthologs, that
CC       are non-covalently linked homodimers. {ECO:0000269|PubMed:19393676}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:19393676}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:19393676}.
CC   -!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:P81382}.
CC   -!- SIMILARITY: Belongs to the flavin monoamine oxidase family. FIG1
CC       subfamily. {ECO:0000305}.
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DR   EMBL; EF080833; ABN72540.1; -; mRNA.
DR   AlphaFoldDB; A8QL52; -.
DR   SMR; A8QL52; -.
DR   BRENDA; 1.4.3.2; 1026.
DR   SABIO-RK; A8QL52; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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: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; 3.90.660.10; -; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR   Gene3D; 1.10.405.10; Guanine Nucleotide Dissociation Inhibitor, domain 1; 1.
DR   InterPro; IPR002937; Amino_oxidase.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR001613; Flavin_amine_oxidase.
DR   PANTHER; PTHR10742:SF235; AMINE OXIDASE; 1.
DR   PANTHER; PTHR10742; FLAVIN MONOAMINE OXIDASE; 1.
DR   Pfam; PF01593; Amino_oxidase; 1.
DR   PRINTS; PR00757; AMINEOXDASEF.
DR   SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
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   Hemostasis impairing toxin; Oxidoreductase;
KW   Platelet aggregation activating toxin; Secreted; Signal; Toxin.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000269|PubMed:19393676"
FT   CHAIN           20..517
FT                   /note="L-amino-acid oxidase"
FT                   /id="PRO_0000412599"
FT   BINDING         62..63
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P81382"
FT   BINDING         82..83
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P81382"
FT   BINDING         90
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P81382"
FT   BINDING         106..109
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P81382"
FT   BINDING         109
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P81382"
FT   BINDING         280
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P81382"
FT   BINDING         391
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P81382"
FT   BINDING         476
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P81382"
FT   BINDING         483..488
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P81382"
FT   BINDING         483..484
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P81382"
FT   CARBOHYD        191
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        380
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        29..192
FT                   /evidence="ECO:0000250|UniProtKB:P81382"
FT   DISULFID        350..431
FT                   /evidence="ECO:0000250|UniProtKB:P81382"
SQ   SEQUENCE   517 AA;  58764 MW;  E869950FB941B11D CRC64;
     MNVFSIFSLV FLAAFGSCAD DRRSALEECF READYEEFLE IARNGLKKTS NPKHVVVVGA
     GMAGLSAAYV LAGAGHRVTL LEASDRVGGR VNTYRDEKEG WYVNMGPMRL PERHRIVRTY
     IAKFGLKLNE FFQENENAWY FIRNIRKRVW EVKKDPGVFK YPVKPSEEGK SASQLYRESL
     KKVIEELKRT NCSYILDKYD TYSTKEYLIK EGNLSRGAVD MIGDLLNEDS SYYLSFIESL
     KNDDLFSYEK RFDEISDGFD QLPKSMHQAI AEMVHLNAQV IKIQRDAEKV RVAYQTPAKT
     LSYVTADYVI VCATSRAVRR ISFEPPLPPK KAHALRSIHY KSATKIFLTC TRKFWEADGI
     HGGKSTTDLP SRFIYYPNHN FTSGVGVIVA YVLADDSDFF QALDIKTSAD IVINDLSLIH
     QLPKNEIQAL CYPSLIKKWS LDKYTMGALT SFTPYQFQDY IETVAAPVGR IYFAGEYTAT
     VHGWLDSTIK SGLTAARNVN RASQKPSRIH LINDNQL
//