OXLA_BUNFA
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-AUG-2022, entry version 57.
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: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..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
