OXLA_BUNMU
ID OXLA_BUNMU Reviewed; 517 AA.
AC A8QL51;
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=Bm-LAAO {ECO:0000303|PubMed:17543361};
DE Short=LAO;
DE EC=1.4.3.2 {ECO:0000250|UniProtKB:P81382};
DE Flags: Precursor;
OS Bungarus multicinctus (Many-banded krait).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Elapidae; Bungarinae; Bungarus.
OX NCBI_TaxID=8616;
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).
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. Exhibits diverse biological activities, such as hemorrhage,
CC hemolysis, edema, apoptosis of vascular endothelial cells or tumor cell
CC lines, antibacterial and antiparasitic activities, as well as
CC regulation of platelet aggregation. 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 (By similarity).
CC {ECO:0000250|UniProtKB:P0CC17}.
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:0000250|UniProtKB:P81382};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000250|UniProtKB:P81382};
CC -!- SUBUNIT: Homodimer; non-covalently linked.
CC {ECO:0000250|UniProtKB:P81382}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:17543361}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000305|PubMed:17543361}.
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; EF080832; ABN72539.1; -; mRNA.
DR AlphaFoldDB; A8QL51; -.
DR SMR; A8QL51; -.
DR PRIDE; A8QL51; -.
DR BRENDA; 1.4.3.2; 1027.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0001716; F:L-amino-acid oxidase activity; IEA:UniProtKB-EC.
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 2: Evidence at transcript level;
KW Antibiotic; Antimicrobial; Apoptosis; Cytolysis; Disulfide bond; FAD;
KW Flavoprotein; Glycoprotein; Hemolysis; Hemostasis impairing toxin;
KW Oxidoreductase; Secreted; Signal; Toxin.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..517
FT /note="L-amino-acid oxidase"
FT /id="PRO_0000412600"
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; 58811 MW; A9F28766C1B3AB97 CRC64;
MNVFSIFSLV FLAAFGSCAD DRRSPLEECF READYEEFLE IARNGLKKTS NPKHVVVVGA
GMAGLSAAYV LEKAGHRVTL LEASDRVGGR ANTYRDEKEG WYVNMGPMRL PERHRIVRTY
IAKFGLKLNE FFQENENAWY FIRNIRKRVW EVKKDPGVFK YPVKPSEEGK SASQLYRESL
KKIIEELKRT NCSYILDKYD SYSTKEYLIK EGNLSRGAVD MIGDLLNEDS SYYLSFIESL
KNDDLFSYEK RFDEISGGFD QLPKSMHQDI AEMVHLNAQV TKIQHDAEKV RVAYQTPAKT
LSYVTADYVI VCATSRAVRR ISFEPPLPSK KAHALRSIHY KSATKIFLTC TQKFWEADGI
HGGKSTTDLP SRFIYYPNHN FTSGVGVIVA YVLADDSDFF QALDIKTSAD IVINDLSLIH
QLPKNEIQAL CYPSLIKKWS LDKYTMGALT SFTPYQFQDY SETVAAPVGR IYFAGEYTAR
VHGWLDSTIK SGLTAARDVN RASQKPSRIH LISDNQL
