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-MAY-2023, entry version 61. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; EF080832; ABN72539.1; -; mRNA. DR AlphaFoldDB; A8QL51; -. DR SMR; 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: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 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 //