ID OXLA_OXYSC Reviewed; 517 AA. AC Q4JHE3; DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot. DT 02-AUG-2005, sequence version 1. DT 03-MAY-2023, entry version 79. DE RecName: Full=L-amino-acid oxidase; DE Short=LAAO {ECO:0000303|PubMed:16261251}; DE Short=LAO; DE EC=1.4.3.2 {ECO:0000250|UniProtKB:P81382}; DE Flags: Precursor; OS Oxyuranus scutellatus scutellatus (Australian taipan) (Coastal taipan). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera; OC Serpentes; Colubroidea; Elapidae; Acanthophiinae; Oxyuranus. OX NCBI_TaxID=8667; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Venom gland; RX PubMed=16261251; DOI=10.1007/s00018-005-5384-9; RA St Pierre L., Woods R., Earl S.T.H., Masci P.P., Lavin M.F.; RT "Identification and analysis of venom gland-specific genes from the coastal RT taipan (Oxyuranus scutellatus) and related species."; RL Cell. Mol. Life Sci. 62:2679-2693(2005). 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:16261251}. CC -!- TISSUE SPECIFICITY: Expressed by the venom gland. CC {ECO:0000305|PubMed:16261251}. 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; DQ088990; AAY89680.1; -; mRNA. DR AlphaFoldDB; Q4JHE3; -. DR SMR; Q4JHE3; -. 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_5000140378" 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; 59070 MW; 1509F4998BFD08A2 CRC64; MNVFFMFSLL FLAALESCAD VRRNPLEECF READYEEFLE IARNGLKKTS NPKHVVVVGA GMAGLSAAYV LAGAGHKVTL LEASERVGGR VHTYRNEKEG WYVNLGPMRL PERHRIIREY IRKFGLKLNE FFQENENAWY FIRNIRKRVW EVKKDPGVFK YPVKPSEEGK SASQLYRESL KKVIEELKRT NCSYILNKYD TYSTKEYLIK EGNLSRGAVD MIGDLLNEDS SYYLSFIESL KSDDLFSYEK RFDEIVGGFD QLPISMYQAI AEMVHLNAQV IKIQHNAEKV RVAYQTPAKT LSYVTADYVI VCSSSRAARR IYFEPPLPPK KAHALRSIHY KSGTKIFLTC SKKFWEADGI HGGKSTTDLP SRFIYYPNHN FTSGVGVIVA YTISDDADFF QSLDIKTSAD IVINDLSLIH QLPKKEIQAL CYPSMIKKWS LDKYAMGSIT SFAPYQFQDF IERVAAPVGR IYFAGEYTAR VHGWLDSTIK SGLTAARDVN RASQKPSRRQ LSNDNEL //