ID OXLA_GLOBL Reviewed; 504 AA. AC Q90W54; DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2001, sequence version 1. DT 03-MAY-2023, entry version 87. DE RecName: Full=L-amino-acid oxidase; DE Short=LAAO; DE Short=M-LAO {ECO:0000303|PubMed:11341935}; DE EC=1.4.3.2 {ECO:0000269|PubMed:11341935}; DE Flags: Precursor; OS Gloydius blomhoffii (Mamushi) (Agkistrodon halys blomhoffi). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera; OC Serpentes; Colubroidea; Viperidae; Crotalinae; Gloydius. OX NCBI_TaxID=242054; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 19-52; 62-104; 226-257; RP 266-299 AND 435-443, FUNCTION, SUBCELLULAR LOCATION, AND CATALYTIC RP ACTIVITY. RC TISSUE=Venom, and Venom gland; RX PubMed=11341935; DOI=10.1016/s0167-4838(00)00229-6; RA Takatsuka H., Sakurai Y., Yoshioka A., Kokubo T., Usami Y., Suzuki M., RA Matsui T., Titani K., Yagi H., Matsumoto M., Fujimura Y.; RT "Molecular characterization of L-amino acid oxidase from Agkistrodon halys RT blomhoffii with special reference to platelet aggregation."; RL Biochim. Biophys. Acta 1544:267-277(2001). RN [2] RP FUNCTION, AND SUBUNIT. RC TISSUE=Venom; RX PubMed=8694800; DOI=10.1006/bbrc.1996.0996; RA Suhr S.M., Kim D.S.; RT "Identification of the snake venom substance that induces apoptosis."; RL Biochem. Biophys. Res. Commun. 224:134-139(1996). 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:11341935). Shows activity on L-Leu (PubMed:11341935). CC Exhibits diverse biological activities, such as apoptosis, and CC inhibition of agonist- and shear stress-induced platelet aggregation CC (SIPA). Effects of snake L-amino oxidases on platelets are CC controversial, since they either induce aggregation or inhibit agonist- CC induced aggregation. These different effects are probably due to CC different experimental conditions. This protein may also induce CC hemorrhage, hemolysis, edema, antibacterial and antiparasitic CC activities. {ECO:0000269|PubMed:11341935, ECO:0000269|PubMed:8694800}. 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:11341935}; 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:11341935}; CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000250|UniProtKB:P81382}; CC -!- SUBUNIT: Homodimer; non-covalently linked. CC {ECO:0000269|PubMed:8694800}. CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:11341935}. CC -!- TISSUE SPECIFICITY: Expressed by the venom gland. CC {ECO:0000305|PubMed:11341935}. 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; AB072392; BAB69450.1; -; mRNA. DR AlphaFoldDB; Q90W54; -. DR SMR; Q90W54; -. DR BRENDA; 1.4.3.2; 194. 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 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 inhibiting toxin; Secreted; Signal; Toxin. FT SIGNAL 1..18 FT /evidence="ECO:0000269|PubMed:11341935" FT CHAIN 19..504 FT /note="L-amino-acid oxidase" FT /id="PRO_5000049916" FT BINDING 61..62 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000250|UniProtKB:P81382" FT BINDING 81..82 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000250|UniProtKB:P81382" FT BINDING 89 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000250|UniProtKB:P81382" FT BINDING 105..108 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000250|UniProtKB:P81382" FT BINDING 108 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P81382" FT BINDING 241 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P81382" FT BINDING 279 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000250|UniProtKB:P81382" FT BINDING 390 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P81382" FT BINDING 475 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000250|UniProtKB:P81382" FT BINDING 482..487 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000250|UniProtKB:P81382" FT BINDING 482..483 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P81382" FT CARBOHYD 190 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 379 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 28..191 FT /evidence="ECO:0000250|UniProtKB:P81382" FT DISULFID 349..430 FT /evidence="ECO:0000250|UniProtKB:P81382" SQ SEQUENCE 504 AA; 57092 MW; 17F57B46E646F12A CRC64; MNVFFMFSLL FLAALGSCAD DRNPLEECFR ETDYEEFLEI ARNGLKATSN PKHVVIVGAG MSGLSAAYVL SGAGHQVTVL EASERAGGRV RTYRNDKEGW YANLGPMRLP EKHRIVREYI RKFGLQLNEF SQENDNAWYF IKNIRKRVGE VKKDPGVLKY PVKPSEEGKS AGQLYEESLG KVVEELKRTN CSYILNKYDT YSTKEYLLKE GNLSPGAVDM IGDLMNEDSG YYVSFPESLR HDDIFAYEKR FDEIVGGMDK LPTSMYRAIE EKVHLNAQVI KIQKNAEKVT VVYQTPAKEM ASVTADYVIV CTTSRATRRI KFEPPLPPKK AHALRSVHYR SGTKIFLTCT KKFWEDEGIH GGKSTTDLPS RFIYYPNHNF TSGVGVIIAY GIGDDANFFQ ALDFKDCADI VINDLSLIHQ LPREEIQTFC YPSMIQKWSL DKYAMGGITT FTPYQFQHFS EPLTASVDRI YFAGEHTAEA HGWIDSTIKS GLRAARDVNR ASEQ //