ID OXLA_TRIST Reviewed; 516 AA. AC Q6WP39; Q7T062; DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2004, sequence version 1. DT 03-MAY-2023, entry version 80. DE RecName: Full=L-amino-acid oxidase; DE Short=LAAO; DE Short=TSV-LAO {ECO:0000303|PubMed:12963032}; DE EC=1.4.3.2 {ECO:0000250|UniProtKB:P81382}; DE Flags: Precursor; OS Trimeresurus stejnegeri (Chinese green tree viper) (Viridovipera OS stejnegeri). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera; OC Serpentes; Colubroidea; Viperidae; Crotalinae; Trimeresurus. OX NCBI_TaxID=39682; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], SUBUNIT, GLYCOSYLATION, IDENTIFICATION BY MASS RP SPECTROMETRY, AND SUBCELLULAR LOCATION. RC TISSUE=Venom, and Venom gland; RX PubMed=12963032; DOI=10.1016/j.bbrc.2003.08.044; RA Zhang Y.-J., Wang J.-H., Lee W.-H., Wang Q., Liu H., Zheng Y.-T., Zhang Y.; RT "Molecular characterization of Trimeresurus stejnegeri venom L-amino acid RT oxidase with potential anti-HIV activity."; RL Biochem. Biophys. Res. Commun. 309:598-604(2003). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Venom gland; RA Wang J., Huang Q., Teng M., Niu L.; RT "Purification, cloning and characterization of the L-amino acid oxidase in RT snake Trimeresurus stejnegeri."; RL Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases. 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 Displays dose-dependent inhibition on HIV-1 infection and replication CC (PubMed:12963032). {ECO:0000250|UniProtKB:P0CC17, CC ECO:0000269|PubMed:12963032}. 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:0000269|PubMed:12963032}. CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:12963032}. CC -!- TISSUE SPECIFICITY: Expressed by the venom gland. CC {ECO:0000305|PubMed:12963032}. CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:12963032}. 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; AY277739; AAQ56232.1; -; mRNA. DR EMBL; AY338966; AAQ16182.1; -; mRNA. DR AlphaFoldDB; Q6WP39; -. DR SMR; Q6WP39; -. DR BRENDA; 1.4.3.2; 7401. 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; -; 2. 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 PANTHER; PTHR10742:SF235; AMINE OXIDASE; 1. DR PANTHER; PTHR10742; FLAVIN MONOAMINE OXIDASE; 1. DR Pfam; PF01593; Amino_oxidase; 1. 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; 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..516 FT /note="L-amino-acid oxidase" FT /id="PRO_0000273572" 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" FT BINDING 481..486 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000250|UniProtKB:P81382" FT BINDING 481..482 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P81382" FT BINDING 482..487 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000250" FT BINDING 482..483 FT /ligand="substrate" FT /evidence="ECO:0000250" 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" FT CONFLICT 16 FT /note="G -> E (in Ref. 2; AAQ16182)" FT /evidence="ECO:0000305" FT CONFLICT 53 FT /note="H -> R (in Ref. 2; AAQ16182)" FT /evidence="ECO:0000305" FT CONFLICT 73 FT /note="A -> T (in Ref. 2; AAQ16182)" FT /evidence="ECO:0000305" FT CONFLICT 181 FT /note="K -> E (in Ref. 2; AAQ16182)" FT /evidence="ECO:0000305" FT CONFLICT 294 FT /note="H -> Q (in Ref. 2; AAQ16182)" FT /evidence="ECO:0000305" FT CONFLICT 315 FT /note="R -> G (in Ref. 2; AAQ16182)" FT /evidence="ECO:0000305" FT CONFLICT 354 FT /note="R -> W (in Ref. 2; AAQ16182)" FT /evidence="ECO:0000305" FT CONFLICT 514 FT /note="D -> N (in Ref. 2; AAQ16182)" FT /evidence="ECO:0000305" SQ SEQUENCE 516 AA; 58601 MW; FB5AC0BC171B9288 CRC64; MNVFFMFSLL FLAALGSCAD DRNPLEECFR ETDYEEFLEI ARNGLKATSN PKHVVIVGAG MSGLSAAYVL AGAGHEVTVL EASERAGGRV RTYRNDEEGW YANLGPMRLP EKHRIVREYI RKFNLQLNEF SQENDNAWHF VKNIRKTVGE VKKDPGVLKY PVKPSEEGKS AEQLYEESLR KVEKELKRTN CSYILNKYDT YSTKEYLIKE GNLSPGAVDM IGDLMNEDAG YYVSFIESMK HDDIFAYEKR FDEIVDGMDK LPTSMYRAIE EKVHFNAQVI KIQKNAEEVT VTYHTPEKDT SFVTADYVIV CTTSRAARRI KFEPPLPLKK AHALRSVHYR SGTKIFLTCT KKFREDEGIH GGKSTTDLPS RFIYYPNHNF TSGVGVIIAY GIGDDANFFQ ALDLKDCGDI VINDLSLIHQ LPREEIQTFC YPSMIQKWSL DKYAMGGITT FTPYQFQHFS EALTSHVDRI YFAGEYTAHA HGWIDSSIKS GLTAARDVNR ASENPSGIHL SNDDEL //