ID OXLA_SISCA Reviewed; 516 AA. AC B0VXW0; DT 21-SEP-2011, integrated into UniProtKB/Swiss-Prot. DT 08-APR-2008, sequence version 1. DT 03-MAY-2023, entry version 45. DE RecName: Full=L-amino-acid oxidase; DE Short=LAAO; DE Short=LAO {ECO:0000303|PubMed:18096037}; DE EC=1.4.3.2 {ECO:0000250|UniProtKB:P81382}; DE Flags: Precursor; OS Sistrurus catenatus edwardsii (Desert massasauga) (Crotalophorus OS edwardsii). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera; OC Serpentes; Colubroidea; Viperidae; Crotalinae; Sistrurus. OX NCBI_TaxID=8762; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Venom gland; RX PubMed=18096037; DOI=10.1186/1471-2199-8-115; RA Pahari S., Mackessy S.P., Kini R.M.; RT "The venom gland transcriptome of the Desert Massasauga rattlesnake RT (Sistrurus catenatus edwardsii): towards an understanding of venom RT composition among advanced snakes (Superfamily Colubroidea)."; RL BMC Mol. Biol. 8:115-115(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. 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:18096037}. CC -!- TISSUE SPECIFICITY: Expressed by the venom gland. CC {ECO:0000305|PubMed:18096037}. 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; DQ464267; ABG26996.1; -; mRNA. DR AlphaFoldDB; B0VXW0; -. DR SMR; B0VXW0; -. 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 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 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..516 FT /note="L-amino-acid oxidase" FT /id="PRO_0000412605" 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 103..106 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000250|UniProtKB:P81382" FT BINDING 106 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P81382" FT BINDING 239 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" 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 379 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 28..189 FT /evidence="ECO:0000250|UniProtKB:P81382" FT DISULFID 349..430 FT /evidence="ECO:0000250|UniProtKB:P81382" SQ SEQUENCE 516 AA; 58569 MW; BABA9844650EB381 CRC64; MNVFFMFSLL FLAALGSCAD DRNPLEECFR ETDYEEFLEI AKNGLTATSN PKRVVIVGAG MSGLSAAYVL AGAGHQVTVL EASERVGGRV RTYRKEDWYA NLGPMRLPTK HRIVREYIKK FGLELNEFFQ ENDNAWYFIK NIRKRVQEVK NNPGLLKYPV KPSETGKSAG QLYEESLRKV VEELRSTNCK YILDKYDTYS TKEYLLKEGN LSPGAVDMIG DLLNEDSGYY VSFIESLKHD DIFGYEKRFD EIVGGMDQLP TSMYEAIKEK VQVHFNARVI EIQQNDREAT VTYQTSANEM SSVTADYVIV CTTSRAARRI KFEPPLPPKK AHALRSVHYR SGTKIFLTCT KKFWEDEGIH GGKSTTDLPS RSIYYPNHNF TSGVGVIIAY GIGDDANFFQ ALDFKDCADI VINDLSLIHQ LPKEDIQTFC HPSKIQRWSL DRYAMGGITT FTPYQFQHFS EALTAPFNRI YFAGEYTAQF HGWIDSTIKS GLTAARDVNR ASENPSGIHL SNDNEF //