ID OXLA_CROAD Reviewed; 516 AA. AC O93364; DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1998, sequence version 1. DT 03-MAY-2023, entry version 106. DE RecName: Full=L-amino-acid oxidase; DE Short=LAAO {ECO:0000303|PubMed:9703950}; DE Short=LAO; DE EC=1.4.3.2 {ECO:0000269|PubMed:6067195}; DE Flags: Precursor; OS Crotalus adamanteus (Eastern diamondback rattlesnake). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera; OC Serpentes; Colubroidea; Viperidae; Crotalinae; Crotalus. OX NCBI_TaxID=8729; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 19-44 AND 106-130, AND RP SUBCELLULAR LOCATION. RC TISSUE=Venom, and Venom gland; RX PubMed=9703950; DOI=10.1006/bbrc.1998.9024; RA Raibekas A.A., Massey V.; RT "Primary structure of the snake venom L-amino acid oxidase shows high RT homology with the mouse B cell interleukin 4-induced Fig1 protein."; RL Biochem. Biophys. Res. Commun. 248:476-478(1998). RN [2] RP CATALYTIC ACTIVITY, COFACTOR, AND SUBSTRATE SPECIFICITY. RC TISSUE=Venom; RX PubMed=6067195; DOI=10.1016/s0021-9258(18)96172-7; RA Massey V., Curti B.; RT "On the reaction mechanism of Crotalus adamanteus L-amino acid oxidase."; RL J. Biol. Chem. 242:1259-1264(1967). 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:6067195). Is active on L-Arg, L-Phe, L-Met, and L-Leu CC and is weakly active on L-Val (PubMed:6067195). Exhibits diverse CC biological activities, such as hemorrhage, hemolysis, edema, apoptosis CC of vascular endothelial cells or tumor cell lines, antibacterial and CC antiparasitic activities, as well as regulation of platelet CC aggregation. Its effect on platelets is controversial, since it either CC induces aggregation or inhibits agonist-induced aggregation. These CC different effects are probably due to different experimental conditions CC (By similarity). {ECO:0000250|UniProtKB:P0CC17, CC ECO:0000269|PubMed:6067195}. 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; Evidence={ECO:0000269|PubMed:6067195}; 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:6067195}; CC -!- CATALYTIC ACTIVITY: CC Reaction=H2O + L-phenylalanine + O2 = 3-phenylpyruvate + H2O2 + NH4(+); CC Xref=Rhea:RHEA:61240, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, CC ChEBI:CHEBI:16240, ChEBI:CHEBI:18005, ChEBI:CHEBI:28938, CC ChEBI:CHEBI:58095; Evidence={ECO:0000269|PubMed:6067195}; CC -!- CATALYTIC ACTIVITY: CC Reaction=H2O + L-methionine + O2 = 4-methylsulfanyl-2-oxobutanoate + CC H2O2 + NH4(+); Xref=Rhea:RHEA:61236, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:16723, CC ChEBI:CHEBI:28938, ChEBI:CHEBI:57844; CC Evidence={ECO:0000269|PubMed:6067195}; CC -!- CATALYTIC ACTIVITY: CC Reaction=H2O + L-arginine + O2 = 5-guanidino-2-oxopentanoate + H2O2 + CC NH4(+); Xref=Rhea:RHEA:51404, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, CC ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:32682, CC ChEBI:CHEBI:58489; Evidence={ECO:0000269|PubMed:6067195}; CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000269|PubMed:6067195}; CC -!- SUBUNIT: Homodimer; non-covalently linked. CC {ECO:0000250|UniProtKB:P81382}. CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:9703950}. CC -!- TISSUE SPECIFICITY: Expressed by the venom gland. CC {ECO:0000305|PubMed:9703950}. 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; AF071564; AAC32267.1; -; mRNA. DR PIR; JE0266; JE0266. DR AlphaFoldDB; O93364; -. DR SMR; O93364; -. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0106329; F:L-phenylalaine oxidase activity; IEA:RHEA. 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 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; Secreted; Signal; Toxin. FT SIGNAL 1..18 FT /evidence="ECO:0000269|PubMed:9703950" FT CHAIN 19..516 FT /note="L-amino-acid oxidase" FT /id="PRO_0000001706" 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; 58662 MW; FDFAA77A49FDA05A CRC64; MNVFFMFSLL FLAALGSCAH DRNPLEECFR ETDYEEFLEI AKNGLTATSN PKRVVIVGAG MAGLSAAYVL AGAGHQVTVL EASERVGGRV RTYRKKDWYA NLGPMRLPTK HRIVREYIKK FDLKLNEFSQ ENENAWYFIK NIRKRVREVK NNPGLLEYPV KPSEEGKSAA QLYVESLRKV VEELRSTNCK YILDKYDTYS TKEYLLKEGN LSPGAVDMIG DLLNEDSGYY VSFIESLKHD DIFGYEKRFD EIVGGMDQLP TSMYEAIKEK VQVHFNARVI EIQQNDREAT VTYQTSANEM SSVTADYVIV CTTSRAARRI KFEPPLPPKK AHALRSVHYR SGTKIFLTCT KKFWEDDGIH GGKSTTDLPS RFIYYPNHNF TSGVGVIIAY GIGDDANFFQ ALDFKDCADI VINDLSLIHE LPKEDIQTFC HPSMIQRWSL DKYAMGGITT FTPYQFQHFS EALTAPFKRI YFAGEYTAQF HGWIDSTIKS GLTAARDVNR ASENPSGIHL SNDNEF //