ID OXLA_VIPAA Reviewed; 484 AA. AC P0DI84; DT 21-SEP-2011, integrated into UniProtKB/Swiss-Prot. DT 21-SEP-2011, sequence version 1. DT 03-MAY-2023, entry version 42. DE RecName: Full=L-amino-acid oxidase; DE Short=LAO; DE Short=VAA-LAAO I {ECO:0000303|PubMed:18931435}; DE EC=1.4.3.2 {ECO:0000250|UniProtKB:P81382}; OS Vipera ammodytes ammodytes (Western sand viper). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera; OC Serpentes; Colubroidea; Viperidae; Viperinae; Vipera. OX NCBI_TaxID=8705; RN [1] RP IDENTIFICATION BY MASS SPECTROMETRY, CRYSTALLIZATION, AND SUBCELLULAR RP LOCATION. RC TISSUE=Venom; RX PubMed=18931435; DOI=10.1107/s1744309108027036; RA Georgieva D., Kardas A., Buck F., Perbandt M., Betzel C.; RT "Isolation, crystallization and preliminary X-ray diffraction analysis of RT L-amino-acid oxidase from Vipera ammodytes ammodytes venom."; RL Acta Crystallogr. F 64:918-921(2008). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY. RC TISSUE=Venom; RX PubMed=18257516; DOI=10.1021/pr070376c; RA Georgieva D., Risch M., Kardas A., Buck F., von Bergen M., Betzel C.; RT "Comparative analysis of the venom proteomes of Vipera ammodytes ammodytes RT and Vipera ammodytes meridionalis."; RL J. Proteome Res. 7:866-886(2008). RN [3] RP X-RAY CRYSTALLOGRAPHY (2.57 ANGSTROMS) IN COMPLEX WITH FAD AND ZINC IONS, RP COFACTOR, SUBUNIT, DISULFIDE BONDS, AND GLYCOSYLATION AT ASN-170. RC TISSUE=Venom; RX PubMed=20938508; DOI=10.1039/c0mb00101e; RA Georgieva D., Murakami M., Perband M., Arni R., Betzel C.; RT "The structure of a native L-amino acid oxidase, the major component of the RT Vipera ammodytes ammodytes venomic, reveals dynamic active site and RT quaternary structure stabilization by divalent ions."; RL Mol. Biosyst. 7:379-384(2011). 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:0000269|PubMed:20938508}; CC -!- SUBUNIT: Homodimer; non-covalently linked. CC {ECO:0000269|PubMed:20938508}. CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:18931435}. CC -!- TISSUE SPECIFICITY: Expressed by the venom gland. CC {ECO:0000305|PubMed:18931435}. 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 PDB; 3KVE; X-ray; 2.57 A; A/B/C/D=1-484. DR PDBsum; 3KVE; -. DR AlphaFoldDB; P0DI84; -. DR SMR; P0DI84; -. DR iPTMnet; P0DI84; -. DR EvolutionaryTrace; P0DI84; -. 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:0046872; F:metal ion binding; IEA:UniProtKB-KW. 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 3D-structure; Antibiotic; Antimicrobial; Apoptosis; Cytolysis; KW Disulfide bond; FAD; Flavoprotein; Glycoprotein; Hemolysis; KW Hemostasis impairing toxin; Metal-binding; Oxidoreductase; Secreted; Toxin; KW Zinc. FT CHAIN 1..484 FT /note="L-amino-acid oxidase" FT /id="PRO_0000412591" FT BINDING 41..42 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000269|PubMed:20938508, FT ECO:0007744|PDB:3KVE" FT BINDING 61..62 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000269|PubMed:20938508, FT ECO:0007744|PDB:3KVE" FT BINDING 69 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000269|PubMed:20938508, FT ECO:0007744|PDB:3KVE" FT BINDING 73 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000269|PubMed:20938508, FT ECO:0007744|PDB:3KVE" FT BINDING 85..88 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000269|PubMed:20938508, FT ECO:0007744|PDB:3KVE" FT BINDING 88 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P81382" FT BINDING 221 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P81382" FT BINDING 259 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000269|PubMed:20938508, FT ECO:0007744|PDB:3KVE" FT BINDING 277 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000269|PubMed:20938508, FT ECO:0007744|PDB:3KVE" FT BINDING 370 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P81382" FT BINDING 455 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000269|PubMed:20938508, FT ECO:0007744|PDB:3KVE" FT BINDING 462..467 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000269|PubMed:20938508, FT ECO:0007744|PDB:3KVE" FT BINDING 462..463 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P81382" FT CARBOHYD 170 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:20938508, FT ECO:0007744|PDB:3KVE" FT DISULFID 8..171 FT /evidence="ECO:0000269|PubMed:20938508" FT DISULFID 329..410 FT /evidence="ECO:0000269|PubMed:20938508" FT HELIX 6..9 FT /evidence="ECO:0007829|PDB:3KVE" FT HELIX 14..23 FT /evidence="ECO:0007829|PDB:3KVE" FT STRAND 33..37 FT /evidence="ECO:0007829|PDB:3KVE" FT HELIX 41..52 FT /evidence="ECO:0007829|PDB:3KVE" FT STRAND 56..60 FT /evidence="ECO:0007829|PDB:3KVE" FT STRAND 62..67 FT /evidence="ECO:0007829|PDB:3KVE" FT STRAND 72..75 FT /evidence="ECO:0007829|PDB:3KVE" FT TURN 76..79 FT /evidence="ECO:0007829|PDB:3KVE" FT STRAND 80..85 FT /evidence="ECO:0007829|PDB:3KVE" FT HELIX 94..102 FT /evidence="ECO:0007829|PDB:3KVE" FT STRAND 107..110 FT /evidence="ECO:0007829|PDB:3KVE" FT STRAND 117..121 FT /evidence="ECO:0007829|PDB:3KVE" FT STRAND 124..127 FT /evidence="ECO:0007829|PDB:3KVE" FT HELIX 128..133 FT /evidence="ECO:0007829|PDB:3KVE" FT HELIX 135..138 FT /evidence="ECO:0007829|PDB:3KVE" FT HELIX 144..146 FT /evidence="ECO:0007829|PDB:3KVE" FT HELIX 151..158 FT /evidence="ECO:0007829|PDB:3KVE" FT HELIX 160..166 FT /evidence="ECO:0007829|PDB:3KVE" FT HELIX 171..177 FT /evidence="ECO:0007829|PDB:3KVE" FT HELIX 178..180 FT /evidence="ECO:0007829|PDB:3KVE" FT HELIX 183..189 FT /evidence="ECO:0007829|PDB:3KVE" FT HELIX 195..204 FT /evidence="ECO:0007829|PDB:3KVE" FT HELIX 208..210 FT /evidence="ECO:0007829|PDB:3KVE" FT HELIX 215..225 FT /evidence="ECO:0007829|PDB:3KVE" FT STRAND 231..234 FT /evidence="ECO:0007829|PDB:3KVE" FT HELIX 240..248 FT /evidence="ECO:0007829|PDB:3KVE" FT HELIX 249..252 FT /evidence="ECO:0007829|PDB:3KVE" FT STRAND 253..256 FT /evidence="ECO:0007829|PDB:3KVE" FT STRAND 258..264 FT /evidence="ECO:0007829|PDB:3KVE" FT STRAND 269..274 FT /evidence="ECO:0007829|PDB:3KVE" FT STRAND 276..278 FT /evidence="ECO:0007829|PDB:3KVE" FT STRAND 281..290 FT /evidence="ECO:0007829|PDB:3KVE" FT HELIX 294..297 FT /evidence="ECO:0007829|PDB:3KVE" FT STRAND 300..304 FT /evidence="ECO:0007829|PDB:3KVE" FT HELIX 308..316 FT /evidence="ECO:0007829|PDB:3KVE" FT STRAND 322..331 FT /evidence="ECO:0007829|PDB:3KVE" FT HELIX 333..337 FT /evidence="ECO:0007829|PDB:3KVE" FT STRAND 341..348 FT /evidence="ECO:0007829|PDB:3KVE" FT STRAND 352..354 FT /evidence="ECO:0007829|PDB:3KVE" FT STRAND 365..372 FT /evidence="ECO:0007829|PDB:3KVE" FT HELIX 373..380 FT /evidence="ECO:0007829|PDB:3KVE" FT HELIX 384..399 FT /evidence="ECO:0007829|PDB:3KVE" FT HELIX 403..409 FT /evidence="ECO:0007829|PDB:3KVE" FT STRAND 410..417 FT /evidence="ECO:0007829|PDB:3KVE" FT HELIX 418..420 FT /evidence="ECO:0007829|PDB:3KVE" FT TURN 422..424 FT /evidence="ECO:0007829|PDB:3KVE" FT STRAND 425..429 FT /evidence="ECO:0007829|PDB:3KVE" FT HELIX 435..444 FT /evidence="ECO:0007829|PDB:3KVE" FT STRAND 450..452 FT /evidence="ECO:0007829|PDB:3KVE" FT HELIX 455..457 FT /evidence="ECO:0007829|PDB:3KVE" FT STRAND 458..462 FT /evidence="ECO:0007829|PDB:3KVE" FT HELIX 464..481 FT /evidence="ECO:0007829|PDB:3KVE" SQ SEQUENCE 484 AA; 54748 MW; FF2BBFB0EB5D1C47 CRC64; DRNPLEECFR ETDYEEFLEI ARNGLKKTSN PKHVVVVGAG MSGLSAAYVL AGAGHKVTVL EASERAGGRV RTHRNSKEGW YANLGPMRIP EKHRIVREYI RKFGLNLNEF SQENDNAWYF IKNIRKRVGE VNKDPGLLKY PVKPSEEGKS AGQLYEESLG SAVKDLKRTN CSYILNKYDT YSTKEYLIKE GNLSPGAVDM IGDLLNEDSG YYVSFIESLK HDDIFAYEKR FDEIVGGMDQ LPTSMYRAIE EKVKFNARVI KIQQNANQVT VTYQTPEKDT SSNTADYVIV CTTSRAARRI QFEPPLPPKK QHALRSVHYR SGTKIFLTCS SKFWEDDGIH GGKSTTDLPS RFIYYPNHNF STGVGVIIAY GIGDDANFFQ ALKFKDCADI VFNDLSLIHQ LPKEEIQSFC YPSMIQKWSL DKYAMGAITT FTPYQFQRFS EALTAPQGRI FFAGEYTAEA HGWIDSTIKS GLTAARDVNR ASEQ //