OXLA_VIPAA
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-AUG-2022, entry version 39.
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}.
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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:0044179; P:hemolysis in another organism; IEA:UniProtKB-KW.
DR Gene3D; 3.50.50.60; -; 1.
DR InterPro; IPR002937; Amino_oxidase.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR001613; Flavin_amine_oxidase.
DR Pfam; PF01593; Amino_oxidase; 1.
DR PRINTS; PR00757; AMINEOXDASEF.
DR SUPFAM; SSF51905; SSF51905; 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
