OXLA_PSEAU
ID OXLA_PSEAU Reviewed; 517 AA.
AC Q4JHE1;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 02-AUG-2005, sequence version 1.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=L-amino-acid oxidase;
DE Short=LAAO {ECO:0000303|PubMed:16261251};
DE Short=LAO;
DE EC=1.4.3.2;
DE Flags: Precursor;
OS Pseudechis australis (Mulga snake) (King brown snake).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Elapidae; Acanthophiinae; Pseudechis.
OX NCBI_TaxID=8670;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Venom gland;
RX PubMed=16261251; DOI=10.1007/s00018-005-5384-9;
RA St Pierre L., Woods R., Earl S.T.H., Masci P.P., Lavin M.F.;
RT "Identification and analysis of venom gland-specific genes from the coastal
RT taipan (Oxyuranus scutellatus) and related species.";
RL Cell. Mol. Life Sci. 62:2679-2693(2005).
RN [2]
RP FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
RC TISSUE=Venom;
RX PubMed=1796476; DOI=10.1016/0041-0101(91)90210-i;
RA Stiles B.G., Sexton F.W., Weinstein S.A.;
RT "Antibacterial effects of different snake venoms: purification and
RT characterization of antibacterial proteins from Pseudechis australis
RT (Australian king brown or mulga snake) venom.";
RL Toxicon 29:1129-1141(1991).
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, antiparasitic activities, as well as regulation of platelet
CC aggregation. Effects of snake L-amino oxidases on platelets are
CC controversial, since they either induce aggregation or inhibit agonist-
CC induced aggregation. These different effects are probably due to
CC different experimental conditions (By similarity). This protein has
CC antibacterial activities (PubMed:1796476).
CC {ECO:0000250|UniProtKB:P0CC17, ECO:0000269|PubMed:1796476}.
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 -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000250|UniProtKB:P81382};
CC -!- SUBUNIT: Homodimer; non-covalently linked.
CC {ECO:0000269|PubMed:1796476}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:1796476}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000305|PubMed:1796476}.
CC -!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:P81382}.
CC -!- SIMILARITY: Belongs to the flavin monoamine oxidase family. FIG1
CC subfamily. {ECO:0000305}.
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DR EMBL; DQ088992; AAY89682.1; -; mRNA.
DR AlphaFoldDB; Q4JHE1; -.
DR SMR; Q4JHE1; -.
DR PRIDE; Q4JHE1; -.
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: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 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..517
FT /note="L-amino-acid oxidase"
FT /id="PRO_5000140380"
FT BINDING 62..63
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P81382"
FT BINDING 82..83
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P81382"
FT BINDING 90
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P81382"
FT BINDING 106..109
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P81382"
FT BINDING 109
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P81382"
FT BINDING 280
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P81382"
FT BINDING 391
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P81382"
FT BINDING 476
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P81382"
FT BINDING 483..488
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P81382"
FT BINDING 483..484
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P81382"
FT CARBOHYD 191
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 29..192
FT /evidence="ECO:0000250|UniProtKB:P81382"
FT DISULFID 350..431
FT /evidence="ECO:0000250|UniProtKB:P81382"
SQ SEQUENCE 517 AA; 58744 MW; 9E0ACCD728782BE5 CRC64;
MNVFFMFSLL FLAALGSCAD DRRRPLEECF READYEEFLE IAKNGLQRTS NPKRVVVVGA
GMAGLSAAYV LAGAGHQVTL LEASERVGGR VNTYRNEKDG WYVNLGPMRL PERHRIIREY
IRKFGLELNE FIQENDNAWY FIKNIRKRVS EVKKDPGVFK YPVKPSEEGK SASQLYRESL
QKVIEELKRT NCSYILNKYD TYSTKEYLIK EGNLSPGAVD MIGDLLNEDS SYYLSFIESL
KSDDIFSYEK RFDEIVGGFD QLPRSMYQAI AEKVHLNAQV IKIQQNAEDV RVTYQTPAKT
LSYVIADYVI VCSTSRAARR IHFEPPLPPK KAHALRSIHY RSSTKIFLTC SQKFWEADGI
HGGKSTTDLP SRFIYYPNHS FTSGIGVIVA YTLADDTDFF QALDIETSAD IVINDLSLIH
QLPKEQIQAL CYPSKIQKWS LDEYAMGAIT SFTPYQFQDF FEIVAAPVGR IYFAGEYTAS
VHGWLDSTIK SGLTAARDVN LASQKPSRIQ LSNDNEL
