OXLA_OXYSC
ID OXLA_OXYSC Reviewed; 517 AA.
AC Q4JHE3;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 02-AUG-2005, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=L-amino-acid oxidase;
DE Short=LAAO {ECO:0000303|PubMed:16261251};
DE Short=LAO;
DE EC=1.4.3.2 {ECO:0000250|UniProtKB:P81382};
DE Flags: Precursor;
OS Oxyuranus scutellatus scutellatus (Australian taipan) (Coastal taipan).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Elapidae; Acanthophiinae; Oxyuranus.
OX NCBI_TaxID=8667;
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).
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 (By similarity).
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:16261251}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000305|PubMed:16261251}.
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; DQ088990; AAY89680.1; -; mRNA.
DR AlphaFoldDB; Q4JHE3; -.
DR SMR; Q4JHE3; -.
DR PRIDE; Q4JHE3; -.
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 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..517
FT /note="L-amino-acid oxidase"
FT /id="PRO_5000140378"
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 CARBOHYD 380
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; 59070 MW; 1509F4998BFD08A2 CRC64;
MNVFFMFSLL FLAALESCAD VRRNPLEECF READYEEFLE IARNGLKKTS NPKHVVVVGA
GMAGLSAAYV LAGAGHKVTL LEASERVGGR VHTYRNEKEG WYVNLGPMRL PERHRIIREY
IRKFGLKLNE FFQENENAWY FIRNIRKRVW EVKKDPGVFK YPVKPSEEGK SASQLYRESL
KKVIEELKRT NCSYILNKYD TYSTKEYLIK EGNLSRGAVD MIGDLLNEDS SYYLSFIESL
KSDDLFSYEK RFDEIVGGFD QLPISMYQAI AEMVHLNAQV IKIQHNAEKV RVAYQTPAKT
LSYVTADYVI VCSSSRAARR IYFEPPLPPK KAHALRSIHY KSGTKIFLTC SKKFWEADGI
HGGKSTTDLP SRFIYYPNHN FTSGVGVIVA YTISDDADFF QSLDIKTSAD IVINDLSLIH
QLPKKEIQAL CYPSMIKKWS LDKYAMGSIT SFAPYQFQDF IERVAAPVGR IYFAGEYTAR
VHGWLDSTIK SGLTAARDVN RASQKPSRRQ LSNDNEL
