OXLA_TRIST
ID OXLA_TRIST Reviewed; 516 AA.
AC Q6WP39; Q7T062;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=L-amino-acid oxidase;
DE Short=LAAO;
DE Short=TSV-LAO {ECO:0000303|PubMed:12963032};
DE EC=1.4.3.2 {ECO:0000250|UniProtKB:P81382};
DE Flags: Precursor;
OS Trimeresurus stejnegeri (Chinese green tree viper) (Viridovipera
OS stejnegeri).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Trimeresurus.
OX NCBI_TaxID=39682;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBUNIT, GLYCOSYLATION, IDENTIFICATION BY MASS
RP SPECTROMETRY, AND SUBCELLULAR LOCATION.
RC TISSUE=Venom, and Venom gland;
RX PubMed=12963032; DOI=10.1016/j.bbrc.2003.08.044;
RA Zhang Y.-J., Wang J.-H., Lee W.-H., Wang Q., Liu H., Zheng Y.-T., Zhang Y.;
RT "Molecular characterization of Trimeresurus stejnegeri venom L-amino acid
RT oxidase with potential anti-HIV activity.";
RL Biochem. Biophys. Res. Commun. 309:598-604(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Venom gland;
RA Wang J., Huang Q., Teng M., Niu L.;
RT "Purification, cloning and characterization of the L-amino acid oxidase in
RT snake Trimeresurus stejnegeri.";
RL Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
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 Displays dose-dependent inhibition on HIV-1 infection and replication
CC (PubMed:12963032). {ECO:0000250|UniProtKB:P0CC17,
CC ECO:0000269|PubMed:12963032}.
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:0000269|PubMed:12963032}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:12963032}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000305|PubMed:12963032}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:12963032}.
CC -!- SIMILARITY: Belongs to the flavin monoamine oxidase family. FIG1
CC subfamily. {ECO:0000305}.
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DR EMBL; AY277739; AAQ56232.1; -; mRNA.
DR EMBL; AY338966; AAQ16182.1; -; mRNA.
DR AlphaFoldDB; Q6WP39; -.
DR SMR; Q6WP39; -.
DR BRENDA; 1.4.3.2; 7401.
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 Pfam; PF01593; Amino_oxidase; 1.
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..516
FT /note="L-amino-acid oxidase"
FT /id="PRO_0000273572"
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 105..108
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P81382"
FT BINDING 108
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P81382"
FT BINDING 241
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|UniProtKB:P81382"
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"
FT BINDING 481..486
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P81382"
FT BINDING 481..482
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P81382"
FT BINDING 482..487
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 482..483
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CARBOHYD 190
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 379
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 28..191
FT /evidence="ECO:0000250|UniProtKB:P81382"
FT DISULFID 349..430
FT /evidence="ECO:0000250|UniProtKB:P81382"
FT CONFLICT 16
FT /note="G -> E (in Ref. 2; AAQ16182)"
FT /evidence="ECO:0000305"
FT CONFLICT 53
FT /note="H -> R (in Ref. 2; AAQ16182)"
FT /evidence="ECO:0000305"
FT CONFLICT 73
FT /note="A -> T (in Ref. 2; AAQ16182)"
FT /evidence="ECO:0000305"
FT CONFLICT 181
FT /note="K -> E (in Ref. 2; AAQ16182)"
FT /evidence="ECO:0000305"
FT CONFLICT 294
FT /note="H -> Q (in Ref. 2; AAQ16182)"
FT /evidence="ECO:0000305"
FT CONFLICT 315
FT /note="R -> G (in Ref. 2; AAQ16182)"
FT /evidence="ECO:0000305"
FT CONFLICT 354
FT /note="R -> W (in Ref. 2; AAQ16182)"
FT /evidence="ECO:0000305"
FT CONFLICT 514
FT /note="D -> N (in Ref. 2; AAQ16182)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 516 AA; 58601 MW; FB5AC0BC171B9288 CRC64;
MNVFFMFSLL FLAALGSCAD DRNPLEECFR ETDYEEFLEI ARNGLKATSN PKHVVIVGAG
MSGLSAAYVL AGAGHEVTVL EASERAGGRV RTYRNDEEGW YANLGPMRLP EKHRIVREYI
RKFNLQLNEF SQENDNAWHF VKNIRKTVGE VKKDPGVLKY PVKPSEEGKS AEQLYEESLR
KVEKELKRTN CSYILNKYDT YSTKEYLIKE GNLSPGAVDM IGDLMNEDAG YYVSFIESMK
HDDIFAYEKR FDEIVDGMDK LPTSMYRAIE EKVHFNAQVI KIQKNAEEVT VTYHTPEKDT
SFVTADYVIV CTTSRAARRI KFEPPLPLKK AHALRSVHYR SGTKIFLTCT KKFREDEGIH
GGKSTTDLPS RFIYYPNHNF TSGVGVIIAY GIGDDANFFQ ALDLKDCGDI VINDLSLIHQ
LPREEIQTFC YPSMIQKWSL DKYAMGGITT FTPYQFQHFS EALTSHVDRI YFAGEYTAHA
HGWIDSSIKS GLTAARDVNR ASENPSGIHL SNDDEL
