OXLA_SISCA
ID OXLA_SISCA Reviewed; 516 AA.
AC B0VXW0;
DT 21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 42.
DE RecName: Full=L-amino-acid oxidase;
DE Short=LAAO;
DE Short=LAO {ECO:0000303|PubMed:18096037};
DE EC=1.4.3.2 {ECO:0000250|UniProtKB:P81382};
DE Flags: Precursor;
OS Sistrurus catenatus edwardsii (Desert massasauga) (Crotalophorus
OS edwardsii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Sistrurus.
OX NCBI_TaxID=8762;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Venom gland;
RX PubMed=18096037; DOI=10.1186/1471-2199-8-115;
RA Pahari S., Mackessy S.P., Kini R.M.;
RT "The venom gland transcriptome of the Desert Massasauga rattlesnake
RT (Sistrurus catenatus edwardsii): towards an understanding of venom
RT composition among advanced snakes (Superfamily Colubroidea).";
RL BMC Mol. Biol. 8:115-115(2007).
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:0000250|UniProtKB:P81382};
CC -!- SUBUNIT: Homodimer; non-covalently linked.
CC {ECO:0000250|UniProtKB:P81382}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:18096037}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000305|PubMed:18096037}.
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; DQ464267; ABG26996.1; -; mRNA.
DR AlphaFoldDB; B0VXW0; -.
DR SMR; B0VXW0; -.
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 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..516
FT /note="L-amino-acid oxidase"
FT /id="PRO_0000412605"
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 103..106
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P81382"
FT BINDING 106
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P81382"
FT BINDING 239
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"
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|UniProtKB:P81382"
FT BINDING 482..487
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P81382"
FT BINDING 482..483
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P81382"
FT CARBOHYD 379
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 28..189
FT /evidence="ECO:0000250|UniProtKB:P81382"
FT DISULFID 349..430
FT /evidence="ECO:0000250|UniProtKB:P81382"
SQ SEQUENCE 516 AA; 58569 MW; BABA9844650EB381 CRC64;
MNVFFMFSLL FLAALGSCAD DRNPLEECFR ETDYEEFLEI AKNGLTATSN PKRVVIVGAG
MSGLSAAYVL AGAGHQVTVL EASERVGGRV RTYRKEDWYA NLGPMRLPTK HRIVREYIKK
FGLELNEFFQ ENDNAWYFIK NIRKRVQEVK NNPGLLKYPV KPSETGKSAG QLYEESLRKV
VEELRSTNCK YILDKYDTYS TKEYLLKEGN LSPGAVDMIG DLLNEDSGYY VSFIESLKHD
DIFGYEKRFD EIVGGMDQLP TSMYEAIKEK VQVHFNARVI EIQQNDREAT VTYQTSANEM
SSVTADYVIV CTTSRAARRI KFEPPLPPKK AHALRSVHYR SGTKIFLTCT KKFWEDEGIH
GGKSTTDLPS RSIYYPNHNF TSGVGVIIAY GIGDDANFFQ ALDFKDCADI VINDLSLIHQ
LPKEDIQTFC HPSKIQRWSL DRYAMGGITT FTPYQFQHFS EALTAPFNRI YFAGEYTAQF
HGWIDSTIKS GLTAARDVNR ASENPSGIHL SNDNEF
