OXLA2_CROAD
ID OXLA2_CROAD Reviewed; 516 AA.
AC F8S0Z5; J3S821;
DT 11-JUL-2012, integrated into UniProtKB/Swiss-Prot.
DT 21-SEP-2011, sequence version 1.
DT 03-AUG-2022, entry version 40.
DE RecName: Full=L-amino-acid oxidase;
DE Short=LAAO {ECO:0000303|PubMed:21255598, ECO:0000303|PubMed:24231107};
DE Short=LAO;
DE EC=1.4.3.2 {ECO:0000250|UniProtKB:P81382};
DE Flags: Precursor;
OS Crotalus adamanteus (Eastern diamondback rattlesnake).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Crotalus.
OX NCBI_TaxID=8729;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Venom gland;
RX PubMed=21255598; DOI=10.1016/j.toxicon.2011.01.008;
RA Rokyta D.R., Wray K.P., Lemmon A.R., Lemmon E.M., Caudle S.B.;
RT "A high-throughput venom-gland transcriptome for the eastern diamondback
RT rattlesnake (Crotalus adamanteus) and evidence for pervasive positive
RT selection across toxin classes.";
RL Toxicon 57:657-671(2011).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Venom gland;
RA Rokyta D.R., Lemmon A.R., Margres M.J., Aronow K.;
RT "The venom-gland transcriptome of the eastern diamondback rattlesnake
RT (Crotalus adamanteus).";
RL BMC Genomics 13:312-312(2012).
RN [3]
RP PROTEIN SEQUENCE OF 19-27, IDENTIFICATION BY MASS SPECTROMETRY, AND
RP SUBCELLULAR LOCATION.
RC TISSUE=Venom;
RX PubMed=24231107; DOI=10.1016/j.jprot.2013.11.001;
RA Margres M.J., McGivern J.J., Wray K.P., Seavy M., Calvin K., Rokyta D.R.;
RT "Linking the transcriptome and proteome to characterize the venom of the
RT eastern diamondback rattlesnake (Crotalus adamanteus).";
RL J. Proteomics 96:145-158(2014).
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 hemolysis,
CC edema, hemorrhage, apoptosis, antibacterial and antiparasitic
CC activities, as well as regulation of platelet aggregation. Effects of
CC snake L-amino oxidases on platelets are controversial, since they
CC either induce aggregation or inhibit agonist-induced aggregation. These
CC different effects are probably due to different experimental
CC conditions. {ECO:0000250|UniProtKB:P81382}.
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:0000269|PubMed:24231107}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000305|PubMed:24231107}.
CC -!- SIMILARITY: Belongs to the flavin monoamine oxidase family. FIG1
CC subfamily. {ECO:0000305}.
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DR EMBL; HQ414099; AEJ31977.1; -; mRNA.
DR EMBL; JU173667; AFJ49193.1; -; mRNA.
DR AlphaFoldDB; F8S0Z5; -.
DR SMR; F8S0Z5; -.
DR BioCyc; MetaCyc:MON-20109; -.
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; Direct protein sequencing;
KW Disulfide bond; FAD; Flavoprotein; Glycoprotein; Hemolysis;
KW Hemostasis impairing toxin; Oxidoreductase; Secreted; Signal; Toxin.
FT SIGNAL 1..18
FT /evidence="ECO:0000269|PubMed:24231107"
FT CHAIN 19..516
FT /note="L-amino-acid oxidase"
FT /id="PRO_5000771366"
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; 58767 MW; 6CB90A49A0C015E5 CRC64;
MNVFFMFSLL FLAALGSCAH DRNPLEECFR ETDYEEFLEI AKNGLTATSN PKRVVIVGAG
MAGLSAAYVL AGAGHQVTVL EASERVGGRV RTYRKKDWYA NLGPMRLPTK HRIVREYIKK
FDLKLNEFSQ ENENAWYFIK NIRKRVREVK NNPGLLEYPV KPSEEGKSAA QLYVESLRKV
VKELKRTNCK YILDKYDTYS TKEYLLKEGN LSPGAVDMIG DLLNEDSGYY VSFIESLKHD
DIFGYEKRFD EIVGGMDQLP TSMYEAIKEK VQVHFNARVI EIQQNDREAT VTYQTSANEM
SSVTADYVIV CTTSRAARRI KFEPPLPPKK AHALRSVHYR SGTKIFLTCK KKFWEDDGIR
GGKSTTDLPS RFIYYPNHNF TSGVGVIIAY GIGDDANFFQ ALDFKDCADI VINDLSLIHQ
LPKEDIQTFC RPSMIQRWSL DKYAMGGITT FTPYQFQHFS EALTAPFKRI YFAGEYTAQF
HGWIDSTIKS GLTAARDVNR ASENPSGIHL SNDNEF
