OXLA_BOTPC
ID OXLA_BOTPC Reviewed; 498 AA.
AC X2L4E2;
DT 29-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT 11-JUN-2014, sequence version 1.
DT 03-AUG-2022, entry version 26.
DE RecName: Full=L-amino acid oxidase {ECO:0000303|PubMed:29024770};
DE Short=Bpic-LAAO {ECO:0000303|PubMed:29024770};
DE Short=LAO;
DE EC=1.4.3.2 {ECO:0000269|PubMed:29024770};
DE Flags: Precursor; Fragment;
OS Bothrops pictus (Desert lancehead).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Bothrops.
OX NCBI_TaxID=133440;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 12-32, FUNCTION,
RP BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, CATALYTIC ACTIVITY,
RP SUBCELLULAR LOCATION, GLYCOSYLATION, AND 3D-STRUCTURE MODELING.
RC TISSUE=Venom, and Venom gland;
RX PubMed=29024770; DOI=10.1016/j.toxicon.2017.10.001;
RA Lazo F., Vivas-Ruiz D.E., Sandoval G.A., Rodriguez E.F., Kozlova E.E.G.,
RA Costal-Oliveira F., Chavez-Olortegui C., Severino R., Yarleque A.,
RA Sanchez E.F.;
RT "Biochemical, biological and molecular characterization of an L-amino acid
RT oxidase (LAAO) purified from Bothrops pictus Peruvian snake venom.";
RL Toxicon 139:74-86(2017).
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 (By similarity). This enyzme shows activity on L-Leu
CC (PubMed:29024770). This enzyme inhibits platelet aggregation in human
CC platelet rich plasma induced by ADP (IC(50)=3.2 mg/mL), and shows
CC antibacterial activities on both Gram-positive and Gram-negative
CC bacteria (P.aeruginosa, V.cholerae, S.aureus, E.faecalis and E.coli)
CC (PubMed:29024770). These two effects are due to hydrogen peroxide,
CC since they are inhibited by catalase (PubMed:29024770). It also induces
CC edema in mouse paw pads but does not show hemolytic activity
CC (PubMed:29024770). This protein may also have activities in hemorrhage,
CC and apoptosis (By similarity). {ECO:0000250|UniProtKB:P0CC17,
CC ECO:0000269|PubMed:29024770}.
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:0000269|PubMed:29024770};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-leucine + O2 = 4-methyl-2-oxopentanoate + H2O2 +
CC NH4(+); Xref=Rhea:RHEA:60996, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16240, ChEBI:CHEBI:17865, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:57427; Evidence={ECO:0000269|PubMed:29024770};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000250|UniProtKB:P81382};
CC -!- ACTIVITY REGULATION: Strongly inhibited by glutathione, and moderately
CC inhibited by PMSF, acetate iodine and glutamic acid. Is also inhibited
CC by Zn(2+) ions, but not by Ca(2+), Mg(2+) and Mn(2+).
CC {ECO:0000269|PubMed:29024770}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 7.0-10.0. {ECO:0000269|PubMed:29024770};
CC Temperature dependence:
CC Optimum temperature is 35-45 degrees Celsius.
CC {ECO:0000269|PubMed:29024770};
CC -!- SUBUNIT: Homodimer; non-covalently linked.
CC {ECO:0000305|PubMed:29024770}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:29024770}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000305|PubMed:29024770}.
CC -!- PTM: N-glycosylated. Contains 18.73% carbohydrates.
CC {ECO:0000305|PubMed:29024770}.
CC -!- SIMILARITY: Belongs to the flavin monoamine oxidase family. FIG1
CC subfamily. {ECO:0000305}.
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DR EMBL; KJ094993; AHN91985.1; -; mRNA.
DR AlphaFoldDB; X2L4E2; -.
DR SMR; X2L4E2; -.
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 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; Direct protein sequencing;
KW Disulfide bond; FAD; Flavoprotein; Glycoprotein;
KW Hemostasis impairing toxin; Oxidoreductase;
KW Platelet aggregation inhibiting toxin; Secreted; Signal; Toxin.
FT SIGNAL <1..11
FT /evidence="ECO:0000269|PubMed:29024770"
FT CHAIN 12..>498
FT /note="L-amino acid oxidase"
FT /id="PRO_0000432791"
FT BINDING 54..55
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q6TGQ9"
FT BINDING 74..78
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q6TGQ9"
FT BINDING 74..75
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P81382"
FT BINDING 82
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q6TGQ9"
FT BINDING 98..101
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q6TGQ9"
FT BINDING 101
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P81382"
FT BINDING 234
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P81382"
FT BINDING 272
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q6TGQ9"
FT BINDING 383
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P81382"
FT BINDING 468
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q6TGQ9"
FT BINDING 475..480
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P81382"
FT BINDING 475..476
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P81382"
FT BINDING 476..480
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q6TGQ9"
FT CARBOHYD 183
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 21..184
FT /evidence="ECO:0000250|UniProtKB:P81382"
FT DISULFID 342..423
FT /evidence="ECO:0000250|UniProtKB:P81382"
FT NON_TER 1
FT /evidence="ECO:0000303|PubMed:29024770"
FT NON_TER 498
FT /evidence="ECO:0000303|PubMed:29024770"
SQ SEQUENCE 498 AA; 56349 MW; D1C7C61A02C7CC4B CRC64;
SLLFLAAVGS CADDRNPLEE CFRETDYEEF LEIAKNGLST TSNPKRVVIV GAGMSGLSAA
YVLANAGHQV TVLEASERAG GRVKTYRNEK EGWYANLGPM RLPEKHRIVR EYIKKFDLRL
NEFSQENENA WYFLQNIKKR VREVNKDPGV LEYPVKPSEV GKSAGQLYEE SLRKAVEELR
RTNCSYMLNK YDTYSTKEYL LKEGNLSPGA VDMIGDLLNE DSGYYVSFIE SLKHDDIFAY
EKRFDEIVGG MDKLPTSMYQ AIQEKVHLNA RVIEIQQDVK EVTVTYQTSQ KETLSVTADY
VIVCTTSRAA RRITFEPPLP PKKAHALLSV HYRSGTKIFL TCTKKFWEDD GIHGGKSTTD
LPSRFIYYPN HNFPNGVGVI IAYGIGDDAN YFQALDFEDC GDIVINDLSL IHQLPKEEIQ
AICRPSMIQR WSLDNYAMGG ITTFTPYHFQ HFSEALTAPV DRIYFAGEYT AQAHGWIDST
IKSGLRAATD VNRASENK
