OXLA_BOTSC
ID OXLA_BOTSC Reviewed; 498 AA.
AC A0A024BTN9;
DT 29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 09-JUL-2014, sequence version 1.
DT 03-AUG-2022, entry version 23.
DE RecName: Full=L-amino acid oxidase Bs29 {ECO:0000303|PubMed:18444672};
DE AltName: Full=BsLAAO {ECO:0000303|PubMed:24875315};
DE Short=LAO;
DE EC=1.4.3.2 {ECO:0000269|PubMed:24875315};
DE Flags: Precursor; Fragment;
OS Bothriechis schlegelii (Eyelash palm pitviper).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Bothriechis.
OX NCBI_TaxID=44725;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, ACTIVITY REGULATION,
RP BIOPHYSICOCHEMICAL PROPERTIES, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION,
RP AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Venom, and Venom gland;
RX PubMed=24875315; DOI=10.1016/j.ijbiomac.2014.05.039;
RA Vargas Munoz L.J., Estrada-Gomez S., Nunez V., Sanz L., Calvete J.J.;
RT "Characterization and cDNA sequence of Bothriechis schlegeliil-amino acid
RT oxidase with antibacterial activity.";
RL Int. J. Biol. Macromol. 69:200-207(2014).
RN [2]
RP PROTEIN SEQUENCE OF 4-19, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Venom;
RX PubMed=18444672; DOI=10.1021/pr8000139;
RA Lomonte B., Escolano J., Fernandez J., Sanz L., Angulo Y., Gutierrez J.M.,
RA Calvete J.J.;
RT "Snake venomics and antivenomics of the arboreal neotropical pitvipers
RT Bothriechis lateralis and Bothriechis schlegelii.";
RL J. Proteome Res. 7:2445-2457(2008).
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 (PubMed:24875315). Shows activity on L-Leu (PubMed:24875315).
CC Damage cell membranes of the Gram-positive bacteria S.aureus (MIC=4
CC ug/ml and MBC=8 ug/ml) and the Gram-negative bacteria A.baumanni (MIC=2
CC ug/ml and MBC=4 ug/ml) (PubMed:24875315). This antibacterial activity
CC is dependent on the production of hydrogen peroxyde, since it is
CC inhibited by catalase, a hydrogen peroxyde scavenger (PubMed:24875315).
CC {ECO:0000269|PubMed:24875315}.
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:24875315};
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:24875315};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000250|UniProtKB:P81382};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=16.37 uM for L-Leu {ECO:0000269|PubMed:24875315};
CC Vmax=0.39 umol/min/mg enzyme {ECO:0000269|PubMed:24875315};
CC -!- SUBUNIT: Monomer. This is in contrast with most of its orthologs, that
CC are non-covalently linked homodimers. {ECO:0000305|PubMed:24875315}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:24875315}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000305|PubMed:24875315}.
CC -!- MISCELLANEOUS: Does not induce cytotoxicity to C2C12 cells (40 ug/ml),
CC peripheral blood mononuclear cells and to E.coli (200 ug/ml).
CC {ECO:0000269|PubMed:24875315}.
CC -!- SIMILARITY: Belongs to the flavin monoamine oxidase family. FIG1
CC subfamily. {ECO:0000305}.
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DR EMBL; KJ513472; AHZ20792.1; -; mRNA.
DR AlphaFoldDB; A0A024BTN9; -.
DR SMR; A0A024BTN9; -.
DR SABIO-RK; A0A024BTN9; -.
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: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 Pfam; PF01593; Amino_oxidase; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
PE 1: Evidence at protein level;
KW Antibiotic; Antimicrobial; Direct protein sequencing; Disulfide bond; FAD;
KW Flavoprotein; Glycoprotein; Oxidoreductase; Secreted; Signal.
FT SIGNAL <1..3
FT /evidence="ECO:0000269|PubMed:18444672"
FT CHAIN 4..>498
FT /note="L-amino acid oxidase Bs29"
FT /id="PRO_0000430747"
FT BINDING 45..46
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q6STF1"
FT BINDING 65..66
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q6STF1"
FT BINDING 73
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q6STF1"
FT BINDING 89..92
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q6STF1"
FT BINDING 92
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q6STF1"
FT BINDING 225
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q6STF1"
FT BINDING 263
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q6STF1"
FT BINDING 374
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q6STF1"
FT BINDING 459
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q6STF1"
FT BINDING 466..471
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q6STF1"
FT BINDING 466..467
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q6STF1"
FT CARBOHYD 174
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 12..175
FT /evidence="ECO:0000250|UniProtKB:Q6STF1"
FT DISULFID 333..414
FT /evidence="ECO:0000250|UniProtKB:Q6STF1"
FT NON_TER 1
FT /evidence="ECO:0000303|PubMed:24875315"
FT NON_TER 498
FT /evidence="ECO:0000303|PubMed:24875315"
SQ SEQUENCE 498 AA; 56376 MW; 9ED50FF5EA5F8031 CRC64;
SCADDRNPLE ECFQETDYEE FLEIARNGLK ATSNPKHVVI VGAGMSGLSA AYVLAGAGHQ
VTVLEASERA GGRVRTYRND KEGWYANLGP MRLPEKHRIV REYITKFGLQ LNEFSQENEN
AWYFIKNIRK RVGEVKKDPG LLQYPVKPSE EGKSAGQLYE ESLGKVVEEL KRTNCSYILD
KYDTYSTKEY LIKEGNLSPG AVDMIGDLLN EDSGYYVSFI ESLKHDNIFG YEKRFNEIVD
GMDKLPTSMY QAIEEKVRFN ARVIKIQQND NEVTVTYQTS ENEMSPVTAD YVIVCTTSRA
ARRITFEPPL PPKKAHALRS VHYRSGTKIF LTCTKKFWED DGIHGGKSTT DLPSRFVYYP
NHDFSSGSAV IMAYGIGDDA NFFQALDHKD CGDTVINDLS LIHQLTKEEI QSFCYLSKIQ
RWSLDKYAMG GITTFTPYQF QHFSEALTAP FKRIYFAGEY TAQFHGWIDS TIKSGLTAAR
DVNRASENPS GIHLSNDN
