OXLA_CRODM
ID OXLA_CRODM Reviewed; 498 AA.
AC K9N7B7;
DT 29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2013, sequence version 1.
DT 03-AUG-2022, entry version 25.
DE RecName: Full=L-amino acid oxidase Cdc18 {ECO:0000303|PubMed:19863078};
DE AltName: Full=CdcLAAO {ECO:0000303|PubMed:23287728};
DE Short=LAO;
DE EC=1.4.3.2 {ECO:0000269|PubMed:23287728};
DE Flags: Precursor; Fragment;
OS Crotalus durissus cumanensis (South American rattlesnake).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Crotalus.
OX NCBI_TaxID=184542;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION,
RP CATALYTIC ACTIVITY, AND 3D-STRUCTURE MODELING.
RC TISSUE=Venom, and Venom gland;
RX PubMed=23287728; DOI=10.1016/j.toxicon.2012.11.027;
RA Vargas L.J., Quintana J.C., Pereanez J.A., Nunez V., Sanz L., Calvete J.J.;
RT "Cloning and characterization of an antibacterial L-amino acid oxidase from
RT Crotalus durissus cumanensis venom.";
RL Toxicon 64:1-11(2013).
RN [2]
RP PROTEIN SEQUENCE OF 3-17, IDENTIFICATION BY MASS SPECTROMETRY, AND
RP SUBCELLULAR LOCATION.
RC TISSUE=Venom;
RX PubMed=19863078; DOI=10.1021/pr9008749;
RA Calvete J.J., Sanz L., Cid P., de la Torre P., Flores-Diaz M.,
RA Dos Santos M.C., Borges A., Bremo A., Angulo Y., Lomonte B.,
RA Alape-Giron A., Gutierrez J.M.;
RT "Snake venomics of the Central American rattlesnake Crotalus simus and the
RT South American Crotalus durissus complex points to neurotoxicity as an
RT adaptive paedomorphic trend along Crotalus dispersal in South America.";
RL J. Proteome Res. 9:528-544(2010).
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:23287728). Shows activity on L-Leu (PubMed:23287728).
CC Damages cell membranes of the Gram-positive bacteria S.aureus (MIC=8
CC ug/ml and MBC=16 ug/ml) and the Gram-negative bacteria A.baumannii
CC (MIC=16 ug/ml and MBC=32 ug/ml). This antimicrobial activity is
CC dependent on the production of hydrogen peroxyde, since it is inhibited
CC by catalase, a hydrogen peroxyde scavenger.
CC {ECO:0000269|PubMed:23287728}.
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:23287728};
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:23287728};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000250|UniProtKB:P81382};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=9.23 uM for L-Leu {ECO:0000269|PubMed:23287728};
CC Vmax=0.46 uM/min/mg enzyme for L-Leu {ECO:0000269|PubMed:23287728};
CC -!- SUBUNIT: Monomer. This is in contrast with most of its orthologs, that
CC are non-covalently linked homodimers. {ECO:0000305|PubMed:23287728}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:19863078}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000305|PubMed:19863078}.
CC -!- MISCELLANEOUS: Does not show antimicrobial activities against E.coli.
CC Does not induce cytotoxicity toward C2C12 cells (at 40 ug/ml) and
CC peripheral blood mononuclear cells (up to 200 ug/ml).
CC {ECO:0000269|PubMed:23287728}.
CC -!- SIMILARITY: Belongs to the flavin monoamine oxidase family. FIG1
CC subfamily. {ECO:0000250|UniProtKB:P56742}.
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DR EMBL; KC154267; AFY13334.1; -; mRNA.
DR AlphaFoldDB; K9N7B7; -.
DR SMR; K9N7B7; -.
DR SABIO-RK; K9N7B7; -.
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..2
FT /evidence="ECO:0000269|PubMed:19863078"
FT CHAIN 3..498
FT /note="L-amino acid oxidase Cdc18"
FT /id="PRO_0000430748"
FT BINDING 45..46
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P81382"
FT BINDING 65..66
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P81382"
FT BINDING 73
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P81382"
FT BINDING 87..90
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P81382"
FT BINDING 90
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P81382"
FT BINDING 223
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P81382"
FT BINDING 263
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P81382"
FT BINDING 374
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P81382"
FT BINDING 459
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P81382"
FT BINDING 466..471
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P81382"
FT BINDING 466..467
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P81382"
FT CARBOHYD 363
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 12..173
FT /evidence="ECO:0000250|UniProtKB:P81382"
FT DISULFID 333..414
FT /evidence="ECO:0000250|UniProtKB:P81382"
FT NON_TER 1
FT /evidence="ECO:0000303|PubMed:23287728"
SQ SEQUENCE 498 AA; 56827 MW; 766AD523DD75FF5B CRC64;
SCADDRNPLE ECFRETDYEE FLEIARNGLT VTSNPKHVVI VGAGMAGLSA AYVLAGAGHQ
VTVLEASERV GGRVRTYRKK DWYANLGPMR LPTKHRIVRE YIRKFGLQLN EFFQENENAW
YFIKNIRKRV REVKNNPGIL EYPVKPSEEG KSAAQLYVES LRKVVKELKR TNCKYILDKY
DTYSTKEYLL KEGNLSPGAV DMIGDLLNED SGYYVSFIES LKHDDIFGYE KRFDEIVGGM
DQLPTSMYEA IKEKVQVHFN ARVIEIQQND RETKVTYQTS ANEMPSVTAD YVIVCTTSRA
ARRIKFEPPL PPKKAHALRS VHYRSGTKIF LTCKRKFWED DGIRGGKSTT DLPSRFIYYP
NHNFTSGVGV IIAYGIGDDA NFFQALDFKD CADIVINDLS LIHQLPKEDI QTFCRPSMIQ
RWSLDKYAMG GITTFTPYQF QHFSEALTAP FKRIYFAGEY TAQFHGWIDS TIKSGLTAAR
DVNRASENPS GIHLSNDN
