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L-amino-acid oxidase (DRS-LAAO) (LAAO) (LAO) (EC 1.4.3.2) (Fragments)

 OXLA_DABSI              Reviewed;         407 AA.
Q4F867;
15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
19-JAN-2010, sequence version 2.
23-MAY-2018, entry version 49.
RecName: Full=L-amino-acid oxidase;
Short=DRS-LAAO;
Short=LAAO;
Short=LAO;
EC=1.4.3.2;
Flags: Fragments;
Daboia siamensis (Eastern Russel's viper) (Daboia russelii siamensis).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata;
Toxicofera; Serpentes; Colubroidea; Viperidae; Viperinae; Daboia.
NCBI_TaxID=343250;
[1]
PROTEIN SEQUENCE OF 1-15, NUCLEOTIDE SEQUENCE [MRNA] OF 16-407,
FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, SUBCELLULAR LOCATION, TISSUE
SPECIFICITY, GLYCOSYLATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
TISSUE=Venom, and Venom gland;
PubMed=19523971; DOI=10.1016/j.toxicon.2009.06.004;
Zhong S.-R., Jin Y., Wu J.-B., Jia Y.-H., Xu G.-L., Wang G.-C.,
Xiong Y.-L., Lu Q.-M.;
"Purification and characterization of a new L-amino acid oxidase from
Daboia russellii siamensis venom.";
Toxicon 54:763-771(2009).
-!- FUNCTION: Catalyzes an oxidative deamination of predominantly
hydrophobic and aromatic L-amino acids (highly active against L-
Leu followed by L-Phe and L-Ile and not active against L-Pro, L-
Asn, L-Gly, L-Ser and L-Cys), thus producing hydrogen peroxide
that may contribute to the diverse toxic effects of this enzyme.
Exhibits diverse biological activities such as antibacterial
activity (Minimal inhibitory concentrations (MIC) are 9.0 ug/ml
against S.aureus, 144.0 ug/ml against P.aeruginosa and 288.0 ug/ml
against E.coli) and inhibition of ADP- and TMVA-induced platelet
aggregation. Effects of snake L-amino oxidases on platelets are
controversial, since they either induce aggregation or inhibit
agonist-induced aggregation. These different effects are probably
due to different experimental conditions. Unlike other snake venom
L-amino acid oxidases, does not induce hemorrhage. This protein
may also induce hemolysis, edema, apoptosis and have antiparasitic
activities. {ECO:0000269|PubMed:19523971}.
-!- CATALYTIC ACTIVITY: An L-amino acid + H(2)O + O(2) = a 2-oxo acid
+ NH(3) + H(2)O(2). {ECO:0000269|PubMed:19523971}.
-!- COFACTOR:
Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
-!- BIOPHYSICOCHEMICAL PROPERTIES:
pH dependence:
Optimum pH is 8.8. {ECO:0000269|PubMed:19523971};
-!- SUBUNIT: Homodimer; non-covalently linked.
{ECO:0000269|PubMed:19523971}.
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:19523971}.
-!- TISSUE SPECIFICITY: Expressed by the venom gland.
{ECO:0000269|PubMed:19523971}.
-!- PTM: N-glycosylated. {ECO:0000305|PubMed:19523971}.
-!- SIMILARITY: Belongs to the flavin monoamine oxidase family. FIG1
subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; DQ104365; AAZ08620.1; -; mRNA.
ProteinModelPortal; Q4F867; -.
SMR; Q4F867; -.
PRIDE; Q4F867; -.
HOVERGEN; HBG005729; -.
BRENDA; 1.4.3.2; 6667.
GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
GO; GO:0001716; F:L-amino-acid oxidase activity; IDA:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
GO; GO:0042742; P:defense response to bacterium; IDA:UniProtKB.
GO; GO:0044179; P:hemolysis in other organism; IEA:UniProtKB-KW.
GO; GO:0035893; P:negative regulation of platelet aggregation in other organism; IDA:UniProtKB.
GO; GO:0055114; P:oxidation-reduction process; IDA:UniProtKB.
GO; GO:0009405; P:pathogenesis; IDA:UniProtKB.
Gene3D; 3.50.50.60; -; 2.
InterPro; IPR002937; Amino_oxidase.
InterPro; IPR036188; FAD/NAD-bd_sf.
Pfam; PF01593; Amino_oxidase; 1.
SUPFAM; SSF51905; SSF51905; 2.
1: Evidence at protein level;
Antibiotic; Antimicrobial; Apoptosis; Cytolysis;
Direct protein sequencing; Disulfide bond; FAD; Flavoprotein;
Glycoprotein; Hemolysis; Hemostasis impairing toxin; Oxidoreductase;
Platelet aggregation inhibiting toxin; Secreted; Toxin.
CHAIN <1 407 L-amino-acid oxidase.
/FTId=PRO_0000315372.
NP_BIND 385 390 FAD. {ECO:0000250}.
REGION 385 386 Substrate binding. {ECO:0000250}.
BINDING 144 144 Substrate. {ECO:0000250}.
BINDING 182 182 FAD; via amide nitrogen and carbonyl
oxygen. {ECO:0000250}.
BINDING 293 293 Substrate. {ECO:0000250}.
BINDING 378 378 FAD. {ECO:0000250}.
CARBOHYD 93 93 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 282 282 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 10 94 {ECO:0000250}.
DISULFID 252 333 {ECO:0000250}.
NON_CONS 15 16 {ECO:0000305}.
NON_TER 1 1
SEQUENCE 407 AA; 46372 MW; 8B7B22226EF561B9 CRC64;
ADDKNPLEEC FREDDHRIVR EYIRKFGLKL NEFVQETENG WYFIKNIRKR VGEVKKDPGL
LKYPVKPSEA GKSAGQLYQE SLGKAVEELK RTNCSYILNK YDTYSTKEYL IKEGNLSPGA
VDMIGDLLNE DSGYYVSFIE SLKHDDIFAY EKRFDEIVGG MDQLPTSMYR AIEESVRFKA
RVIKIQQNAE KVTVTYQTTQ KNLLLETVDY VIVCTTSRAA RRITFKPPLP PKKAHALRSV
HYRSGTKIFL TCTKKFWEDD GIQGGKSTTD LPSRFIYYPN HNFTTGVGVI IAYGIGDDAN
FFQALNLNEC ADIVFNDLSS IHQLPKKDLQ TFCYPSIIQK WSLDKYAMGA ITTFTPYQFQ
HFSEALTAPV GRIFFAGEYT ANAHGWIDST IKSGLTAARD VNRASEL


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