ID   OXLA_APLDA              Reviewed;          26 AA.
AC   P86163;
DT   19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT   19-OCT-2011, sequence version 1.
DT   25-MAY-2022, entry version 17.
DE   RecName: Full=L-amino-acid oxidase {ECO:0000250|UniProtKB:P81383};
DE            Short=LAAO {ECO:0000250|UniProtKB:P81383};
DE            Short=LAO {ECO:0000250|UniProtKB:P81383};
DE            EC=1.4.3.2 {ECO:0000269|Ref.1};
DE   AltName: Full=Dactylomelin-P {ECO:0000303|PubMed:10758276};
DE   Flags: Fragment;
OS   Aplysia dactylomela (Spotted sea hare).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Heterobranchia; Euthyneura; Tectipleura; Aplysiida; Aplysioidea;
OC   Aplysiidae; Aplysia.
OX   NCBI_TaxID=144766;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP   PROPERTIES, AND SUBCELLULAR LOCATION.
RC   TISSUE=Ink {ECO:0000269|Ref.1};
RX   DOI=10.1016/j.jembe.2011.06.035;
RA   Tavares T.C.L., Nogueira V.L.R., Vasconcelos I.M., Gomes V.M., da Cunha M.,
RA   Carvalho A.F.U., Melo V.M.M.;
RT   "Further characterization and mode of action of dactylomelin-P, an
RT   antibacterial protein isolated from the ink of the sea hare Aplysia
RT   dactylomela (Rang, 1828).";
RL   J. Exp. Mar. Biol. Ecol. 0:0-0(2011).
RN   [2] {ECO:0000305}
RP   FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND LACK OF GLYCOSYLATION.
RC   TISSUE=Ink {ECO:0000269|PubMed:10758276};
RX   PubMed=10758276; DOI=10.1016/s0041-0101(99)00234-2;
RA   Melo V.M.M., Duarte A.B.G., Carvalho A.F.F.U., Siebra E.A.,
RA   Vasconcelos I.M.;
RT   "Purification of a novel antibacterial and haemagglutinating protein from
RT   the purple gland of the sea hare, Aplysia dactylomela rang, 1828.";
RL   Toxicon 38:1415-1427(2000).
RN   [3] {ECO:0000305}
RP   LACK OF GLYCOSYLATION.
RX   PubMed=16155232; DOI=10.1242/jeb.01795;
RA   Yang H., Johnson P.M., Ko K.C., Kamio M., Germann M.W., Derby C.D.,
RA   Tai P.C.;
RT   "Cloning, characterization and expression of escapin, a broadly
RT   antimicrobial FAD-containing L-amino acid oxidase from ink of the sea hare
RT   Aplysia californica.";
RL   J. Exp. Biol. 208:3609-3622(2005).
RN   [4] {ECO:0000305}
RP   SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC   TISSUE=Ink {ECO:0000269|PubMed:16354780};
RX   PubMed=16354780; DOI=10.1242/jeb.01972;
RA   Johnson P.M., Kicklighter C.E., Schmidt M., Kamio M., Yang H., Elkin D.,
RA   Michel W.C., Tai P.C., Derby C.D.;
RT   "Packaging of chemicals in the defensive secretory glands of the sea hare
RT   Aplysia californica.";
RL   J. Exp. Biol. 209:78-88(2006).
CC   -!- FUNCTION: Catalyzes the oxidative deamination of positively charged L-
CC       amino acids L-Lys and L-Arg but not of amino acids L-His, L-Asp or L-
CC       Glu. Has antibacterial activity against the Gram-positive bacterium
CC       S.aureus (MIC=15 ug/ml). This antibacterial activity is bacteriostatic
CC       in the absence of amino acids L-Lys or L-Arg but bactericidal in their
CC       presence. The antibacterial effect is largely dependent on H(2)O(2)
CC       produced in the oxidative deamination of substrates. Has
CC       hemagglutinating activity towards rabbit erythrocytes. Hemagglutinating
CC       activity is inhibited by the glycoprotein fetuin, but not by glucose,
CC       mannose, galactose, N-acetylglucosamine, N-acetylgalactosamine or
CC       sialic acid. {ECO:0000269|PubMed:10758276, ECO:0000269|Ref.1}.
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; Evidence={ECO:0000269|Ref.1};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000305|Ref.1};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.22 mM for L-Lys {ECO:0000269|Ref.1};
CC         KM=0.015 mM for L-Arg {ECO:0000269|Ref.1};
CC       pH dependence:
CC         Optimum pH is 8. More than 50% activity is retained between pH 3 and
CC         12. Inactive at pH 2. {ECO:0000269|Ref.1};
CC       Temperature dependence:
CC         Activity remains stable after 30 min at 55 degrees Celsius.
CC         {ECO:0000269|Ref.1};
CC   -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:10758276}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10758276,
CC       ECO:0000269|PubMed:16354780, ECO:0000269|Ref.1}.
CC   -!- TISSUE SPECIFICITY: Expressed by the ink gland.
CC       {ECO:0000269|PubMed:16354780}.
CC   -!- PTM: Not glycosylated. {ECO:0000269|PubMed:10758276,
CC       ECO:0000269|PubMed:16155232}.
CC   -!- SIMILARITY: Belongs to the flavin monoamine oxidase family.
CC       {ECO:0000255}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   AlphaFoldDB; P86163; -.
DR   GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR   GO; GO:0001716; F:L-amino-acid oxidase activity; IDA:UniProtKB.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   GO; GO:0042742; P:defense response to bacterium; IDA:UniProtKB.
DR   GO; GO:0035806; P:modulation of blood coagulation in another organism; IDA:UniProtKB.
PE   1: Evidence at protein level;
KW   Antibiotic; Antimicrobial; Direct protein sequencing; FAD; Flavoprotein;
KW   Hemagglutinin; Oxidoreductase; Secreted; Toxin.
FT   CHAIN           1..>26
FT                   /note="L-amino-acid oxidase"
FT                   /id="PRO_0000413471"
FT   NON_TER         26
FT                   /evidence="ECO:0000303|Ref.1"
SQ   SEQUENCE   26 AA;  2731 MW;  9B38D1C8D14C510E CRC64;
     DGVCSNRRQC NKEVCGSSYD VAIVGA