OXLA_SIGCA
ID OXLA_SIGCA Reviewed; 527 AA.
AC P86810; F8S6K5;
DT 30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 19-OCT-2011, sequence version 2.
DT 03-AUG-2022, entry version 26.
DE RecName: Full=L-amino-acid oxidase {ECO:0000303|PubMed:21333741};
DE EC=1.4.3.2 {ECO:0000250|UniProtKB:Q90W54};
DE AltName: Full=Antiparasitic protein {ECO:0000303|PubMed:20117218};
DE Short=APP {ECO:0000303|PubMed:20117218};
DE AltName: Full=Serum L-amino-acid oxidase;
DE Short=SR-LAAO {ECO:0000303|PubMed:21333741};
DE Flags: Precursor;
OS Siganus canaliculatus (White-spotted spinefoot) (Chaetodon canaliculatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Siganidae; Siganus.
OX NCBI_TaxID=75042;
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 28-42; 98-118; 131-152;
RP 209-218 AND 373-382, FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP AND MASS SPECTROMETRY.
RC TISSUE=Spleen {ECO:0000269|PubMed:21333741};
RX PubMed=21333741; DOI=10.1016/j.fsi.2011.02.004;
RA Wang F., Li R., Xie M., Li A.;
RT "The serum of rabbitfish (Siganus oramin) has antimicrobial activity to
RT some pathogenic organisms and a novel serum L-amino acid oxidase is
RT isolated.";
RL Fish Shellfish Immunol. 30:1095-1108(2011).
RN [2] {ECO:0000305}
RP PROTEIN SEQUENCE OF 28-42, FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND MASS SPECTROMETRY.
RC TISSUE=Serum {ECO:0000269|PubMed:20117218};
RX PubMed=20117218; DOI=10.1016/j.fsi.2010.01.006;
RA Wang F.H., Xie M.Q., Li A.X.;
RT "A novel protein isolated from the serum of rabbitfish (Siganus oramin) is
RT lethal to Cryptocaryon irritans.";
RL Fish Shellfish Immunol. 29:32-41(2010).
CC -!- FUNCTION: Inhibits the growth of both Gram-negative and Gram-positive
CC bacteria. Displays strong antibacterial activity towards V.cholerae and
CC E.tarda. Causes deformation of the surface of S.aureus and the
CC formation of pores on the surface of E.coli. Strong antiparasitic
CC activity is seen towards C.irritans, T.brucei and I.multifiliis. Cilia
CC of treated theronts are lost and the macronucleus swells, inducing cell
CC membrane rupture and efflux of the cytoplasm.
CC {ECO:0000269|PubMed:20117218, ECO:0000269|PubMed:21333741}.
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:0000250|UniProtKB:Q90W54};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000250|UniProtKB:Q90W54};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:20117218}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:20117218,
CC ECO:0000269|PubMed:21333741}.
CC -!- TISSUE SPECIFICITY: Expression mainly observed in plasma, spleen,
CC kidney and gills with low levels detected in blood and no expression
CC detected in brain, liver, heart, muscle or intestine (at protein
CC level). {ECO:0000269|PubMed:20117218, ECO:0000269|PubMed:21333741}.
CC -!- MASS SPECTROMETRY: Mass=61739.871; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:20117218, ECO:0000269|PubMed:21333741};
CC -!- MASS SPECTROMETRY: Mass=58810.79; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:20117218, ECO:0000269|PubMed:21333741};
CC -!- SIMILARITY: Belongs to the flavin monoamine oxidase family. FIG1
CC subfamily. {ECO:0000255}.
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DR EMBL; HQ540313; ADW77183.1; -; mRNA.
DR AlphaFoldDB; P86810; -.
DR SMR; P86810; -.
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 GO; GO:0045087; P:innate immune response; 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; Direct protein sequencing; Disulfide bond; FAD;
KW Flavoprotein; Glycoprotein; Immunity; Innate immunity; Oxidoreductase;
KW Secreted; Signal.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT CHAIN 28..527
FT /note="L-amino-acid oxidase"
FT /evidence="ECO:0000269|PubMed:21333741"
FT /id="PRO_0000401107"
FT BINDING 70..71
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q90W54"
FT BINDING 90..91
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q90W54"
FT BINDING 98
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q90W54"
FT BINDING 114..117
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q90W54"
FT BINDING 117
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q90W54"
FT BINDING 288
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q90W54"
FT BINDING 403
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q90W54"
FT BINDING 485
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q90W54"
FT BINDING 492..497
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q90W54"
FT BINDING 492..493
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q90W54"
FT CARBOHYD 58
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 393
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 37..200
FT /evidence="ECO:0000250|UniProtKB:Q90W54"
SQ SEQUENCE 527 AA; 58811 MW; 856A038A55654C03 CRC64;
MDLHRAPWKS SAAAAVLLLA LFSGAAASSV EKNLAACLRD NDYDQLLQTV QDGLPHINTS
NHVVIVGAGV AGLTAAKLLQ DAGHRVTIVE ANSRIGGRVE TYRNKEEGWY ADLGAMRIPS
DHSIFRWFAK TLGVKLNPFI MDDHNTFYFV NGLLKRTYTV EANPDILNYK VRSSEKGKSA
NTLFQDALQK VKDEVEAHGC RAALMKYDKY SAKEYLKEVA GLSSEALRMI GDLLNEQSLM
YTALSEMIYD QADVNDNVQY DEVTGGTDLF PRAFLSVLDV PILLNSKVQR IRRSRDGVTV
SFKESQRSSL TDLHADMVLV TTTAKAALYM DFEPSLSIRK MEALRAVHYD SSTKIILTFS
SRFWEEDGIR GGKSITDRPS RYIYYPSHTF PANSSVGVLL ASYTWSDDSL LLQAASDEEL
KEMALRDLVK IHGERVRALC TGVVVKKWSL DPYSFGAFAL FTPYQHLEYA KELFRSEGRV
HFAGEHTAFP HAWMESAMKS AIRAATNINK QTLLNEGMNE CPAPDEL
