ID A0A090N331_OSTTA Unreviewed; 483 AA.
AC A0A090N331;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Flavin amine oxidase {ECO:0000313|EMBL:CEF97408.1};
GN ORFNames=OT_ostta04g00240 {ECO:0000313|EMBL:CEF97408.1};
OS Ostreococcus tauri.
OC Eukaryota; Viridiplantae; Chlorophyta; Mamiellophyceae; Mamiellales;
OC Bathycoccaceae; Ostreococcus.
OX NCBI_TaxID=70448 {ECO:0000313|EMBL:CEF97408.1, ECO:0000313|Proteomes:UP000009170};
RN [1] {ECO:0000313|Proteomes:UP000009170}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OTTH0595 {ECO:0000313|Proteomes:UP000009170};
RX PubMed=16868079; DOI=10.1073/pnas.0604795103;
RA Derelle E., Ferraz C., Rombauts S., Rouze P., Worden A.Z., Robbens S.,
RA Partensky F., Degroeve S., Echeynie S., Cooke R., Saeys Y., Wuyts J.,
RA Jabbari K., Bowler C., Panaud O., Piegu B., Ball S.G., Ral J.-P.,
RA Bouget F.-Y., Piganeau G., De Baets B., Picard A., Delseny M., Demaille J.,
RA Van de Peer Y., Moreau H.;
RT "Genome analysis of the smallest free-living eukaryote Ostreococcus tauri
RT unveils many unique features.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:11647-11652(2006).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- PATHWAY: Amine and polyamine degradation; spermine degradation.
CC {ECO:0000256|ARBA:ARBA00004723}.
CC -!- SIMILARITY: Belongs to the flavin monoamine oxidase family.
CC {ECO:0000256|ARBA:ARBA00005995}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:CEF97408.1}.
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DR EMBL; CAID01000004; CEF97408.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A090N331; -.
DR STRING; 70448.A0A090N331; -.
DR InParanoid; A0A090N331; -.
DR OrthoDB; 63690at2759; -.
DR Proteomes; UP000009170; Chromosome 4.
DR GO; GO:0046592; F:polyamine oxidase activity; IEA:UniProt.
DR GO; GO:0006598; P:polyamine catabolic process; IEA:UniProt.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR InterPro; IPR002937; Amino_oxidase.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR001613; Flavin_amine_oxidase.
DR PANTHER; PTHR10742:SF417; AMINO_OXIDASE DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR10742; FLAVIN MONOAMINE OXIDASE; 1.
DR Pfam; PF01593; Amino_oxidase; 1.
DR PRINTS; PR00757; AMINEOXDASEF.
DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000009170}.
FT DOMAIN 53..470
FT /note="Amine oxidase"
FT /evidence="ECO:0000259|Pfam:PF01593"
SQ SEQUENCE 483 AA; 52871 MW; 2D6B1EE1228E541F CRC64;
MADASEGRDV RVRDVVVLGG GFAGLHAARC ATMVHPERVG GGGGGDDGRF RRLDVVVLEG
GDEPGGRVKV TRDLAPWDVN LGPEFVHGDE NSALKRFADA CGFATFEREW PDRYFLGDEG
VLMGADEAET KNVDVKLVHE LFDELPNAPK EGEGDLTALE WLTTRVKAPE RVIKLAENIY
ANDFCASLGK LGMRELIEEK KGWIYGEKYL ILDRPLREVA LALADGLDVR LGWEIESVDY
SRPGAVKIKR RGSNEVITAR KCIVTLPVTT LRSECPGNRV KFIPRLPAAK VRAAETIQMG
NASKVFLGFR KRLWPSDLFD VVCTNCFLPE FWITEYPKSS VAREAKSTKE AALIAETVGL
VTFFVAGDLA GELDRMPEHI VFKRAIEQLD MIFDTSCAEH VTTKKIVSWS QERLVQGAYT
HPTVNAGDAR MMLAAPVANT LFFAGEATHT GVNPCLQGAM ETGERAAAQV RASILGIGGH
SKL
//
