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Database: UniProt
Entry: S8E4F7_9LAMI
LinkDB: S8E4F7_9LAMI
Original site: S8E4F7_9LAMI 
ID   S8E4F7_9LAMI            Unreviewed;       476 AA.
AC   S8E4F7;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=Amine oxidase domain-containing protein {ECO:0000259|Pfam:PF01593};
DE   Flags: Fragment;
GN   ORFNames=M569_07574 {ECO:0000313|EMBL:EPS67202.1};
OS   Genlisea aurea.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Lamiales; Lentibulariaceae; Genlisea.
OX   NCBI_TaxID=192259 {ECO:0000313|EMBL:EPS67202.1, ECO:0000313|Proteomes:UP000015453};
RN   [1] {ECO:0000313|EMBL:EPS67202.1, ECO:0000313|Proteomes:UP000015453}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23855885;
RA   Leushkin E.V., Sutormin R.A., Nabieva E.R., Penin A.A., Kondrashov A.S.,
RA   Logacheva M.D.;
RT   "The miniature genome of a carnivorous plant Genlisea aurea contains a low
RT   number of genes and short non-coding sequences.";
RL   BMC Genomics 14:476-476(2013).
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:EPS67202.1}.
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DR   EMBL; AUSU01003240; EPS67202.1; -; Genomic_DNA.
DR   AlphaFoldDB; S8E4F7; -.
DR   OrthoDB; 353170at2759; -.
DR   Proteomes; UP000015453; Unassembled WGS sequence.
DR   GO; GO:0046592; F:polyamine oxidase activity; IEA:UniProt.
DR   GO; GO:0006598; P:polyamine catabolic process; IEA:UniProt.
DR   Gene3D; 3.90.660.10; -; 1.
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; FLAVIN MONOAMINE OXIDASE; 1.
DR   PANTHER; PTHR10742:SF313; POLYAMINE OXIDASE 2; 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:UP000015453}.
FT   DOMAIN          23..443
FT                   /note="Amine oxidase"
FT                   /evidence="ECO:0000259|Pfam:PF01593"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:EPS67202.1"
SQ   SEQUENCE   476 AA;  52508 MW;  B56195BCF7DE3E4C CRC64;
     DICYSTRRKT PASPSVIVVG AGIAGIAAAN ALRDASFQVT VVESRDRIGG RVHTDYSFGF
     PVDLGASWLH GVCKENPLAS VIGRLGLPLY RTSGDNSVLY DHDLESYALF DMEGNQVPQD
     LVTKIGETFE KILEETSLIR QEFTEDMSIE RAISIALERR PDLRMEGLEH KVLQWYLCRM
     EGWFAADADT ISVKGWDQEV LLPGGHGLMV RGYLPVINTL AKGLDICLGH RVTKIARRYN
     GVKVTVEGGR TLVADAAVIT VPLGVLKSNA IQFEPKLPEW KEEAIRDIGV GIENKIVLHF
     DGVFWPNVEF IGVVAETSYG CSYFLNLHKA TGHSVLVYMP AGRLALDIEK MSDDAAANFA
     FTQLRRILPN ASEPIDYLVS RWGSDGNTYG SYSYDVVGKS HDLFERLRIP VDNLFFAGEA
     TSSEYTGSVH GAYSTGLMAA EDCRMRVLER YGELDLFQPA MAEDAPISAP LLISRM
//
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