ID A0A3P9QDK9_POERE Unreviewed; 468 AA.
AC A0A3P9QDK9;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Peroxisomal N(1)-acetyl-spermine/spermidine oxidase-like {ECO:0000313|Ensembl:ENSPREP00000031843.1};
GN Name=PAOX {ECO:0000313|Ensembl:ENSPREP00000031843.1};
OS Poecilia reticulata (Guppy) (Acanthophacelus reticulatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Poecilia.
OX NCBI_TaxID=8081 {ECO:0000313|Ensembl:ENSPREP00000031843.1, ECO:0000313|Proteomes:UP000242638};
RN [1] {ECO:0000313|Proteomes:UP000242638}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Guanapo {ECO:0000313|Proteomes:UP000242638};
RA Kuenstner A., Dreyer C.;
RT "The genomic landscape of the Guanapo guppy.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSPREP00000031843.1}
RP IDENTIFICATION.
RC STRAIN=Guanapo {ECO:0000313|Ensembl:ENSPREP00000031843.1};
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
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; A0A3P9QDK9; -.
DR Ensembl; ENSPRET00000032203.1; ENSPREP00000031843.1; ENSPREG00000021569.1.
DR GeneTree; ENSGT00940000158274; -.
DR Proteomes; UP000242638; Unassembled WGS sequence.
DR Bgee; ENSPREG00000021569; Expressed in caudal fin and 1 other cell type or tissue.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
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 PANTHER; PTHR10742; FLAVIN MONOAMINE OXIDASE; 1.
DR PANTHER; PTHR10742:SF419; SI:DKEY-275B16.2; 1.
DR Pfam; PF01593; Amino_oxidase; 1.
DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE 4: Predicted;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000242638};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 374..396
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 16..322
FT /note="Amine oxidase"
FT /evidence="ECO:0000259|Pfam:PF01593"
SQ SEQUENCE 468 AA; 51987 MW; 42AA39EF43689E3E CRC64;
MAGNKNINIV IVGSGIAGIA AAHRLVTSGF TNVHILEATE RSGGRVKTGR FGDKVIEIGA
NWIHGPSEEN PVFCLARHYG LLDPEALTPE NQAYDLGGET PWVTNIFSSS GRKLSEKDIY
PALEMFTMLL NESSEFQNQQ GEPYASVGDF IRSEVRQRCV EKWKDIDSAN RSLQLCVISG
MLKRECCVNG SHSLDEVGLG AFGQYKTFPG LDCTFPGGYE GLIANLMSEL PDDIVRYNRP
VQSVFWSNTD KQSSVIVECE DGERMNADHV IVTVPLGYLK KHHTRLFRPP LPLHKLHSIQ
RLGFGTNNKI FVEFDEPWWD ADCDVIQLVW EDEDTLVDQV SDLKSSWIKK LFGFTVLKPA
ERSSDTSISD TVQLMLNFMF GNACVFLLCP SGMVILSVGG SQDMSLSTWR RCLRRRSHML
SHNLSADSQG ILPSLHGGSC APSGSRTPGQ TDLTATWQRA AHSRIWRT
//