ID A0A2U9B417_SCOMX Unreviewed; 545 AA.
AC A0A2U9B417;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE RecName: Full=Amine oxidase {ECO:0000256|RuleBase:RU362067};
DE EC=1.4.3.- {ECO:0000256|RuleBase:RU362067};
GN ORFNames=SMAX5B_008392 {ECO:0000313|EMBL:AWO98478.1};
OS Scophthalmus maximus (Turbot) (Psetta maxima).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Pleuronectiformes; Pleuronectoidei; Scophthalmidae;
OC Scophthalmus.
OX NCBI_TaxID=52904 {ECO:0000313|EMBL:AWO98478.1, ECO:0000313|Proteomes:UP000246464};
RN [1] {ECO:0000313|EMBL:AWO98478.1, ECO:0000313|Proteomes:UP000246464}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Martinez P.;
RT "Integrating genomic resources of turbot (Scophthalmus maximus) in depth
RT evaluation of genetic and physical mapping variation across individuals.";
RL Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974,
CC ECO:0000256|RuleBase:RU362067};
CC -!- SIMILARITY: Belongs to the flavin monoamine oxidase family.
CC {ECO:0000256|RuleBase:RU362067}.
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DR EMBL; CP026245; AWO98478.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2U9B417; -.
DR STRING; 52904.ENSSMAP00000026386; -.
DR Proteomes; UP000246464; Chromosome 3.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0008131; F:primary amine oxidase activity; IEA:UniProt.
DR Gene3D; 1.10.10.1620; -; 1.
DR Gene3D; 3.30.70.2100; -; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR Gene3D; 1.10.405.10; Guanine Nucleotide Dissociation Inhibitor, domain 1; 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:SF21; L-AMINO-ACID 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 FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|RuleBase:RU362067};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW ECO:0000256|RuleBase:RU362067}; Membrane {ECO:0000256|RuleBase:RU362067};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU362067};
KW Reference proteome {ECO:0000313|Proteomes:UP000246464};
KW Transmembrane {ECO:0000256|RuleBase:RU362067};
KW Transmembrane helix {ECO:0000256|RuleBase:RU362067}.
FT TRANSMEM 40..60
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362067"
FT DOMAIN 101..540
FT /note="Amine oxidase"
FT /evidence="ECO:0000259|Pfam:PF01593"
SQ SEQUENCE 545 AA; 60565 MW; 31580B671DFF2C2E CRC64;
MIPPTRPDRL EASFPSYGVS SGGNKSKPWS SILKMIPHMA LCKFFPLVLV GVVVIAVSGI
TGDPLYDCLQ DTDYSELLDI VNKGLPTATT PRHVAIIGGG MAGLTAAKLL EDAGHKVTII
EASDRIGGRV ETFRNRREGW YAEVGAMRIP SFHKILLSLV SKLQIPLNPF IQDDINTYYL
VNGILEKTYA VENNPGLLNY SLNERERGKT AGQLFSQALW KVRDDLKAFG CSAMLDKYDA
YTVKEYLVKE GNLSRGALRM IGDILNENSL FYTSLIEMLY IQSDINDNIE YFEVTDGFDH
LPRAFYQVLN STILLNSKVK LINQTSGSDV TVTFQDWSNS DSPHSLTVDY ALITATAKAT
LFINFQPPLD GDKMEALRSV HYTSSTKVVL SFRERFWEEQ GIKGGKSITD RPSRFIYYPS
HSFPGTDAGA LLASYTCSDD STLFQGMSEE ELMAVVLEDL VTIHGEVIRN LWTGGLVKKW
GLDPYSLGAF ALFTPYQQGH YAGELFQSEG RVHFAGEHTA TPHGWIETAM KSAIRAARNI
NRLTL
//
