ID   AOF_ONCMY               Reviewed;         522 AA.
AC   P49253;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-1998, sequence version 2.
DT   10-JUN-2026, entry version 110.
DE   RecName: Full=Amine oxidase [flavin-containing];
DE            EC=1.4.3.4;
DE   AltName: Full=Monoamine oxidase;
DE            Short=MAO;
GN   Name=mao;
OS   Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC   Salmonidae; Salmoninae; Oncorhynchus.
OX   NCBI_TaxID=8022;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND ACTIVITY.
RC   TISSUE=Liver;
RX   PubMed=7808446; DOI=10.1016/s0026-895x(25)09873-6;
RA   Chen K., Wu H.-F., Grimsby J., Shih J.C.;
RT   "Cloning of a novel monoamine oxidase cDNA from trout liver.";
RL   Mol. Pharmacol. 46:1226-1233(1994).
CC   -!- FUNCTION: Catalyzes the oxidative deamination of biogenic and
CC       xenobiotic amines and has important functions in the metabolism of
CC       neuroactive and vasoactive amines in the central nervous system and
CC       peripheral tissues. Oxidizes both 5-hydroxytryptamine (5-HT) and beta-
CC       phenylethylamine (PEA).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a secondary aliphatic amine + O2 + H2O = a primary amine + an
CC         aldehyde + H2O2; Xref=Rhea:RHEA:26414, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:17478,
CC         ChEBI:CHEBI:58855, ChEBI:CHEBI:65296; EC=1.4.3.4;
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000250|UniProtKB:P27338};
CC   -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane; Single-pass type IV
CC       membrane protein; Cytoplasmic side.
CC   -!- SIMILARITY: Belongs to the flavin monoamine oxidase family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA64302.1; Type=Frameshift; Note=Probable frameshift identified on the basis of homology with other members of this family.; Evidence={ECO:0000305};
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DR   EMBL; L37878; AAA64302.1; ALT_FRAME; mRNA.
DR   PIR; I51346; I51346.
DR   AlphaFoldDB; P49253; -.
DR   SMR; P49253; -.
DR   KEGG; omy:100136729; -.
DR   OrthoDB; 7777654at2759; -.
DR   Proteomes; UP000694395; Unplaced.
DR   GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:TreeGrafter.
DR   GO; GO:0097621; F:monoamine oxidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008131; F:primary methylamine oxidase activity; IEA:TreeGrafter.
DR   GO; GO:0009308; P:amine metabolic process; IEA:UniProtKB-ARBA.
DR   FunFam; 1.10.405.10:FF:000005; Amine oxidase [flavin-containing]; 1.
DR   Gene3D; 3.90.660.10; -; 1.
DR   Gene3D; 6.10.250.130; -; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
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   InterPro; IPR050703; Flavin_MAO.
DR   PANTHER; PTHR43563; AMINE OXIDASE; 1.
DR   PANTHER; PTHR43563:SF11; AMINE OXIDASE [FLAVIN-CONTAINING] A; 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   2: Evidence at transcript level;
KW   FAD; Flavoprotein; Membrane; Mitochondrion; Mitochondrion outer membrane;
KW   Oxidoreductase; Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..522
FT                   /note="Amine oxidase [flavin-containing]"
FT                   /id="PRO_0000099864"
FT   TOPO_DOM        1..492
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        493..513
FT                   /note="Helical; Anchor for type IV membrane protein"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        514..522
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000250"
FT   SITE            158
FT                   /note="Important for catalytic activity"
FT                   /evidence="ECO:0000250"
FT   SITE            367
FT                   /note="Important for catalytic activity"
FT                   /evidence="ECO:0000250"
FT   SITE            384
FT                   /note="Important for catalytic activity"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         399
FT                   /note="S-8alpha-FAD cysteine"
FT                   /evidence="ECO:0000250|UniProtKB:P27338"
SQ   SEQUENCE   522 AA;  58937 MW;  F82D6D15364D646D CRC64;
     MTAQNTFDVI VIGGGISGLS AAKLLKEKGL SPVVLEARDR VGGRTFTVQN EQTKYVDLGG
     AYVGPTQNRI LRLAKECGVK TIKVNEEERL VHYVKGKSYP FKGSFPPMWN PFALMDYNNL
     WRKMDEMGSE IPREAPWKAP HAEEWDKMTM KQLFDKICWT SSARRFATLF VNVNVTSEPH
     EVSALWFLWY VKQCGGTMRI FSTTNGGQER KFLGGSSQIS ECMAKELGER VKMESPVYKI
     DQTGDMVEVE TLNKETYKAK YVIVATPPGL NLKMHFNPEL PPLRNQLIHR VPMGSVIKCI
     VYYRENFWRK KGYCGTMVIE EEEAPIGLTL DDTKPDGTVP AIMGFILARK CRKLCGLTKE
     ERKKRICEIY SRVLGSEEAL HPVHYEEKNW CEEEYSGGCY TAYFPPGILT QYGKVLREPV
     GRLYFAGTET ATEWSGYMEG AVQAGERAAR EVMYEMGRIP QSQIWQTEPE SVEVPALPFV
     TTFWERNLPS VGGFINFLAA SVLSVATAAG MLAYQKGLLT RS
//