ID   AOF_DANRE               Reviewed;         522 AA.
AC   Q6NSN2; Q804D6;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   27-MAR-2024, entry version 131.
DE   RecName: Full=Amine oxidase [flavin-containing] {ECO:0000250|UniProtKB:P21397};
DE            EC=1.4.3.21 {ECO:0000269|PubMed:15621520, ECO:0000269|PubMed:16917825};
DE            EC=1.4.3.4 {ECO:0000250|UniProtKB:P21397};
DE   AltName: Full=Monoamine oxidase;
DE            Short=MAO;
DE            Short=Z-MAO;
GN   Name=mao {ECO:0000312|EMBL:AAH70013.1,
GN   ECO:0000312|ZFIN:ZDB-GENE-040329-3}; ORFNames=zgc:85761;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:AAO16681.3}
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, ACTIVITY
RP   REGULATION, AND 3D-STRUCTURE MODELING.
RC   TISSUE=Liver {ECO:0000312|EMBL:AAO16681.3};
RX   PubMed=15621520; DOI=10.1016/j.cbpc.2004.10.002;
RA   Setini A., Pierucci F., Senatori O., Nicotra A.;
RT   "Molecular characterization of monoamine oxidase in zebrafish (Danio
RT   rerio).";
RL   Comp. Biochem. Physiol. 140B:153-161(2005).
RN   [2] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, ACTIVITY
RP   REGULATION, AND TISSUE SPECIFICITY.
RC   TISSUE=Brain {ECO:0000269|PubMed:16917825};
RX   PubMed=16917825; DOI=10.1002/cne.21057;
RA   Anichtchik O., Sallinen V., Peitsaro N., Panula P.;
RT   "Distinct structure and activity of monoamine oxidase in the brain of
RT   zebrafish (Danio rerio).";
RL   J. Comp. Neurol. 498:593-610(2006).
RN   [3] {ECO:0000312|EMBL:AAH70013.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney {ECO:0000312|EMBL:AAH70013.1};
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
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 (PubMed:15621520, PubMed:16917825). Preferentially
CC       oxidizes serotonin and tyramine (PubMed:15621520, PubMed:16917825).
CC       Also catalyzes the oxidative deamination of kynuramine to 3-(2-
CC       aminophenyl)-3-oxopropanal that can spontaneously condense to 4-
CC       hydroxyquinoline (By similarity). {ECO:0000250|UniProtKB:P21396,
CC       ECO:0000269|PubMed:15621520, ECO:0000269|PubMed:16917825}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a secondary aliphatic amine + H2O + O2 = 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         Evidence={ECO:0000250|UniProtKB:P21397};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an aliphatic amine + H2O + O2 = an aldehyde + H2O2 + NH4(+);
CC         Xref=Rhea:RHEA:16153, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:16240, ChEBI:CHEBI:17478, ChEBI:CHEBI:28938,
CC         ChEBI:CHEBI:58001; EC=1.4.3.21;
CC         Evidence={ECO:0000269|PubMed:15621520, ECO:0000269|PubMed:16917825};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + O2 + serotonin = (5-hydroxyindol-3-yl)acetaldehyde +
CC         H2O2 + NH4(+); Xref=Rhea:RHEA:69072, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:28938,
CC         ChEBI:CHEBI:50157, ChEBI:CHEBI:350546;
CC         Evidence={ECO:0000269|PubMed:15621520, ECO:0000269|PubMed:16917825};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-phenylethylamine + H2O + O2 = 2-phenylacetaldehyde + H2O2 +
CC         NH4(+); Xref=Rhea:RHEA:25265, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:16240, ChEBI:CHEBI:16424, ChEBI:CHEBI:28938,
CC         ChEBI:CHEBI:225237; Evidence={ECO:0000269|PubMed:15621520,
CC         ECO:0000269|PubMed:16917825};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + O2 + tyramine = (4-hydroxyphenyl)acetaldehyde + H2O2 +
CC         NH4(+); Xref=Rhea:RHEA:30591, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:15621, ChEBI:CHEBI:16240, ChEBI:CHEBI:28938,
CC         ChEBI:CHEBI:327995; Evidence={ECO:0000269|PubMed:16917825};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=dopamine + H2O + O2 = 3,4-dihydroxyphenylacetaldehyde + H2O2 +
CC         NH4(+); Xref=Rhea:RHEA:27946, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:16240, ChEBI:CHEBI:27978, ChEBI:CHEBI:28938,
CC         ChEBI:CHEBI:59905; Evidence={ECO:0000269|PubMed:16917825};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(R)-adrenaline + H2O + O2 = (R)-3,4-dihydroxymandelaldehyde +
CC         H2O2 + methylamine; Xref=Rhea:RHEA:51168, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:59338,
CC         ChEBI:CHEBI:71406, ChEBI:CHEBI:180943;
CC         Evidence={ECO:0000250|UniProtKB:P21396};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(R)-noradrenaline + H2O + O2 = (R)-3,4-dihydroxymandelaldehyde
CC         + H2O2 + NH4(+); Xref=Rhea:RHEA:69076, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:28938,
CC         ChEBI:CHEBI:72587, ChEBI:CHEBI:180943;
CC         Evidence={ECO:0000250|UniProtKB:P21396};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + kynuramine + O2 = 3-(2-aminophenyl)-3-oxopropanal + H2O2
CC         + NH4(+); Xref=Rhea:RHEA:59596, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:180898,
CC         ChEBI:CHEBI:180899; Evidence={ECO:0000250|UniProtKB:P21396};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59597;
CC         Evidence={ECO:0000250|UniProtKB:P21396};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + O2 + tryptamine = H2O2 + indole-3-acetaldehyde + NH4(+);
CC         Xref=Rhea:RHEA:59416, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:16240, ChEBI:CHEBI:18086, ChEBI:CHEBI:28938,
CC         ChEBI:CHEBI:57887; Evidence={ECO:0000250|UniProtKB:P21396};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000250|UniProtKB:P27338};
CC   -!- ACTIVITY REGULATION: Inhibited by both clorgyline (selective MAOA
CC       inhibitor) and deprenyl (selective MAOB inhibitor).
CC       {ECO:0000269|PubMed:15621520, ECO:0000269|PubMed:16917825}.
CC   -!- SUBUNIT: Monomer, homo- or heterodimer (containing two subunits of
CC       similar size). Each subunit contains a covalently bound flavin.
CC       Enzymatically active as monomer (By similarity).
CC       {ECO:0000250|UniProtKB:P21397}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane
CC       {ECO:0000250|UniProtKB:P21396}; Single-pass type IV membrane protein
CC       {ECO:0000250|UniProtKB:P21396}; Cytoplasmic side
CC       {ECO:0000250|UniProtKB:P21396}.
CC   -!- TISSUE SPECIFICITY: Strongest expression in brain and intestine,
CC       followed by liver, heart and gill. Little expression in spleen, eye or
CC       muscle. In brain, highest activity in noradrenergic and serotonergic
CC       cell groups and those of the habenulointerpeduncular pathway; moderate
CC       levels in dopaminergic cell clusters. {ECO:0000269|PubMed:16917825}.
CC   -!- MISCELLANEOUS: There appears to be only one form of this enzyme in
CC       zebrafish, whereas in mammals two forms (MAOA and MAOB) exist.
CC       {ECO:0000269|PubMed:15621520, ECO:0000269|PubMed:16917825}.
CC   -!- SIMILARITY: Belongs to the flavin monoamine oxidase family.
CC       {ECO:0000255}.
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DR   EMBL; AY185211; AAO16681.3; -; mRNA.
DR   EMBL; BC070013; AAH70013.1; -; mRNA.
DR   RefSeq; NP_997992.2; NM_212827.3.
DR   AlphaFoldDB; Q6NSN2; -.
DR   SMR; Q6NSN2; -.
DR   STRING; 7955.ENSDARP00000032834; -.
DR   BindingDB; Q6NSN2; -.
DR   ChEMBL; CHEMBL1681610; -.
DR   DrugCentral; Q6NSN2; -.
DR   PaxDb; 7955-ENSDARP00000032834; -.
DR   DNASU; 404730; -.
DR   GeneID; 404730; -.
DR   KEGG; dre:404730; -.
DR   AGR; ZFIN:ZDB-GENE-040329-3; -.
DR   CTD; 404730; -.
DR   ZFIN; ZDB-GENE-040329-3; mao.
DR   eggNOG; KOG0029; Eukaryota.
DR   HOGENOM; CLU_004498_0_1_1; -.
DR   InParanoid; Q6NSN2; -.
DR   OMA; GGGMISH; -.
DR   OrthoDB; 5471885at2759; -.
DR   PhylomeDB; Q6NSN2; -.
DR   TreeFam; TF313314; -.
DR   BRENDA; 1.4.3.4; 928.
DR   Reactome; R-DRE-141333; Biogenic amines are oxidatively deaminated to aldehydes by MAOA and MAOB.
DR   Reactome; R-DRE-181430; Norepinephrine Neurotransmitter Release Cycle.
DR   Reactome; R-DRE-379397; Enzymatic degradation of dopamine by COMT.
DR   Reactome; R-DRE-379398; Enzymatic degradation of Dopamine by monoamine oxidase.
DR   Reactome; R-DRE-379401; Dopamine clearance from the synaptic cleft.
DR   Reactome; R-DRE-380612; Metabolism of serotonin.
DR   PRO; PR:Q6NSN2; -.
DR   Proteomes; UP000000437; Chromosome 9.
DR   Bgee; ENSDARG00000023712; Expressed in intestine and 52 other cell types or tissues.
DR   GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0052595; F:aliphatic amine oxidase activity; IEA:RHEA.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IBA:GO_Central.
DR   GO; GO:0097621; F:monoamine oxidase activity; ISS:UniProtKB.
DR   GO; GO:0052596; F:phenethylamine:oxygen oxidoreductase (deaminating) activity; IEA:RHEA.
DR   GO; GO:0008131; F:primary amine oxidase activity; IDA:UniProtKB.
DR   GO; GO:0006584; P:catecholamine metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0042402; P:cellular biogenic amine catabolic process; IDA:UniProtKB.
DR   GO; GO:0035176; P:social behavior; IMP:ZFIN.
DR   GO; GO:0001964; P:startle response; IMP:ZFIN.
DR   GO; GO:0036269; P:swimming behavior; IMP:ZFIN.
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   PANTHER; PTHR43563; AMINE OXIDASE; 1.
DR   PANTHER; PTHR43563:SF21; AMINE OXIDASE [FLAVIN-CONTAINING] B; 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   1: Evidence at protein level;
KW   Catecholamine metabolism; FAD; Flavoprotein; Membrane; Mitochondrion;
KW   Mitochondrion outer membrane; Neurotransmitter degradation; Oxidoreductase;
KW   Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..522
FT                   /note="Amine oxidase [flavin-containing]"
FT                   /id="PRO_0000283788"
FT   TOPO_DOM        1..492
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        493..513
FT                   /note="Helical; Anchor for type IV membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        514..522
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000255"
FT   SITE            157
FT                   /note="Important for catalytic activity"
FT                   /evidence="ECO:0000250|UniProtKB:P27338"
FT   SITE            366
FT                   /note="Important for catalytic activity"
FT                   /evidence="ECO:0000250|UniProtKB:P27338"
FT   SITE            383
FT                   /note="Important for catalytic activity"
FT                   /evidence="ECO:0000250|UniProtKB:P27338"
FT   MOD_RES         398
FT                   /note="S-8alpha-FAD cysteine"
FT                   /evidence="ECO:0000250|UniProtKB:P27338"
FT   CONFLICT        223..224
FT                   /note="AR -> QK (in Ref. 1; AAO16681)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        234
FT                   /note="R -> K (in Ref. 1; AAO16681)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   522 AA;  58765 MW;  8FC58B2A13BFE15C CRC64;
     MTANAYDVIV IGGGISGLSA AKLLVDSGLN PVVLEARSRV GGRTYTVQNK ETKWVDLGGA
     YIGPTQNRIL RIAKQYGVKT YKVNEEESLV HYVKGKSYPF KGPFPPMWNP FAYMDYNNLW
     RTMDKMGMEI PKEAPWRAPH AEEWDKMTMQ QLFDKICWTR SARRFATLFV NVNVTSEPHE
     VSALWFLWYV KQCGGTMRIF STTNGGQERK FAGGANQISE GMARELGDRV KLSRAVCSID
     QTGDLVEVRT VNEEVYKAKY VILAIPPGLN LKIHFNPELP PLRNQLIHRV PMGSVIKCMV
     YYKENFWRKK GYCGSMVIEE EDAPIGLTLD DTKPDGSVPA IMGFILARKS RKLANLTRDE
     RKRRICEIYA RVLGSEEALY PVHYEEKNWC EEEYSGGCYT AYFPPGIMTQ FGRVLREPVG
     RLYFAGTETA TEWSGYMEGA VQAGERASRE VMCAMGKLHA SQIWQSEPES MDVPARPFVT
     TFWERNLPSV GGFLKFMGVS SFLAAATAAG LVACKKGLLP RC
//