ID D4QF58_COTJA Unreviewed; 148 AA. AC D4QF58; DT 15-JUN-2010, integrated into UniProtKB/TrEMBL. DT 15-JUN-2010, sequence version 1. DT 27-MAR-2024, entry version 35. DE RecName: Full=Amine oxidase {ECO:0000256|RuleBase:RU362067}; DE EC=1.4.3.- {ECO:0000256|RuleBase:RU362067}; DE Flags: Fragment; GN Name=MAOA {ECO:0000313|EMBL:BAJ04630.1}; OS Coturnix japonica (Japanese quail) (Coturnix coturnix japonica). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda; OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae; OC Perdicinae; Coturnix. OX NCBI_TaxID=93934 {ECO:0000313|EMBL:BAJ04630.1}; RN [1] {ECO:0000313|EMBL:BAJ04630.1} RP NUCLEOTIDE SEQUENCE. RC TISSUE=Brain stem {ECO:0000313|EMBL:BAJ04630.1}; RX PubMed=20211759; DOI=10.1016/j.cbpc.2010.03.002; RA Kamata R., Shiraishi F., Takahashi S., Shimizu A., Shiraishi H.; RT "Reevaluation of the developmental toxicity of dieldrin by the use of RT fertilized Japanese quail eggs."; RL Comp. Biochem. Physiol. C Toxicol. Pharmacol. 152:84-90(2010). 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:0000256|ARBA:ARBA00036170}; 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:0000256|ARBA:ARBA00036674}; 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:0000256|ARBA:ARBA00036934}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59597; CC Evidence={ECO:0000256|ARBA:ARBA00036934}; 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:0000256|ARBA:ARBA00000205}; 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:0000256|ARBA:ARBA00001138}; CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|ARBA:ARBA00001974, CC ECO:0000256|RuleBase:RU362067}; CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane CC {ECO:0000256|ARBA:ARBA00004362}; Single-pass type IV membrane protein CC {ECO:0000256|ARBA:ARBA00004362}; Cytoplasmic side CC {ECO:0000256|ARBA:ARBA00004362}. CC -!- SIMILARITY: Belongs to the flavin monoamine oxidase family. CC {ECO:0000256|ARBA:ARBA00005995, ECO:0000256|RuleBase:RU362067}. 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 EMBL; AB533267; BAJ04630.1; -; mRNA. DR AlphaFoldDB; D4QF58; -. DR GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell. DR GO; GO:0097621; F:monoamine oxidase activity; IEA:RHEA. DR GO; GO:0008131; F:primary amine oxidase activity; 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; 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 Catecholamine metabolism {ECO:0000256|ARBA:ARBA00022939}; KW FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|RuleBase:RU362067}; KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630, KW ECO:0000256|RuleBase:RU362067}; Membrane {ECO:0000256|ARBA:ARBA00023136}; KW Mitochondrion {ECO:0000256|ARBA:ARBA00022787}; KW Mitochondrion outer membrane {ECO:0000256|ARBA:ARBA00022787}; KW Neurotransmitter degradation {ECO:0000256|ARBA:ARBA00022867}; KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, KW ECO:0000256|RuleBase:RU362067}; KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}. FT DOMAIN 2..147 FT /note="Amine oxidase" FT /evidence="ECO:0000259|Pfam:PF01593" FT NON_TER 1 FT /evidence="ECO:0000313|EMBL:BAJ04630.1" FT NON_TER 148 FT /evidence="ECO:0000313|EMBL:BAJ04630.1" SQ SEQUENCE 148 AA; 16978 MW; 1BA58E5D40813EC2 CRC64; IKCMMYYKEA FWKRKGCCAA LFIDDEECPI GITLDDTKPD GSFPAIMGFI LTRKAVKLAS LSKEERRKKI CESFAKAMQM EEALHPVHYE EKNWTMEQYS GGCYTAYFPP GIMYSYGRII RQPVDRIYFA GTETATQWSG YMEGAVQA //