ID Q5ULA1_PANTR Unreviewed; 103 AA.
AC Q5ULA1;
DT 07-DEC-2004, integrated into UniProtKB/TrEMBL.
DT 07-DEC-2004, sequence version 1.
DT 24-JAN-2024, entry version 42.
DE RecName: Full=Amine oxidase [flavin-containing] A {ECO:0000256|ARBA:ARBA00039695};
DE EC=1.4.3.21 {ECO:0000256|ARBA:ARBA00011922};
DE EC=1.4.3.4 {ECO:0000256|ARBA:ARBA00012804};
DE AltName: Full=Monoamine oxidase type A {ECO:0000256|ARBA:ARBA00042435};
DE Flags: Fragment;
GN Name=MAOA {ECO:0000313|EMBL:AAV34713.1};
OS Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598 {ECO:0000313|EMBL:AAV34713.1};
RN [1] {ECO:0000313|EMBL:AAV34713.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=15349769; DOI=10.1007/s00439-004-1179-6;
RA Andres A.M., Soldevila M., Navarro A., Kidd K.K., Oliva B.,
RA Bertranpetit J.;
RT "Positive selection in MAOA gene is human exclusive: determination of the
RT putative amino acid change selected in the human lineage.";
RL Hum. Genet. 115:377-386(2004).
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:0000256|ARBA:ARBA00033614};
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:0000256|ARBA:ARBA00033618};
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:0000256|ARBA:ARBA00033669};
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 + 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:0000256|ARBA:ARBA00033622};
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 -!- 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:0000256|ARBA:ARBA00033704};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
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. {ECO:0000256|ARBA:ARBA00025863}.
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}.
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DR EMBL; AY684860; AAV34713.1; -; Genomic_DNA.
DR AlphaFoldDB; Q5ULA1; -.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
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; PTHR43563; AMINE OXIDASE; 1.
DR PANTHER; PTHR43563:SF11; AMINE OXIDASE [FLAVIN-CONTAINING] A; 1.
DR Pfam; PF01593; Amino_oxidase; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE 4: Predicted;
KW Catecholamine metabolism {ECO:0000256|ARBA:ARBA00022939};
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Neurotransmitter degradation {ECO:0000256|ARBA:ARBA00022867}.
FT DOMAIN 5..102
FT /note="Amine oxidase"
FT /evidence="ECO:0000259|Pfam:PF01593"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AAV34713.1"
FT NON_TER 103
FT /evidence="ECO:0000313|EMBL:AAV34713.1"
SQ SEQUENCE 103 AA; 11962 MW; 02C129E501D44420 CRC64;
ERKFVGGSGQ VSERIMDLLG DQVKLNHPVT HVDQSSDNII IETLNHEHYE CKYVINAIPP
TLTAKIHFRP ELPAERNQLI QRLPMGAIIK CMMYYKEAFW KKK
//