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Database: UniProt
Entry: Q5ULA1_PANTR
LinkDB: Q5ULA1_PANTR
Original site: Q5ULA1_PANTR 
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
//
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