AOFA_PIG
ID AOFA_PIG Reviewed; 527 AA.
AC Q6Q2J0;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Amine oxidase [flavin-containing] A {ECO:0000250|UniProtKB:P21397};
DE EC=1.4.3.21 {ECO:0000250|UniProtKB:P21396};
DE EC=1.4.3.4 {ECO:0000250|UniProtKB:P21396};
DE AltName: Full=Monoamine oxidase type A;
DE Short=MAO-A;
GN Name=MAOA {ECO:0000250|UniProtKB:P21397};
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Bai C.Y., Zhao W., Meng H., Pan Y.C.;
RT "Cloning of the porcine MAO-A and -B gene.";
RL Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the oxidative deamination of primary and some
CC secondary amine such as neurotransmitters, with concomitant reduction
CC of oxygen to hydrogen peroxide and has important functions in the
CC metabolism of neuroactive and vasoactive amines in the central nervous
CC system and peripheral tissues. Preferentially oxidizes serotonin. Also
CC catalyzes the oxidative deamination of kynuramine to 3-(2-aminophenyl)-
CC 3-oxopropanal that can spontaneously condense to 4-hydroxyquinoline.
CC {ECO:0000250|UniProtKB:P21396}.
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:P21396};
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:0000250|UniProtKB:P21396};
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=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:0000250|UniProtKB:P21396};
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: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 + 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: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 -!- 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:0000250|UniProtKB:P21396};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000250|UniProtKB:P21397};
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 -!- SIMILARITY: Belongs to the flavin monoamine oxidase family.
CC {ECO:0000305}.
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DR EMBL; AY563632; AAS68020.1; -; mRNA.
DR RefSeq; NP_001001640.1; NM_001001640.1.
DR AlphaFoldDB; Q6Q2J0; -.
DR SMR; Q6Q2J0; -.
DR STRING; 9823.ENSSSCP00000013044; -.
DR PaxDb; Q6Q2J0; -.
DR PeptideAtlas; Q6Q2J0; -.
DR PRIDE; Q6Q2J0; -.
DR GeneID; 414424; -.
DR KEGG; ssc:414424; -.
DR CTD; 4128; -.
DR eggNOG; KOG0029; Eukaryota.
DR InParanoid; Q6Q2J0; -.
DR OrthoDB; 1034142at2759; -.
DR BRENDA; 1.4.3.4; 6170.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0052595; F:aliphatic-amine oxidase activity; IEA:RHEA.
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; ISS:UniProtKB.
DR GO; GO:0006584; P:catecholamine metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0042135; P:neurotransmitter catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 3.50.50.60; -; 2.
DR InterPro; IPR002937; Amino_oxidase.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR001613; Flavin_amine_oxidase.
DR Pfam; PF01593; Amino_oxidase; 1.
DR PRINTS; PR00757; AMINEOXDASEF.
DR SUPFAM; SSF51905; SSF51905; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Catecholamine metabolism; FAD; Flavoprotein; Membrane;
KW Mitochondrion; Mitochondrion outer membrane; Neurotransmitter degradation;
KW Oxidoreductase; Phosphoprotein; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..527
FT /note="Amine oxidase [flavin-containing] A"
FT /id="PRO_0000099852"
FT TOPO_DOM 1..497
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 498..518
FT /note="Helical; Anchor for type IV membrane protein"
FT /evidence="ECO:0000250"
FT TOPO_DOM 519..527
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000250"
FT REGION 520..522
FT /note="Interaction with membrane phospholipid headgroups"
FT /evidence="ECO:0000250"
FT SITE 335
FT /note="Important for substrate specificity"
FT /evidence="ECO:0000250"
FT SITE 374
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P21397"
FT MOD_RES 383
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P21396"
FT MOD_RES 406
FT /note="S-8alpha-FAD cysteine"
FT /evidence="ECO:0000250|UniProtKB:P21397"
SQ SEQUENCE 527 AA; 59763 MW; 9A07272AFBFD730B CRC64;
MERQEKANNA GHMVDVVVIG GGISGLSAAK LLNEYGINVL VLEARDRVGG RTYTVRNENV
DYVDVGGAYV GPTQNRILRL SKELGLETYK VNVNECLVQY VKGKSYPFRG AFPPVWNPIA
YLDYNNLWRT MDDMGKKIPA DAPWESPHAE EWDKMTMKDL IDKICWTKTA KRFASLFVNI
NVTSEPHEVS ALWFLWYVKQ CGGTTRIFSV TNGGQERKFV GGSGQVSERI MHLLGDRVKL
RCPVTYVDQS GDNIIVETLN HELYECQYVI SAIPPTLTAK IHFRPELPSE RNQLIQRLPM
GAIIKCMMYY KEAFWKKKNY CGCMIIEDEE APISITLDDT KPDGSLPAIM GFILARKADR
LAKVHKEVRK RKICELYAKV LGSQEASHPV HYEEKNWCEE QYSGGCYTAY FPPGIMTQYG
RVIRQPVGRI FFAGTETATQ WSGYMEGAVE AGERAAREIL NALGKVSKKD IWLREPESED
VPAFEITRTF WERNLPSVTG LLKIIGFSTS VTALWLAVYK FRLLTRS
