ID AOFA_BOVIN Reviewed; 527 AA.
AC P21398; Q0IIE7;
DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 24-JAN-2024, entry version 166.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2719656; DOI=10.1042/bj2590407;
RA Powell J.F., Hsu Y.-P.P., Weyler W., Chen S.A., Salach J.,
RA Andrikopoulos K., Mallet J., Breakefield X.O.;
RT "The primary structure of bovine monoamine oxidase type A. Comparison with
RT peptide sequences of bovine monoamine oxidase type B and other
RT flavoenzymes.";
RL Biochem. J. 259:407-413(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Thalamus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2006) 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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA33633.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; X15609; CAA33632.1; -; mRNA.
DR EMBL; X15609; CAA33633.1; ALT_INIT; mRNA.
DR EMBL; BC122682; AAI22683.1; -; mRNA.
DR PIR; S03974; S03974.
DR RefSeq; NP_851357.2; NM_181014.2.
DR AlphaFoldDB; P21398; -.
DR SMR; P21398; -.
DR STRING; 9913.ENSBTAP00000021570; -.
DR BindingDB; P21398; -.
DR ChEMBL; CHEMBL3254; -.
DR DrugCentral; P21398; -.
DR PaxDb; 9913-ENSBTAP00000021570; -.
DR PeptideAtlas; P21398; -.
DR Ensembl; ENSBTAT00000021570.5; ENSBTAP00000021570.4; ENSBTAG00000016206.5.
DR GeneID; 281293; -.
DR KEGG; bta:281293; -.
DR CTD; 4128; -.
DR VEuPathDB; HostDB:ENSBTAG00000016206; -.
DR VGNC; VGNC:31174; MAOA.
DR eggNOG; KOG0029; Eukaryota.
DR GeneTree; ENSGT00940000160514; -.
DR HOGENOM; CLU_004498_0_1_1; -.
DR InParanoid; P21398; -.
DR OMA; EWTRGAY; -.
DR OrthoDB; 5471885at2759; -.
DR TreeFam; TF313314; -.
DR BRENDA; 1.4.3.4; 908.
DR Reactome; R-BTA-141333; Biogenic amines are oxidatively deaminated to aldehydes by MAOA and MAOB.
DR Reactome; R-BTA-181430; Norepinephrine Neurotransmitter Release Cycle.
DR Reactome; R-BTA-379397; Enzymatic degradation of dopamine by COMT.
DR Reactome; R-BTA-379398; Enzymatic degradation of Dopamine by monoamine oxidase.
DR Reactome; R-BTA-379401; Dopamine clearance from the synaptic cleft.
DR Reactome; R-BTA-380612; Metabolism of serotonin.
DR PRO; PR:P21398; -.
DR Proteomes; UP000009136; Chromosome X.
DR Bgee; ENSBTAG00000016206; Expressed in rumen epithelium and 102 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; ISS:UniProtKB.
DR GO; GO:0006584; P:catecholamine metabolic process; IEA:UniProtKB-KW.
DR Gene3D; 3.90.660.10; -; 2.
DR Gene3D; 6.10.250.130; -; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
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 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_0000099847"
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"
FT CONFLICT 376
FT /note="L -> R (in Ref. 1; CAA33632/CAA33633)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 527 AA; 59758 MW; BC69ED43644DAF37 CRC64;
MESLQKTSDA GQMFDVVVIG GGISGLSAAK LLAEHEVNVL VLEARERVGG RTYTVRNEHV
DYVDVGGAYV GPTQNRILRL SKQLGLETYK VNVNERLVHY VKGKTYPFRG AFPPVWNPIA
YLDYNNLWRT MDNMGKEIPA DAPWEAPHAV EWDKMTMKDL IEKICWTKTA RQFASLFVNI
NVTSEPHEVS ALWFLWYVKQ CGGTTRIFSI TNGGQERKFV GGSGQVSERI MQLLGDRVKL
RSPVTYVDQS SENITVETLN RELYECRYVI SAIPPTLTAK IHFRPELPSE RNQLIQRLPM
GAVIKCMMYY KEAFWKKKDY CGCMIIEDEE APISITLDDT KPDGSLPAIM GFILARKADR
LAKVHKDIRK RKICELYAKV LGSQEALHPV HYEEKNWCQE QYSGGCYTAY FPPGIMTQYG
RVIRQPVGRI YFAGTETATQ WSGYMEGAVE AGERAAREVL NALGKLSAKD IWIQEPEAED
VPAVEITPSF WERNLPSVSG LLKIVGFSTS ITALWFVMYR FRLLSRS
//
