ID   AOFB_PIG                Reviewed;         520 AA.
AC   Q6PLK3;
DT   26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   02-SEP-2026, entry version 108.
DE   RecName: Full=Amine oxidase [flavin-containing] B {ECO:0000250|UniProtKB:P27338};
DE            EC=1.4.3.21 {ECO:0000250|UniProtKB:P27338};
DE            EC=1.4.3.4 {ECO:0000250|UniProtKB:P27338};
DE   AltName: Full=Monoamine oxidase type B;
DE            Short=MAO-B;
GN   Name=MAOB {ECO:0000250|UniProtKB:P27338};
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 (APR-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the oxidative deamination of primary and some
CC       secondary amines such as neurotransmitters, and exogenous amines
CC       including the tertiary amine, neurotoxin 1-methyl-4-phenyl-1,2,3,6-
CC       tetrahydropyridine (MPTP), with concomitant reduction of oxygen to
CC       hydrogen peroxide and participates in the metabolism of neuroactive and
CC       vasoactive amines in the central nervous system and peripheral tissues.
CC       Preferentially degrades benzylamine and phenylethylamine.
CC       {ECO:0000250|UniProtKB:P27338}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a secondary aliphatic amine + O2 + H2O = 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:P27338};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(R)-adrenaline + O2 + H2O = (R)-3,4-dihydroxymandelaldehyde +
CC         methylamine + H2O2; 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:P27338};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a primary methyl amine + O2 + H2O = an aldehyde + H2O2 +
CC         NH4(+); Xref=Rhea:RHEA:16153, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:16240, ChEBI:CHEBI:17478, ChEBI:CHEBI:28938,
CC         ChEBI:CHEBI:228804; EC=1.4.3.21;
CC         Evidence={ECO:0000250|UniProtKB:P27338};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=benzylamine + O2 + H2O = benzaldehyde + H2O2 + NH4(+);
CC         Xref=Rhea:RHEA:59424, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:16240, ChEBI:CHEBI:17169, ChEBI:CHEBI:28938,
CC         ChEBI:CHEBI:225238; Evidence={ECO:0000250|UniProtKB:P27338};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59425;
CC         Evidence={ECO:0000250|UniProtKB:P27338};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=dopamine + O2 + H2O = 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:P27338};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=tyramine + O2 + H2O = (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:P27338};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(R)-noradrenaline + O2 + H2O = (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:P27338};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-phenylethylamine + O2 + H2O = 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:P27338};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=N-acetylputrescine + O2 + H2O = 4-acetamidobutanal + H2O2 +
CC         NH4(+); Xref=Rhea:RHEA:70283, ChEBI:CHEBI:7386, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:28938,
CC         ChEBI:CHEBI:58263; Evidence={ECO:0000250|UniProtKB:P19643};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70284;
CC         Evidence={ECO:0000250|UniProtKB:P19643};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000250|UniProtKB:P27338};
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). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000250};
CC       Single-pass type IV membrane protein {ECO:0000250}; Cytoplasmic side
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the flavin monoamine oxidase family.
CC       {ECO:0000305}.
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DR   EMBL; AY596820; AAT06259.1; -; mRNA.
DR   RefSeq; NP_001001864.1; NM_001001864.1.
DR   AlphaFoldDB; Q6PLK3; -.
DR   SMR; Q6PLK3; -.
DR   FunCoup; Q6PLK3; 243.
DR   STRING; 9823.ENSSSCP00000022462; -.
DR   BindingDB; Q6PLK3; -.
DR   ChEMBL; CHEMBL6067586; -.
DR   PaxDb; 9823-ENSSSCP00000022462; -.
DR   PeptideAtlas; Q6PLK3; -.
DR   GeneID; 414909; -.
DR   KEGG; ssc:414909; -.
DR   CTD; 4129; -.
DR   eggNOG; KOG0029; Eukaryota.
DR   InParanoid; Q6PLK3; -.
DR   OrthoDB; 7777654at2759; -.
DR   Proteomes; UP000008227; Unplaced.
DR   GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR   GO; GO:0097621; F:monoamine oxidase activity; ISS:UniProtKB.
DR   GO; GO:0008131; F:primary methylamine oxidase activity; ISS:UniProtKB.
DR   GO; GO:0019607; P:phenylethylamine catabolic process; IBA:GO_Central.
DR   GO; GO:0042428; P:serotonin metabolic process; IBA:GO_Central.
DR   FunFam; 1.10.405.10:FF:000005; Amine oxidase [flavin-containing]; 1.
DR   Gene3D; 3.90.660.10; -; 1.
DR   Gene3D; 6.10.250.130; -; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR   Gene3D; 1.10.405.10; Guanine Nucleotide Dissociation Inhibitor, domain 1; 1.
DR   InterPro; IPR002937; Amino_oxidase.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR001613; Flavin_amine_oxidase.
DR   InterPro; IPR050703; Flavin_MAO.
DR   PANTHER; PTHR43563; AMINE OXIDASE; 1.
DR   PANTHER; PTHR43563:SF1; AMINE OXIDASE [FLAVIN-CONTAINING] B; 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; FAD; Flavoprotein; Membrane; Mitochondrion;
KW   Mitochondrion outer membrane; Oxidoreductase; Reference proteome;
KW   Transmembrane; Transmembrane helix.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P56560"
FT   CHAIN           2..520
FT                   /note="Amine oxidase [flavin-containing] B"
FT                   /id="PRO_0000099861"
FT   TOPO_DOM        2..489
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        490..516
FT                   /note="Helical; Anchor for type IV membrane protein"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        517..520
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000250"
FT   SITE            156
FT                   /note="Important for catalytic activity"
FT                   /evidence="ECO:0000250"
FT   SITE            365
FT                   /note="Important for catalytic activity"
FT                   /evidence="ECO:0000250"
FT   SITE            382
FT                   /note="Important for catalytic activity"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0000250|UniProtKB:P56560"
FT   MOD_RES         52
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8BW75"
FT   MOD_RES         397
FT                   /note="S-8alpha-FAD cysteine"
FT                   /evidence="ECO:0000250|UniProtKB:P27338"
SQ   SEQUENCE   520 AA;  58265 MW;  18106D07B6151357 CRC64;
     MSSKCDVVVV GGGISGMAAA KLLHDSGLNV IVLEARDRVG GRTYTVRNQQ VKYVDLGGSY
     VGPTQNRILR LSKELGLETY KVNEVERLIH YVKGKSYPFR GPLPPVRNPI TFLDLNNLWR
     TVDDMGREIP SDAPWKAPLA EQWDQMTMKE LLDKLCWTES SKQLATLFVN LCVTAETHEV
     SALWFLWYVK QCGGTTRIIS TTNGGQERKF VGGSGQVTER IKDLLGDRVK LERPVVHIDQ
     TGENVLVETL NHEVYEAKYV ISAIPPVLGM KIHFSPPLPM MRNQLITRVP LGSVIKCIVY
     YKEPFWRHKD YCGSMIIEGE EAPIAYTLDD SKPDGSCAAI IGFILAHKAR KLARLTKEER
     LKKLCDLYAK VLGSKEALNP VHYEEKNWCE EQYSAGCYTT YFPPGIMTQY GRVLRQPVGR
     IYFAGTETAT HWSGYMEGAV EAGERAAREI LHAMGKIPED EIWQSEPESV DVPAKPITTT
     FLERHLPSVP GLLRLIGLTA IFSATALGYL AHKRGLLVRV
//