ID   AOFB_CAVPO              Reviewed;         520 AA.
AC   P58028;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   27-MAR-2024, entry version 119.
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   Cavia porcellus (Guinea pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC   Cavia.
OX   NCBI_TaxID=10141;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain, and Liver;
RX   PubMed=15035816; DOI=10.1163/156856003765764317;
RA   Yaekashiwa N., Tamate H.B., Takeuchi T., Sugimoto H., Shibata K.,
RA   Kinemuchi H.;
RT   "Nucleotide sequences of putative cDNAs for guinea-pig monoamine oxidase.";
RL   Inflammopharmacology 11:145-154(2003).
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 + 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:P27338};
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:P27338};
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:P27338};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=benzylamine + H2O + O2 = 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 + 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:P27338};
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:P27338};
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:P27338};
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:P27338};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + N-acetylputrescine + O2 = 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; Single-pass type IV
CC       membrane protein; Cytoplasmic side.
CC   -!- SIMILARITY: Belongs to the flavin monoamine oxidase family.
CC       {ECO:0000305}.
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DR   EMBL; AB047271; BAB40418.1; -; mRNA.
DR   RefSeq; NP_001166452.1; NM_001172981.1.
DR   AlphaFoldDB; P58028; -.
DR   SMR; P58028; -.
DR   STRING; 10141.ENSCPOP00000000879; -.
DR   GeneID; 100135573; -.
DR   KEGG; cpoc:100135573; -.
DR   CTD; 4129; -.
DR   eggNOG; KOG0029; Eukaryota.
DR   InParanoid; P58028; -.
DR   OrthoDB; 5471885at2759; -.
DR   Proteomes; UP000005447; Unassembled WGS sequence.
DR   GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
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; IDA:UniProtKB.
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:SF21; 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   CHAIN           1..520
FT                   /note="Amine oxidase [flavin-containing] B"
FT                   /id="PRO_0000099858"
FT   TOPO_DOM        1..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         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;  58410 MW;  0AEBAE99A48BC206 CRC64;
     MNSKCDVVVV GGGISGLAAA KLLHDSGLNV VVLEARDCVG GRTYTLRNQN VKYVDLGGAY
     VGPTQNRILR LAKELGLETY RVNDVERQIH HVKGKSYPFR GPFPPAWNPI SYLDHNNLWR
     TMDDMGKEIP SDAPWKAPLA EEWDHMTMKE LLNKICWTNC PRQFGTLFVN LCFTAETHEV
     SALWFLWYVK QCGGTTRIIS TTNGGQERKF VGGSGQISER IMNLLGDRVK LQRPVVYIDQ
     TGESVLVETL NHEIYEAKYV ISAIPPALGM KIHFKPPLPM MKNQLVSRVP LGSVIKCIVY
     YKDPFWRKKD FCGTMVIEGE EAPVLYTMDD TKPDGSYAAI IGFIAAHKAR KLARLTKEER
     LKKLCELYAK VLGSKEALKP VHYEEKNWCE EQYSGGCYTA YFPPGIMTQY GRFLRQPVGR
     IFFAGTETAT HWSGYMEGAV EAGERAAREV LNAIGKIPED EIWQPEPESV DVPAQPITTT
     FLERHLPSVP GLLRLIRLTT VVSAVALGFL AQKRGLLLRI
//