AOFB_CAVPO
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 03-AUG-2022, entry version 115.
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; 1151887at2759; -.
DR Proteomes; UP000005447; Unassembled WGS sequence.
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: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; 3.50.50.60; -; 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; 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
