AOFB_CANLF
ID AOFB_CANLF Reviewed; 520 AA.
AC Q7YRB7;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 106.
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 Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Beagle; TISSUE=Brain;
RA Hashizume C., Mori Y.;
RL Submitted (SEP-2001) 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 + 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 {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; AB070958; BAB86936.1; -; mRNA.
DR RefSeq; NP_001002970.1; NM_001002970.1.
DR AlphaFoldDB; Q7YRB7; -.
DR SMR; Q7YRB7; -.
DR STRING; 9615.ENSCAFP00000021330; -.
DR PaxDb; Q7YRB7; -.
DR Ensembl; ENSCAFT00000022963; ENSCAFP00000021330; ENSCAFG00000014451.
DR Ensembl; ENSCAFT00845048615; ENSCAFP00845038135; ENSCAFG00845027440.
DR GeneID; 403451; -.
DR KEGG; cfa:403451; -.
DR CTD; 4129; -.
DR VEuPathDB; HostDB:ENSCAFG00845027440; -.
DR VGNC; VGNC:42954; MAOB.
DR eggNOG; KOG0029; Eukaryota.
DR GeneTree; ENSGT00940000161545; -.
DR InParanoid; Q7YRB7; -.
DR OrthoDB; 1151887at2759; -.
DR Proteomes; UP000002254; Chromosome X.
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; ISS: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; ISS:UniProtKB.
DR Gene3D; 3.50.50.60; -; 1.
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 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_0000099857"
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; 58384 MW; D5C6295875D7D8BE CRC64;
MSGKCDVVVV GGGISGMAAA KLLHDFGLNV VVLEARDRVG GRTYTIRNQK VKYLDLGGSY
VGPTQNCILR LAKELGLETY KVNEVERLIH HVKGKSYPFR GPFPPVWNPI AYLDHNNLWR
TMDDMGREIP SDAPWKAPLA EEWDHMTMKE LLDKICWTES AKQLATLFVN LCVTAETHEV
SALWFLWYVK QCGGTTRIIS TTNGGQERKF VGGSGQVSER IMDLLGDQVK LERPVTHIDQ
TGENVLVETL NHEVYEAKYV ISAIPPTLGM KIHFNPPLPM MRNQLITRVP LGSVIKCIVY
YKEPFWRKKD YCGTMIIEGE EAPIAYTLDD TKPDGNYAAI MGFILAHKAR KLARLTKDER
MKKLCELYAK VLGSQEALQP VHYEEKNWCE EQYSGGCYTT YFPPGIMTQY GRVLRQPVGR
IYFAGTETAT HWSGYMEGAV EAGERAAREI LHAMGKIPED EIWQSEPESV DVPAQPITTT
FLERHLPSVP GLLRLIGLTA IFSATALGVL AHKRGLLVRV
