AOFB_BOVIN
ID AOFB_BOVIN Reviewed; 520 AA.
AC P56560; Q0P5K2; Q864W3;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Amine oxidase [flavin-containing] B {ECO:0000250|UniProtKB:P27338};
DE EC=1.4.3.21 {ECO:0000269|PubMed:8003474};
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 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].
RA Chung P.P., Vaidyanathan G., Lanier S.M.;
RL Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Basal ganglia;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PROTEIN SEQUENCE OF 2-17, ACETYLATION AT SER-2, AND MASS SPECTROMETRY.
RX PubMed=11049757; DOI=10.1006/prep.2000.1309;
RA Newton-Vinson P., Hubalek F., Edmondson D.E.;
RT "High-level expression of human liver monoamine oxidase B in Pichia
RT pastoris.";
RL Protein Expr. Purif. 20:334-345(2000).
RN [4]
RP PROTEIN SEQUENCE OF 22-36; 53-70; 101-120; 259-279; 289-323; 327-346;
RP 362-403; 420-431 AND 456-485.
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 [5]
RP DETERMINATION OF PROTEIN-FAD RATIO, AND COFACTOR.
RC TISSUE=Liver;
RX PubMed=2764901; DOI=10.1042/bj2600725;
RA Weyler W.;
RT "Monoamine oxidase A from human placenta and monoamine oxidase B from
RT bovine liver both have one FAD per subunit.";
RL Biochem. J. 260:725-729(1989).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=8003474; DOI=10.1021/bi00189a011;
RA Walker M.C., Edmondson D.E.;
RT "Structure-activity relationships in the oxidation of benzylamine analogues
RT by bovine liver mitochondrial monoamine oxidase B.";
RL Biochemistry 33:7088-7098(1994).
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 (PubMed:8003474). Preferentially degrades benzylamine and
CC phenylethylamine (PubMed:8003474). {ECO:0000269|PubMed:8003474}.
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=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:0000269|PubMed:8003474};
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:0000269|PubMed:8003474};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59425;
CC Evidence={ECO:0000305|PubMed:8003474};
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=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:0000269|PubMed:2764901};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.5 mM for benzylamine {ECO:0000269|PubMed:8003474};
CC KM=0.28 mM for dioxygen {ECO:0000269|PubMed:8003474};
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.
CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane; Single-pass type IV
CC membrane protein; Cytoplasmic side.
CC -!- MASS SPECTROMETRY: Mass=59163.5; Mass_error=10.0; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:11049757};
CC -!- SIMILARITY: Belongs to the flavin monoamine oxidase family.
CC {ECO:0000305}.
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DR EMBL; AF217955; AAF23179.1; -; mRNA.
DR EMBL; BC119941; AAI19942.1; -; mRNA.
DR PIR; S07573; S07573.
DR RefSeq; NP_808813.2; NM_177944.2.
DR AlphaFoldDB; P56560; -.
DR SMR; P56560; -.
DR STRING; 9913.ENSBTAP00000001698; -.
DR BindingDB; P56560; -.
DR ChEMBL; CHEMBL2756; -.
DR DrugCentral; P56560; -.
DR iPTMnet; P56560; -.
DR PaxDb; P56560; -.
DR PeptideAtlas; P56560; -.
DR GeneID; 338445; -.
DR KEGG; bta:338445; -.
DR CTD; 4129; -.
DR eggNOG; KOG0029; Eukaryota.
DR HOGENOM; CLU_004498_0_1_1; -.
DR InParanoid; P56560; -.
DR OrthoDB; 1151887at2759; -.
DR TreeFam; TF313314; -.
DR BRENDA; 1.4.3.4; 908.
DR PRO; PR:P56560; -.
DR Proteomes; UP000009136; Unplaced.
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; -; 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 1: Evidence at protein level;
KW Acetylation; Direct protein sequencing; FAD; Flavoprotein; Membrane;
KW Mitochondrion; Mitochondrion outer membrane; Oxidoreductase;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:11049757"
FT CHAIN 2..520
FT /note="Amine oxidase [flavin-containing] B"
FT /id="PRO_0000099856"
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:0000269|PubMed:11049757"
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"
FT CONFLICT 3
FT /note="S -> N (in Ref. 1; AAF23179)"
FT /evidence="ECO:0000305"
FT CONFLICT 270
FT /note="M -> G (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 286
FT /note="I -> T (in Ref. 1; AAF23179)"
FT /evidence="ECO:0000305"
FT CONFLICT 297..299
FT /note="SIV -> PIM (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 307
FT /note="R -> K (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 341
FT /note="I -> L (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 344
FT /note="I -> K (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 400
FT /note="S -> A (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 478..485
FT /note="TTTFLQRH -> STSSMMMP (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 509
FT /note="F -> Y (in Ref. 2; AAI19942)"
FT /evidence="ECO:0000305"
FT CONFLICT 520
FT /note="I -> V (in Ref. 1; AAF23179)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 520 AA; 58421 MW; A594889B4495C410 CRC64;
MSSKCDVVVV GGGISGMAAA KLLHDSGLNV IVLEARDRVG GRTYTLRNQK VKYVDLGGSY
VGPTQNHILR LSKELGLETY KVNEVERLIH HTKGKSYPFR GSFPSVWNPI TYLDHNNLWR
TMDDMGREIP SDAPWKAPLA EQWDLMTMKE LLDKICWTES SKQLAILFVN LCVTAEIHEV
SALWFLWYVK QCGGTTRIFS TSNGGQERKF VGGSGQVSER IMDLLGDRVK LERPVIHIDQ
TGENVLVETL NHELYEAKYV ISAVPPVLGM KIHFNPPLPM MRNQLITRVP LGSVIKSIVY
YKEPFWRNMD YCGSMIIEGE EAPVAYALDD TKPDGSYPAI IGFILAHKAR KLARLTKEER
LKKLCDLYAK VLGSQEALHP VHYEEKNWCE EQYSGGCYTS YFPPGIMTQY GRVLRQPVGR
IYFAGTETAT HWSGYMEGAV EAGERAAREI LHAMGKIPED EIWLPEPESV DVPAKPITTT
FLQRHLPSVP GLLKLIGLTT IFSATALGFL AHKRGLLVRI
