ID AOFB_RAT Reviewed; 520 AA. AC P19643; Q5EBB5; DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 10-JUN-2026, entry version 175. DE RecName: Full=Amine oxidase [flavin-containing] B {ECO:0000305}; DE EC=1.4.3.21 {ECO:0000269|PubMed:20493079, ECO:0000269|PubMed:4156831}; DE EC=1.4.3.4 {ECO:0000269|PubMed:20493079}; DE AltName: Full=Monoamine oxidase type B; DE Short=MAO-B; GN Name=Maob {ECO:0000312|RGD:3041}; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Liver; RX PubMed=2974701; DOI=10.1016/s0006-291x(88)80969-0; RA Ito A., Kuwahara T., Inadome S., Sagara Y.; RT "Molecular cloning of a cDNA for rat liver monoamine oxidase B."; RL Biochem. Biophys. Res. Commun. 157:970-976(1988). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Liver; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [3] RP FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=4156831; DOI=10.1042/bj1440029; RA Seiler N., Al-Therib M.J.; RT "Putrescine catabolism in mammalian brain."; RL Biochem. J. 144:29-35(1974). RN [4] RP FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES. RX PubMed=6428396; DOI=10.1016/0006-291x(84)91293-2; RA Chiba K., Trevor A., Castagnoli N. Jr.; RT "Metabolism of the neurotoxic tertiary amine, MPTP, by brain monoamine RT oxidase."; RL Biochem. Biophys. Res. Commun. 120:574-578(1984). RN [5] RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES. RX PubMed=20493079; DOI=10.1016/0197-0186(86)90182-8; RA O'Carroll A.M., Bardsley M.E., Tipton K.F.; RT "The oxidation of adrenaline and noradrenaline by the two forms of RT monoamine oxidase from human and rat brain."; RL Neurochem. Int. 8:493-500(1986). RN [6] RP MUTAGENESIS OF ILE-199. RX PubMed=9162023; DOI=10.1074/jbc.272.22.14033; RA Tsugeno Y., Ito A.; RT "A key amino acid responsible for substrate selectivity of monoamine RT oxidase A and B."; RL J. Biol. Chem. 272:14033-14036(1997). 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:20493079). Preferentially degrades benzylamine and CC phenylethylamine (PubMed:20493079). {ECO:0000269|PubMed:20493079}. 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:0000269|PubMed:20493079}; 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:0000269|PubMed:20493079}; 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:0000269|PubMed:20493079, ECO:0000269|PubMed:4156831}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16154; CC Evidence={ECO:0000305|PubMed:4156831}; 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:0000269|PubMed:20493079}; 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:0000269|PubMed:20493079}; 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:0000269|PubMed:20493079}; 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=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:0000269|PubMed:20493079}; 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:0000269|PubMed:4156831}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70284; CC Evidence={ECO:0000269|PubMed:4156831}; CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000250|UniProtKB:P27338}; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=840 uM for (R)-adrenaline {ECO:0000269|PubMed:20493079}; CC KM=290 uM for dopamine {ECO:0000269|PubMed:20493079}; CC KM=533 uM for serotonin {ECO:0000269|PubMed:20493079}; CC KM=1954 uM for (R)-noradrenaline {ECO:0000269|PubMed:20493079}; CC KM=5 uM for 2-phenylethylamine {ECO:0000269|PubMed:20493079}; CC KM=328 uM for tyramine {ECO:0000269|PubMed:20493079}; CC Vmax=531 pmol/min/mg enzyme toward (R)-adrenaline CC {ECO:0000269|PubMed:20493079}; CC Vmax=396 pmol/min/mg enzyme toward dopamine CC {ECO:0000269|PubMed:20493079}; CC Vmax=125 pmol/min/mg enzyme toward serotonin CC {ECO:0000269|PubMed:20493079}; CC Vmax=383 pmol/min/mg enzyme toward (R)-noradrenaline CC {ECO:0000269|PubMed:20493079}; CC Vmax=489 pmol/min/mg enzyme toward 2-phenylethylamine CC {ECO:0000269|PubMed:20493079}; CC Vmax=687 pmol/min/mg enzyme toward tyramine CC {ECO:0000269|PubMed:20493079}; 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; M23601; AAA41566.1; -; mRNA. DR EMBL; BC089814; AAH89814.1; -; mRNA. DR PIR; A31870; A31870. DR RefSeq; NP_037330.1; NM_013198.1. DR AlphaFoldDB; P19643; -. DR SMR; P19643; -. DR BioGRID; 247778; 1. DR FunCoup; P19643; 129. DR STRING; 10116.ENSRNOP00000043466; -. DR BindingDB; P19643; -. DR ChEMBL; CHEMBL2993; -. DR DrugCentral; P19643; -. DR GuidetoPHARMACOLOGY; 2490; -. DR iPTMnet; P19643; -. DR PhosphoSitePlus; P19643; -. DR PaxDb; 10116-ENSRNOP00000043466; -. DR DNASU; 25750; -. DR Ensembl; ENSRNOT00000164539.1; ENSRNOP00000101104.1; ENSRNOG00000029778.7. DR Ensembl; ENSRNOT00055027658; ENSRNOP00055022193; ENSRNOG00055016304. DR Ensembl; ENSRNOT00060032306; ENSRNOP00060026318; ENSRNOG00060018700. DR Ensembl; ENSRNOT00065035977; ENSRNOP00065029013; ENSRNOG00065021133. DR GeneID; 25750; -. DR KEGG; rno:25750; -. DR UCSC; RGD:3041; rat. DR AGR; RGD:3041; -. DR CTD; 4129; -. DR RGD; 3041; Maob. DR eggNOG; KOG0029; Eukaryota. DR GeneTree; ENSGT00940000161545; -. DR HOGENOM; CLU_004498_0_1_1; -. DR InParanoid; P19643; -. DR OMA; PIHWAGT; -. DR OrthoDB; 7777654at2759; -. DR PhylomeDB; P19643; -. DR BRENDA; 1.4.3.4; 5301. DR Reactome; R-RNO-141333; Biogenic amines are oxidatively deaminated to aldehydes by MAOA and MAOB. DR SABIO-RK; P19643; -. DR PRO; PR:P19643; -. DR Proteomes; UP000002494; Chromosome X. DR Bgee; ENSRNOG00000029778; Expressed in liver and 19 other cell types or tissues. DR ExpressionAtlas; P19643; baseline and differential. DR GO; GO:0030425; C:dendrite; IDA:RGD. DR GO; GO:0005741; C:mitochondrial outer membrane; IDA:RGD. DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central. DR GO; GO:0043025; C:neuronal cell body; IDA:RGD. DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IDA:RGD. DR GO; GO:0042802; F:identical protein binding; IPI:RGD. DR GO; GO:0097621; F:monoamine oxidase activity; IDA:UniProtKB. DR GO; GO:0008131; F:primary methylamine oxidase activity; IDA:UniProtKB. DR GO; GO:0014063; P:negative regulation of serotonin secretion; IMP:RGD. DR GO; GO:0019607; P:phenylethylamine catabolic process; IDA:RGD. DR GO; GO:0045964; P:positive regulation of dopamine metabolic process; IMP:RGD. DR GO; GO:0010044; P:response to aluminum ion; IEP:RGD. DR GO; GO:0051412; P:response to corticosterone; IEP:RGD. DR GO; GO:0045471; P:response to ethanol; IEP:RGD. DR GO; GO:0032496; P:response to lipopolysaccharide; IEP:RGD. DR GO; GO:0010269; P:response to selenium ion; IEP:RGD. DR GO; GO:0048545; P:response to steroid hormone; IDA:RGD. DR GO; GO:0009636; P:response to toxic substance; IEP:RGD. DR GO; GO:0009410; P:response to xenobiotic stimulus; IEP:RGD. 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 1: Evidence at protein 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_0000099863" 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" FT MUTAGEN 139 FT /note="L->H: No change in substrate affinity." FT MUTAGEN 199 FT /note="I->F: Increased affinity for serotonin and FT tyramine." FT /evidence="ECO:0000269|PubMed:9162023" FT CONFLICT 38 FT /note="R -> C (in Ref. 1; AAA41566)" FT /evidence="ECO:0000305" FT CONFLICT 335..336 FT /note="GS -> AG (in Ref. 1; AAA41566)" FT /evidence="ECO:0000305" SQ SEQUENCE 520 AA; 58459 MW; F2C230BC6CDE5840 CRC64; MSNKCDVIVV GGGISGMAAA KLLHDCGLSV VVLEARDRVG GRTYTIRNKN VKYVDLGGSY VGPTQNRILR LAKELGLETY KVNEVERLIH FVKGKSYAFR GPFPPVWNPI TYLDYNNLWR TMDEMGQEIP SDAPWKAPLA EEWDYMTMKE LLDKICWTNS TKQIATLFVN LCVTAETHEV SALWFLWYVK QCGGTTRIIS TTNGGQERKF IGGSGQVSER IKDILGDRVK LERPVIHIDQ TGENVVVKTL NHEIYEAKYV ISAIPPVLGM KIHHSPPLPI LRNQLITRVP LGSVIKCMVY YKEPFWRKKD FCGTMVIEGE EAPIAYTLDD TKPDGSCAAI MGFILAHKAR KLVRLTKEER LRKLCELYAK VLNSQEALQP VHYEEKNWCE EQYSGGCYTA YFPPGILTQY GRVLRQPVGK IFFAGTETAS HWSGYMEGAV EAGERAAREI LHAIGKIPED EIWQPEPESV DVPARPITNT FLERHLPSVP GLLKLLGLTT ILSATALGFL AHKKGLFVRF //