ID A0A8B9XJK6_BOSMU Unreviewed; 932 AA. AC A0A8B9XJK6; DT 19-JAN-2022, integrated into UniProtKB/TrEMBL. DT 19-JAN-2022, sequence version 1. DT 03-MAY-2023, entry version 6. DE RecName: Full=Amine oxidase {ECO:0000256|RuleBase:RU362067}; DE EC=1.4.3.- {ECO:0000256|RuleBase:RU362067}; OS Bos mutus grunniens (Wild yak) (Bos grunniens). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae; OC Bovinae; Bos. OX NCBI_TaxID=30521 {ECO:0000313|Ensembl:ENSBGRP00000021645.1, ECO:0000313|Proteomes:UP000694520}; RN [1] {ECO:0000313|Ensembl:ENSBGRP00000021645.1} RP IDENTIFICATION. RG Ensembl; RL Submitted (JAN-2023) to UniProtKB. 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:0000256|ARBA:ARBA00033614}; 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:0000256|ARBA:ARBA00033618}; 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:0000256|ARBA:ARBA00033669}; 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:0000256|ARBA:ARBA00033622}; 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:0000256|ARBA:ARBA00000205}; 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:0000256|ARBA:ARBA00001138}; 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:0000256|ARBA:ARBA00033704}; CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|ARBA:ARBA00001974, CC ECO:0000256|RuleBase:RU362067}; 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. {ECO:0000256|ARBA:ARBA00025863}. CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane CC {ECO:0000256|ARBA:ARBA00004362}; Single-pass type IV membrane protein CC {ECO:0000256|ARBA:ARBA00004362}; Cytoplasmic side CC {ECO:0000256|ARBA:ARBA00004362}. CC -!- SIMILARITY: Belongs to the flavin monoamine oxidase family. CC {ECO:0000256|ARBA:ARBA00005995, ECO:0000256|RuleBase:RU362067}. 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 Ensembl; ENSBGRT00000024960.1; ENSBGRP00000021645.1; ENSBGRG00000013578.1. DR Ensembl; ENSBGRT00000025157.1; ENSBGRP00000021814.1; ENSBGRG00000013578.1. DR GeneTree; ENSGT00940000160514; -. DR Proteomes; UP000694520; Chromosome X. DR GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell. DR GO; GO:0008131; F:primary amine oxidase activity; IEA:UniProt. 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:SF11; AMINE OXIDASE [FLAVIN-CONTAINING] A; 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 3: Inferred from homology; KW FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|RuleBase:RU362067}; KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630, KW ECO:0000256|RuleBase:RU362067}; Membrane {ECO:0000256|ARBA:ARBA00022787}; KW Mitochondrion {ECO:0000256|ARBA:ARBA00022787}; KW Mitochondrion outer membrane {ECO:0000256|ARBA:ARBA00022787}; KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, KW ECO:0000256|RuleBase:RU362067}; KW Reference proteome {ECO:0000313|Proteomes:UP000694520}. FT DOMAIN 441..878 FT /note="Amine oxidase" FT /evidence="ECO:0000259|Pfam:PF01593" FT REGION 1..35 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 123..287 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 304..426 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 123..188 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 199..213 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 214..234 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 243..284 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 304..349 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 357..371 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 409..426 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 932 AA; 100982 MW; 8A5D45C8BC507ADA CRC64; MSAPNSAAPF SSGRRGGNER ELQRSPGVGN LPAQIPEAAN IAGVASSSSW NTSSEWLTSH QHSSRLSNTS TAADARYTRG FSAPSQLIPG FGLRTDTGLR VDIWGFGTRG LNDRVRMSAL HPTTTDEAAS ASNPGPSSPR VSVQGSVQPS RSPRLPLHTT LHSAPGSTRI SIGETPRPTN TFRGSVQGSI SPVKPAFIKI SAPAPPPPNN TPPVSLLGLT SPSVSGSPLG SVQGPPTPSN SPPLSGQESS RVSMSDFQQL SAKRSAPLSA LSRESVQGSA PPSVVSFPES LARGSIAISD FSRVSIRGSS PPSDLSTPRS SIPGPLSPVN SQVSTQESTQ LSEQSYPQRL VEGSAPPPDS PGVPVPGVAP PSAPGSAQES VEESAPPSGS PRDSVEKSAP PSARPTPVPT PRENRNQSME SLQKTSDAGQ MFDVVVIGGG ISGLSAAKLL AEHEVNVLVL EARERVGGRT YTVRNEHVDY VDVGGAYVGP TQNRILRLSK QLGLETYKVN VNERLVHYVK GKTYPFRGAF PPVWNPIAYL DYNNLWRTMD NMGKEIPADA PWEAPHAVEW DKMTMKDLIE KICWTKTARQ FASLFVNINV TSEPHEVSAL WFLWYVKQCG GTTRIFSITN GGQERKFVGG SGQVSERIMQ LLGDRVKLRS PVTYVDQSSE NITVETLNRE LYECRYVISA IPPTLTAKIH FRPELPSERN QLIQRLPMGA VIKCMMYYKE AFWKKKDYCG CMIIEDEEAP ISITLDDTKP DGSLPAIMGF ILARKADRLA KVHKDIRKRK ICELYAKVLG SQEALRPVHY EEKNWCQEQY SGGCYTAYFP PGIMTQYGRV IRQPVGRIYF AGTETATQWS GYMEGAVEAG ERAAREVLNA LGKLSAKDIW IQEPEAEDVP AVEITPSFWE RNLPSVSGLL KIVGFSTSIT AL //