ID A0A562RIA3_9BRAD Unreviewed; 662 AA. AC A0A562RIA3; DT 16-OCT-2019, integrated into UniProtKB/TrEMBL. DT 16-OCT-2019, sequence version 1. DT 12-OCT-2022, entry version 10. DE RecName: Full=Amine oxidase {ECO:0000256|RuleBase:RU000672}; DE EC=1.4.3.- {ECO:0000256|RuleBase:RU000672}; GN ORFNames=IQ16_03991 {ECO:0000313|EMBL:TWI68798.1}; OS Bradyrhizobium huanghuaihaiense. OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales; OC Nitrobacteraceae; Bradyrhizobium. OX NCBI_TaxID=990078 {ECO:0000313|EMBL:TWI68798.1, ECO:0000313|Proteomes:UP000316291}; RN [1] {ECO:0000313|EMBL:TWI68798.1, ECO:0000313|Proteomes:UP000316291} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CGMCC 1.10948 {ECO:0000313|EMBL:TWI68798.1, RC ECO:0000313|Proteomes:UP000316291}; RX PubMed=26203337; DOI=.1186/s40793-015-0017-x; RA Whitman W.B., Woyke T., Klenk H.P., Zhou Y., Lilburn T.G., Beck B.J., RA De Vos P., Vandamme P., Eisen J.A., Garrity G., Hugenholtz P., RA Kyrpides N.C.; RT "Genomic Encyclopedia of Bacterial and Archaeal Type Strains, Phase III: RT the genomes of soil and plant-associated and newly described type RT strains."; RL Stand. Genomic Sci. 10:26-26(2015). 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 -!- COFACTOR: CC Name=L-topaquinone; Xref=ChEBI:CHEBI:79027; CC Evidence={ECO:0000256|RuleBase:RU000672}; CC Name=Cu cation; Xref=ChEBI:CHEBI:23378; CC Evidence={ECO:0000256|RuleBase:RU000672}; CC Note=Contains 1 topaquinone per subunit. CC {ECO:0000256|RuleBase:RU000672}; CC -!- COFACTOR: CC Name=L-topaquinone; Xref=ChEBI:CHEBI:79027; CC Evidence={ECO:0000256|PIRSR:PIRSR600269-51}; CC Note=Contains 1 topaquinone per subunit. CC {ECO:0000256|PIRSR:PIRSR600269-51}; CC -!- PTM: Topaquinone (TPQ) is generated by copper-dependent autoxidation of CC a specific tyrosyl residue. {ECO:0000256|PIRSR:PIRSR600269-51, CC ECO:0000256|RuleBase:RU000672}. CC -!- SIMILARITY: Belongs to the copper/topaquinone oxidase family. CC {ECO:0000256|ARBA:ARBA00007983, ECO:0000256|RuleBase:RU000672}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:TWI68798.1}. 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; VLLA01000009; TWI68798.1; -; Genomic_DNA. DR RefSeq; WP_035666101.1; NZ_VLLA01000009.1. DR Proteomes; UP000316291; Unassembled WGS sequence. DR GO; GO:0052594; F:aminoacetone:oxygen oxidoreductase(deaminating) activity; IEA:UniProtKB-EC. DR GO; GO:0005507; F:copper ion binding; IEA:InterPro. DR GO; GO:0052596; F:phenethylamine:oxygen oxidoreductase (deaminating) activity; IEA:UniProtKB-EC. DR GO; GO:0008131; F:primary amine oxidase activity; IEA:UniProtKB-EC. DR GO; GO:0048038; F:quinone binding; IEA:InterPro. DR GO; GO:0052593; F:tryptamine:oxygen oxidoreductase (deaminating) activity; IEA:UniProtKB-EC. DR GO; GO:0009308; P:amine metabolic process; IEA:UniProtKB-UniRule. DR Gene3D; 2.70.98.20; -; 1. DR InterPro; IPR000269; Cu_amine_oxidase. DR InterPro; IPR015798; Cu_amine_oxidase_C. DR InterPro; IPR036460; Cu_amine_oxidase_C_sf. DR InterPro; IPR016182; Cu_amine_oxidase_N-reg. DR InterPro; IPR015800; Cu_amine_oxidase_N2. DR InterPro; IPR015802; Cu_amine_oxidase_N3. DR PANTHER; PTHR10638; PTHR10638; 1. DR Pfam; PF01179; Cu_amine_oxid; 1. DR Pfam; PF02727; Cu_amine_oxidN2; 1. DR Pfam; PF02728; Cu_amine_oxidN3; 1. DR SUPFAM; SSF49998; SSF49998; 1. DR SUPFAM; SSF54416; SSF54416; 2. DR PROSITE; PS01164; COPPER_AMINE_OXID_1; 1. PE 3: Inferred from homology; KW Copper {ECO:0000256|ARBA:ARBA00023008, ECO:0000256|RuleBase:RU000672}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, KW ECO:0000256|RuleBase:RU000672}; KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, KW ECO:0000256|RuleBase:RU000672}; KW TPQ {ECO:0000256|ARBA:ARBA00022772, ECO:0000256|PIRSR:PIRSR600269-50}. FT DOMAIN 17..95 FT /note="Cu_amine_oxidN2" FT /evidence="ECO:0000259|Pfam:PF02727" FT DOMAIN 108..212 FT /note="Cu_amine_oxidN3" FT /evidence="ECO:0000259|Pfam:PF02728" FT DOMAIN 234..635 FT /note="Cu_amine_oxid" FT /evidence="ECO:0000259|Pfam:PF01179" FT ACT_SITE 310 FT /note="Proton acceptor" FT /evidence="ECO:0000256|PIRSR:PIRSR600269-50" FT ACT_SITE 394 FT /note="Schiff-base intermediate with substrate; via FT topaquinone" FT /evidence="ECO:0000256|PIRSR:PIRSR600269-50" FT MOD_RES 394 FT /note="2',4',5'-topaquinone" FT /evidence="ECO:0000256|PIRSR:PIRSR600269-51" SQ SEQUENCE 662 AA; 73650 MW; 4312C6A0C07D96F3 CRC64; MLDTVKAKPQ AQAAAPHPLD PLTAEEITAA CTLVRAAATS PENCRFPTVR LEEPTKQELA AGGAGRRAFV LTLDVATGEA IEHIVDLSRG EIVARKIIPN REAPYGQPPV MLEEFFKCEA VVKADARWRA AMVRRGLSDK DIELVQVDPF SSGFFDKEFE RGARIVRAVS YFREHLQDNG YAHPIEGVVA VVDLIGGEVI DLTDEDPIVP IPRKKRNYGA HELQNPRTDI KPLHIEQPEG ASFRVDGWKV DWQKWSFRVG FTPREGLVLH QLAYQDGARK RSLIHRASVT EMVVPYADPT ANHFWKSAFD AGEYGLGMLA NALELGCDCI GNIHYFDVPA ADGKGEPFVM QNAICMHEED YGIAWKHYEF RNGLFEVRRS RRLVISFFAT VGNYDYGFYW YLYQDGTIQL ETKLTGIIQT AAVPSGETYR WGGMVDDNLG GPTHQHFFNV RLHMDLDGGG NTVTEHDFVP RPWGHDNPHG NVFDTTTRVL SRERDAAAVA NGETGRFWKI SNPNEINSVG NAPAYKLVVN PSPLMLAQEG SYVRKRGGFA TKHVWVTAFD RDEKYASGDY PNVHAGGDGL PRYAAQNRNI ENTDLVVWHS FGHTHVCKPE DFPIMPVEYA GFMLKPTGFF AANAAFDIPP ERNSRSVLAG EGKGAASCCD KD //