ID   AMO2_ARTS1              Reviewed;         648 AA.
AC   Q07123;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   03-AUG-2022, entry version 82.
DE   RecName: Full=Copper methylamine oxidase;
DE            EC=1.4.3.21 {ECO:0000250|UniProtKB:P46883};
DE   AltName: Full=MAOXII;
DE   AltName: Full=Primary amine oxidase;
DE   Flags: Precursor;
GN   Name=maoII;
OS   Arthrobacter sp. (strain P1).
OC   Bacteria; Actinobacteria; Micrococcales; Micrococcaceae; Arthrobacter.
OX   NCBI_TaxID=47915;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 10-54; 358-381
RP   AND 456-466.
RX   PubMed=8366046; DOI=10.1128/jb.175.17.5617-5627.1993;
RA   Zhang X., Fuller J.H., McIntire W.S.;
RT   "Cloning, sequencing, expression, and regulation of the structural gene for
RT   the copper/topa quinone-containing methylamine oxidase from Arthrobacter
RT   strain P1, a Gram-positive facultative methylotroph.";
RL   J. Bacteriol. 175:5617-5627(1993).
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:P46883};
CC   -!- COFACTOR:
CC       Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC         Evidence={ECO:0000250|UniProtKB:P46883};
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000250|UniProtKB:P12807};
CC       Note=Binds 1 copper ion per subunit (By similarity). Can also use zinc
CC       ion as cofactor (By similarity). {ECO:0000250|UniProtKB:P12807,
CC       ECO:0000250|UniProtKB:P46883};
CC   -!- COFACTOR:
CC       Name=L-topaquinone; Xref=ChEBI:CHEBI:79027;
CC         Evidence={ECO:0000250|UniProtKB:P46883};
CC       Note=Contains 1 topaquinone per subunit.
CC       {ECO:0000250|UniProtKB:P46883};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000250|UniProtKB:Q43077};
CC       Note=Binds 1 Mn(2+) ion per subunit. {ECO:0000250|UniProtKB:Q43077};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P46883}.
CC   -!- INDUCTION: By methylamine.
CC   -!- PTM: Topaquinone (TPQ) is generated by copper-dependent autoxidation of
CC       a specific tyrosyl residue. {ECO:0000250|UniProtKB:P46883}.
CC   -!- SIMILARITY: Belongs to the copper/topaquinone oxidase family.
CC       {ECO:0000305}.
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DR   EMBL; L12990; AAA22074.1; -; Genomic_DNA.
DR   PIR; A48646; A48646.
DR   AlphaFoldDB; Q07123; -.
DR   SMR; Q07123; -.
DR   GO; GO:0052595; F:aliphatic-amine oxidase activity; IEA:UniProtKB-EC.
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:InterPro.
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.
DR   PROSITE; PS01165; COPPER_AMINE_OXID_2; 1.
PE   1: Evidence at protein level;
KW   Copper; Direct protein sequencing; Disulfide bond; Manganese;
KW   Metal-binding; Oxidoreductase; TPQ.
FT   PROPEP          1..9
FT                   /evidence="ECO:0000269|PubMed:8366046"
FT                   /id="PRO_0000035677"
FT   CHAIN           10..648
FT                   /note="Copper methylamine oxidase"
FT                   /id="PRO_0000035678"
FT   REGION          629..648
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        301
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P12807"
FT   ACT_SITE        385
FT                   /note="Schiff-base intermediate with substrate; via
FT                   topaquinone"
FT                   /evidence="ECO:0000250|UniProtKB:P12807"
FT   BINDING         299..310
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P12807"
FT   BINDING         382..387
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P46883"
FT   BINDING         436
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000250|UniProtKB:P12807"
FT   BINDING         438
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000250|UniProtKB:P12807"
FT   BINDING         445
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250|UniProtKB:Q43077"
FT   BINDING         446
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250|UniProtKB:Q43077"
FT   BINDING         584
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250|UniProtKB:Q43077"
FT   BINDING         595
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000250|UniProtKB:P12807"
FT   MOD_RES         385
FT                   /note="2',4',5'-topaquinone"
FT                   /evidence="ECO:0000250|UniProtKB:P12807"
FT   DISULFID        320..346
FT                   /evidence="ECO:0000250|UniProtKB:P12807"
SQ   SEQUENCE   648 AA;  72806 MW;  B2FB2787492253B5 CRC64;
     MTLNAESEAL VGVSHPLDPL SRVEIARAVA ILKEGPAAAE SFRFISVELR EPSKDDLRAG
     VAVAREADAV LVDRAQARSF EAVVDLEAGT VDSWKLLAEN IQPPFMLDEF AECEDACRKD
     PEVIAALAKR GLTNLDLVCF EPWSVGYFGE DNEGRRLMRA LVFVRDEADD SPYAHPIENF
     IVFYDLNAGK VVRLEDDQAI PVPSARGNYL PKYVGEARTD LKPLNITQPE GASFTVTGNH
     VTWADWSFRV GFTPREGLVL HQLKFKDQGV DRPVINRASL SEMVVPYGDT APVQAKKNAF
     DSGEYNIGNM ANSLTLGCDC LGEIKYFDGH SVDSHGNPWT IENAICMHEE DDSILWKHFD
     FREGTAETRR SRKLVISFIA TVANYEYAFY WHLFLDGSIE FLVKATGILS TAGQLPGEKN
     PYGQSLNNDG LYAPIHQHMF NVRMDFELDG VKNAVYEVDM EYPEHNPTGT AFMAVDRLLE
     TEQKAIRKTN EAKHRFWKIA NHESKNLVNE PVAYRLIPTN GIQLAARDDA YVSKRAQFAR
     NNLWVTAYDR TERFAAGEYP NQATGADDGL HIWTQKDRNI VDTDLVVWYT FGMHHVVRLE
     DWPVMPRQNI GFMLEPHGFF NQNPTLNLPT STSTTQTGEA DTCCHTDK