ID   AMO1_ASPNG              Reviewed;         671 AA.
AC   Q12556;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2001, sequence version 2.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=Copper amine oxidase 1;
DE            EC=1.4.3.22 {ECO:0000250|UniProtKB:P19801};
GN   Name=AO-I;
OS   Aspergillus niger.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=5061;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 1-35; 538-565; 570-597
RP   AND 635-654.
RC   STRAIN=AKU 3302 / M-62;
RX   PubMed=8620882; DOI=10.1111/j.1432-1033.1996.0255n.x;
RA   Frebort I., Tamaki H., Ishida H., Pec P., Luhova L., Tsuno H., Halata M.,
RA   Asano Y., Kato Y., Matsushita K., Toyama H., Kumagai H., Adachi O.;
RT   "Two distinct quinoprotein amine oxidases are induced by n-butylamine in
RT   the mycelia of Aspergillus niger AKU 3302. Purification, characterization,
RT   cDNA cloning and sequencing.";
RL   Eur. J. Biochem. 237:255-265(1996).
RN   [2]
RP   SEQUENCE REVISION.
RC   STRAIN=AKU 3302 / M-62;
RA   Frebort I., Cernikova V., Hirota S., Yamada M., Adachi O., Pec P.;
RT   "Reassessment of the active site and the primary structure of the amine
RT   oxidase AO-I from Aspergillus niger AKU 3302.";
RL   Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + histamine + O2 = H2O2 + imidazole-4-acetaldehyde +
CC         NH4(+); Xref=Rhea:RHEA:25625, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:16240, ChEBI:CHEBI:27398, ChEBI:CHEBI:28938,
CC         ChEBI:CHEBI:58432; EC=1.4.3.22;
CC         Evidence={ECO:0000250|UniProtKB:P19801};
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 N-butylamine.
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; U31869; AAB03385.2; -; mRNA.
DR   PIR; S71320; S71320.
DR   AlphaFoldDB; Q12556; -.
DR   SMR; Q12556; -.
DR   STRING; 5061.CADANGAP00007551; -.
DR   VEuPathDB; FungiDB:An09g01550; -.
DR   VEuPathDB; FungiDB:ASPNIDRAFT2_1155673; -.
DR   VEuPathDB; FungiDB:ATCC64974_7100; -.
DR   VEuPathDB; FungiDB:M747DRAFT_371613; -.
DR   eggNOG; KOG1186; Eukaryota.
DR   BRENDA; 1.4.3.22; 518.
DR   GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR   GO; GO:0052597; F:diamine oxidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0052598; F:histamine oxidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0052599; F:methylputrescine oxidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008131; F:primary amine oxidase activity; IEA:InterPro.
DR   GO; GO:0052600; F:propane-1,3-diamine oxidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0048038; F:quinone binding; IEA:InterPro.
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   PANTHER; PTHR10638; PTHR10638; 1.
DR   Pfam; PF01179; Cu_amine_oxid; 1.
DR   SUPFAM; SSF49998; SSF49998; 1.
DR   SUPFAM; SSF54416; SSF54416; 2.
DR   PROSITE; PS01164; COPPER_AMINE_OXID_1; 1.
PE   1: Evidence at protein level;
KW   Copper; Direct protein sequencing; Disulfide bond; Glycoprotein; Manganese;
KW   Metal-binding; Oxidoreductase; TPQ.
FT   CHAIN           1..671
FT                   /note="Copper amine oxidase 1"
FT                   /id="PRO_0000064110"
FT   REGION          3..106
FT                   /note="N2"
FT   REGION          107..211
FT                   /note="N3"
FT   ACT_SITE        321
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P12807"
FT   ACT_SITE        405
FT                   /note="Schiff-base intermediate with substrate; via
FT                   topaquinone"
FT                   /evidence="ECO:0000250|UniProtKB:P12807"
FT   BINDING         319..330
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P12807"
FT   BINDING         402..407
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P46883"
FT   BINDING         455
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000250|UniProtKB:P12807"
FT   BINDING         457
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000250|UniProtKB:P12807"
FT   BINDING         464
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250|UniProtKB:Q43077"
FT   BINDING         606
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250|UniProtKB:Q43077"
FT   BINDING         617
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000250|UniProtKB:P12807"
FT   MOD_RES         405
FT                   /note="2',4',5'-topaquinone"
FT                   /evidence="ECO:0000250|UniProtKB:P12807"
FT   CARBOHYD        471
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   DISULFID        340..366
FT                   /evidence="ECO:0000250|UniProtKB:P12807"
SQ   SEQUENCE   671 AA;  75303 MW;  7413DF262A1BAE82 CRC64;
     MLPHPLAILS EEETNIARNV ILAQHPNTVI DFREIYLSEP PKAQLLEFLA LEHSGRLSPT
     SPRPPRLALC QYDVIGNDRI PSFEESVVDV GTRQRVQHRV VGKEHHASLT LSEFDTLVER
     CFASPLFQKA LADFDLPEGF EVVIEPWPYG GLDYVEEKRR YFQGLCFATD KRKNNPDANF
     YSYPLPLIPV MDALTQEIIR VDRPATGGKG EGLTEQTFKR DIIGHCKDSD YVPELNPGGT
     RKDLKPLNVV QPEGPSFRIT EESLVEWQKW RFRVAFNPRE GATIHDVWYD GRSVLYRLSV
     SEMTVPYADP RPPFHRKQAF DFGDGGGGNM ANNLSIGCDC LGVIKYFDAV MTGADGSAKK
     MPNAICLHEQ DNGIGWKHSN WRTGRAVVTR HRELVVQFII TLANYEYIFA YKFDQSGGIT
     VESRATGILN VVNIDAGKVS EYGNVVSGGV LAQNHQHIFC VRIDPAIDGP NNSVQVEESH
     PVPMNAVTNP NGNFYKVNTE TMERAGFFDA APELNRTVKM VNPHKKNPIS QKPVGYKFIP
     LATQRLLADP NSIQARRAQF AQHHVWVTKY RDGELYAGGR YTLQSQEEIE GVSDAVKRGD
     SVVDTDVVVW STFGITHNPR VEDWPVMPVE IFQLMIRPAD FFTANPSLDV PSDKNISSRV
     VGNDCCRNAH I