ID   A0A1J9PPX1_9EURO        Unreviewed;       684 AA.
AC   A0A1J9PPX1;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   RecName: Full=Amine oxidase {ECO:0000256|RuleBase:RU000672};
DE            EC=1.4.3.- {ECO:0000256|RuleBase:RU000672};
GN   ORFNames=AJ78_01977 {ECO:0000313|EMBL:OJD17946.1};
OS   Emergomyces pasteurianus Ep9510.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Ajellomycetaceae; Emergomyces.
OX   NCBI_TaxID=1447872 {ECO:0000313|EMBL:OJD17946.1, ECO:0000313|Proteomes:UP000182235};
RN   [1] {ECO:0000313|EMBL:OJD17946.1, ECO:0000313|Proteomes:UP000182235}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UAMH 9510 {ECO:0000313|EMBL:OJD17946.1,
RC   ECO:0000313|Proteomes:UP000182235};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C.A., Munoz J.F., Imamovic A., Priest M.E., Young S., Clay O.K.,
RA   McEwen J.G.;
RT   "Emmonsia species relationships and genome sequence.";
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
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   -!- 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:OJD17946.1}.
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DR   EMBL; LGRN01000050; OJD17946.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1J9PPX1; -.
DR   STRING; 1447872.A0A1J9PPX1; -.
DR   VEuPathDB; FungiDB:AJ78_01977; -.
DR   OrthoDB; 34972at2759; -.
DR   Proteomes; UP000182235; Unassembled WGS sequence.
DR   GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR   GO; GO:0008131; F:primary amine oxidase activity; IEA:InterPro.
DR   GO; GO:0048038; F:quinone binding; IEA:InterPro.
DR   GO; GO:0009308; P:amine metabolic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.10.450.40; -; 2.
DR   Gene3D; 2.70.98.20; Copper amine oxidase, catalytic domain; 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   PANTHER; PTHR10638:SF33; AMINE OXIDASE; 1.
DR   PANTHER; PTHR10638; COPPER AMINE OXIDASE; 1.
DR   Pfam; PF01179; Cu_amine_oxid; 1.
DR   Pfam; PF02727; Cu_amine_oxidN2; 1.
DR   SUPFAM; SSF49998; Amine oxidase catalytic domain; 1.
DR   SUPFAM; SSF54416; Amine oxidase N-terminal region; 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   Reference proteome {ECO:0000313|Proteomes:UP000182235};
KW   TPQ {ECO:0000256|ARBA:ARBA00022772, ECO:0000256|PIRSR:PIRSR600269-50}.
FT   DOMAIN          7..100
FT                   /note="Copper amine oxidase N2-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02727"
FT   DOMAIN          245..652
FT                   /note="Copper amine oxidase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01179"
FT   REGION          653..684
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        317
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600269-50"
FT   ACT_SITE        401
FT                   /note="Schiff-base intermediate with substrate; via
FT                   topaquinone"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600269-50"
FT   MOD_RES         401
FT                   /note="2',4',5'-topaquinone"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600269-51"
SQ   SEQUENCE   684 AA;  77268 MW;  659CE587AF77FD86 CRC64;
     MNAATPHPFD PLTPEEISRA GRLVRPHFGG NDPNFRVITL QEPPKEQMIH FLEKEHRRQP
     IGEIPTRSAR VEVVVKGHDD ANELFELSVD LHNDKVSHKQ HLKGKHSYID ADYMKAVETA
     CLANEEVQAE IRSLDLPRGS TVVVEPWAYA TDGMNDMTQR VSMCWFYLRF EENPNANYYA
     YPLDICAEVS ESLKVSRIYR LPTKPNGRIN NEQRPFDRRK IRPTAATEYH PDLRPSPRTT
     TKAYQVVQPD GPSFRISGNH VKWEKWSFRV GFNYREGLTL HDIRYDGRSL FYRLSLAEMF
     VPYGDPRAPY PRKAAFDLGN DGAGINANNL QLGCDCLGTI KYFDGYHNTP SGEPLKMPNV
     VCCHEQDDGI LWKHTNFRTQ TPVVARSRIL VLQTIITVSN YEYILAFHFY QDASIFYEVR
     ATGILSTVPA DIDTKSKFPY GTTVAPGVLA PYHQHLFSLR IDPAVDGHSN SLVVEESKPL
     PVGNPSVHNP FGVGYCTESQ TIEEEGGFDL DITKNRTFKF VNEGKINPIT GTPVGFKLLP
     AYSQMLLSHP DSYHAKRSEF TKHAVWVTRY EDGDHFPAGR YTMQSTGGDG IASAIAERKN
     SKMAQSVRDQ DIVIWHTFGS THNPRIEDWP VMPSEKLMVG LKPVNFFSSN PGLDVAPSTQ
     EKNKSVLYSG DDSQTPETCC HSKL
//