ID   A0A428TQV1_9HYPO        Unreviewed;       681 AA.
AC   A0A428TQV1;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   24-JAN-2024, entry version 16.
DE   RecName: Full=Amine oxidase {ECO:0000256|RuleBase:RU000672};
DE            EC=1.4.3.- {ECO:0000256|RuleBase:RU000672};
GN   ORFNames=CEP52_006853 {ECO:0000313|EMBL:RSM04423.1};
OS   Fusarium oligoseptatum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC   Fusarium solani species complex.
OX   NCBI_TaxID=2604345 {ECO:0000313|EMBL:RSM04423.1, ECO:0000313|Proteomes:UP000287144};
RN   [1] {ECO:0000313|EMBL:RSM04423.1, ECO:0000313|Proteomes:UP000287144}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL62579 {ECO:0000313|EMBL:RSM04423.1,
RC   ECO:0000313|Proteomes:UP000287144};
RA   Stajich J.E., Carrillo J., Kijimoto T., Eskalen A., O'Donnell K.,
RA   Kasson M.;
RT   "Comparative genomic analysis of Ambrosia Fusariam Clade fungi.";
RL   Submitted (JUN-2017) 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:RSM04423.1}.
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DR   EMBL; NKCK01000059; RSM04423.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A428TQV1; -.
DR   STRING; 1325735.A0A428TQV1; -.
DR   Proteomes; UP000287144; 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:UP000287144};
KW   TPQ {ECO:0000256|ARBA:ARBA00022772, ECO:0000256|PIRSR:PIRSR600269-50}.
FT   DOMAIN          6..98
FT                   /note="Copper amine oxidase N2-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02727"
FT   DOMAIN          244..651
FT                   /note="Copper amine oxidase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01179"
FT   ACT_SITE        316
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600269-50"
FT   ACT_SITE        400
FT                   /note="Schiff-base intermediate with substrate; via
FT                   topaquinone"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600269-50"
FT   MOD_RES         400
FT                   /note="2',4',5'-topaquinone"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600269-51"
SQ   SEQUENCE   681 AA;  77404 MW;  A8B2B65C5FB957AD CRC64;
     MALSIHPFDP LQPDEISRAA EIVHPHFAGR DINFRVITLR EPPKKEMIQF LEKEHRKQSA
     GQPPARCARV EVVLESKTGN HELFELLVDL DNNRVTAKQH HKGKHSYIDS EYMRKVEEAC
     LADDRVREEI RTLDLPSGAT VVVEPWAYAT DGMNDMTQRV TMCWFYLRLL ENPDANYYAY
     PLDICAEVSE QLQVTKVYRL PTTPHERIHN ESRPFDRKTI HATAASEYHP DLRPSPRTTT
     KPYQVIQPEG PSFKIRRNHV NWEKWSFRVG FNYREGMTLH DIYYDGRSLF YRLSLAEMFV
     PYGDPRAPYP RKAAFDLGND GAGINANNLQ LGCDCLGTIK YFDGYHNTSS GEPMKMPNVI
     CCHEQDDGIL WKHTNPRTGN AVVTRSRILV LQTIITVSNY EYIFAFHFCQ DASIFYEVRA
     TGIVSTAPTG VGLKETTPYG TVLAPGVLAP YHQHLFSLRI DPAIDGHSNS LAIEESKALP
     YRDPSVHNPF GVGYVTEQKI VEREGGFDLD HTKARTFKFI NENKVNPITN TPVGFKLLPA
     YSQMLLSHPD SFHAKRSEFG KHAVWITRYE DDDHFPSGKH TMQSPGGDGI ASRISKRNAE
     GVAHSVRNND IVIWHTFGST HNPRIEDWPV MPSEKMMVGL KPVNFFSGNP GLDVAVSTQD
     KNKSVLYTDE EKPNHCCHSR L
//