ID   A0A428PGI1_9HYPO        Unreviewed;       681 AA.
AC   A0A428PGI1;
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=CEP53_008183 {ECO:0000313|EMBL:RSL52127.1};
OS   Fusarium sp. AF-6.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC   Fusarium solani species complex.
OX   NCBI_TaxID=1325737 {ECO:0000313|EMBL:RSL52127.1, ECO:0000313|Proteomes:UP000287544};
RN   [1] {ECO:0000313|EMBL:RSL52127.1, ECO:0000313|Proteomes:UP000287544}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL62590 {ECO:0000313|EMBL:RSL52127.1,
RC   ECO:0000313|Proteomes:UP000287544};
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:RSL52127.1}.
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DR   EMBL; NKCJ01000188; RSL52127.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A428PGI1; -.
DR   STRING; 1325737.A0A428PGI1; -.
DR   Proteomes; UP000287544; 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:UP000287544};
KW   TPQ {ECO:0000256|ARBA:ARBA00022772, ECO:0000256|PIRSR:PIRSR600269-50}.
FT   DOMAIN          3..72
FT                   /note="Copper amine oxidase N2-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02727"
FT   DOMAIN          234..643
FT                   /note="Copper amine oxidase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01179"
FT   REGION          563..587
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        567..587
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        306
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600269-50"
FT   ACT_SITE        390
FT                   /note="Schiff-base intermediate with substrate; via
FT                   topaquinone"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600269-50"
FT   MOD_RES         390
FT                   /note="2',4',5'-topaquinone"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600269-51"
SQ   SEQUENCE   681 AA;  76099 MW;  66F74625CC2890E7 CRC64;
     MHHPLDPLSA AEIAVVATLI KSSQPEGAVH FKNITLVEPP KTETRRFLAA ERKGATGSVK
     PTRRASALFY HRRTVDLFLA TVNLDASRLE QVEKLDEKYH GHADMDEVIE VRDTCLRHPA
     VKARIGRYEL PDNFTVVCDT WPYGRDTGGK LRRLAQCFLY AKDSSHPGSN SYDNPLPFSP
     IIDYVTKELV DIMDLPIGSD HNLSPEVKYI PHPPKEWHHD LQPEPKRTDL KPLTVSQPLG
     ASFTVDGCLV QWQKWRFRVG FNWREGMVIH DVTYAGRELF HRLSLSEMFV PYGDPRTPYS
     RKSVFDVGDI GAGVAANNLS LGCDCLGLIK YFSFTLSDSN GRPVEKPNVI CMHEIDDGIG
     WKHTDGATKE TSIVRSRVLV LQTIITVGNY EYIFMWNFDQ AAALHYKIQA TGILSTVPIA
     PGATVPYGTN VNQGVMAPYH QHVFSLRIDP ALDGDKNSFL EEDSVAMPFD SSNPVGVGYI
     TEKRVIRNAG YSTAKPNRVH KIINPSVINK ISGCPVAYAI HSPQKQMLLA HPDSWHGKRA
     KFALQPYWVT TYRDGELYAA GDHTYQSLPD GEDEGNESLG KERKGDLATW AGRGDKVDGE
     DIVLWHSISL THNPRPEDYP VMPCETMMVS LKPSGFFEHN PALDVPQSTQ RSNQSTLYEG
     QLMPTVLGKH KSAQICCESK L
//