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Database: UniProt
Entry: A0A0G4LLP8_9PEZI
LinkDB: A0A0G4LLP8_9PEZI
Original site: A0A0G4LLP8_9PEZI 
ID   A0A0G4LLP8_9PEZI        Unreviewed;       632 AA.
AC   A0A0G4LLP8;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   RecName: Full=Amine oxidase {ECO:0000256|RuleBase:RU000672};
DE            EC=1.4.3.- {ECO:0000256|RuleBase:RU000672};
GN   ORFNames=BN1708_013568 {ECO:0000313|EMBL:CRK22972.1};
OS   Verticillium longisporum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Plectosphaerellaceae; Verticillium.
OX   NCBI_TaxID=100787 {ECO:0000313|EMBL:CRK22972.1, ECO:0000313|Proteomes:UP000044602};
RN   [1] {ECO:0000313|EMBL:CRK22972.1, ECO:0000313|Proteomes:UP000044602}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VL1 {ECO:0000313|EMBL:CRK22972.1};
RA   Wang D.B., Wang M.;
RL   Submitted (MAY-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}.
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DR   EMBL; CVQH01014891; CRK22972.1; -; Genomic_DNA.
DR   STRING; 100787.A0A0G4LLP8; -.
DR   OrthoDB; 34972at2759; -.
DR   Proteomes; UP000044602; 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:UP000044602};
KW   TPQ {ECO:0000256|ARBA:ARBA00022772, ECO:0000256|PIRSR:PIRSR600269-50}.
FT   DOMAIN          36..123
FT                   /note="Copper amine oxidase N2-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02727"
FT   DOMAIN          269..625
FT                   /note="Copper amine oxidase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01179"
FT   ACT_SITE        341
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600269-50"
FT   ACT_SITE        425
FT                   /note="Schiff-base intermediate with substrate; via
FT                   topaquinone"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600269-50"
FT   MOD_RES         425
FT                   /note="2',4',5'-topaquinone"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600269-51"
SQ   SEQUENCE   632 AA;  70968 MW;  279C53B3EC349AC1 CRC64;
     MSERESTHSS KNAASCIGYF TFSPTDLSIL SIMSIHPFEP LTPSEINETT NILKKSWPAD
     KLFFRAITLA EPPKKDMIVF LDDEQSSPGS GARPPRQTRV QVFIEKLLHE IIVNLDQQAV
     ASNKELHGRH SYIDTDFMKQ VGDACLADEQ VQREIESLKL PEGATVVVEP WAYATDGVKD
     MKERWTMGWF YMRLSDHPEA NYYAYPLDIC AEVSPDLKVT SVYRLPSAAG DKTHTRQAEF
     DERKIVDAGK SEYHPDLLTS HRTTTKPYHV SQPEGPSFST EGNLITWEKW TMRVGFNYRE
     GMTLHDVRYD GRSLFYRLSL AEMFVPYADP RAPYPRKAAF DLGNDGAGVN ANNLGLGCDC
     LGHIRYFDGW LTTAAGEPLR MPNVVCCHEI DDGILWKHTN FRTGNAVVTR SRVLVLQTII
     TVSNYEYLFL FYFQQDASLF YEVRATGIMS TAPIDIGDTV PYGTIVAPGT LAPYHQHLFC
     LRIDPAIGGH ANSLVVEESH AMAFEEEDAS GEDCNPFGVG YTTTSQVIEK ETGLDLDFHT
     NRVFKMVNEA KRNTITGTPI GFKLLPCYSQ LLLAHPKSYH ARRSEYAAHA VWVTRHDDEE
     LFPAGRHTMQ SLGGEGIASW IAARRHDEAX SG
//
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