ID   A0A0G4L798_9PEZI        Unreviewed;       944 AA.
AC   A0A0G4L798;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=Amine oxidase {ECO:0000256|RuleBase:RU000672};
DE            EC=1.4.3.- {ECO:0000256|RuleBase:RU000672};
GN   ORFNames=BN1708_012110 {ECO:0000313|EMBL:CRK17610.1};
OS   Verticillium longisporum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Plectosphaerellaceae; Verticillium.
OX   NCBI_TaxID=100787 {ECO:0000313|EMBL:CRK17610.1, ECO:0000313|Proteomes:UP000044602};
RN   [1] {ECO:0000313|EMBL:CRK17610.1, ECO:0000313|Proteomes:UP000044602}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VL1 {ECO:0000313|EMBL:CRK17610.1};
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; CVQH01008779; CRK17610.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G4L798; -.
DR   STRING; 100787.A0A0G4L798; -.
DR   OrthoDB; 34972at2759; -.
DR   Proteomes; UP000044602; Unassembled WGS sequence.
DR   GO; GO:0052595; F:aliphatic amine oxidase activity; IEA:RHEA.
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   InterPro; IPR015802; Cu_amine_oxidase_N3.
DR   PANTHER; PTHR10638; COPPER AMINE OXIDASE; 1.
DR   PANTHER; PTHR10638:SF86; COPPER AMINE OXIDASE 1-RELATED; 1.
DR   Pfam; PF01179; Cu_amine_oxid; 1.
DR   Pfam; PF02727; Cu_amine_oxidN2; 1.
DR   Pfam; PF02728; Cu_amine_oxidN3; 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.
DR   PROSITE; PS01165; COPPER_AMINE_OXID_2; 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          29..112
FT                   /note="Copper amine oxidase N2-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02727"
FT   DOMAIN          119..220
FT                   /note="Copper amine oxidase N3-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02728"
FT   DOMAIN          246..657
FT                   /note="Copper amine oxidase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01179"
FT   ACT_SITE        323
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600269-50"
FT   ACT_SITE        407
FT                   /note="Schiff-base intermediate with substrate; via
FT                   topaquinone"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600269-50"
FT   MOD_RES         407
FT                   /note="2',4',5'-topaquinone"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600269-51"
SQ   SEQUENCE   944 AA;  105081 MW;  A7D8D951D7BF17DB CRC64;
     MYPYQLNLRN LPVSYSSVMP AAVNGTLPHP FDPLTSAEIE QAIVAVQKAH GELFYNVVSL
     HEPRKAEMTA WLADPAAAPR PARIADVVVI AKGGKVYEGF VDLVEDKITQ WDLLDGVQPI
     ITMEELVVVE HICRKDPKVI EQCEISGIPK EEMHKVYCDP WTIGYDERHG NVVRLQQALM
     YYRPDVDTCQ YQYPLDFCPI YDVDKQEIVD IDIPKIRRPI SKTKPVDYHP AAIEKNGGYR
     KDIKPINITQ PEGVSFKIEG RELEWQNWKF HIGFNYREGI VLNNITYNDK GNVRPIFYRL
     SLAEMVVPYG NPEHPHQRKH AFDLGEYGAG YMTNALTLGC DCKGSIHYLD AEFPTRAGGV
     RTIKNAICIH EEDSGILFKH SDFRDDSIIV TRARKLIVQQ IFTAANYEYA IQWIFHQDGT
     IQPEIKLTGI LNTYAMNEGE DTKGWGTQVF PGVNAHNHQH LFCLRVDPNI DGPRNTVFQV
     DTVASDAPVG SRENFYGNAF GARRTKLDTT GNSKTDYNGA TSRTWEIANT SKLHPYSGKP
     ASYKLVSREV PGLLPKEGSL VLKRAAFARH AVHVTKYRDD QLWPAGQHVP QTSGEPSRGI
     PEWIGDGTES IEDEDVVLWH TFGVTHIPAP EDFPVMPVEP ITLLLRPRNF FRNNPVLDVP
     PSYASTPSQV AAGKGALDAA DKENCHLPIR HLADNRSWNA TGTVAVPPLD NGDEDWFVST
     TLTDIRKTNV YFDGWPTAQD LAVFLSVPQS FVGTETGNAT RVCGYTMPGQ NATSVGDASS
     EDSCSGVLSE ERIEEALKTP MTPSDGSCPE LDLGDKCDVS TGFRTSNPVQ LNPSVCVLDN
     LPHTDVPNGY RSFAGFPGWR IMPPDEEENE FDVYDLRVQQ TVPMLFTVQS GSQEKVYLVC
     LAPNKVVDGS REPQAEFPPS DAGVVWRGSG LAFAVTFMAA AMQL
//