ID   A0A2X0MXS3_9BASI        Unreviewed;       747 AA.
AC   A0A2X0MXS3;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=Amine oxidase {ECO:0000256|RuleBase:RU000672};
DE            EC=1.4.3.- {ECO:0000256|RuleBase:RU000672};
GN   ORFNames=BZ3500_MVSOF-1268-A1-R1_CHR4-3G07289
GN   {ECO:0000313|EMBL:SCZ97604.1};
OS   Microbotryum saponariae.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC   Microbotryomycetes; Microbotryales; Microbotryaceae; Microbotryum.
OX   NCBI_TaxID=289078 {ECO:0000313|EMBL:SCZ97604.1, ECO:0000313|Proteomes:UP000249723};
RN   [1] {ECO:0000313|Proteomes:UP000249723}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Jeantristanb JTB J.-T., Ricardo R.;
RL   Submitted (OCT-2016) 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; FMWP01000093; SCZ97604.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2X0MXS3; -.
DR   STRING; 289078.A0A2X0MXS3; -.
DR   Proteomes; UP000249723; 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; 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; 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.
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:UP000249723};
KW   TPQ {ECO:0000256|ARBA:ARBA00022772, ECO:0000256|PIRSR:PIRSR600269-50}.
FT   DOMAIN          132..221
FT                   /note="Copper amine oxidase N3-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02728"
FT   DOMAIN          297..723
FT                   /note="Copper amine oxidase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01179"
FT   REGION          237..264
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        237..251
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        376
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600269-50"
FT   ACT_SITE        461
FT                   /note="Schiff-base intermediate with substrate; via
FT                   topaquinone"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600269-50"
FT   MOD_RES         461
FT                   /note="2',4',5'-topaquinone"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600269-51"
SQ   SEQUENCE   747 AA;  83051 MW;  2B21735E28EFDC18 CRC64;
     MPSVEAISSA PGACGARNAA KAHPLDPLTV GEIQLVSAAF KNEMFQRGVL SVKSCHVDLV
     EPPKLEVIAY LGISTSPTDV SPVSSGVMPK RRAEAALIDT LTGDVYVLTA EIVAGTKAIV
     EKVEKLPEGV QPAITNEEMT QSEEVVRNDP EVIRLCAEVG VKKEQIMCDC WSIGYEHRFG
     KGVRLQQAFV YARLGADEHL YAHPLDFNCV VDTNAEKILK IGELIGHFAP HRTSATAPDA
     LSGTTAPHTV EGDSFKDSGR DRIPPPLERH DYLPDLIREK AQSEGRDWDV RQDLKPLHVQ
     QPEGVSFEMK GNRIKWQNWD MHIGFNYREG IVLNHVQHFD REEGRYRPIM YRASFAEMVV
     PYAAPEWPHP RKFAFDVGEY GIGMMANSLT LGCDCLGSIH YLDAVMSGHD GQPIKLDRAV
     CIHEEDDGLL WKHTDFRPGG RAHSVRSRKL IIQMICTVAN YEYLFAWGFK QDGTMELEIK
     LTGILNTYLL AQGEHAEAFG TQVAPRIVAH HHQHIFCLRL DPMIDGLNNS VVETEIHPLE
     APTGSDENWA GNGFEARKRV LQTTKEGARL ADAPSSRMWS FVNQDKKHYS TGTAAGYKLM
     CKDFPPLLAK EDSLVARRAT FAKKNLWVTP FVDGQFFPAG KYPTQSFKAP EDSLEFWIKD
     DKPIVQKDIV TWVSFGVTHL PRAEDFPVSF IGLTTSCCNP IVPAEHVLLQ LKPVNFFRAN
     PSLDTPASSD ARSVMALPPN AGNECCH
//