ID   A0A0K3CAM7_RHOTO        Unreviewed;       781 AA.
AC   A0A0K3CAM7;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   RecName: Full=Amine oxidase {ECO:0000256|RuleBase:RU000672};
DE            EC=1.4.3.- {ECO:0000256|RuleBase:RU000672};
GN   Name=FGENESH: predicted gene_5.180 {ECO:0000313|EMBL:CTR06774.1};
GN   ORFNames=BN2166_0026350 {ECO:0000313|EMBL:CTR06774.1};
OS   Rhodotorula toruloides (Yeast) (Rhodosporidium toruloides).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC   Microbotryomycetes; Sporidiobolales; Sporidiobolaceae; Rhodotorula.
OX   NCBI_TaxID=5286 {ECO:0000313|EMBL:CTR06774.1, ECO:0000313|Proteomes:UP000199069};
RN   [1] {ECO:0000313|EMBL:CTR06774.1, ECO:0000313|Proteomes:UP000199069}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Single colony {ECO:0000313|EMBL:CTR06774.1};
RA   Cajimat M.N.B., Milazzo M.L., Fulhorst C.F.;
RL   Submitted (JUL-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; CWKI01000005; CTR06774.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0K3CAM7; -.
DR   STRING; 5286.A0A0K3CAM7; -.
DR   OMA; PYNSQDV; -.
DR   Proteomes; UP000199069; 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   InterPro; IPR015328; DUF1965.
DR   PANTHER; PTHR10638:SF20; 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   Pfam; PF09248; DUF1965; 1.
DR   PRINTS; PR00766; CUDAOXIDASE.
DR   SUPFAM; SSF49998; Amine oxidase catalytic domain; 1.
DR   SUPFAM; SSF54416; Amine oxidase N-terminal region; 2.
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:UP000199069};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   TPQ {ECO:0000256|ARBA:ARBA00022772, ECO:0000256|PIRSR:PIRSR600269-51}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..781
FT                   /note="Amine oxidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5005495303"
FT   DOMAIN          78..154
FT                   /note="Copper amine oxidase N2-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02727"
FT   DOMAIN          243..311
FT                   /note="DUF1965"
FT                   /evidence="ECO:0000259|Pfam:PF09248"
FT   DOMAIN          324..711
FT                   /note="Copper amine oxidase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01179"
FT   MOD_RES         464
FT                   /note="2',4',5'-topaquinone"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600269-51"
SQ   SEQUENCE   781 AA;  87518 MW;  AFED2A5E67AD4E1C CRC64;
     MHVAGLLGAL LAATAVTAAP SPKLPYFRGT RPRPAIQNFV SNVASAQYNL TDIPGEPTTK
     APHSNIWATL SNDEAAEVVA FLHNQTALNL TAASDAGSWD NQITVIDLAV PNKTETLKYL
     SGKGPRPPRM AYATIMFNSV EEPYVEDYLV GPLPVSANTT YHPYSFRTTK GTSKVRNYDA
     DSDATYEFMV DAAKTCDDVV EDLLGAPTES WDIWGIDPLW HEDGRVISWV GFWGVPESVF
     DGETLLPQGL YMKFDFTGRD PSGWAFLGWL HDGIFYPTTA DFRHAWSNGK VAKTTRNAGM
     NETWIGTDRD GAELPYDNRP PPIQVAPGGQ RFAIDEDAQY VEWMDFSFYW SFRRDSGMRL
     WDIKYQNQTV LYELGLNEAL AHCEWYGFGP YAFEAIEGYD CPTYAHYAPT TFFANEVATT
     HRKSVCFFED TESFPIQRHA NGQYVAATKN VVLKMKSVST VGNYDYSFVY SFMLDGSIGV
     EVMASGYIQS AYYAQNGEYG YRIHDGLSGS MHDHVLNWKA DFDVLGTKNT FAMHTVEAKE
     VKYPWSNHTR STMHLVRDTL KNEENATLHW PANGKSMYLV YNAEEKNKYG EERAWRIMPH
     IGGAGMHATI QNSSNLGPSL NFAKAPLYVT KHHDSEFSSA HASNAYDPYN PVIDFAKYLD
     GENLEQEDLV LWFNLGMHHV PHTGDLGNTV HTTAHAGMIM SPHNYLLRDP SRRSSQMIRL
     NYNSSASDVV SEVLTFGGQQ ASGLFNLTAI QPDYKAYIGD SNVRKFPYDP QHPYNDTESI
     V
//