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
//