ID A0A0E0K1U9_ORYPU Unreviewed; 158 AA.
AC A0A0E0K1U9;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Amine oxidase {ECO:0000256|RuleBase:RU000672};
DE EC=1.4.3.- {ECO:0000256|RuleBase:RU000672};
OS Oryza punctata (Red rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX NCBI_TaxID=4537 {ECO:0000313|EnsemblPlants:OPUNC02G20460.1};
RN [1] {ECO:0000313|EnsemblPlants:OPUNC02G20460.1}
RP NUCLEOTIDE SEQUENCE.
RA Wing R.;
RT "Oryza genome evolution.";
RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblPlants:OPUNC02G20460.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (APR-2015) to UniProtKB.
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|RuleBase:RU000672}.
CC -!- SIMILARITY: Belongs to the copper/topaquinone oxidase family.
CC {ECO:0000256|RuleBase:RU000672}.
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DR AlphaFoldDB; A0A0E0K1U9; -.
DR STRING; 4537.A0A0E0K1U9; -.
DR EnsemblPlants; OPUNC02G20460.1; OPUNC02G20460.1; OPUNC02G20460.
DR Gramene; OPUNC02G20460.1; OPUNC02G20460.1; OPUNC02G20460.
DR eggNOG; KOG1186; Eukaryota.
DR HOGENOM; CLU_1672133_0_0_1; -.
DR Proteomes; UP000026962; Chromosome 2.
DR GO; GO:0052594; F:aminoacetone:oxygen oxidoreductase(deaminating) activity; IEA:UniProtKB-EC.
DR GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR GO; GO:0052596; F:phenethylamine:oxygen oxidoreductase (deaminating) activity; IEA:UniProtKB-EC.
DR GO; GO:0048038; F:quinone binding; IEA:InterPro.
DR GO; GO:0052593; F:tryptamine:oxygen oxidoreductase (deaminating) activity; IEA:UniProtKB-EC.
DR GO; GO:0009308; P:amine metabolic process; IEA:UniProtKB-UniRule.
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 PANTHER; PTHR10638:SF18; AMINE OXIDASE; 1.
DR PANTHER; PTHR10638; COPPER AMINE OXIDASE; 1.
DR Pfam; PF01179; Cu_amine_oxid; 1.
DR SUPFAM; SSF49998; Amine oxidase catalytic domain; 1.
PE 3: Inferred from homology;
KW Copper {ECO:0000256|RuleBase:RU000672};
KW Metal-binding {ECO:0000256|RuleBase:RU000672};
KW Oxidoreductase {ECO:0000256|RuleBase:RU000672};
KW Reference proteome {ECO:0000313|Proteomes:UP000026962};
KW TPQ {ECO:0000256|RuleBase:RU000672}.
FT DOMAIN 14..91
FT /note="Copper amine oxidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01179"
SQ SEQUENCE 158 AA; 17920 MW; A3C80D80A6F321C1 CRC64;
MRSLRIQKKI SLVISVEQWN FRIGFTPKEG LVIQSVAYVD GNRGSRPIAH RLSFVEMVVP
YGDPNEPHYR KNVFDAGEDG LGKNAHSLKK TIENVVCLHE EDHGILWKHQ DWRTGLAEVI
RSRKLTVSLI EAEVKLTGIL SLGSLMPGEQ GNMYYYCP
//