ID   A0A3B3Y001_9TELE        Unreviewed;       158 AA.
AC   A0A3B3Y001;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   RecName: Full=Amine oxidase {ECO:0000256|RuleBase:RU000672};
DE            EC=1.4.3.- {ECO:0000256|RuleBase:RU000672};
OS   Poecilia mexicana.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC   Poecilia.
OX   NCBI_TaxID=48701 {ECO:0000313|Ensembl:ENSPMEP00000020694.1, ECO:0000313|Proteomes:UP000261480};
RN   [1] {ECO:0000313|Ensembl:ENSPMEP00000020694.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) 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; A0A3B3Y001; -.
DR   STRING; 48701.ENSPMEP00000020694; -.
DR   Ensembl; ENSPMET00000030380.1; ENSPMEP00000020694.1; ENSPMEG00000023854.1.
DR   Proteomes; UP000261480; Unplaced.
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; 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; COPPER AMINE OXIDASE; 1.
DR   PANTHER; PTHR10638:SF4; RETINA-SPECIFIC COPPER AMINE OXIDASE; 1.
DR   Pfam; PF01179; Cu_amine_oxid; 1.
DR   SUPFAM; SSF49998; Amine oxidase catalytic domain; 1.
DR   PROSITE; PS01165; COPPER_AMINE_OXID_2; 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   TPQ {ECO:0000256|RuleBase:RU000672}.
FT   DOMAIN          16..107
FT                   /note="Copper amine oxidase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01179"
SQ   SEQUENCE   158 AA;  17841 MW;  5DDB9DA3046E79CF CRC64;
     IFRDNKSVCY SIFSIFSRYK VAITKHKDSE QTSSSLYSQN DVWTPAVDFS KYIEDNESIE
     DQDLVAWVTT GFLHIPHAED IPNTVTVGNG GGVILRPHNY FDEDPSISST DSVYFSPGAE
     GSCENNRMAC LTHETCTPTL ETFTYHGFDG VMKFEDWK
//