ID A0A1S3W1W9_VIGRR Unreviewed; 773 AA.
AC A0A1S3W1W9;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Amine oxidase {ECO:0000256|RuleBase:RU000672};
DE EC=1.4.3.- {ECO:0000256|RuleBase:RU000672};
GN Name=LOC106780771 {ECO:0000313|RefSeq:XP_014524565.1};
OS Vigna radiata var. radiata (Mung bean) (Phaseolus aureus).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Vigna.
OX NCBI_TaxID=3916 {ECO:0000313|Proteomes:UP000087766, ECO:0000313|RefSeq:XP_014524565.1};
RN [1] {ECO:0000313|RefSeq:XP_014524565.1}
RP IDENTIFICATION.
RC TISSUE=Leaf {ECO:0000313|RefSeq:XP_014524565.1};
RG RefSeq;
RL Submitted (NOV-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|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 RefSeq; XP_014524565.1; XM_014669079.2.
DR AlphaFoldDB; A0A1S3W1W9; -.
DR STRING; 3916.A0A1S3W1W9; -.
DR GeneID; 106780771; -.
DR KEGG; vra:106780771; -.
DR OrthoDB; 34972at2759; -.
DR Proteomes; UP000087766; Unplaced.
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 GO; GO:0042221; P:response to chemical; IEA:UniProt.
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; IPR015802; Cu_amine_oxidase_N3.
DR PANTHER; PTHR10638:SF18; 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; PF02728; Cu_amine_oxidN3; 1.
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:UP000087766};
KW TPQ {ECO:0000256|ARBA:ARBA00022772, ECO:0000256|PIRSR:PIRSR600269-50}.
FT DOMAIN 80..169
FT /note="Copper amine oxidase N2-terminal"
FT /evidence="ECO:0000259|Pfam:PF02727"
FT DOMAIN 205..308
FT /note="Copper amine oxidase N3-terminal"
FT /evidence="ECO:0000259|Pfam:PF02728"
FT DOMAIN 334..743
FT /note="Copper amine oxidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01179"
FT REGION 1..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 747..773
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 412
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600269-50"
FT ACT_SITE 496
FT /note="Schiff-base intermediate with substrate; via
FT topaquinone"
FT /evidence="ECO:0000256|PIRSR:PIRSR600269-50"
FT MOD_RES 496
FT /note="2',4',5'-topaquinone"
FT /evidence="ECO:0000256|PIRSR:PIRSR600269-51"
SQ SEQUENCE 773 AA; 86492 MW; 9449C3B8A09DA510 CRC64;
MATAQEKTTP CCATGTNKPS SSASLQLQQQ PQQQPQQQQQ PSQQQQQRPS VATFIPAIDS
PPKTASAKGI TVMVRAQTSH PLDPLSAAEI SVAVATVRAA GTTPEVRDGM RFIEVDLVEP
EKQVVALADA YFFPPFQPSL LPRTKGGPVI PTKLPPRKAR LVVYNKKSNE TSIWIVELRE
VHAATRGGHH RGKVVSSTVV PDVQPPMDAV EYAECEAVVK DFPPFREAMK KRGIEDMDLV
MVDPWCAGYH SEADAPSRRL AKPLIFCRTE SDCPMENGYA RPVEGIHVLV DMQNMVVLEF
EDRKLVPLPP ADPLRNYTSG ETRGGVDRSD VKPLQIIQPE GPSFRVNGHF IEWQKWNFRI
GFTPREGLVI HSVAYIDGSR GRRPVAHRLS FVEMVVPYGD PNDPHYRKNA FDAGEDGLGK
NAHSLKKGCD CLGYIKYFDA HFTNFYGGVE TIENCVCLHE EDHGILWKHQ DWRTGLAEVR
RSRRLTVSFI CTVANYEYGF FWHFYQDGKI EAEVKLTGIL SLGALQPGET RKYGTTIAPG
LYAPVHQHFF VARMDMAVDC KPGEAFNQVV EMNVKVEDPG ENNIHNNAFY AEEKLLKSEL
EAMRDCDPLS ARHWIVRNTR TVNRTGHLTG YKLVPGSNCL PLAGSEAKFL RRASFLKHNL
WVTPYARDEM HPGGEFPNQN PRVGEGLATW VKQNRSLEEA DIVLWYVFGV THIPRLEDWP
VMPVERIGFM LMPHGFFNCS PAIDVPPNPG DLDDKENNGL PAKPIQNGLI AKL
//
