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Database: UniProt
Entry: A0A4P1QXD5_LUPAN
LinkDB: A0A4P1QXD5_LUPAN
Original site: A0A4P1QXD5_LUPAN 
ID   A0A4P1QXD5_LUPAN        Unreviewed;       716 AA.
AC   A0A4P1QXD5;
DT   03-JUL-2019, integrated into UniProtKB/TrEMBL.
DT   03-JUL-2019, sequence version 1.
DT   27-MAR-2024, entry version 14.
DE   RecName: Full=Amine oxidase {ECO:0000256|RuleBase:RU000672};
DE            EC=1.4.3.- {ECO:0000256|RuleBase:RU000672};
GN   ORFNames=TanjilG_00530 {ECO:0000313|EMBL:OIV96948.1};
OS   Lupinus angustifolius (Narrow-leaved blue lupine).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   genistoids sensu lato; core genistoids; Genisteae; Lupinus.
OX   NCBI_TaxID=3871 {ECO:0000313|EMBL:OIV96948.1, ECO:0000313|Proteomes:UP000188354};
RN   [1] {ECO:0000313|EMBL:OIV96948.1, ECO:0000313|Proteomes:UP000188354}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Tanjil {ECO:0000313|Proteomes:UP000188354};
RC   TISSUE=Whole plant {ECO:0000313|EMBL:OIV96948.1};
RX   PubMed=27557478; DOI=10.1111/pbi.12615;
RA   Hane J.K., Ming Y., Kamphuis L.G., Nelson M.N., Garg G., Atkins C.A.,
RA   Bayer P.E., Bravo A., Bringans S., Cannon S., Edwards D., Foley R.,
RA   Gao L.L., Harrison M.J., Huang W., Hurgobin B., Li S., Liu C.W.,
RA   McGrath A., Morahan G., Murray J., Weller J., Jian J., Singh K.B.;
RT   "A comprehensive draft genome sequence for lupin (Lupinus angustifolius),
RT   an emerging health food: insights into plant-microbe interactions and
RT   legume evolution.";
RL   Plant Biotechnol. J. 15:318-330(2017).
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|ARBA:ARBA00007983, ECO:0000256|RuleBase:RU000672}.
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DR   EMBL; CM007375; OIV96948.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A4P1QXD5; -.
DR   STRING; 3871.A0A4P1QXD5; -.
DR   Proteomes; UP000188354; Chromosome LG15.
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; 2.
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; IPR015802; Cu_amine_oxidase_N3.
DR   PANTHER; PTHR10638:SF97; AMINE OXIDASE; 1.
DR   PANTHER; PTHR10638; COPPER AMINE OXIDASE; 1.
DR   Pfam; PF01179; Cu_amine_oxid; 2.
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:UP000188354};
KW   TPQ {ECO:0000256|ARBA:ARBA00022772, ECO:0000256|RuleBase:RU000672}.
FT   DOMAIN          196..299
FT                   /note="Copper amine oxidase N3-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02728"
FT   DOMAIN          325..445
FT                   /note="Copper amine oxidase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01179"
FT   DOMAIN          446..683
FT                   /note="Copper amine oxidase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01179"
SQ   SEQUENCE   716 AA;  79196 MW;  BC80F3B0C6650155 CRC64;
     MVPPSCACCS AGNDSAIIPH IAAAAAPSAD WTANVPDDGR LNKMTIVHPV DSLPQPSINA
     KGIITLPRPQ PSHPLDPLSP AEISLAVATV RAAGKTPELK DGLRFMEIAL LEPDKHVVAL
     ADAYFFPPFQ PSLLPKGGFV IPTKLPPRCA RLLVYNRKTN ETSLWIVELS QVHAVTRGGN
     HLGKVISSQV VPDVQPPMDA VEYAECEAAV KSYPPFIEAM KKRGIENMEL VMVDPWCAGY
     FSEADDPNRR LAKPIIFCKC ESDCPMENGY ARPVEGIFVL VDMQKMEVIQ FEDRKLVPLP
     PVDPLRNYTH AATRGGTDRS DLKPLKIVQP EGPSFSVNGY YVEWQKWNFR IGFTPKEGLV
     IYSVAYVDGS QGLRPVAHRL SFVEMVVPYG DPNDPHYRKN AFDAGEDGLG RNAHSLKKGC
     DCSGIVKYFD AHFTNFTGGV ETIENCDGKM EAEVKLTGIL SMGALMPGEY RKYGTVIAPG
     LYAPVHQHFF VARMNMAVDS RPGEALNQVV EVNVKAEEPG DHNVHNNAFY AEETLLRSEM
     EAMRDCDPMT ARSWIVRNTR STNRTGHLTG YKLVPGSNCL PFAHSDAKFL RRGAFLKHNL
     WVTAYSPDEL FPGGEFPNQN PRIGDGLPTW VTQNRSLEES DIVLWYVFGV THVPRLEDWP
     VMPVEHIGFM LMPHGFFNCS PAIDVPPSKC ELEAKEKDIK DNGVLKPIEN SLASKL
//
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