ID   V4KDB3_EUTSA            Unreviewed;       712 AA.
AC   V4KDB3;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   02-DEC-2020, entry version 23.
DE   RecName: Full=Amine oxidase {ECO:0000256|RuleBase:RU000672};
DE            EC=1.4.3.- {ECO:0000256|RuleBase:RU000672};
GN   ORFNames=EUTSA_v10023306mg {ECO:0000313|EMBL:ESQ29104.1};
OS   Eutrema salsugineum (Saltwater cress) (Sisymbrium salsugineum).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Eutremeae; Eutrema.
OX   NCBI_TaxID=72664 {ECO:0000313|EMBL:ESQ29104.1, ECO:0000313|Proteomes:UP000030689};
RN   [1] {ECO:0000313|EMBL:ESQ29104.1, ECO:0000313|Proteomes:UP000030689}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23518688; DOI=10.3389/fpls.2013.00046;
RA   Yang R., Jarvis D.E., Chen H., Beilstein M.A., Grimwood J., Jenkins J.,
RA   Shu S., Prochnik S., Xin M., Ma C., Schmutz J., Wing R.A.,
RA   Mitchell-Olds T., Schumaker K.S., Wang X.;
RT   "The Reference Genome of the Halophytic Plant Eutrema salsugineum.";
RL   Front. Plant Sci. 4:46-46(2013).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an aliphatic amine + H2O + O2 = an aldehyde + H2O2 + NH4(+);
CC         Xref=Rhea:RHEA:16153, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:16240, ChEBI:CHEBI:17478, ChEBI:CHEBI:28938,
CC         ChEBI:CHEBI:58001; EC=1.4.3.21;
CC         Evidence={ECO:0000256|ARBA:ARBA00001138};
CC   -!- COFACTOR:
CC       Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC         Evidence={ECO:0000256|ARBA:ARBA00001935};
CC   -!- COFACTOR:
CC       Name=L-topaquinone; Xref=ChEBI:CHEBI:79027;
CC         Evidence={ECO:0000256|PIRSR:PIRSR600269-51};
CC       Note=Contains 1 topaquinone per subunit.
CC       {ECO:0000256|PIRSR:PIRSR600269-51};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
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; KI517881; ESQ29104.1; -; Genomic_DNA.
DR   RefSeq; XP_006391818.1; XM_006391756.1.
DR   STRING; 72664.XP_006391818.1; -.
DR   GeneID; 18010301; -.
DR   KEGG; eus:EUTSA_v10023306mg; -.
DR   eggNOG; KOG1186; Eukaryota.
DR   OrthoDB; 1320015at2759; -.
DR   Proteomes; UP000030689; Unassembled WGS sequence.
DR   GO; GO:0052595; F:aliphatic-amine oxidase activity; IEA:UniProtKB-EC.
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:0008131; F:primary amine oxidase 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; -; 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; PTHR10638; 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; SSF49998; 1.
DR   SUPFAM; SSF54416; SSF54416; 2.
DR   PROSITE; PS01165; COPPER_AMINE_OXID_2; 1.
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:UP000030689};
KW   TPQ {ECO:0000256|ARBA:ARBA00022772, ECO:0000256|PIRSR:PIRSR600269-50,
KW   ECO:0000256|RuleBase:RU000672}.
FT   DOMAIN          60..142
FT                   /note="Cu_amine_oxidN2"
FT                   /evidence="ECO:0000259|Pfam:PF02727"
FT   DOMAIN          152..250
FT                   /note="Cu_amine_oxidN3"
FT                   /evidence="ECO:0000259|Pfam:PF02728"
FT   DOMAIN          275..696
FT                   /note="Cu_amine_oxid"
FT                   /evidence="ECO:0000259|Pfam:PF01179"
FT   ACT_SITE        354
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600269-50"
FT   ACT_SITE        442
FT                   /note="Schiff-base intermediate with substrate; via
FT                   topaquinone"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600269-50"
FT   MOD_RES         442
FT                   /note="2',4',5'-topaquinone"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600269-51"
SQ   SEQUENCE   712 AA;  79856 MW;  6B6101D3C10B67AA CRC64;
     MAQPSFARLS LLFFGFLLLF ATYSWVFGPD SGFLSGTRVR KTLGSDPKLR VDHSSDKPHH
     PLDPLTVREI ERVRSILSGH DPDFRSGSAT IHSMALDEPD KARVVRWKKG NRLPSRRAEV
     VALSGGKSHV ITVDLESGRV VSDLINPSSG YPILTMDDLI AASQVPFKSI EFNRSIEARG
     VKFSDLVCIT PFAGWFGPEE EGRRIIRVQC YTSKDTPNYF MRPLEGLYAM VDMNKLEVIK
     VVDKGPVPIP KAAGTEYRYS VLNKPVHMDP INPISMEQPG GPSFRVEGGH LVKWANWVFH
     VKADQRAGMI ISQATVRDSE TGEPRSVMYK GFPSELFVPY MDPEELWYYK TYMDAGELGL
     GPPAMPLVPL NDCPRNAYYI DGIFASPDGK AIVQPNMICL FERYAGDVSW RHSEILIPNV
     DIKEARPKVT LVARMATSVG NYDYIVDWEF QTDGLIRVTV AASGMLMVKG TPYENVDDLG
     DKEDDSGPLI SENVIGVVHD HFITFHLDMD IDGHTNNSLV KFHLEKQRIP TGKSPRKSYL
     KVKKYVAKTE KDAQIKLNLY DPYEFHIVNP NRKSRIGNPA GYKIVPGGNA ASLLDHDDPP
     QIRGAFTNNQ IWVTQYNRSE QFAGGVLVYQ SHGDDTLQVW SDRDRSIENK DIVLWYTLGF
     HHVPCQEDYP VMPTVAASFE LKPANFFETN PILGVAPFLE KDLPVCRPFA SS
//