ID A0A0R0HYT4_SOYBN Unreviewed; 694 AA.
AC A0A0R0HYT4;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=Amine oxidase {ECO:0000256|RuleBase:RU000672};
DE EC=1.4.3.- {ECO:0000256|RuleBase:RU000672};
GN ORFNames=GLYMA_10G248700 {ECO:0000313|EMBL:KRH35530.1};
OS Glycine max (Soybean) (Glycine hispida).
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; Glycine;
OC Glycine subgen. Soja.
OX NCBI_TaxID=3847 {ECO:0000313|EMBL:KRH35530.1};
RN [1] {ECO:0000313|EMBL:KRH35530.1, ECO:0000313|EnsemblPlants:KRH35530}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Williams 82 {ECO:0000313|EnsemblPlants:KRH35530};
RC TISSUE=Callus {ECO:0000313|EMBL:KRH35530.1};
RX PubMed=20075913; DOI=10.1038/nature08670;
RA Schmutz J., Cannon S.B., Schlueter J., Ma J., Mitros T., Nelson W.,
RA Hyten D.L., Song Q., Thelen J.J., Cheng J., Xu D., Hellsten U., May G.D.,
RA Yu Y., Sakurai T., Umezawa T., Bhattacharyya M.K., Sandhu D.,
RA Valliyodan B., Lindquist E., Peto M., Grant D., Shu S., Goodstein D.,
RA Barry K., Futrell-Griggs M., Abernathy B., Du J., Tian Z., Zhu L., Gill N.,
RA Joshi T., Libault M., Sethuraman A., Zhang X.-C., Shinozaki K.,
RA Nguyen H.T., Wing R.A., Cregan P., Specht J., Grimwood J., Rokhsar D.,
RA Stacey G., Shoemaker R.C., Jackson S.A.;
RT "Genome sequence of the palaeopolyploid soybean.";
RL Nature 463:178-183(2010).
RN [2] {ECO:0000313|EnsemblPlants:KRH35530}
RP IDENTIFICATION.
RC STRAIN=Williams 82 {ECO:0000313|EnsemblPlants:KRH35530};
RG EnsemblPlants;
RL Submitted (FEB-2018) to UniProtKB.
RN [3] {ECO:0000313|EMBL:KRH35530.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Callus {ECO:0000313|EMBL:KRH35530.1};
RA Schmutz J., Cannon S., Schlueter J., Ma J., Mitros T., Nelson W., Hyten D.,
RA Song Q., Thelen J., Cheng J., Xu D., Hellsten U., May G., Yu Y.,
RA Sakurai T., Umezawa T., Bhattacharyya M., Sandhu D., Valliyodan B.,
RA Lindquist E., Peto M., Grant D., Shu S., Goodstein D., Barry K.,
RA Futrell-Griggs M., Abernathy B., Du J., Tian Z., Zhu L., Gill N., Joshi T.,
RA Libault M., Sethuraman A., Zhang X., Shinozaki K., Nguyen H., Wing R.,
RA Cregan P., Specht J., Grimwood J., Rokhsar D., Stacey G., Shoemaker R.,
RA Jackson S.;
RT "WGS assembly of Glycine max.";
RL Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
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 EMBL; CM000843; KRH35530.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0R0HYT4; -.
DR SMR; A0A0R0HYT4; -.
DR STRING; 3847.A0A0R0HYT4; -.
DR PaxDb; 3847-GLYMA10G39430-1; -.
DR EnsemblPlants; KRH35530; KRH35530; GLYMA_10G248700.
DR Gramene; KRH35530; KRH35530; GLYMA_10G248700.
DR InParanoid; A0A0R0HYT4; -.
DR OMA; HCIANEY; -.
DR Proteomes; UP000008827; Chromosome 10.
DR GO; GO:0052594; F:aminoacetone:oxygen oxidoreductase(deaminating) activity; IEA:UniProtKB-EC.
DR GO; GO:0005507; F:copper ion binding; IBA:GO_Central.
DR GO; GO:0052596; F:phenethylamine:oxygen oxidoreductase (deaminating) activity; IEA:UniProtKB-EC.
DR GO; GO:0008131; F:primary amine oxidase activity; IBA:GO_Central.
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; IBA:GO_Central.
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; COPPER AMINE OXIDASE; 1.
DR PANTHER; PTHR10638:SF40; PRIMARY AMINE OXIDASE 1; 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.
DR PROSITE; PS01164; COPPER_AMINE_OXID_1; 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:UP000008827};
KW TPQ {ECO:0000256|ARBA:ARBA00022772, ECO:0000256|PIRSR:PIRSR600269-50}.
FT DOMAIN 62..151
FT /note="Copper amine oxidase N2-terminal"
FT /evidence="ECO:0000259|Pfam:PF02727"
FT DOMAIN 158..250
FT /note="Copper amine oxidase N3-terminal"
FT /evidence="ECO:0000259|Pfam:PF02728"
FT DOMAIN 288..692
FT /note="Copper amine oxidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01179"
FT ACT_SITE 358
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600269-50"
FT ACT_SITE 446
FT /note="Schiff-base intermediate with substrate; via
FT topaquinone"
FT /evidence="ECO:0000256|PIRSR:PIRSR600269-50"
FT MOD_RES 446
FT /note="2',4',5'-topaquinone"
FT /evidence="ECO:0000256|PIRSR:PIRSR600269-51"
SQ SEQUENCE 694 AA; 78742 MW; EB4145063877BF03 CRC64;
MCYKIWYYKY NMEVVSIILY IPTPNSAVEN MIRRFGKAVP MIVQCFILVL SLKFISVNCL
AHPLDPLSPA EINKTRDIVQ GSYLGAIPNI TYHFVDAEEP DKKRVLEWLS SNSKEDKPII
PRQAKVVVRA KGETHELVVD LTKKSIVSDK IYTGHGYPPF TFNELFQASK LPLTYPIFKS
SIAKRGLNLS EVSCVPFTLG WYGEKITSRA LKVSCFYRGG SVNVWARPIE GITVLVDVDS
MQITMYNDRY IAPLPKAEGT DFQSSSSNSN SRPKTSSSAS CNVTDIIGFT IKGNEVKWAN
WVFHVGFNAR AGMIISTASI FDAKRQKYRS VLYRGHVSET FVPYMDPTEE WYFRTFMDAG
EFGFGRAADT LQPRVDCPSN AVYMDGYMAG PNGEVQQVPR AICIFERNSG NVAWRHMEIN
NPQKLVRNGE PEITLVVRMV ATVGNYDYVL DWEFLRSGSI KVGVDLTGIM EMKAVPYTEK
SEIKERVFGT LVAENTIANY HDHHITYYLD LDIDDNSNSF INAKLQRARA TGFGTPRKSY
WTVVREIAKR EAEGRIRLGL EPAELLIVNP NKRTKLGNEV GYRLISAQPI TSLLSDDDYP
QRRASYTKYQ LWVTSYNRSE RWAGGFYADR SRGDDGLAVW SQRNREIENT DIVLWHTIGI
HHVPYQEDFA AMPAIHGGFE LRPANFFESS PLLE
//
