IFR_SOYBN
ID IFR_SOYBN Reviewed; 318 AA.
AC I1LHU6; I1LHU8;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2012, sequence version 1.
DT 03-AUG-2022, entry version 54.
DE RecName: Full=Isoflavone reductase {ECO:0000303|PubMed:28394400};
DE Short=GmIFR {ECO:0000303|PubMed:28394400};
DE EC=1.3.1.45 {ECO:0000269|PubMed:28394400};
DE AltName: Full=2'-hydroxyisoflavone reductase {ECO:0000305};
DE AltName: Full=NADPH:isoflavone oxidoreductase {ECO:0000305};
GN Name=IFR {ECO:0000303|PubMed:28394400};
GN ORFNames=GLYMA_11G070500 {ECO:0000312|EMBL:KRH28705.1};
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Jiao Y.;
RT "Duplications and functional specialization force distinct evolution of
RT isoflavonoid biosynthetic genes in legumes.";
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Williams 82;
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 [3]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=28394400; DOI=10.1093/pcp/pcw213;
RA Uchida K., Akashi T., Aoki T.;
RT "The missing link in leguminous pterocarpan biosynthesis is a dirigent
RT domain-containing protein with isoflavanol dehydratase activity.";
RL Plant Cell Physiol. 58:398-408(2017).
CC -!- FUNCTION: Reduces achiral isoflavones to chiral isoflavanones during
CC the biosynthesis of chiral pterocarpan phytoalexins (PubMed:28394400).
CC The reduction product is a third isomer, which represents the
CC penultimate intermediate in the synthesis of the phytoalexin (-)-
CC medicarpin, the major phytoalexin in soybean (PubMed:28394400).
CC {ECO:0000269|PubMed:28394400}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(3R)-vestitone + NADP(+) = 2'-hydroxyformononetin + 2 H(+) +
CC NADPH; Xref=Rhea:RHEA:22560, ChEBI:CHEBI:15378, ChEBI:CHEBI:16786,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:77687; EC=1.3.1.45;
CC Evidence={ECO:0000269|PubMed:28394400};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:22562;
CC Evidence={ECO:0000269|PubMed:28394400};
CC -!- SEQUENCE CAUTION:
CC Sequence=KRH28706.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; MH450263; QBF58795.1; -; mRNA.
DR EMBL; CM000844; KRH28705.1; -; Genomic_DNA.
DR EMBL; CM000844; KRH28706.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; NP_001276127.1; NM_001289198.1.
DR AlphaFoldDB; I1LHU6; -.
DR SMR; I1LHU6; -.
DR PRIDE; I1LHU6; -.
DR EnsemblPlants; KRH28705; KRH28705; GLYMA_11G070500.
DR GeneID; 100781316; -.
DR Gramene; KRH28705; KRH28705; GLYMA_11G070500.
DR KEGG; gmx:100781316; -.
DR eggNOG; ENOG502QPMY; Eukaryota.
DR HOGENOM; CLU_060833_0_1_1; -.
DR InParanoid; I1LHU6; -.
DR Proteomes; UP000008827; Chromosome 11.
DR ExpressionAtlas; I1LHU6; baseline and differential.
DR GO; GO:0047526; F:2'-hydroxyisoflavone reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR GO; GO:0009807; P:lignan biosynthetic process; IEA:UniProt.
DR CDD; cd05259; PCBER_SDR_a; 1.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR008030; NmrA-like.
DR InterPro; IPR045312; PCBER-like.
DR Pfam; PF05368; NmrA; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 1: Evidence at protein level;
KW NADP; Oxidoreductase; Plant defense; Reference proteome.
FT CHAIN 1..318
FT /note="Isoflavone reductase"
FT /id="PRO_0000450382"
FT ACT_SITE 144
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P52575"
FT BINDING 11..17
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P52575"
FT BINDING 36
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q9LD14"
FT BINDING 44
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q9LD14"
FT BINDING 148
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q9LD14"
SQ SEQUENCE 318 AA; 35523 MW; 6A67E09BCBF00975 CRC64;
MAGKDRILIL GPTGAIGRHI VWASVKAGNP TFVLVRNTPG SNNRVNLVKA ANPETKEELI
ESFKNSGVNL IQGDMNDHES LVNAIKQVDV VICAFGRLLI EDQLKIIAAI KEAGNVKRFF
PSEFGLDVDR HDSVDPVREV FEEKARIRRI IEAEGIPYTY LCCHAFTGYF LRNLAQIDIT
VPPRDKVFIL GDGNVKGAFV TEADVGTLTI EAANDPNALN KTVHIRLPKN YLTINEIISL
WENKIGKTLE KTYVSEEKVL KDIKEASFPN NYLLALYHSQ QIKGDAVYEI DTAKDLEASE
AYPNVEYTTV DEYLNQFV