ID   IFR_PEA                 Reviewed;         318 AA.
AC   P52576;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   28-JAN-2026, entry version 87.
DE   RecName: Full=Isoflavone reductase;
DE            Short=IFR;
DE            EC=1.3.1.45;
DE   AltName: Full=2'-hydroxyisoflavone reductase;
DE   AltName: Full=NADPH:isoflavone oxidoreductase;
GN   Name=IFR;
OS   Pisum sativum (Garden pea) (Lathyrus oleraceus).
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; Hologalegina; IRL clade; Fabeae; Lathyrus.
OX   NCBI_TaxID=3888;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Alaska Green;
RX   PubMed=8037464; DOI=10.1006/abbi.1994.1338;
RA   Paiva N.L., Sun Y., Dixon R.A., Vanetten H.D., Hrazdina G.;
RT   "Molecular cloning of isoflavone reductase from pea (Pisum sativum L.):
RT   evidence for a 3R-isoflavanone intermediate in (+)-pisatin biosynthesis.";
RL   Arch. Biochem. Biophys. 312:501-510(1994).
CC   -!- FUNCTION: Reduces achiral isoflavones to chiral isoflavanones during
CC       the biosynthesis of chiral pterocarpan phytoalexins. The reduction
CC       product (sophrol) is a third isomer, which represents the penultimate
CC       intermediate in the synthesis of the phytoalexin (+)-pisatin, the major
CC       phytoalexin in pea.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(3R)-vestitone + NADP(+) = 2'-hydroxyformononetin + NADPH + 2
CC         H(+); 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   -!- PATHWAY: Phytoalexin biosynthesis; pterocarpan phytoalexin
CC       biosynthesis.
CC   -!- SIMILARITY: Belongs to the NmrA-type oxidoreductase family. Isoflavone
CC       reductase subfamily. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; S72472; AAB31368.1; -; mRNA.
DR   PIR; S48631; S48631.
DR   AlphaFoldDB; P52576; -.
DR   SMR; P52576; -.
DR   UniPathway; UPA00901; -.
DR   GO; GO:0047526; F:2'-hydroxyisoflavone reductase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009807; P:lignan biosynthetic process; IEA:UniProtKB-ARBA.
DR   CDD; cd05259; PCBER_SDR_a; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   Gene3D; 3.90.25.10; UDP-galactose 4-epimerase, domain 1; 1.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR008030; NmrA-like.
DR   InterPro; IPR050608; NmrA-type/Isoflavone_red_sf.
DR   InterPro; IPR045312; PCBER-like.
DR   PANTHER; PTHR43349:SF53; ISOFLAVONE REDUCTASE; 1.
DR   PANTHER; PTHR43349; PINORESINOL REDUCTASE-RELATED; 1.
DR   Pfam; PF05368; NmrA; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE   2: Evidence at transcript level;
KW   NADP; Oxidoreductase.
FT   CHAIN           1..318
FT                   /note="Isoflavone reductase"
FT                   /id="PRO_0000204547"
FT   ACT_SITE        144
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q9LD14"
FT   BINDING         11..17
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q9LD14"
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;  35429 MW;  6318CF6617CDE28F CRC64;
     MATENKILIL GATGAIGRHI VWASIKAGNP TYALVRKTSD NVNKPKLTEA ANPETKEELL
     KNYQASGVIL LEGDINDHET LVNAIKQVDT VICAAGRLLI EDQVKVIKAI KEAGNVKRFF
     PSEFGLDVDR HDAVEPVRQV FEEKASIRRV VESEGVPYTY LCCHAFTGYF LRNLAQIDAT
     DPPRDKVVIL GDGNVRGAYV TEADVGTYTI RAANDPNTLN KAVHIRLPNN YLTANEVIAL
     WEKKIGKTLE KTYVSEEQVL KDIQTSSFPH NYLLALYHSQ QIKGDAVYEI DPAKDVEAYD
     AYPDVKYTTA DEYLNQFV
//