IFR_PEA
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 03-AUG-2022, entry version 79.
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).
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; Pisum.
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 + 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 -!- PATHWAY: Phytoalexin biosynthesis; pterocarpan phytoalexin
CC biosynthesis.
CC -!- SIMILARITY: Belongs to the NmrA-type oxidoreductase family. Isoflavone
CC reductase subfamily. {ECO:0000305}.
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DR EMBL; S72472; AAB31368.1; -; mRNA.
DR PIR; S48631; S48631.
DR AlphaFoldDB; P52576; -.
DR SMR; P52576; -.
DR PRIDE; 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: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 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