ID   IFR_CICAR               Reviewed;         318 AA.
AC   Q00016;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 92.
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   Cicer arietinum (Chickpea) (Garbanzo).
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; Cicereae; Cicer.
OX   NCBI_TaxID=3827;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC   STRAIN=cv. ILC 3279;
RX   PubMed=1915347; DOI=10.1111/j.1432-1033.1991.tb16241.x;
RA   Tiemann K., Inze D., van Montagu M., Barz W.;
RT   "Pterocarpan phytoalexin biosynthesis in elicitor-challenged chickpea
RT   (Cicer arietinum L.) cell cultures. Purification, characterization and cDNA
RT   cloning of NADPH:isoflavone oxidoreductase.";
RL   Eur. J. Biochem. 200:751-757(1991).
RN   [2]
RP   CHARACTERIZATION.
RC   STRAIN=cv. ILC 3279;
RA   Tiemann K., Hinderer W., Barz W.;
RT   "Isolation of NADPH:isoflavone oxidoreductase, a new enzyme of Pterocarpan
RT   phytoalexin biosynthesis in cell suspension cultures of Cicer arietinum.";
RL   FEBS Lett. 213:324-328(1987).
CC   -!- FUNCTION: Reduces achiral isoflavones to chiral isoflavanones during
CC       the biosynthesis of chiral pterocarpan phytoalexins.
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; X60755; CAA43167.1; -; mRNA.
DR   PIR; S17830; S17830.
DR   RefSeq; NP_001266030.1; NM_001279101.1.
DR   AlphaFoldDB; Q00016; -.
DR   SMR; Q00016; -.
DR   STRING; 3827.XP_004512065.1; -.
DR   GeneID; 101508729; -.
DR   KEGG; cam:101508729; -.
DR   eggNOG; ENOG502QPMY; Eukaryota.
DR   OrthoDB; 936727at2759; -.
DR   UniPathway; UPA00901; -.
DR   Proteomes; UP000087171; Chromosome Ca8.
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   1: Evidence at protein level;
KW   Direct protein sequencing; NADP; Oxidoreductase; Reference proteome.
FT   CHAIN           1..318
FT                   /note="Isoflavone reductase"
FT                   /id="PRO_0000204545"
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;  35408 MW;  437A1AD6843E0773 CRC64;
     MASQNRILVL GPTGAIGRHV VWASIKAGNP TYALIRKTPG DINKPSLVAA ANPESKEELL
     QSFKAAGVIL LEGDMNDHEA LVKAIKQVDT VICTFGRLLI LDQVKIIKAI KEAGNVKRFF
     PSEFGLDVDR HDAVDPVRPV FDEKASIRRV VEAEGVPYTY LCCHAFTGYF LRNLAQFDAT
     EPPRDKVIIL GDGNVKGAYV TEADVGTYTI RAANDPRTLN KAVHIRLPHN YLTSNEVVSL
     WEKKIGKTLE KSYISEEKVL KDINVSTFPH NYLLALYHSQ QIKGDAVYEI DPAKDAEAYD
     LYPDVKYTTA DEYLDQFV