ID   IFRH_LUPAL              Reviewed;         312 AA.
AC   P52581;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   27-MAR-2024, entry version 75.
DE   RecName: Full=Isoflavone reductase homolog;
DE            EC=1.3.1.-;
OS   Lupinus albus (White lupine) (Lupinus termis).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   genistoids sensu lato; core genistoids; Genisteae; Lupinus.
OX   NCBI_TaxID=3870;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Primovski; TISSUE=Root;
RA   Attucci S., Aitken S.M., Ibrahim R.K., Gulick P.J.;
RT   "A cDNA clone encoding an isoflavone reductase-like protein from white
RT   lupin.";
RL   (er) Plant Gene Register PGR96-012(1996).
CC   -!- SIMILARITY: Belongs to the NmrA-type oxidoreductase family. Isoflavone
CC       reductase subfamily. {ECO:0000305}.
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DR   EMBL; U48590; AAB67729.1; -; mRNA.
DR   PIR; T11035; T11035.
DR   AlphaFoldDB; P52581; -.
DR   SMR; P52581; -.
DR   GO; GO:0010283; F:pinoresinol reductase activity; IEA:UniProt.
DR   GO; GO:0009807; P:lignan biosynthetic process; IEA:UniProt.
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; IPR045312; PCBER-like.
DR   PANTHER; PTHR43349:SF4; PINORESINOL REDUCTASE 1-RELATED; 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..312
FT                   /note="Isoflavone reductase homolog"
FT                   /id="PRO_0000204552"
FT   ACT_SITE        138
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q9LD14"
FT   BINDING         10..16
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q9LD14"
FT   BINDING         35
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         142
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q9LD14"
FT   BINDING         270
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9LD14"
SQ   SEQUENCE   312 AA;  35129 MW;  6355CCB341411218 CRC64;
     MGKSKVLVVG GTGYVGRRIV KASLEHGHET FILQRPEIGL DIEKLQILLS FKKQGAILVE
     ASFSDHKSLV DAVKLVDVVI CTMSGVHFRS HNLLTQLKLV EAIKDAGNIK RFLPSEFGMD
     PALMGHALEP GRVTFDEKMT VRKAIEEANI PFTYISANCF AGYFAGNLSQ MKTLLPPRDK
     VLLYGDGNVK PVYMDEDDVA TYTIKTIDDP RTLNKTVYLR PPENILTHKE LIEKWEELIG
     KQLEKNSISE KDFLSTLKGL DFASQVGVGH FYHIFYEGCL TNFEIGENGE EASELYPEVN
     YTRMDQYLKV YV
//