ID   DFRA_PYRCO              Reviewed;         347 AA.
AC   Q84KP0; Q84K59;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 62.
DE   RecName: Full=Bifunctional dihydroflavonol 4-reductase/flavanone 4-reductase;
DE   AltName: Full=Dihydroflavonol 4-reductase;
DE            Short=DFR;
DE            EC=1.1.1.219 {ECO:0000269|PubMed:12667486};
DE   AltName: Full=Flavanone 4-reductase;
DE            Short=FNR;
DE            EC=1.1.1.234 {ECO:0000269|PubMed:12667486};
GN   Name=DFR;
OS   Pyrus communis (Pear) (Pyrus domestica).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Rosales; Rosaceae; Amygdaloideae; Maleae; Pyrus.
OX   NCBI_TaxID=23211;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP   BIOPHYSICOCHEMICAL PROPERTIES.
RC   STRAIN=cv. Abbe Fetel, cv. Conference, and cv. Pyrodwarf;
RX   PubMed=12667486; DOI=10.1016/s0003-9861(03)00013-4;
RA   Fischer T.C., Halbwirth H., Meisel B., Stich K., Forkmann G.;
RT   "Molecular cloning, substrate specificity of the functionally expressed
RT   dihydroflavonol 4-reductases from Malus domestica and Pyrus communis
RT   cultivars and the consequences for flavonoid metabolism.";
RL   Arch. Biochem. Biophys. 412:223-230(2003).
CC   -!- FUNCTION: Bifunctional enzyme involved in the flavonoid metabolism. May
CC       use dihydroquercetin, eriodictyol, garbanzol (5-
CC       deoxydihydrokaempferol), dihydrofisetin (5-deoxydihydroquercetin),
CC       dihydrokaempferol to a low extent (5%), but not naringenin, 5-
CC       deoxynaringenin or butin (5-deoxyeriodictyol) as substrate.
CC       {ECO:0000269|PubMed:12667486}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a (2R,3S,4S)-leucoanthocyanidin + NADP(+) = a (2R,3R)-
CC         dihydroflavonol + H(+) + NADPH; Xref=Rhea:RHEA:54444,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC         ChEBI:CHEBI:138176, ChEBI:CHEBI:138188; EC=1.1.1.219;
CC         Evidence={ECO:0000269|PubMed:12667486};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2S)-flavan-4-ol + NADP(+) = (2S)-flavanone + H(+) + NADPH;
CC         Xref=Rhea:RHEA:11228, ChEBI:CHEBI:15378, ChEBI:CHEBI:15605,
CC         ChEBI:CHEBI:15606, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC         EC=1.1.1.234; Evidence={ECO:0000269|PubMed:12667486};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=3.8 uM for eriodictyol {ECO:0000269|PubMed:12667486};
CC         KM=3.0 uM for dihydroquercetin {ECO:0000269|PubMed:12667486};
CC         Vmax=1.6 nmol/sec/g enzyme toward eriodictyol
CC         {ECO:0000269|PubMed:12667486};
CC         Vmax=4.7 nmol/sec/g enzyme toward dihydroquercetin
CC         {ECO:0000269|PubMed:12667486};
CC       pH dependence:
CC         Optimum pH is 5.75 with dihydroquercetin as substrate.
CC         {ECO:0000269|PubMed:12667486};
CC   -!- SIMILARITY: Belongs to the NAD(P)-dependent epimerase/dehydratase
CC       family. Dihydroflavonol-4-reductase subfamily. {ECO:0000305}.
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DR   EMBL; AY227730; AAO39818.1; -; mRNA.
DR   EMBL; AY227731; AAO39819.1; -; mRNA.
DR   EMBL; AY227732; AAO39820.1; -; mRNA.
DR   AlphaFoldDB; Q84KP0; -.
DR   SMR; Q84KP0; -.
DR   GO; GO:0045552; F:dihydrokaempferol 4-reductase activity; IEA:UniProtKB-EC.
DR   GO; GO:0047890; F:flavanone 4-reductase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009813; P:flavonoid biosynthetic process; IEA:UniProtKB-KW.
DR   InterPro; IPR001509; Epimerase_deHydtase.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   Pfam; PF01370; Epimerase; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
PE   1: Evidence at protein level;
KW   Flavonoid biosynthesis; NADP; Oxidoreductase.
FT   CHAIN           1..347
FT                   /note="Bifunctional dihydroflavonol 4-reductase/flavanone
FT                   4-reductase"
FT                   /id="PRO_0000367057"
FT   BINDING         44
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:A0A059TC02"
FT   BINDING         163
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:A0A059TC02"
FT   VARIANT         93
FT                   /note="R -> K (in strain: cv. Conference and cv.
FT                   Pyrodwarf)"
FT   VARIANT         347
FT                   /note="S -> G (in strain: cv. Conference and cv.
FT                   Pyrodwarf)"
SQ   SEQUENCE   347 AA;  38934 MW;  048D1FE898418E9E CRC64;
     MGSESESVCV TGASGFIGSW LVMRLLEHGY TVRATVRDPT NQKKVKHLLD LPKAETHLTL
     WKADLADEGS FDEAIQGCSG VFHVATPMDF ESRDPENEVI KPTINGLLDI LKACQKAKTV
     RKLVFTSSAG TVNVEEHQKP VYDESNWSDV EFCRSVKMTG WMYFVSKTLA EQAAWKYAKE
     NNIDFITIIP TLVIGPFLMP SMPPSLITGL SPILRNESHY GIIKQGQYVH LDDLCLSHIY
     LYKHPKAEGR YICSSHDATI HELVKMLREK YPEYNIPTKF KGIDDNLEPV HFSSKKLREI
     GFEFKYSLED MFVGAVDACR AKGLIPIPAE KTEAAEESNL VDVKVGS