ID   DFRA_PETHY              Reviewed;         380 AA.
AC   P14720;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 2.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=Dihydroflavonol 4-reductase;
DE            Short=DFR;
DE            EC=1.1.1.219 {ECO:0000250|UniProtKB:Q9XES5};
DE   AltName: Full=Dihydrokaempferol 4-reductase;
DE   AltName: Full=Flavanone 4-reductase;
DE            Short=FNR;
DE            EC=1.1.1.234 {ECO:0000250|UniProtKB:Q9XES5};
GN   Name=DFRA; Synonyms=AN6;
OS   Petunia hybrida (Petunia).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Petunioideae; Petunia.
OX   NCBI_TaxID=4102;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=cv. Violet 30; TISSUE=Leaf;
RX   PubMed=7920718; DOI=10.1046/j.1365-313x.1994.06030295.x;
RA   Huits H., Gerats A.G.M., Kreike M.M., Mol J.N., Koes R.E.;
RT   "Genetic control of dihydroflavonol 4-reductase gene expression in Petunia
RT   hybrida.";
RL   Plant J. 6:295-310(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. R27;
RX   PubMed=2491667; DOI=10.1007/bf00027309;
RA   Beld M., Martin C., Huits H., Stuitje A.R., Gerats A.G.M.;
RT   "Flavonoid synthesis in Petunia hybrida: partial characterization of
RT   dihydroflavonol-4-reductase genes.";
RL   Plant Mol. Biol. 13:491-502(1989).
CC   -!- FUNCTION: Bifunctional enzyme involved in flavonoid metabolism.
CC       {ECO:0000250|UniProtKB:Q9XES5}.
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:0000250|UniProtKB:Q9XES5};
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:0000250|UniProtKB:Q9XES5};
CC   -!- PATHWAY: Pigment biosynthesis; anthocyanin biosynthesis.
CC   -!- SIMILARITY: Belongs to the NAD(P)-dependent epimerase/dehydratase
CC       family. Dihydroflavonol-4-reductase subfamily. {ECO:0000305}.
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DR   EMBL; X79723; CAA56160.1; -; Genomic_DNA.
DR   EMBL; X15537; CAA33544.1; -; mRNA.
DR   PIR; S07463; S07463.
DR   AlphaFoldDB; P14720; -.
DR   SMR; P14720; -.
DR   ABCD; P14720; 5 sequenced antibodies.
DR   UniPathway; UPA00009; -.
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:0009718; P:anthocyanin-containing compound biosynthetic process; IEA:UniProtKB-UniPathway.
DR   InterPro; IPR001509; Epimerase_deHydtase.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   Pfam; PF01370; Epimerase; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
PE   2: Evidence at transcript level;
KW   Flavonoid biosynthesis; NADP; Oxidoreductase.
FT   CHAIN           1..380
FT                   /note="Dihydroflavonol 4-reductase"
FT                   /id="PRO_0000215571"
FT   BINDING         54
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:A0A059TC02"
FT   BINDING         173
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:A0A059TC02"
FT   CONFLICT        1..16
FT                   /note="MASEAVHAPSPPVAVP -> MPLHLRCSA (in Ref. 2)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        71
FT                   /note="W -> L (in Ref. 2; CAA33544)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   380 AA;  42435 MW;  6D7138AD5126868A CRC64;
     MASEAVHAPS PPVAVPTVCV TGAAGFIGSW LVMRLLERGY NVHATVRDPE NKKKVKHLLE
     LPKADTNLTL WKADLTVEGS FDEAIQGCQG VFHVATPMDF ESKDPENEVI KPTVRGMLSI
     IESCAKANTV KRLVFTSSAG TLDVQEQQKL FYDQTSWSDL DFIYAKKMTG WMYFASKILA
     EKAAMEEAKK KNIDFISIIP PLVVGPFITP TFPPSLITAL SLITGNEAHY CIIKQGQYVH
     LDDLCEAHIF LYEHPKADGR FICSSHHAII YDVAKMVREK WPEYYVPTEF KGIDKDLPVV
     SFSSKKLTDM GFQFKYTLED MYKGAIDTCR QKQLLPFSTR SAEDNGHNRE AIAISAQNYA
     SGKENAPVAN HTEMLSNVEV