ID   DFRA_HORVU              Reviewed;         354 AA.
AC   P51106;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 89.
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=ANT18;
OS   Hordeum vulgare (Barley).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Pooideae; Triticodae; Triticeae; Hordeinae; Hordeum.
OX   NCBI_TaxID=4513;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=cv. Gula;
RX   PubMed=1720864; DOI=10.1007/bf00290650;
RA   Kristiansen K.N., Rohde W.;
RT   "Structure of the Hordeum vulgare gene encoding dihydroflavonol-4-reductase
RT   and molecular analysis of ant18 mutants blocked in flavonoid synthesis.";
RL   Mol. Gen. Genet. 230:49-59(1991).
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; S69616; AAB20555.1; -; Genomic_DNA.
DR   PIR; S18595; S18595.
DR   AlphaFoldDB; P51106; -.
DR   SMR; P51106; -.
DR   EnsemblPlants; HORVU.MOREX.r2.3HG0227210.1; HORVU.MOREX.r2.3HG0227210.1; HORVU.MOREX.r2.3HG0227210.
DR   EnsemblPlants; HORVU.MOREX.r2.3HG0227210.1.mrna1; HORVU.MOREX.r2.3HG0227210.1.mrna1; HORVU.MOREX.r2.3HG0227210.1.
DR   Gramene; HORVU.MOREX.r2.3HG0227210.1; HORVU.MOREX.r2.3HG0227210.1; HORVU.MOREX.r2.3HG0227210.
DR   Gramene; HORVU.MOREX.r2.3HG0227210.1.mrna1; HORVU.MOREX.r2.3HG0227210.1.mrna1; HORVU.MOREX.r2.3HG0227210.1.
DR   OMA; KERLTLW; -.
DR   UniPathway; UPA00009; -.
DR   ExpressionAtlas; P51106; baseline and differential.
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   3: Inferred from homology;
KW   Flavonoid biosynthesis; NADP; Oxidoreductase.
FT   CHAIN           1..354
FT                   /note="Dihydroflavonol 4-reductase"
FT                   /id="PRO_0000215567"
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"
SQ   SEQUENCE   354 AA;  38435 MW;  528524A832815AC9 CRC64;
     MDGNKGPVVV TGASGFVGSW LVMKLLQAGY TVRATVRDPA NVEKTKPLLE LPGAKERLSI
     WKADLSEDGS FNEAIAGCTG VFHVATPMDF DSQDPENEVI KPTVEGMLSI MRACKEAGTV
     KRIVFTSSAG SVNIEERPRP AYDQDNWSDI DYCRRVKMTG WMYFVSKALA EKAAMEYASE
     NGLDFISIIP TLVVGPFLSA GMPPSLVTAL ALITGNEAHY SILKQVQLVH LDDLCDAMTF
     LFEHPEANGR YICSSHDATI HGLARMLQDR FPEYDIPQKF AGVDDNLQPI HFSSKKLLDH
     GFSFRYTTED MFDAAIHTCR DKGLIPLGDV PAPAAGGKLG ALAAGEGQAI GAET