ID   DFRA_MAIZE              Reviewed;         357 AA.
AC   P51108;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 102.
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=A1;
OS   Zea mays (Maize).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC   Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX   NCBI_TaxID=4577;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=cv. Wisconsin 22;
RX   PubMed=15981326; DOI=10.1002/j.1460-2075.1987.tb04752.x;
RA   Schwarz-Sommer Z., Shepherd N., Tacke E., Gierl A., Rohde W., Leclercq L.,
RA   Mattes M., Berndtgen R., Peterson P.A., Saedler H.;
RT   "Influence of transposable elements on the structure and function of the A1
RT   gene of Zea mays.";
RL   EMBO J. 6:287-294(1987).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=cv. Wisconsin 22;
RX   PubMed=1538691; DOI=10.1007/bf00292701;
RA   Meyer P., Linn F., Heidmann I., Heiner Meyer Z.A., Niedenhof I.,
RA   Saedler H.;
RT   "Endogenous and environmental factors influence 35S promoter methylation of
RT   a maize A1 gene construct in transgenic petunia and its colour phenotype.";
RL   Mol. Gen. Genet. 231:345-352(1992).
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; X05068; CAA28734.1; -; Genomic_DNA.
DR   AlphaFoldDB; P51108; -.
DR   SMR; P51108; -.
DR   STRING; 4577.GRMZM2G026930_P01; -.
DR   PaxDb; P51108; -.
DR   MaizeGDB; 13795; -.
DR   eggNOG; KOG1502; Eukaryota.
DR   BioCyc; MetaCyc:MON-18488; -.
DR   UniPathway; UPA00009; -.
DR   Proteomes; UP000007305; Unplaced.
DR   ExpressionAtlas; P51108; 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:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IBA:GO_Central.
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; Reference proteome.
FT   CHAIN           1..357
FT                   /note="Dihydroflavonol 4-reductase"
FT                   /id="PRO_0000215569"
FT   BINDING         49
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:A0A059TC02"
FT   BINDING         168
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:A0A059TC02"
SQ   SEQUENCE   357 AA;  38856 MW;  6892B51E30E52804 CRC64;
     MERGAGASEK GTVLVTGASG FVGSWLVMKL LQAGYTVRAT VRDPANVGKT KPLMDLPGAT
     ERLSIWKADL AEEGSFHDAI RGCTGVFHVA TPMDFLSKDP ENEVIKPTVE GMISIMRACK
     EAGTVRRIVF TSSAGTVNLE ERQRPVYDEE SWTDVDFCRR VKMTGWMYFV SKTLAEKAAL
     AYAAEHGLDL VTIIPTLVVG PFISASMPPS LITALALITG NAPHYSILKQ VQLIHLDDLC
     DAEIFLFENP AAAGRYVCSS HDVTIHGLAA MLRDRYPEYD VPQRFPGIQD DLQPVRFSSK
     KLQDLGFTFR YKTLEDMFDA AIRTCQEKGL IPLATAAGGD GFASVRAPGE TEATIGA