ID   DFRA_ANTMA              Reviewed;         446 AA.
AC   P14721;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1990, 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=DFRA;
OS   Antirrhinum majus (Garden snapdragon).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Lamiales; Plantaginaceae; Antirrhineae; Antirrhinum.
OX   NCBI_TaxID=4151;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. JI:522;
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).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-51.
RX   PubMed=3021338; DOI=10.1016/0092-8674(86)90451-4;
RA   Coen E.S., Carpenter R., Martin C.;
RT   "Transposable elements generate novel spatial patterns of gene expression
RT   in Antirrhinum majus.";
RL   Cell 47:285-296(1986).
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; X15536; CAA33543.1; -; mRNA.
DR   EMBL; M14756; AAA32664.1; -; Genomic_DNA.
DR   PIR; S07464; S07464.
DR   AlphaFoldDB; P14721; -.
DR   SMR; P14721; -.
DR   PRIDE; P14721; -.
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..446
FT                   /note="Dihydroflavonol 4-reductase"
FT                   /id="PRO_0000215562"
FT   REGION          421..446
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         56
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:A0A059TC02"
FT   BINDING         175
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:A0A059TC02"
SQ   SEQUENCE   446 AA;  49633 MW;  8BF4352EFBAC88D8 CRC64;
     MSPTSLNTSS ETAPPSSTTV CVTGAAGFIG SWLVMRLLER GYTVRATVRD PGNMKKVKHL
     IELPKADTNL TLWKADMTVE GSFDEAIQGC EGVFHLATSM EFDSVDPENE VIKPTIDGML
     NIIKSCVQAK TVKKFIFTTS GGTVNVEEHQ KPVYDETDSS DMDFINSKKM TGWMYFVSKI
     LAEKAGMEAA KENNIDFISI IPPLVVGPFI MPTFPPSLIT ALSPITGNEA HYSIIKQCQY
     VHLDDLCEGH IFLFEYPKAE GRYICSSHDA TIYDIAKLIT ENWPEYHIPD EFEGIDKDIP
     VVSFSSKKMI GMGFIFKYTL EDMVRGAIDT CREKGMLPYS TKNNKGDEKE PILNSLENNY
     NIQDKELFPI SEEKHINGQE NALLSNTQDK ELLPTSEEKR VNGLESALLS KIQDKEVLPT
     SGVKHAKGQE NALLPDIAND HTDGRI