ID   DFRA_SOLLC              Reviewed;         379 AA.
AC   P51107;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 94.
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};
OS   Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum;
OC   Solanum subgen. Lycopersicon.
OX   NCBI_TaxID=4081;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Hypocotyl;
RX   PubMed=7907304; DOI=10.1016/0378-1119(94)90799-4;
RA   Bongue-Bartelsman M., O'Neill S.D., Tong Y., Yoder J.I.;
RT   "Characterization of the gene encoding dihydroflavonol 4-reductase in
RT   tomato.";
RL   Gene 138:153-157(1994).
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   -!- TISSUE SPECIFICITY: Expressed in both leaf and hypocotyl tissues.
CC   -!- SIMILARITY: Belongs to the NAD(P)-dependent epimerase/dehydratase
CC       family. Dihydroflavonol-4-reductase subfamily. {ECO:0000305}.
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DR   EMBL; Z18277; CAA79154.1; -; mRNA.
DR   PIR; S38474; S38474.
DR   RefSeq; NP_001234408.1; NM_001247479.1.
DR   AlphaFoldDB; P51107; -.
DR   SMR; P51107; -.
DR   STRING; 4081.Solyc02g085020.2.1; -.
DR   PaxDb; P51107; -.
DR   PRIDE; P51107; -.
DR   GeneID; 544150; -.
DR   KEGG; sly:544150; -.
DR   eggNOG; KOG1502; Eukaryota.
DR   OrthoDB; 992332at2759; -.
DR   BRENDA; 1.1.1.219; 3101.
DR   UniPathway; UPA00009; -.
DR   Proteomes; UP000004994; Unplaced.
DR   ExpressionAtlas; P51107; baseline and differential.
DR   GO; GO:0045552; F:dihydrokaempferol 4-reductase activity; IBA:GO_Central.
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; IBA:GO_Central.
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; Reference proteome.
FT   CHAIN           1..379
FT                   /note="Dihydroflavonol 4-reductase"
FT                   /id="PRO_0000215568"
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   379 AA;  42429 MW;  8B23708B01E4A989 CRC64;
     MASEAHAVVD AHSPPKTTTV WVTGGAGFIG SWLVMRLLER GYNVHATVRD PENQKKVKHL
     LELPKADTNL TLWKADLAVE GSFDEAIQGC QGVFHVATPM DFESKDPENE VIKPTVRGML
     SIIESCAKAN TVKRLVFTSS AGTLDVQEDQ KLFYDETSWS DLDFIYAKKM TGWMYFVSKI
     LAEKAAMEEA RKNNIDFISI IPPLVVGPFI TSTFPPSLIT ALSLITAHYG IIKQGQYVHL
     DDLCEAHIFL YEHPKAEGRF ICSSHHAIIY DVAKMVRQKW PEYYVPTEFK GIDKDLALVS
     FSSKKLMDIK FQFKHTLEDM YKGAIETCRQ KQLLPFSTRS TADNGKDKEA IPISTENYSS
     GKENAPVANC TGKFTNGEI