DFRA_VITVI
ID DFRA_VITVI Reviewed; 337 AA.
AC P51110;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 98.
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=DFR;
OS Vitis vinifera (Grape).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; Vitales; Vitaceae; Viteae; Vitis.
OX NCBI_TaxID=29760;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Lambrusco Foglia Frastagliata;
RX PubMed=8193299; DOI=10.1007/bf00029856;
RA Sparvoli F., Martin C., Scienza A., Gavazzi G., Tonelli C.;
RT "Cloning and molecular analysis of structural genes involved in flavonoid
RT and stilbene biosynthesis in grape (Vitis vinifera L.).";
RL Plant Mol. Biol. 24:743-755(1994).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) IN COMPLEX WITH NADP AND SUBSTRATE.
RA Petit P., Langlois D'Estaintot B., Granier T., Gallois B.;
RT "Binding of two substrate analogue molecules to dihydroflavonol-4-reductase
RT alters the functional geometry of the catalytic site.";
RL Submitted (OCT-2006) to the PDB data bank.
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 -!- INDUCTION: By light.
CC -!- SIMILARITY: Belongs to the NAD(P)-dependent epimerase/dehydratase
CC family. Dihydroflavonol-4-reductase subfamily. {ECO:0000305}.
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DR EMBL; X75964; CAA53578.1; -; mRNA.
DR PDB; 2IOD; X-ray; 2.06 A; A/B/C/D=1-337.
DR PDB; 2NNL; X-ray; 2.10 A; D/F=1-337.
DR PDB; 3BXX; X-ray; 2.90 A; A/B/C/D/E/F=1-337.
DR PDB; 3C1T; X-ray; 2.25 A; A/B/C/D=1-337.
DR PDBsum; 2IOD; -.
DR PDBsum; 2NNL; -.
DR PDBsum; 3BXX; -.
DR PDBsum; 3C1T; -.
DR AlphaFoldDB; P51110; -.
DR SMR; P51110; -.
DR STRING; 29760.VIT_18s0001g12800.t01; -.
DR PRIDE; P51110; -.
DR eggNOG; KOG1502; Eukaryota.
DR BRENDA; 1.1.1.219; 6671.
DR UniPathway; UPA00009; -.
DR EvolutionaryTrace; P51110; -.
DR ExpressionAtlas; P51110; 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 1: Evidence at protein level;
KW 3D-structure; Flavonoid biosynthesis; NADP; Oxidoreductase.
FT CHAIN 1..337
FT /note="Dihydroflavonol 4-reductase"
FT /id="PRO_0000215572"
FT ACT_SITE 167
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:Q12068"
FT BINDING 12..18
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|Ref.2, ECO:0007744|PDB:2NNL"
FT BINDING 37
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|Ref.2, ECO:0007744|PDB:2NNL"
FT BINDING 44
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|Ref.2, ECO:0007744|PDB:2NNL"
FT BINDING 64..65
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|Ref.2, ECO:0007744|PDB:2NNL"
FT BINDING 84..86
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|Ref.2, ECO:0007744|PDB:2NNL"
FT BINDING 128
FT /ligand="substrate"
FT /evidence="ECO:0000269|Ref.2, ECO:0007744|PDB:2NNL"
FT BINDING 133
FT /ligand="substrate"
FT /evidence="ECO:0000269|Ref.2, ECO:0007744|PDB:2NNL"
FT BINDING 163
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:A0A059TC02"
FT BINDING 163
FT /ligand="substrate"
FT /evidence="ECO:0000269|Ref.2, ECO:0007744|PDB:2NNL"
FT BINDING 167
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|Ref.2, ECO:0007744|PDB:2NNL"
FT BINDING 190..193
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|Ref.2, ECO:0007744|PDB:2NNL"
FT BINDING 204
FT /ligand="substrate"
FT /evidence="ECO:0000269|Ref.2, ECO:0007744|PDB:2NNL"
FT BINDING 205
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|Ref.2, ECO:0007744|PDB:2NNL"
FT BINDING 208
FT /ligand="substrate"
FT /evidence="ECO:0000269|Ref.2, ECO:0007744|PDB:2NNL"
FT BINDING 227
FT /ligand="substrate"
FT /evidence="ECO:0000269|Ref.2, ECO:0007744|PDB:2NNL"
FT STRAND 7..12
FT /evidence="ECO:0007829|PDB:2IOD"
FT HELIX 16..27
FT /evidence="ECO:0007829|PDB:2IOD"
FT STRAND 31..37
FT /evidence="ECO:0007829|PDB:2IOD"
FT HELIX 42..49
FT /evidence="ECO:0007829|PDB:2IOD"
FT HELIX 54..57
FT /evidence="ECO:0007829|PDB:2IOD"
FT STRAND 58..62
FT /evidence="ECO:0007829|PDB:2IOD"
FT TURN 68..71
FT /evidence="ECO:0007829|PDB:2IOD"
FT HELIX 72..75
FT /evidence="ECO:0007829|PDB:2IOD"
FT STRAND 79..83
FT /evidence="ECO:0007829|PDB:2IOD"
FT HELIX 95..98
FT /evidence="ECO:0007829|PDB:2IOD"
FT HELIX 100..116
FT /evidence="ECO:0007829|PDB:2IOD"
FT STRAND 121..126
FT /evidence="ECO:0007829|PDB:2IOD"
FT HELIX 129..131
FT /evidence="ECO:0007829|PDB:2IOD"
FT STRAND 135..137
FT /evidence="ECO:0007829|PDB:2IOD"
FT STRAND 140..142
FT /evidence="ECO:0007829|PDB:2IOD"
FT HELIX 150..156
FT /evidence="ECO:0007829|PDB:2IOD"
FT HELIX 161..180
FT /evidence="ECO:0007829|PDB:2IOD"
FT STRAND 185..190
FT /evidence="ECO:0007829|PDB:2IOD"
FT STRAND 192..195
FT /evidence="ECO:0007829|PDB:2IOD"
FT STRAND 198..201
FT /evidence="ECO:0007829|PDB:2NNL"
FT HELIX 204..209
FT /evidence="ECO:0007829|PDB:2IOD"
FT HELIX 211..214
FT /evidence="ECO:0007829|PDB:2IOD"
FT HELIX 217..219
FT /evidence="ECO:0007829|PDB:2IOD"
FT TURN 221..224
FT /evidence="ECO:0007829|PDB:2IOD"
FT STRAND 225..230
FT /evidence="ECO:0007829|PDB:2IOD"
FT HELIX 231..243
FT /evidence="ECO:0007829|PDB:2IOD"
FT STRAND 249..253
FT /evidence="ECO:0007829|PDB:2IOD"
FT STRAND 256..259
FT /evidence="ECO:0007829|PDB:2IOD"
FT HELIX 260..270
FT /evidence="ECO:0007829|PDB:2IOD"
FT HELIX 295..299
FT /evidence="ECO:0007829|PDB:2IOD"
FT HELIX 308..321
FT /evidence="ECO:0007829|PDB:2IOD"
SQ SEQUENCE 337 AA; 37757 MW; 73EDB67A03DF94E9 CRC64;
MGSQSETVCV TGASGFIGSW LVMRLLERRL TVRATVRDPT NVKKVKHLLD LPKAETHLTL
WKADLADEGS FDEAIKGCTG VFHVATPMDF ESKDPENEVI KPTIEGMLGI MKSCAAAKTV
RRLVFTSSAG TVNIQEHQLP VYDESCWSDM EFCRAKKMTA WMYFVSKTLA EQAAWKYAKE
NNIDFITIIP TLVVGPFIMS SMPPSLITAL SPITGNEAHY SIIRQGQFVH LDDLCNAHIY
LFENPKAEGR YICSSHDCII LDLAKMLREK YPEYNIPTEF KGVDENLKSV CFSSKKLTDL
GFEFKYSLED MFTGAVDTCR AKGLLRPSHE KPVDGKT
