DFRA_MALDO
ID DFRA_MALDO Reviewed; 348 AA.
AC Q9XES5; Q84KP1; Q8L5N3;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=Bifunctional dihydroflavonol 4-reductase/flavanone 4-reductase;
DE AltName: Full=Dihydroflavonol 4-reductase;
DE Short=DFR;
DE EC=1.1.1.219 {ECO:0000269|PubMed:12667486};
DE AltName: Full=Dihydrokaempferol 4-reductase;
DE AltName: Full=Flavanone 4-reductase;
DE Short=FNR;
DE EC=1.1.1.234 {ECO:0000269|PubMed:12667486};
GN Name=DFR;
OS Malus domestica (Apple) (Pyrus malus).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Rosales; Rosaceae; Amygdaloideae; Maleae; Malus.
OX NCBI_TaxID=3750;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Fuji; TISSUE=Peelings;
RA Lee J.-R., Hong S.-T., Yoo Y.G., Kim S.-R.;
RT "Molecular cloning and expression of anthocyanin biosynthesis genes from
RT 'Fuji apple'.";
RL Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=cv. M9, and cv. Weirouge;
RX PubMed=12667486; DOI=10.1016/s0003-9861(03)00013-4;
RA Fischer T.C., Halbwirth H., Meisel B., Stich K., Forkmann G.;
RT "Molecular cloning, substrate specificity of the functionally expressed
RT dihydroflavonol 4-reductases from Malus domestica and Pyrus communis
RT cultivars and the consequences for flavonoid metabolism.";
RL Arch. Biochem. Biophys. 412:223-230(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 4-317, AND DEVELOPMENTAL STAGE.
RC STRAIN=cv. Jonathan; TISSUE=Peelings;
RA Honda C., Kotoda N., Wada M., Kondo S., Kobayashi S., Soejima J., Zhang Z.,
RA Tsuda T., Moriguchi T.;
RT "Anthocyanin biosynthetic genes are coordinately expressed during red
RT coloration in apple skin.";
RL Plant Physiol. Biochem. 40:955-962(2002).
CC -!- FUNCTION: Bifunctional enzyme involved in flavonoid metabolism. May use
CC dihydroquercetin, dihydrokaempferol, eriodictyol, garbanzol (5-
CC deoxydihydrokaempferol), dihydrofisetin (5-deoxydihydroquercetin),
CC naringenin to a low extent (10%), but not 5-deoxynaringenin or butin
CC (5-deoxyeriodictyol) as substrate. {ECO:0000269|PubMed:12667486}.
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:0000269|PubMed:12667486};
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:0000269|PubMed:12667486};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=3.9 uM for eriodictyol {ECO:0000269|PubMed:12667486};
CC KM=34.0 uM for dihydrokaempferol {ECO:0000269|PubMed:12667486};
CC KM=26.0 uM for dihydroquercetin {ECO:0000269|PubMed:12667486};
CC Vmax=4.6 nmol/sec/g enzyme toward eriodictyol
CC {ECO:0000269|PubMed:12667486};
CC Vmax=186.0 nmol/sec/g enzyme toward dihydrokaempferol
CC {ECO:0000269|PubMed:12667486};
CC Vmax=91.0 nmol/sec/g enzyme toward dihydroquercetin
CC {ECO:0000269|PubMed:12667486};
CC pH dependence:
CC Optimum pH is 5.75 with dihydroquercetin as substrate.
CC {ECO:0000269|PubMed:12667486};
CC -!- DEVELOPMENTAL STAGE: Expressed during fruit ripening.
CC {ECO:0000269|Ref.3}.
CC -!- SIMILARITY: Belongs to the NAD(P)-dependent epimerase/dehydratase
CC family. Dihydroflavonol-4-reductase subfamily. {ECO:0000305}.
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DR EMBL; AF117268; AAD26204.1; -; mRNA.
DR EMBL; AY227729; AAO39817.1; -; mRNA.
DR EMBL; AY227728; AAO39816.1; -; mRNA.
DR EMBL; AB074488; BAB92999.1; -; mRNA.
DR RefSeq; NP_001280868.1; NM_001293939.1.
DR AlphaFoldDB; Q9XES5; -.
DR SMR; Q9XES5; -.
DR STRING; 3750.XP_008388041.1; -.
DR EnsemblPlants; mRNA:MD15G0020300; mRNA:MD15G0020300; MD15G0020300.
DR GeneID; 103450464; -.
DR Gramene; mRNA:MD15G0020300; mRNA:MD15G0020300; MD15G0020300.
DR KEGG; mdm:103450464; -.
DR OrthoDB; 992332at2759; -.
DR BRENDA; 1.1.1.234; 3164.
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:0009813; P:flavonoid biosynthetic process; IEA:UniProtKB-KW.
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 Flavonoid biosynthesis; NADP; Oxidoreductase.
FT CHAIN 1..348
FT /note="Bifunctional dihydroflavonol 4-reductase/flavanone
FT 4-reductase"
FT /id="PRO_0000367056"
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"
FT VARIANT 347
FT /note="V -> A (in strain: cv. M9)"
SQ SEQUENCE 348 AA; 39030 MW; 02056428FB2F9372 CRC64;
MGSESESVCV TGASGFIGSW LVMRLLEHGY TVRATVRDPT NQKKVKHLLD LPKAETHLTL
WKADLADEGS FDEAIQGCSG VFHVATPMDF ESKDPENEVI KPTINGLLDI LKACQKAKTV
RKLVFTSSAG TVNVEEHQKP VYDESNWSDV EFCRSVKMTG WMYFVSKTLA EQAAWKYAKE
NNIDFITIIP TLVIGPFLMP SMPPSLITGL SPILRNESHY GIIKQGQYVH LDDLCLSHIY
LYEHPKAEGR YICSSHDATI HELVKMLREK YPEYNIPTKF KGIDDNLEPV HFSSKKLREI
GFEFKYSLED MFVGAVDACR AKGLIPIPIP AEKTEAAEES NLVDVKVG
