DFRA_ARATH
ID DFRA_ARATH Reviewed; 382 AA.
AC P51102; Q9FEB1;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2002, sequence version 2.
DT 03-AUG-2022, entry version 147.
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};
DE AltName: Full=Protein TRANSPARENT TESTA 3;
GN Name=DFRA; Synonyms=DFR, TT3; OrderedLocusNames=At5g42800;
GN ORFNames=MJB21.18;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Columbia, and cv. Landsberg erecta;
RX PubMed=1354004; DOI=10.2307/3869544;
RA Shirley B.W., Hanley S., Goodman H.M.;
RT "Effects of ionizing radiation on a plant genome: analysis of two
RT Arabidopsis transparent testa mutations.";
RL Plant Cell 4:333-347(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Landsberg erecta;
RA Ichikawa H., Okano E., Shirley B.W.;
RT "Structure of dihydroflavonol 4-reductase (DFR) gene and its flanking
RT sequences from Arabidopsis thaliana ecotype Landsberg erecta.";
RL Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Est;
RA Bharti A.K., Khurana J.P.;
RT "Physiological and molecular characterization of transparent testa mutants
RT of Arabidopsis impaired in phenylpropanoid pathway.";
RL Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9501997; DOI=10.1093/dnares/4.6.401;
RA Nakamura Y., Sato S., Kaneko T., Kotani H., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. III. Sequence
RT features of the regions of 1,191,918 bp covered by seventeen physically
RT assigned P1 clones.";
RL DNA Res. 4:401-414(1997).
RN [5]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [6]
RP REVIEW, AND NOMENCLATURE.
RX PubMed=23473981; DOI=10.1016/j.plaphy.2013.02.001;
RA Saito K., Yonekura-Sakakibara K., Nakabayashi R., Higashi Y., Yamazaki M.,
RA Tohge T., Fernie A.R.;
RT "The flavonoid biosynthetic pathway in Arabidopsis: Structural and genetic
RT diversity.";
RL Plant Physiol. Biochem. 72:21-34(2013).
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 -!- INTERACTION:
CC P51102; P13114: CHS; NbExp=4; IntAct=EBI-1546795, EBI-1546775;
CC -!- SIMILARITY: Belongs to the NAD(P)-dependent epimerase/dehydratase
CC family. Dihydroflavonol-4-reductase subfamily. {ECO:0000305}.
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DR EMBL; M86359; AAA32783.1; -; Genomic_DNA.
DR EMBL; AB033294; BAA85261.1; -; Genomic_DNA.
DR EMBL; AJ251982; CAC10525.1; -; Genomic_DNA.
DR EMBL; AB007647; BAB10636.1; -; Genomic_DNA.
DR EMBL; CP002688; AED94866.1; -; Genomic_DNA.
DR PIR; JQ1688; JQ1688.
DR RefSeq; NP_199094.1; NM_123645.4.
DR AlphaFoldDB; P51102; -.
DR SMR; P51102; -.
DR BioGRID; 19541; 5.
DR IntAct; P51102; 4.
DR MINT; P51102; -.
DR STRING; 3702.AT5G42800.1; -.
DR PaxDb; P51102; -.
DR PRIDE; P51102; -.
DR ProteomicsDB; 224580; -.
DR EnsemblPlants; AT5G42800.1; AT5G42800.1; AT5G42800.
DR GeneID; 834291; -.
DR Gramene; AT5G42800.1; AT5G42800.1; AT5G42800.
DR KEGG; ath:AT5G42800; -.
DR Araport; AT5G42800; -.
DR TAIR; locus:2165427; AT5G42800.
DR eggNOG; KOG1502; Eukaryota.
DR HOGENOM; CLU_007383_9_0_1; -.
DR InParanoid; P51102; -.
DR OMA; KERLTLW; -.
DR OrthoDB; 992332at2759; -.
DR PhylomeDB; P51102; -.
DR BRENDA; 1.1.1.219; 399.
DR UniPathway; UPA00009; -.
DR PRO; PR:P51102; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; P51102; baseline and differential.
DR Genevisible; P51102; AT.
DR GO; GO:0042406; C:extrinsic component of endoplasmic reticulum membrane; TAS:TAIR.
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 1: Evidence at protein level;
KW Flavonoid biosynthesis; NADP; Oxidoreductase; Reference proteome.
FT CHAIN 1..382
FT /note="Dihydroflavonol 4-reductase"
FT /id="PRO_0000215563"
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 CONFLICT 57
FT /note="L -> Q (in Ref. 1; AAA32783 and 2; BAA85261)"
FT /evidence="ECO:0000305"
FT CONFLICT 168
FT /note="T -> S (in Ref. 1; AAA32783 and 2; BAA85261)"
FT /evidence="ECO:0000305"
FT CONFLICT 299
FT /note="D -> E (in Ref. 1; AAA32783 and 2; BAA85261)"
FT /evidence="ECO:0000305"
FT CONFLICT 338
FT /note="K -> KVP (in Ref. 1; AAA32783 and 2; BAA85261)"
FT /evidence="ECO:0000305"
FT CONFLICT 343
FT /note="N -> I (in Ref. 1; AAA32783 and 2; BAA85261)"
FT /evidence="ECO:0000305"
FT CONFLICT 345
FT /note="D -> E (in Ref. 1; AAA32783 and 2; BAA85261)"
FT /evidence="ECO:0000305"
FT CONFLICT 366
FT /note="I -> V (in Ref. 1; AAA32783 and 2; BAA85261)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 382 AA; 42775 MW; 51F81F96512ECC3F CRC64;
MVSQKETVCV TGASGFIGSW LVMRLLERGY FVRATVRDPG NLKKVQHLLD LPNAKTLLTL
WKADLSEEGS YDDAINGCDG VFHVATPMDF ESKDPENEVI KPTVNGMLGI MKACVKAKTV
RRFVFTSSAG TVNVEEHQKN VYDENDWSDL EFIMSKKMTG WMYFVSKTLA EKAAWDFAEE
KGLDFISIIP TLVVGPFITT SMPPSLITAL SPITRNEAHY SIIRQGQYVH LDDLCNAHIF
LYEQAAAKGR YICSSHDATI LTISKFLRPK YPEYNVPSTF EGVDENLKSI EFSSKKLTDM
GFNFKYSLEE MFIESIETCR QKGFLPVSLS YQSISEIKTK NENIDVKTGD GLTDGMKPCN
KTETGITGER TDAPMLAQQM CA
