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 24-JAN-2024, entry version 154. 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=10.1105/tpc.4.3.333; 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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.P51102; -. DR iPTMnet; P51102; -. DR PaxDb; 3702-AT5G42800-1; -. 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; AT5G42800; DFR. DR eggNOG; KOG1502; Eukaryota. DR HOGENOM; CLU_007383_9_0_1; -. DR InParanoid; P51102; -. DR OMA; KERLTLW; -. DR OrthoDB; 1694166at2759; -. 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 GO; GO:0042406; C:extrinsic component of endoplasmic reticulum membrane; TAS:TAIR. DR GO; GO:0045552; F:dihydrokaempferol 4-reductase activity; TAS:TAIR. DR GO; GO:0047890; F:flavanone 4-reductase activity; IEA:UniProtKB-EC. DR GO; GO:0009718; P:anthocyanin-containing compound biosynthetic process; TAS:TAIR. DR CDD; cd08958; FR_SDR_e; 1. DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1. DR InterPro; IPR001509; Epimerase_deHydtase. DR InterPro; IPR036291; NAD(P)-bd_dom_sf. DR PANTHER; PTHR10366:SF613; DIHYDROFLAVONOL 4-REDUCTASE; 1. DR PANTHER; PTHR10366; NAD DEPENDENT EPIMERASE/DEHYDRATASE; 1. DR Pfam; PF01370; Epimerase; 1. DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1. DR Genevisible; P51102; AT. 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 //