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Protein

Dihydroflavonol-4-reductase

Gene

DFRA

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

Cis-3,4-leucopelargonidin + NADP+ = (+)-dihydrokaempferol + NADPH.

Pathwayi

GO - Molecular functioni

  1. coenzyme binding Source: InterPro
  2. dihydrokaempferol 4-reductase activity Source: TAIR

GO - Biological processi

  1. anthocyanin-containing compound biosynthetic process Source: TAIR
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Flavonoid biosynthesis

Keywords - Ligandi

NADP

Enzyme and pathway databases

BRENDAi1.1.1.219. 399.
UniPathwayiUPA00009.

Names & Taxonomyi

Protein namesi
Recommended name:
Dihydroflavonol-4-reductase (EC:1.1.1.219)
Short name:
DFR
Alternative name(s):
Dihydrokaempferol 4-reductase
Protein TRANSPARENT TESTA 3
Gene namesi
Name:DFRA
Synonyms:DFR, TT3
Ordered Locus Names:At5g42800
ORF Names:MJB21.18
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548 Componenti: Chromosome 5

Organism-specific databases

TAIRiAT5G42800.

Subcellular locationi

GO - Cellular componenti

  1. extrinsic component of endoplasmic reticulum membrane Source: TAIR
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 382382Dihydroflavonol-4-reductasePRO_0000215563Add
BLAST

Proteomic databases

PaxDbiP51102.
PRIDEiP51102.

Expressioni

Gene expression databases

GenevestigatoriP51102.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
CHSP131144EBI-1546795,EBI-1546775

Protein-protein interaction databases

IntActiP51102. 4 interactions.
MINTiMINT-8184604.

Structurei

3D structure databases

ProteinModelPortaliP51102.
SMRiP51102. Positions 6-328.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0451.
InParanoidiP51102.
KOiK13082.
OMAiCEAHIFL.
PhylomeDBiP51102.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR001509. Epimerase_deHydtase_N.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamiPF01370. Epimerase. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P51102-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVSQKETVCV TGASGFIGSW LVMRLLERGY FVRATVRDPG NLKKVQHLLD
60 70 80 90 100
LPNAKTLLTL WKADLSEEGS YDDAINGCDG VFHVATPMDF ESKDPENEVI
110 120 130 140 150
KPTVNGMLGI MKACVKAKTV RRFVFTSSAG TVNVEEHQKN VYDENDWSDL
160 170 180 190 200
EFIMSKKMTG WMYFVSKTLA EKAAWDFAEE KGLDFISIIP TLVVGPFITT
210 220 230 240 250
SMPPSLITAL SPITRNEAHY SIIRQGQYVH LDDLCNAHIF LYEQAAAKGR
260 270 280 290 300
YICSSHDATI LTISKFLRPK YPEYNVPSTF EGVDENLKSI EFSSKKLTDM
310 320 330 340 350
GFNFKYSLEE MFIESIETCR QKGFLPVSLS YQSISEIKTK NENIDVKTGD
360 370 380
GLTDGMKPCN KTETGITGER TDAPMLAQQM CA
Length:382
Mass (Da):42,775
Last modified:July 11, 2002 - v2
Checksum:i51F81F96512ECC3F
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti57 – 571L → Q in AAA32783 (PubMed:1354004).Curated
Sequence conflicti57 – 571L → Q in BAA85261 (Ref. 2) Curated
Sequence conflicti168 – 1681T → S in AAA32783 (PubMed:1354004).Curated
Sequence conflicti168 – 1681T → S in BAA85261 (Ref. 2) Curated
Sequence conflicti299 – 2991D → E in AAA32783 (PubMed:1354004).Curated
Sequence conflicti299 – 2991D → E in BAA85261 (Ref. 2) Curated
Sequence conflicti338 – 3381K → KVP in AAA32783 (PubMed:1354004).Curated
Sequence conflicti338 – 3381K → KVP in BAA85261 (Ref. 2) Curated
Sequence conflicti343 – 3431N → I in AAA32783 (PubMed:1354004).Curated
Sequence conflicti343 – 3431N → I in BAA85261 (Ref. 2) Curated
Sequence conflicti345 – 3451D → E in AAA32783 (PubMed:1354004).Curated
Sequence conflicti345 – 3451D → E in BAA85261 (Ref. 2) Curated
Sequence conflicti366 – 3661I → V in AAA32783 (PubMed:1354004).Curated
Sequence conflicti366 – 3661I → V in BAA85261 (Ref. 2) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M86359 Genomic DNA. Translation: AAA32783.1.
AB033294 Genomic DNA. Translation: BAA85261.1.
AJ251982 Genomic DNA. Translation: CAC10525.1.
AB007647 Genomic DNA. Translation: BAB10636.1.
CP002688 Genomic DNA. Translation: AED94866.1.
PIRiJQ1688.
RefSeqiNP_199094.1. NM_123645.3.
UniGeneiAt.23537.
At.74948.

Genome annotation databases

EnsemblPlantsiAT5G42800.1; AT5G42800.1; AT5G42800.
GeneIDi834291.
KEGGiath:AT5G42800.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M86359 Genomic DNA. Translation: AAA32783.1.
AB033294 Genomic DNA. Translation: BAA85261.1.
AJ251982 Genomic DNA. Translation: CAC10525.1.
AB007647 Genomic DNA. Translation: BAB10636.1.
CP002688 Genomic DNA. Translation: AED94866.1.
PIRiJQ1688.
RefSeqiNP_199094.1. NM_123645.3.
UniGeneiAt.23537.
At.74948.

3D structure databases

ProteinModelPortaliP51102.
SMRiP51102. Positions 6-328.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP51102. 4 interactions.
MINTiMINT-8184604.

Proteomic databases

PaxDbiP51102.
PRIDEiP51102.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT5G42800.1; AT5G42800.1; AT5G42800.
GeneIDi834291.
KEGGiath:AT5G42800.

Organism-specific databases

TAIRiAT5G42800.

Phylogenomic databases

eggNOGiCOG0451.
InParanoidiP51102.
KOiK13082.
OMAiCEAHIFL.
PhylomeDBiP51102.

Enzyme and pathway databases

UniPathwayiUPA00009.
BRENDAi1.1.1.219. 399.

Miscellaneous databases

PROiP51102.

Gene expression databases

GenevestigatoriP51102.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR001509. Epimerase_deHydtase_N.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamiPF01370. Epimerase. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Effects of ionizing radiation on a plant genome: analysis of two Arabidopsis transparent testa mutations."
    Shirley B.W., Hanley S., Goodman H.M.
    Plant Cell 4:333-347(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: cv. Columbia and cv. Landsberg erecta.
  2. "Structure of dihydroflavonol 4-reductase (DFR) gene and its flanking sequences from Arabidopsis thaliana ecotype Landsberg erecta."
    Ichikawa H., Okano E., Shirley B.W.
    Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: cv. Landsberg erecta.
  3. "Physiological and molecular characterization of transparent testa mutants of Arabidopsis impaired in phenylpropanoid pathway."
    Bharti A.K., Khurana J.P.
    Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: cv. Est.
  4. "Structural analysis of Arabidopsis thaliana chromosome 5. III. Sequence features of the regions of 1,191,918 bp covered by seventeen physically assigned P1 clones."
    Nakamura Y., Sato S., Kaneko T., Kotani H., Asamizu E., Miyajima N., Tabata S.
    DNA Res. 4:401-414(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  5. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  6. "The flavonoid biosynthetic pathway in Arabidopsis: Structural and genetic diversity."
    Saito K., Yonekura-Sakakibara K., Nakabayashi R., Higashi Y., Yamazaki M., Tohge T., Fernie A.R.
    Plant Physiol. Biochem. 0:0-0(2013)
    Cited for: REVIEW, NOMENCLATURE.

Entry informationi

Entry nameiDFRA_ARATH
AccessioniPrimary (citable) accession number: P51102
Secondary accession number(s): Q9FEB1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: July 11, 2002
Last modified: April 29, 2015
This is version 109 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.