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Q84KP0 (DFRA_PYRCO) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 40. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Bifunctional dihydroflavonol 4-reductase/flavanone 4-reductase
Alternative name(s):
Dihydroflavonol 4-reductase
Short name=DFR
EC=1.1.1.219
Flavanone 4-reductase
Short name=FNR
EC=1.1.1.234
Gene names
Name:DFR
OrganismPyrus communis (Pear) (Pyrus domestica)
Taxonomic identifier23211 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsRosalesRosaceaeMaloideaeMaleaePyrus

Protein attributes

Sequence length347 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Bifunctional enzyme involved in the flavonoid metabolism. May use dihydroquercetin, eriodictyol, garbanzol (5-deoxydihydrokaempferol), dihydrofisetin (5-deoxydihydroquercetin), dihydrokaempferol to a low extent (5%), but not naringenin, 5-deoxynaringenin or butin (5-deoxyeriodictyol) as substrate.

Catalytic activity

(2S)-flavan-4-ol + NADP+ = (2S)-flavanone + NADPH.

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

Sequence similarities

Belongs to the NAD(P)-dependent epimerase/dehydratase family. Dihydroflavonol-4-reductase subfamily.

Biophysicochemical properties

Kinetic parameters:

KM=3.8 µM for eriodictyol Ref.1

KM=3.0 µM for dihydroquercetin

Vmax=1.6 nmol/sec/g enzyme toward eriodictyol

Vmax=4.7 nmol/sec/g enzyme toward dihydroquercetin

pH dependence:

Optimum pH is 5.75 with dihydroquercetin as substrate.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 347347Bifunctional dihydroflavonol 4-reductase/flavanone 4-reductase
PRO_0000367057

Natural variations

Natural variant931R → K in strain: cv. Conference and cv. Pyrodwarf.
Natural variant3471S → G in strain: cv. Conference and cv. Pyrodwarf.

Sequences

Sequence LengthMass (Da)Tools
Q84KP0 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: 048D1FE898418E9E

FASTA34738,934
        10         20         30         40         50         60 
MGSESESVCV TGASGFIGSW LVMRLLEHGY TVRATVRDPT NQKKVKHLLD LPKAETHLTL 

        70         80         90        100        110        120 
WKADLADEGS FDEAIQGCSG VFHVATPMDF ESRDPENEVI KPTINGLLDI LKACQKAKTV 

       130        140        150        160        170        180 
RKLVFTSSAG TVNVEEHQKP VYDESNWSDV EFCRSVKMTG WMYFVSKTLA EQAAWKYAKE 

       190        200        210        220        230        240 
NNIDFITIIP TLVIGPFLMP SMPPSLITGL SPILRNESHY GIIKQGQYVH LDDLCLSHIY 

       250        260        270        280        290        300 
LYKHPKAEGR YICSSHDATI HELVKMLREK YPEYNIPTKF KGIDDNLEPV HFSSKKLREI 

       310        320        330        340 
GFEFKYSLED MFVGAVDACR AKGLIPIPAE KTEAAEESNL VDVKVGS 

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References

[1]"Molecular cloning, substrate specificity of the functionally expressed dihydroflavonol 4-reductases from Malus domestica and Pyrus communis cultivars and the consequences for flavonoid metabolism."
Fischer T.C., Halbwirth H., Meisel B., Stich K., Forkmann G.
Arch. Biochem. Biophys. 412:223-230(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], BIOPHYSICOCHEMICAL PROPERTIES.
Strain: cv. Abbe Fetel, cv. Conference and cv. Pyrodwarf.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY227730 mRNA. Translation: AAO39818.1.
AY227731 mRNA. Translation: AAO39819.1.
AY227732 mRNA. Translation: AAO39820.1.

3D structure databases

ProteinModelPortalQ84KP0.
SMRQ84KP0. Positions 5-326.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D3.40.50.720. 1 hit.
InterProIPR001509. Epimerase_deHydtase.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamPF01370. Epimerase. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameDFRA_PYRCO
AccessionPrimary (citable) accession number: Q84KP0
Secondary accession number(s): Q84K59
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: June 1, 2003
Last modified: February 19, 2014
This is version 40 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families