Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q9XES5 (DFRA_MALDO) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 51. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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
Dihydrokaempferol 4-reductase
Flavanone 4-reductase
Short name=FNR
EC=1.1.1.234
Gene names
Name:DFR
OrganismMalus domestica (Apple) (Pyrus malus)
Taxonomic identifier3750 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsRosalesRosaceaeMaloideaeMaleaeMalus

Protein attributes

Sequence length348 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Bifunctional enzyme involved in the flavonoid metabolism. May use dihydroquercetin, dihydrokaempferol, eriodictyol, garbanzol (5-deoxydihydrokaempferol), dihydrofisetin (5-deoxydihydroquercetin), naringenin to a low extent (10%), but not 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.

Developmental stage

Expressed during fruit ripening. Ref.3

Sequence similarities

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

Biophysicochemical properties

Kinetic parameters:

KM=3.9 µM for eriodictyol Ref.2

KM=34.0 µM for dihydrokaempferol

KM=26.0 µM for dihydroquercetin

Vmax=4.6 nmol/sec/g enzyme toward eriodictyol

Vmax=186.0 nmol/sec/g enzyme toward dihydrokaempferol

Vmax=91.0 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 – 348348Bifunctional dihydroflavonol 4-reductase/flavanone 4-reductase
PRO_0000367056

Natural variations

Natural variant3471V → A in strain: cv. M9.

Sequences

Sequence LengthMass (Da)Tools
Q9XES5 [UniParc].

Last modified November 1, 1999. Version 1.
Checksum: 02056428FB2F9372

FASTA34839,030
        10         20         30         40         50         60 
MGSESESVCV TGASGFIGSW LVMRLLEHGY TVRATVRDPT NQKKVKHLLD LPKAETHLTL 

        70         80         90        100        110        120 
WKADLADEGS FDEAIQGCSG VFHVATPMDF ESKDPENEVI 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 
LYEHPKAEGR YICSSHDATI HELVKMLREK YPEYNIPTKF KGIDDNLEPV HFSSKKLREI 

       310        320        330        340 
GFEFKYSLED MFVGAVDACR AKGLIPIPIP AEKTEAAEES NLVDVKVG 

« Hide

References

[1]"Molecular cloning and expression of anthocyanin biosynthesis genes from 'Fuji apple'."
Lee J.-R., Hong S.-T., Yoo Y.G., Kim S.-R.
Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: cv. Fuji.
Tissue: Peelings.
[2]"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. M9 and cv. Weirouge.
[3]"Anthocyanin biosynthetic genes are coordinately expressed during red coloration in apple skin."
Honda C., Kotoda N., Wada M., Kondo S., Kobayashi S., Soejima J., Zhang Z., Tsuda T., Moriguchi T.
Plant Physiol. Biochem. 40:955-962(2002)
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 4-317, DEVELOPMENTAL STAGE.
Strain: cv. Jonathan.
Tissue: Peelings.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF117268 mRNA. Translation: AAD26204.1.
AY227729 mRNA. Translation: AAO39817.1.
AY227728 mRNA. Translation: AAO39816.1.
AB074488 mRNA. Translation: BAB92999.1.

3D structure databases

ProteinModelPortalQ9XES5.
SMRQ9XES5. Positions 5-326.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

BRENDA1.1.1.234. 3165.

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_MALDO
AccessionPrimary (citable) accession number: Q9XES5
Secondary accession number(s): Q84KP1, Q8L5N3
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: November 1, 1999
Last modified: February 19, 2014
This is version 51 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