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Q9XES5

- DFRA_MALDO

UniProt

Q9XES5 - DFRA_MALDO

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Protein

Bifunctional dihydroflavonol 4-reductase/flavanone 4-reductase

Gene

DFR

Organism
Malus domestica (Apple) (Pyrus malus)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli

Functioni

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 activityi

(2S)-flavan-4-ol + NADP+ = (2S)-flavanone + NADPH.
Cis-3,4-leucopelargonidin + NADP+ = (+)-dihydrokaempferol + NADPH.

Kineticsi

  1. KM=3.9 µM for eriodictyol1 Publication
  2. KM=34.0 µM for dihydrokaempferol1 Publication
  3. KM=26.0 µM for dihydroquercetin1 Publication

Vmax=4.6 nmol/sec/g enzyme toward eriodictyol1 Publication

Vmax=186.0 nmol/sec/g enzyme toward dihydrokaempferol1 Publication

Vmax=91.0 nmol/sec/g enzyme toward dihydroquercetin1 Publication

pH dependencei

Optimum pH is 5.75 with dihydroquercetin as substrate.1 Publication

GO - Molecular functioni

  1. coenzyme binding Source: InterPro
  2. dihydrokaempferol 4-reductase activity Source: UniProtKB-EC
  3. flavanone 4-reductase activity Source: UniProtKB-EC

GO - Biological processi

  1. flavonoid biosynthetic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Flavonoid biosynthesis

Keywords - Ligandi

NADP

Enzyme and pathway databases

BRENDAi1.1.1.234. 3165.

Names & Taxonomyi

Protein namesi
Recommended name:
Bifunctional dihydroflavonol 4-reductase/flavanone 4-reductase
Alternative name(s):
Dihydroflavonol 4-reductase (EC:1.1.1.219)
Short name:
DFR
Dihydrokaempferol 4-reductase
Flavanone 4-reductase (EC:1.1.1.234)
Short name:
FNR
Gene namesi
Name:DFR
OrganismiMalus domestica (Apple) (Pyrus malus)
Taxonomic identifieri3750 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsRosalesRosaceaeMaloideaeMaleaeMalus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 348348Bifunctional dihydroflavonol 4-reductase/flavanone 4-reductasePRO_0000367056Add
BLAST

Expressioni

Developmental stagei

Expressed during fruit ripening.1 Publication

Structurei

3D structure databases

ProteinModelPortaliQ9XES5.
SMRiQ9XES5. Positions 5-326.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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.

Q9XES5-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MGSESESVCV TGASGFIGSW LVMRLLEHGY TVRATVRDPT NQKKVKHLLD
60 70 80 90 100
LPKAETHLTL WKADLADEGS FDEAIQGCSG VFHVATPMDF ESKDPENEVI
110 120 130 140 150
KPTINGLLDI LKACQKAKTV RKLVFTSSAG TVNVEEHQKP VYDESNWSDV
160 170 180 190 200
EFCRSVKMTG WMYFVSKTLA EQAAWKYAKE NNIDFITIIP TLVIGPFLMP
210 220 230 240 250
SMPPSLITGL SPILRNESHY GIIKQGQYVH LDDLCLSHIY LYEHPKAEGR
260 270 280 290 300
YICSSHDATI HELVKMLREK YPEYNIPTKF KGIDDNLEPV HFSSKKLREI
310 320 330 340
GFEFKYSLED MFVGAVDACR AKGLIPIPIP AEKTEAAEES NLVDVKVG
Length:348
Mass (Da):39,030
Last modified:November 1, 1999 - v1
Checksum:i02056428FB2F9372
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti347 – 3471V → A in strain: cv. M9.

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF117268 mRNA. Translation: AAD26204.1.
AY227729 mRNA. Translation: AAO39817.1.
AY227728 mRNA. Translation: AAO39816.1.
AB074488 mRNA. Translation: BAB92999.1.
RefSeqiNP_001280868.1. NM_001293939.1.
UniGeneiMdo.2977.

Genome annotation databases

GeneIDi103450464.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF117268 mRNA. Translation: AAD26204.1 .
AY227729 mRNA. Translation: AAO39817.1 .
AY227728 mRNA. Translation: AAO39816.1 .
AB074488 mRNA. Translation: BAB92999.1 .
RefSeqi NP_001280868.1. NM_001293939.1.
UniGenei Mdo.2977.

3D structure databases

ProteinModelPortali Q9XES5.
SMRi Q9XES5. Positions 5-326.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 103450464.

Enzyme and pathway databases

BRENDAi 1.1.1.234. 3165.

Family and domain databases

Gene3Di 3.40.50.720. 1 hit.
InterProi IPR001509. Epimerase_deHydtase_N.
IPR016040. NAD(P)-bd_dom.
[Graphical view ]
Pfami PF01370. Epimerase. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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.

Entry informationi

Entry nameiDFRA_MALDO
AccessioniPrimary (citable) accession number: Q9XES5
Secondary accession number(s): Q84KP1, Q8L5N3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: November 1, 1999
Last modified: October 29, 2014
This is version 53 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3