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Protein

Dihydroflavonol-4-reductase

Gene
N/A
Organism
Solanum lycopersicum (Tomato) (Lycopersicon esculentum)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at transcript leveli

Functioni

Catalytic activityi

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

Pathway:ianthocyanin biosynthesis

This protein is involved in the pathway anthocyanin biosynthesis, which is part of Pigment biosynthesis.
View all proteins of this organism that are known to be involved in the pathway anthocyanin biosynthesis and in Pigment biosynthesis.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Flavonoid biosynthesis

Keywords - Ligandi

NADP

Enzyme and pathway databases

BRENDAi1.1.1.219. 3101.
UniPathwayiUPA00009.

Names & Taxonomyi

Protein namesi
Recommended name:
Dihydroflavonol-4-reductase (EC:1.1.1.219)
Short name:
DFR
Alternative name(s):
Dihydrokaempferol 4-reductase
OrganismiSolanum lycopersicum (Tomato) (Lycopersicon esculentum)
Taxonomic identifieri4081 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeasteridslamiidsSolanalesSolanaceaeSolanoideaeSolaneaeSolanumLycopersicon
ProteomesiUP000004994 Componenti: Unplaced

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 379379Dihydroflavonol-4-reductasePRO_0000215568Add
BLAST

Expressioni

Tissue specificityi

Expressed in both leaf and hypocotyl tissues.

Interactioni

Protein-protein interaction databases

STRINGi4081.Solyc02g085020.2.1.

Structurei

3D structure databases

ProteinModelPortaliP51107.
SMRiP51107. Positions 19-337.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

KOiK13082.

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.

P51107-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASEAHAVVD AHSPPKTTTV WVTGGAGFIG SWLVMRLLER GYNVHATVRD
60 70 80 90 100
PENQKKVKHL LELPKADTNL TLWKADLAVE GSFDEAIQGC QGVFHVATPM
110 120 130 140 150
DFESKDPENE VIKPTVRGML SIIESCAKAN TVKRLVFTSS AGTLDVQEDQ
160 170 180 190 200
KLFYDETSWS DLDFIYAKKM TGWMYFVSKI LAEKAAMEEA RKNNIDFISI
210 220 230 240 250
IPPLVVGPFI TSTFPPSLIT ALSLITAHYG IIKQGQYVHL DDLCEAHIFL
260 270 280 290 300
YEHPKAEGRF ICSSHHAIIY DVAKMVRQKW PEYYVPTEFK GIDKDLALVS
310 320 330 340 350
FSSKKLMDIK FQFKHTLEDM YKGAIETCRQ KQLLPFSTRS TADNGKDKEA
360 370
IPISTENYSS GKENAPVANC TGKFTNGEI
Length:379
Mass (Da):42,429
Last modified:October 1, 1996 - v1
Checksum:i8B23708B01E4A989
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z18277 mRNA. Translation: CAA79154.1.
PIRiS38474.
RefSeqiNP_001234408.1. NM_001247479.1.
UniGeneiLes.3659.

Genome annotation databases

GeneIDi544150.
KEGGisly:544150.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z18277 mRNA. Translation: CAA79154.1.
PIRiS38474.
RefSeqiNP_001234408.1. NM_001247479.1.
UniGeneiLes.3659.

3D structure databases

ProteinModelPortaliP51107.
SMRiP51107. Positions 19-337.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi4081.Solyc02g085020.2.1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi544150.
KEGGisly:544150.

Phylogenomic databases

KOiK13082.

Enzyme and pathway databases

UniPathwayiUPA00009.
BRENDAi1.1.1.219. 3101.

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

  1. "Characterization of the gene encoding dihydroflavonol 4-reductase in tomato."
    Bongue-Bartelsman M., O'Neill S.D., Tong Y., Yoder J.I.
    Gene 138:153-157(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Hypocotyl.

Entry informationi

Entry nameiDFRA_SOLLC
AccessioniPrimary (citable) accession number: P51107
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: June 24, 2015
This is version 69 of the entry and version 1 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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. 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.