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Protein

Isoflavone reductase

Gene

IFR

Organism
Medicago sativa (Alfalfa)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Reduces achiral isoflavones to chiral isoflavanones during the biosynthesis of chiral pterocarpan phytoalexins. The reduction product is a third isomer, which represents the penultimate intermediate in the synthesis of the phytoalexin (-)-medicarpin, the major phytoalexin in Alfalfa.

Catalytic activityi

Vestitone + NADP+ = 2'-hydroxyformononetin + NADPH.

Pathwayi: pterocarpan phytoalexin biosynthesis

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

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi6 – 3732NADPSequence analysisAdd
BLAST

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

NADP

Enzyme and pathway databases

UniPathwayiUPA00901.

Names & Taxonomyi

Protein namesi
Recommended name:
Isoflavone reductase (EC:1.3.1.45)
Short name:
IFR
Alternative name(s):
2'-hydroxyisoflavone reductase
NADPH:isoflavone oxidoreductase
Gene namesi
Name:IFR
OrganismiMedicago sativa (Alfalfa)
Taxonomic identifieri3879 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsFabalesFabaceaePapilionoideaeTrifolieaeMedicago

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 318318Isoflavone reductasePRO_0000204546Add
BLAST

Expressioni

Inductioni

By fungal elicitor.

Structurei

Secondary structure

1
318
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi7 – 115Combined sources
Helixi17 – 2711Combined sources
Beta strandi31 – 355Combined sources
Helixi53 – 6513Combined sources
Beta strandi69 – 724Combined sources
Helixi78 – 858Combined sources
Beta strandi89 – 935Combined sources
Beta strandi95 – 984Combined sources
Helixi100 – 1023Combined sources
Helixi103 – 11311Combined sources
Beta strandi117 – 1204Combined sources
Helixi137 – 15418Combined sources
Beta strandi158 – 1625Combined sources
Turni167 – 1704Combined sources
Helixi171 – 1733Combined sources
Beta strandi184 – 1907Combined sources
Beta strandi195 – 2006Combined sources
Helixi202 – 21312Combined sources
Helixi216 – 2183Combined sources
Beta strandi221 – 2244Combined sources
Helixi228 – 2303Combined sources
Beta strandi231 – 2333Combined sources
Helixi234 – 24512Combined sources
Beta strandi250 – 2545Combined sources
Helixi256 – 26510Combined sources
Helixi270 – 28112Combined sources
Turni292 – 2943Combined sources
Beta strandi295 – 2973Combined sources
Helixi298 – 3014Combined sources
Helixi310 – 3145Combined sources
Helixi315 – 3173Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2GASX-ray1.60A/B3-318[»]
ProteinModelPortaliP52575.
SMRiP52575. Positions 3-318.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP52575.

Family & Domainsi

Sequence similaritiesi

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR016040. NAD(P)-bd_dom.
IPR008030. NmrA-like.
[Graphical view]
PfamiPF05368. NmrA. 1 hit.
[Graphical view]
SUPFAMiSSF51735. SSF51735. 1 hit.

Sequencei

Sequence statusi: Complete.

P52575-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MATENKILIL GPTGAIGRHI VWASIKAGNP TYALVRKTPG NVNKPKLITA
60 70 80 90 100
ANPETKEELI DNYQSLGVIL LEGDINDHET LVKAIKQVDI VICAAGRLLI
110 120 130 140 150
EDQVKIIKAI KEAGNVKKFF PSEFGLDVDR HEAVEPVRQV FEEKASIRRV
160 170 180 190 200
IEAEGVPYTY LCCHAFTGYF LRNLAQLDTT DPPRDKVVIL GDGNVKGAYV
210 220 230 240 250
TEADVGTFTI RAANDPNTLN KAVHIRLPEN YLTQNEVIAL WEKKIGKTLE
260 270 280 290 300
KTYVSEEQVL KDIQESSFPH NYLLALYHSQ QIKGDAVYEI DPAKDIEASE
310
AYPDVTYTTA DEYLNQFV
Length:318
Mass (Da):35,455
Last modified:October 1, 1996 - v1
Checksum:i5E2AF9C8CFB79F17
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti132 – 1321E → D in CAA41106 (PubMed:1912490).Curated
Sequence conflicti179 – 1791T → A in CAA41106 (PubMed:1912490).Curated
Sequence conflicti229 – 2291E → K in CAA41106 (PubMed:1912490).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U17436 Genomic DNA. Translation: AAC48976.1.
X58078 mRNA. Translation: CAA41106.1.
PIRiS17744.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U17436 Genomic DNA. Translation: AAC48976.1.
X58078 mRNA. Translation: CAA41106.1.
PIRiS17744.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2GASX-ray1.60A/B3-318[»]
ProteinModelPortaliP52575.
SMRiP52575. Positions 3-318.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00901.

Miscellaneous databases

EvolutionaryTraceiP52575.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR016040. NAD(P)-bd_dom.
IPR008030. NmrA-like.
[Graphical view]
PfamiPF05368. NmrA. 1 hit.
[Graphical view]
SUPFAMiSSF51735. SSF51735. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiIFR_MEDSA
AccessioniPrimary (citable) accession number: P52575
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: December 9, 2015
This is version 74 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

3D-structure

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

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 one 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.