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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)DescriptionActionsGraphical viewLength
Nucleotide bindingi6 – 37NADPSequence analysisAdd BLAST32

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)DescriptionActionsGraphical viewLength
ChainiPRO_00002045461 – 318Isoflavone reductaseAdd BLAST318

Expressioni

Inductioni

By fungal elicitor.

Structurei

Secondary structure

1318
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi7 – 11Combined sources5
Helixi17 – 27Combined sources11
Beta strandi31 – 35Combined sources5
Helixi53 – 65Combined sources13
Beta strandi69 – 72Combined sources4
Helixi78 – 85Combined sources8
Beta strandi89 – 93Combined sources5
Beta strandi95 – 98Combined sources4
Helixi100 – 102Combined sources3
Helixi103 – 113Combined sources11
Beta strandi117 – 120Combined sources4
Helixi137 – 154Combined sources18
Beta strandi158 – 162Combined sources5
Turni167 – 170Combined sources4
Helixi171 – 173Combined sources3
Beta strandi184 – 190Combined sources7
Beta strandi195 – 200Combined sources6
Helixi202 – 213Combined sources12
Helixi216 – 218Combined sources3
Beta strandi221 – 224Combined sources4
Helixi228 – 230Combined sources3
Beta strandi231 – 233Combined sources3
Helixi234 – 245Combined sources12
Beta strandi250 – 254Combined sources5
Helixi256 – 265Combined sources10
Helixi270 – 281Combined sources12
Turni292 – 294Combined sources3
Beta strandi295 – 297Combined sources3
Helixi298 – 301Combined sources4
Helixi310 – 314Combined sources5
Helixi315 – 317Combined sources3

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP52575.

Family & Domainsi

Sequence similaritiesi

Family and domain databases

Gene3Di3.40.50.720. 2 hits.
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)DescriptionActionsGraphical viewLength
Sequence conflicti132E → D in CAA41106 (PubMed:1912490).Curated1
Sequence conflicti179T → A in CAA41106 (PubMed:1912490).Curated1
Sequence conflicti229E → K in CAA41106 (PubMed:1912490).Curated1

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2GASX-ray1.60A/B3-318[»]
ProteinModelPortaliP52575.
SMRiP52575.
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. 2 hits.
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: November 30, 2016
This is version 77 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.