P52575 (IFR_MEDSA) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Isoflavone reductase
Short name=IFR
EC=1.3.1.45

Alternative name(s):
2'-hydroxyisoflavone reductase
NADPH:isoflavone oxidoreductase

Gene names

Name:

IFR

Organism

Medicago sativa (Alfalfa)

Taxonomic identifier

3879 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › fabids › Fabales › Fabaceae › Papilionoideae › Trifolieae › Medicago

Protein attributes

Sequence length	318 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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 activity	Vestitone + NADP+ = 2'-hydroxyformononetin + NADPH.
Pathway	Phytoalexin biosynthesis; pterocarpan phytoalexin biosynthesis.
Induction	By fungal elicitor.
Sequence similarities	Belongs to the NmrA-type oxidoreductase family. Isoflavone reductase subfamily.

Ontologies

Keywords
Ligand	NADP
Molecular function	Oxidoreductase
Technical term	3D-structure
Gene Ontology (GO)
Molecular function	2'-hydroxyisoflavone reductase activity Inferred from electronic annotation. Source: EC nucleotide binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 318

318

Isoflavone reductase

PRO_0000204546

Regions

Nucleotide binding

6 – 37

32

NADP Potential

Experimental info

Sequence conflict

132

1

E → D in CAA41106. Ref.2

Sequence conflict

179

1

T → A in CAA41106. Ref.2

Sequence conflict

229

1

E → K in CAA41106. Ref.2

Secondary structure

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318

Helix Strand Turn

Details...

Beta strand

7 – 11

5

Helix

17 – 27

11

Beta strand

31 – 35

5

Helix

53 – 65

13

Beta strand

69 – 72

4

Helix

78 – 85

8

Beta strand

89 – 93

5

Beta strand

95 – 98

4

Helix

100 – 102

3

Helix

103 – 113

11

Beta strand

117 – 120

4

Helix

137 – 154

18

Beta strand

158 – 162

5

Turn

167 – 170

4

Helix

171 – 173

3

Beta strand

184 – 190

7

Beta strand

195 – 200

6

Helix

202 – 213

12

Helix

216 – 218

3

Beta strand

221 – 224

4

Helix

228 – 230

3

Beta strand

231 – 233

3

Helix

234 – 245

12

Beta strand

250 – 254

5

Helix

256 – 265

10

Helix

270 – 281

12

Turn

292 – 294

3

Beta strand

295 – 297

3

Helix

298 – 301

4

Helix

310 – 314

5

Helix

315 – 317

3

Sequences

	Sequence		Length	Mass (Da)
	P52575 [UniParc]. Last modified October 1, 1996. Version 1. Checksum: 5E2AF9C8CFB79F17	FASTA	318	35,455
	10 20 30 40 50 60 MATENKILIL GPTGAIGRHI VWASIKAGNP TYALVRKTPG NVNKPKLITA ANPETKEELI 70 80 90 100 110 120 DNYQSLGVIL LEGDINDHET LVKAIKQVDI VICAAGRLLI EDQVKIIKAI KEAGNVKKFF 130 140 150 160 170 180 PSEFGLDVDR HEAVEPVRQV FEEKASIRRV IEAEGVPYTY LCCHAFTGYF LRNLAQLDTT 190 200 210 220 230 240 DPPRDKVVIL GDGNVKGAYV TEADVGTFTI RAANDPNTLN KAVHIRLPEN YLTQNEVIAL 250 260 270 280 290 300 WEKKIGKTLE KTYVSEEQVL KDIQESSFPH NYLLALYHSQ QIKGDAVYEI DPAKDIEASE 310 AYPDVTYTTA DEYLNQFV

References

[1]	"The elicitor-inducible alfalfa isoflavone reductase promoter confers different patterns of developmental expression in homologous and heterologous transgenic plants." Oommen A., Dixon R.A., Paiva N.L. Plant Cell 6:1789-1803(1994) [PubMed: 7866024] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Stress responses in alfalfa (Medicago sativa L.) 11. Molecular cloning and expression of alfalfa isoflavone reductase, a key enzyme of isoflavonoid phytoalexin biosynthesis." Paiva N.L., Edwards R., Sun Y., Hrazdina G., Dixon R.A. Plant Mol. Biol. 17:653-667(1991) [PubMed: 1912490] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: cv. Apollo.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U17436 Genomic DNA. Translation: AAC48976.1.
X58078 mRNA. Translation: CAA41106.1.

PIR

S17744.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2GAS	X-ray	1.60	A/B	3-318	[»]

ProteinModelPortal

P52575.

SMR

P52575. Positions 3-318.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Family and domain databases

InterPro

IPR016040. NAD(P)-bd_dom.
IPR008030. NmrA.
[Graphical view]

Gene3D

G3DSA:3.40.50.720. NAD(P)-bd. 1 hit.

Pfam

PF05368. NmrA. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

IFR_MEDSA

Accession

Primary (citable) accession number: P52575

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	December 14, 2011
This is version 59 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program