NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=cv. Alaska Green;
DOI=10.1006/abbi.1994.1338; PubMed=8037464 [NCBI, ExPASy, EBI, Israel, Japan]
Paiva N.L., Sun Y., Dixon R.A., Vanetten H.D., Hrazdina G.;
"Molecular cloning of isoflavone reductase from pea (Pisum sativum L.): evidence for a 3R-isoflavanone intermediate in (+)-pisatin biosynthesis.";
Arch. Biochem. Biophys. 312:501-510(1994).

Comments

FUNCTION: Reduces achiral isoflavones to chiral isoflavanones during the biosynthesis of chiral pterocarpan phytoalexins. The reduction product (sophrol) is a third isomer, which represents the penultimate intermediate in the synthesis of the phytoalexin (+)-pisatin, the major phytoalexin in pea.
CATALYTIC ACTIVITY: Vestitone + NADP⁺ = 2'-hydroxyformononetin + NADPH.
PATHWAY: Phytoalexin biosynthesis; pterocarpan phytoalexin biosynthesis .
SIMILARITY: Belongs to the NmrA-type oxidoreductase family. Isoflavone reductase subfamily.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

S72472; AAB31368.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S48631; S48631.

3D structure databases

SMR

P52576; 3-318.

ModBase

P52576.

Ontologies

GO:0047526;	Molecular function: 2'-hydroxyisoflavone reductase activity (inferred from electronic annotation from EC).
GO:0005488;	Molecular function: binding (inferred from electronic annotation from InterPro).
GO:0016564;	Molecular function: transcription repressor activity (inferred from electronic annotation from InterPro).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
GO:0006808;	Biological process: regulation of nitrogen utilization (inferred from electronic annotation from InterPro).
QuickGo view.

Family and domain databases

InterPro

IPR016040; NAD(P)-bd.
IPR008030; NmrA.
Graphical view of domain structure.

Gene3D

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

Pfam

PF05368; NmrA; 1.
Pfam graphical view of domain structure.

Other

ProtoNet

P52576.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

NADP; Oxidoreductase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 318`	`318`	`Isoflavone reductase.`	`PRO_0000204547`
`NP_BIND`	`6 37`	`32`	`NADP (Potential).`

Sequence information

Length: 318 AA [This is the length of the unprocessed precursor]

Molecular weight: 35429 Da [This is the MW of the unprocessed precursor]

CRC64: 6318CF6617CDE28F [This is a checksum on the sequence]

        10         20         30         40         50         60 
MATENKILIL GATGAIGRHI VWASIKAGNP TYALVRKTSD NVNKPKLTEA ANPETKEELL 

        70         80         90        100        110        120 
KNYQASGVIL LEGDINDHET LVNAIKQVDT VICAAGRLLI EDQVKVIKAI KEAGNVKRFF 

       130        140        150        160        170        180 
PSEFGLDVDR HDAVEPVRQV FEEKASIRRV VESEGVPYTY LCCHAFTGYF LRNLAQIDAT 

       190        200        210        220        230        240 
DPPRDKVVIL GDGNVRGAYV TEADVGTYTI RAANDPNTLN KAVHIRLPNN YLTANEVIAL 

       250        260        270        280        290        300 
WEKKIGKTLE KTYVSEEQVL KDIQTSSFPH NYLLALYHSQ QIKGDAVYEI DPAKDVEAYD 

       310 
AYPDVKYTTA DEYLNQFV

P52576 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools