[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. DOI=10.1105/tpc.6.12.1789; PubMed=7866024 [NCBI, ExPASy, EBI, Israel, Japan] Oommen A., Dixon R.A., Paiva N.L.; "The elicitor-inducible alfalfa isoflavone reductase promoter confers different patterns of developmental expression in homologous and heterologous transgenic plants."; Plant Cell 6:1789-1803(1994).
[2]	NUCLEOTIDE SEQUENCE [MRNA]. STRAIN=cv. Apollo; DOI=10.1007/BF00037051; PubMed=1912490 [NCBI, ExPASy, EBI, Israel, Japan] Paiva N.L., Edwards R., Sun Y., Hrazdina G., Dixon R.A.; "Stress responses in alfalfa (Medicago sativa L.) 11. Molecular cloning and expression of alfalfa isoflavone reductase, a key enzyme of isoflavonoid phytoalexin biosynthesis."; Plant Mol. Biol. 17:653-667(1991).

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.
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

U17436; AAC48976.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X58078; CAA41106.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S17744; S17744.

3D structure databases

PDB

2GAS; X-ray; 1.60 A; A/B=3-318.

[ExPASy / RCSB / EBI]

PDBsum

2GAS; -.

ModBase

P52575.

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

P52575.

UniRef

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

Keywords

3D-structure; NADP; Oxidoreductase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 318`	`318`	`Isoflavone reductase.`	`PRO_0000204546`
`NP_BIND`	`6 37`	`32`	`NADP (Potential).`
`CONFLICT`	`132 132`		`E -> D (in Ref. 2; CAA41106).`
`CONFLICT`	`179 179`		`T -> A (in Ref. 2; CAA41106).`
`CONFLICT`	`229 229`		`E -> K (in Ref. 2; CAA41106).`
`STRAND`	`7 11`	`5`
`HELIX`	`17 27`	`11`
`STRAND`	`31 35`	`5`
`HELIX`	`53 65`	`13`
`STRAND`	`69 72`	`4`
`HELIX`	`78 85`	`8`
`STRAND`	`89 93`	`5`
`STRAND`	`95 98`	`4`
`HELIX`	`100 102`	`3`
`HELIX`	`103 113`	`11`
`STRAND`	`117 120`	`4`
`HELIX`	`137 154`	`18`
`STRAND`	`158 162`	`5`
`TURN`	`167 170`	`4`
`HELIX`	`171 173`	`3`
`STRAND`	`184 190`	`7`
`STRAND`	`195 200`	`6`
`HELIX`	`202 213`	`12`
`HELIX`	`216 218`	`3`
`STRAND`	`221 224`	`4`
`HELIX`	`228 230`	`3`
`STRAND`	`231 233`	`3`
`HELIX`	`234 245`	`12`
`STRAND`	`250 254`	`5`
`HELIX`	`256 265`	`10`
`HELIX`	`270 281`	`12`
`TURN`	`292 294`	`3`
`STRAND`	`295 297`	`3`
`HELIX`	`298 301`	`4`
`HELIX`	`310 314`	`5`
`HELIX`	`315 317`	`3`

Sequence information

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

Molecular weight: 35455 Da [This is the MW of the unprocessed precursor]

CRC64: 5E2AF9C8CFB79F17 [This is a checksum on the sequence]

        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

P52575 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