IFR_MEDSA
ID IFR_MEDSA Reviewed; 318 AA.
AC P52575;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Isoflavone reductase {ECO:0000303|PubMed:7866024};
DE Short=IFR {ECO:0000303|PubMed:7866024};
DE EC=1.3.1.45 {ECO:0000269|PubMed:16600295};
DE AltName: Full=2'-hydroxyisoflavone reductase {ECO:0000305};
DE AltName: Full=NADPH:isoflavone oxidoreductase {ECO:0000305};
GN Name=IFR {ECO:0000303|PubMed:7866024};
OS Medicago sativa (Alfalfa).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; Hologalegina; IRL clade; Trifolieae; Medicago.
OX NCBI_TaxID=3879;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC STRAIN=cv. Apollo;
RX PubMed=1912490; DOI=10.1007/bf00037051;
RA Paiva N.L., Edwards R., Sun Y., Hrazdina G., Dixon R.A.;
RT "Stress responses in alfalfa (Medicago sativa L.) 11. Molecular cloning and
RT expression of alfalfa isoflavone reductase, a key enzyme of isoflavonoid
RT phytoalexin biosynthesis.";
RL Plant Mol. Biol. 17:653-667(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION.
RX PubMed=7866024; DOI=10.2307/3869908;
RA Oommen A., Dixon R.A., Paiva N.L.;
RT "The elicitor-inducible alfalfa isoflavone reductase promoter confers
RT different patterns of developmental expression in homologous and
RT heterologous transgenic plants.";
RL Plant Cell 6:1789-1803(1994).
RN [3]
RP INDUCTION.
RX PubMed=8274775; DOI=10.1094/mpmi-6-655;
RA Esnault R., Buffard D., Breda C., Sallaud C., El-Turk J., Kondorosi A.;
RT "Pathological and molecular characterizations of alfalfa interactions with
RT compatible and incompatible bacteria, Xanthomonas campestris pv. alfalfae
RT and Pseudomonas syringae pv. pisi.";
RL Mol. Plant Microbe Interact. 6:655-664(1993).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 3-318, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, ACTIVE SITE, BINDING SITES, SUBUNIT, AND
RP MUTAGENESIS OF GLY-14 AND LYS-144.
RX PubMed=16600295; DOI=10.1016/j.jmb.2006.03.022;
RA Wang X., He X., Lin J., Shao H., Chang Z., Dixon R.A.;
RT "Crystal structure of isoflavone reductase from alfalfa (Medicago sativa
RT L.).";
RL J. Mol. Biol. 358:1341-1352(2006).
CC -!- FUNCTION: Reduces achiral isoflavones to chiral isoflavanones during
CC the biosynthesis of chiral pterocarpan phytoalexins. The reduction
CC product is a third isomer, which represents the penultimate
CC intermediate in the synthesis of the phytoalexin (-)-medicarpin, the
CC major phytoalexin in Alfalfa. {ECO:0000305|PubMed:1912490}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(3R)-vestitone + NADP(+) = 2'-hydroxyformononetin + 2 H(+) +
CC NADPH; Xref=Rhea:RHEA:22560, ChEBI:CHEBI:15378, ChEBI:CHEBI:16786,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:77687; EC=1.3.1.45;
CC Evidence={ECO:0000269|PubMed:16600295};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=14.2 uM for 2'-hydroxyformononetin {ECO:0000269|PubMed:16600295};
CC -!- PATHWAY: Phytoalexin biosynthesis; pterocarpan phytoalexin
CC biosynthesis. {ECO:0000305}.
CC -!- INDUCTION: By fungal elicitor (PubMed:7866024). Induced by the
CC bacterial pathogens Pseudomonas syringae pv pisi and Xanthomonas
CC campestris pv alfalfae (PubMed:8274775). {ECO:0000269|PubMed:7866024,
CC ECO:0000269|PubMed:8274775}.
CC -!- SIMILARITY: Belongs to the NmrA-type oxidoreductase family. Isoflavone
CC reductase subfamily. {ECO:0000305}.
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DR EMBL; X58078; CAA41106.1; -; mRNA.
DR EMBL; U17436; AAC48976.1; -; Genomic_DNA.
DR PIR; S17744; S17744.
DR PDB; 2GAS; X-ray; 1.60 A; A/B=3-318.
DR PDBsum; 2GAS; -.
DR AlphaFoldDB; P52575; -.
DR SMR; P52575; -.
DR BioCyc; MetaCyc:MON-5681; -.
DR UniPathway; UPA00901; -.
DR EvolutionaryTrace; P52575; -.
DR GO; GO:0047526; F:2'-hydroxyisoflavone reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR GO; GO:0009807; P:lignan biosynthetic process; IEA:UniProt.
DR CDD; cd05259; PCBER_SDR_a; 1.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR008030; NmrA-like.
DR InterPro; IPR045312; PCBER-like.
DR Pfam; PF05368; NmrA; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 1: Evidence at protein level;
KW 3D-structure; NADP; Oxidoreductase; Plant defense.
FT CHAIN 1..318
FT /note="Isoflavone reductase"
FT /id="PRO_0000204546"
FT ACT_SITE 144
FT /note="Proton acceptor"
FT /evidence="ECO:0000305|PubMed:16600295"
FT BINDING 11..17
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000305|PubMed:16600295"
FT BINDING 36
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q9LD14"
FT BINDING 44
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q9LD14"
FT BINDING 148
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q9LD14"
FT MUTAGEN 14
FT /note="G->F: Loss of enzyme activity."
FT /evidence="ECO:0000269|PubMed:16600295"
FT MUTAGEN 144
FT /note="K->A: Loss of enzyme activity."
FT /evidence="ECO:0000269|PubMed:16600295"
FT CONFLICT 132
FT /note="E -> D (in Ref. 1; CAA41106)"
FT /evidence="ECO:0000305"
FT CONFLICT 179
FT /note="T -> A (in Ref. 1; CAA41106)"
FT /evidence="ECO:0000305"
FT CONFLICT 229
FT /note="E -> K (in Ref. 1; CAA41106)"
FT /evidence="ECO:0000305"
FT STRAND 7..11
FT /evidence="ECO:0007829|PDB:2GAS"
FT HELIX 17..27
FT /evidence="ECO:0007829|PDB:2GAS"
FT STRAND 31..35
FT /evidence="ECO:0007829|PDB:2GAS"
FT HELIX 53..65
FT /evidence="ECO:0007829|PDB:2GAS"
FT STRAND 69..72
FT /evidence="ECO:0007829|PDB:2GAS"
FT HELIX 78..85
FT /evidence="ECO:0007829|PDB:2GAS"
FT STRAND 89..93
FT /evidence="ECO:0007829|PDB:2GAS"
FT STRAND 95..98
FT /evidence="ECO:0007829|PDB:2GAS"
FT HELIX 100..102
FT /evidence="ECO:0007829|PDB:2GAS"
FT HELIX 103..113
FT /evidence="ECO:0007829|PDB:2GAS"
FT STRAND 117..120
FT /evidence="ECO:0007829|PDB:2GAS"
FT HELIX 137..154
FT /evidence="ECO:0007829|PDB:2GAS"
FT STRAND 158..162
FT /evidence="ECO:0007829|PDB:2GAS"
FT TURN 167..170
FT /evidence="ECO:0007829|PDB:2GAS"
FT HELIX 171..173
FT /evidence="ECO:0007829|PDB:2GAS"
FT STRAND 184..190
FT /evidence="ECO:0007829|PDB:2GAS"
FT STRAND 195..200
FT /evidence="ECO:0007829|PDB:2GAS"
FT HELIX 202..213
FT /evidence="ECO:0007829|PDB:2GAS"
FT HELIX 216..218
FT /evidence="ECO:0007829|PDB:2GAS"
FT STRAND 221..224
FT /evidence="ECO:0007829|PDB:2GAS"
FT HELIX 228..230
FT /evidence="ECO:0007829|PDB:2GAS"
FT STRAND 231..233
FT /evidence="ECO:0007829|PDB:2GAS"
FT HELIX 234..245
FT /evidence="ECO:0007829|PDB:2GAS"
FT STRAND 250..254
FT /evidence="ECO:0007829|PDB:2GAS"
FT HELIX 256..265
FT /evidence="ECO:0007829|PDB:2GAS"
FT HELIX 270..281
FT /evidence="ECO:0007829|PDB:2GAS"
FT TURN 292..294
FT /evidence="ECO:0007829|PDB:2GAS"
FT STRAND 295..297
FT /evidence="ECO:0007829|PDB:2GAS"
FT HELIX 298..301
FT /evidence="ECO:0007829|PDB:2GAS"
FT HELIX 310..314
FT /evidence="ECO:0007829|PDB:2GAS"
FT HELIX 315..317
FT /evidence="ECO:0007829|PDB:2GAS"
SQ SEQUENCE 318 AA; 35455 MW; 5E2AF9C8CFB79F17 CRC64;
MATENKILIL GPTGAIGRHI VWASIKAGNP TYALVRKTPG NVNKPKLITA ANPETKEELI
DNYQSLGVIL LEGDINDHET LVKAIKQVDI VICAAGRLLI EDQVKIIKAI KEAGNVKKFF
PSEFGLDVDR HEAVEPVRQV FEEKASIRRV IEAEGVPYTY LCCHAFTGYF LRNLAQLDTT
DPPRDKVVIL GDGNVKGAYV TEADVGTFTI RAANDPNTLN KAVHIRLPEN YLTQNEVIAL
WEKKIGKTLE KTYVSEEQVL KDIQESSFPH NYLLALYHSQ QIKGDAVYEI DPAKDIEASE
AYPDVTYTTA DEYLNQFV
