VESTR_MEDSA
ID VESTR_MEDSA Reviewed; 326 AA.
AC Q40316;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=Vestitone reductase;
DE EC=1.1.1.348 {ECO:0000269|PubMed:7625843, ECO:0000269|PubMed:8071365};
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], PARTIAL PROTEIN SEQUENCE, FUNCTION, CATALYTIC
RP ACTIVITY, INDUCTION, AND TISSUE SPECIFICITY.
RX PubMed=7625843; DOI=10.1016/0003-9861(95)90019-5;
RA Guo L., Paiva N.L.;
RT "Molecular cloning and expression of alfalfa (Medicago sativa L.) vestitone
RT reductase, the penultimate enzyme in medicarpin biosynthesis.";
RL Arch. Biochem. Biophys. 320:353-360(1995).
RN [2]
RP FUNCTION.
RX PubMed=7805842; DOI=10.1016/0014-5793(94)01267-9;
RA Guo L., Dixon R.A., Paiva N.L.;
RT "The 'pterocarpan synthase' of alfalfa: association and co-induction of
RT vestitone reductase and 7,2'-dihydroxy-4'-methoxy-isoflavanol (DMI)
RT dehydratase, the two final enzymes in medicarpin biosynthesis.";
RL FEBS Lett. 356:221-225(1994).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY
RP REGULATION, AND SUBUNIT.
RX PubMed=8071365; DOI=10.1016/s0021-9258(17)31799-4;
RA Guo L., Dixon R.A., Paiva N.L.;
RT "Conversion of vestitone to medicarpin in alfalfa (Medicago sativa L.) is
RT catalyzed by two independent enzymes. Identification, purification, and
RT characterization of vestitone reductase and 7,2'-dihydroxy-4'-
RT methoxyisoflavanol dehydratase.";
RL J. Biol. Chem. 269:22372-22378(1994).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.40 ANGSTROMS) OF 5-326, AND PREDICTED NADP BINDING
RP SITES.
RX PubMed=17433362; DOI=10.1016/j.jmb.2007.03.040;
RA Shao H., Dixon R.A., Wang X.;
RT "Crystal structure of vestitone reductase from alfalfa (Medicago sativa
RT L.).";
RL J. Mol. Biol. 369:265-276(2007).
CC -!- FUNCTION: Stereospecific enzyme that catalyzes the NADPH-dependent
CC reduction of (3R)-vestitone to (3R,4R)-4'-methoxyisoflavan-2',4,7-triol
CC (DMI). Has no activity with (3S)-vestitone. Catalyzes the penultimate
CC step in the biosynthesis of the phytoalexin medicarpin, and thereby
CC contributes to plant defense reactions. {ECO:0000269|PubMed:7625843,
CC ECO:0000269|PubMed:7805842, ECO:0000269|PubMed:8071365}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a (3R,4R)-4,2'-dihydroxyisoflavan + NADP(+) = a (3R)-2'-
CC hydroxyisoflavanone + H(+) + NADPH; Xref=Rhea:RHEA:56284,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:140181, ChEBI:CHEBI:140183; EC=1.1.1.348;
CC Evidence={ECO:0000269|PubMed:7625843, ECO:0000269|PubMed:8071365};
CC -!- ACTIVITY REGULATION: Inhibited by vestitone concentrations above 50 uM.
CC {ECO:0000269|PubMed:8071365}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=40 uM for vestitone {ECO:0000269|PubMed:8071365};
CC pH dependence:
CC Optimum pH is 6.0. {ECO:0000269|PubMed:8071365};
CC Temperature dependence:
CC Optimum temperature is 30 degrees Celsius.
CC {ECO:0000269|PubMed:8071365};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:8071365}.
CC -!- TISSUE SPECIFICITY: Detected in roots, and at lower levels in root
CC nodules. Not detected in petioles, leaf and stem.
CC {ECO:0000269|PubMed:7625843}.
CC -!- INDUCTION: Transiently up-regulated by fungal elicitors, peaking 6
CC hours after elicitor treatment. {ECO:0000269|PubMed:7625843}.
CC -!- SIMILARITY: Belongs to the NAD(P)-dependent epimerase/dehydratase
CC family. Dihydroflavonol-4-reductase subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U28213; AAB41550.1; -; mRNA.
DR PIR; S66262; S66262.
DR PDB; 2P4H; X-ray; 1.40 A; X=5-326.
DR PDBsum; 2P4H; -.
DR AlphaFoldDB; Q40316; -.
DR SMR; Q40316; -.
DR KEGG; ag:AAB41550; -.
DR BioCyc; MetaCyc:MON-5044; -.
DR EvolutionaryTrace; Q40316; -.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR GO; GO:0009813; P:flavonoid biosynthetic process; IEA:UniProtKB-KW.
DR InterPro; IPR001509; Epimerase_deHydtase.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR Pfam; PF01370; Epimerase; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Flavonoid biosynthesis; NADP;
KW Oxidoreductase; Plant defense.
FT CHAIN 1..326
FT /note="Vestitone reductase"
FT /id="PRO_0000424198"
FT BINDING 12..18
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255"
FT BINDING 37
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255"
FT BINDING 164
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:A0A059TC02"
FT STRAND 7..12
FT /evidence="ECO:0007829|PDB:2P4H"
FT HELIX 16..27
FT /evidence="ECO:0007829|PDB:2P4H"
FT STRAND 31..35
FT /evidence="ECO:0007829|PDB:2P4H"
FT HELIX 47..50
FT /evidence="ECO:0007829|PDB:2P4H"
FT HELIX 55..58
FT /evidence="ECO:0007829|PDB:2P4H"
FT STRAND 59..61
FT /evidence="ECO:0007829|PDB:2P4H"
FT HELIX 69..72
FT /evidence="ECO:0007829|PDB:2P4H"
FT HELIX 73..76
FT /evidence="ECO:0007829|PDB:2P4H"
FT STRAND 80..84
FT /evidence="ECO:0007829|PDB:2P4H"
FT HELIX 99..115
FT /evidence="ECO:0007829|PDB:2P4H"
FT STRAND 123..129
FT /evidence="ECO:0007829|PDB:2P4H"
FT HELIX 130..132
FT /evidence="ECO:0007829|PDB:2P4H"
FT STRAND 136..138
FT /evidence="ECO:0007829|PDB:2P4H"
FT STRAND 141..143
FT /evidence="ECO:0007829|PDB:2P4H"
FT HELIX 151..157
FT /evidence="ECO:0007829|PDB:2P4H"
FT HELIX 162..181
FT /evidence="ECO:0007829|PDB:2P4H"
FT STRAND 186..191
FT /evidence="ECO:0007829|PDB:2P4H"
FT STRAND 193..196
FT /evidence="ECO:0007829|PDB:2P4H"
FT STRAND 200..202
FT /evidence="ECO:0007829|PDB:2P4H"
FT HELIX 205..210
FT /evidence="ECO:0007829|PDB:2P4H"
FT HELIX 212..215
FT /evidence="ECO:0007829|PDB:2P4H"
FT HELIX 218..220
FT /evidence="ECO:0007829|PDB:2P4H"
FT STRAND 223..230
FT /evidence="ECO:0007829|PDB:2P4H"
FT HELIX 231..243
FT /evidence="ECO:0007829|PDB:2P4H"
FT STRAND 249..252
FT /evidence="ECO:0007829|PDB:2P4H"
FT STRAND 256..259
FT /evidence="ECO:0007829|PDB:2P4H"
FT HELIX 260..270
FT /evidence="ECO:0007829|PDB:2P4H"
FT TURN 279..284
FT /evidence="ECO:0007829|PDB:2P4H"
FT HELIX 296..300
FT /evidence="ECO:0007829|PDB:2P4H"
FT HELIX 309..322
FT /evidence="ECO:0007829|PDB:2P4H"
SQ SEQUENCE 326 AA; 35918 MW; 25B244BCD939F818 CRC64;
MAEGKGRVCV TGGTGFLGSW IIKSLLENGY SVNTTIRADP ERKRDVSFLT NLPGASEKLH
FFNADLSNPD SFAAAIEGCV GIFHTASPID FAVSEPEEIV TKRTVDGALG ILKACVNSKT
VKRFIYTSSG SAVSFNGKDK DVLDESDWSD VDLLRSVKPF GWNYAVSKTL AEKAVLEFGE
QNGIDVVTLI LPFIVGRFVC PKLPDSIEKA LVLVLGKKEQ IGVTRFHMVH VDDVARAHIY
LLENSVPGGR YNCSPFIVPI EEMSQLLSAK YPEYQILTVD ELKEIKGARL PDLNTKKLVD
AGFDFKYTIE DMFDDAIQCC KEKGYL
