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Protein

Vestitone reductase

Gene
N/A
Organism
Medicago sativa (Alfalfa)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Stereospecific enzyme that catalyzes the NADPH-dependent reduction of (3R)-vestitone to (3R,4R)-4'-methoxyisoflavan-2',4,7-triol (DMI). Has no activity with (3S)-vestitone. Catalyzes the penultimate step in the biosynthesis of the phytoalexin medicarpin, and thereby contributes to plant defense reactions.3 Publications

Catalytic activityi

(3R,4R)-4'-methoxyisoflavan-2',4,7-triol + NADP+ = (3R)-vestitone + NADPH.2 Publications

Enzyme regulationi

Inhibited by vestitone concentrations above 50 µM.1 Publication

Kineticsi

  1. KM=40 µM for vestitone1 Publication

    pH dependencei

    Optimum pH is 6.0.1 Publication

    Temperature dependencei

    Optimum temperature is 30 degrees Celsius.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei37 – 371NADPSequence analysis

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi12 – 187NADPSequence analysis

    GO - Molecular functioni

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Flavonoid biosynthesis, Plant defense

    Keywords - Ligandi

    NADP

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-5044.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Vestitone reductase (EC:1.1.1.348)
    OrganismiMedicago sativa (Alfalfa)
    Taxonomic identifieri3879 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsFabalesFabaceaePapilionoideaeTrifolieaeMedicago

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 326326Vestitone reductasePRO_0000424198Add
    BLAST

    Expressioni

    Tissue specificityi

    Detected in roots, and at lower levels in root nodules. Not detected in petioles, leaf and stem.1 Publication

    Inductioni

    Transiently up-regulated by fungal elicitors, peaking 6 hours after elicitor treatment.1 Publication

    Interactioni

    Subunit structurei

    Monomer.1 Publication

    Structurei

    Secondary structure

    1
    326
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi7 – 126Combined sources
    Helixi16 – 2712Combined sources
    Beta strandi31 – 355Combined sources
    Helixi47 – 504Combined sources
    Helixi55 – 584Combined sources
    Beta strandi59 – 613Combined sources
    Helixi69 – 724Combined sources
    Helixi73 – 764Combined sources
    Beta strandi80 – 845Combined sources
    Helixi99 – 11517Combined sources
    Beta strandi123 – 1297Combined sources
    Helixi130 – 1323Combined sources
    Beta strandi136 – 1383Combined sources
    Beta strandi141 – 1433Combined sources
    Helixi151 – 1577Combined sources
    Helixi162 – 18120Combined sources
    Beta strandi186 – 1916Combined sources
    Beta strandi193 – 1964Combined sources
    Beta strandi200 – 2023Combined sources
    Helixi205 – 2106Combined sources
    Helixi212 – 2154Combined sources
    Helixi218 – 2203Combined sources
    Beta strandi223 – 2308Combined sources
    Helixi231 – 24313Combined sources
    Beta strandi249 – 2524Combined sources
    Beta strandi256 – 2594Combined sources
    Helixi260 – 27011Combined sources
    Turni279 – 2846Combined sources
    Helixi296 – 3005Combined sources
    Helixi309 – 32214Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2P4HX-ray1.40X5-326[»]
    ProteinModelPortaliQ40316.
    SMRiQ40316. Positions 5-326.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ40316.

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    KOiK13265.

    Family and domain databases

    Gene3Di3.40.50.720. 1 hit.
    InterProiIPR001509. Epimerase_deHydtase_N.
    IPR016040. NAD(P)-bd_dom.
    [Graphical view]
    PfamiPF01370. Epimerase. 1 hit.
    [Graphical view]
    SUPFAMiSSF51735. SSF51735. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q40316-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MAEGKGRVCV TGGTGFLGSW IIKSLLENGY SVNTTIRADP ERKRDVSFLT
    60 70 80 90 100
    NLPGASEKLH FFNADLSNPD SFAAAIEGCV GIFHTASPID FAVSEPEEIV
    110 120 130 140 150
    TKRTVDGALG ILKACVNSKT VKRFIYTSSG SAVSFNGKDK DVLDESDWSD
    160 170 180 190 200
    VDLLRSVKPF GWNYAVSKTL AEKAVLEFGE QNGIDVVTLI LPFIVGRFVC
    210 220 230 240 250
    PKLPDSIEKA LVLVLGKKEQ IGVTRFHMVH VDDVARAHIY LLENSVPGGR
    260 270 280 290 300
    YNCSPFIVPI EEMSQLLSAK YPEYQILTVD ELKEIKGARL PDLNTKKLVD
    310 320
    AGFDFKYTIE DMFDDAIQCC KEKGYL
    Length:326
    Mass (Da):35,918
    Last modified:November 1, 1996 - v1
    Checksum:i25B244BCD939F818
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U28213 mRNA. Translation: AAB41550.1.
    PIRiS66262.

    Genome annotation databases

    KEGGiag:AAB41550.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U28213 mRNA. Translation: AAB41550.1.
    PIRiS66262.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2P4HX-ray1.40X5-326[»]
    ProteinModelPortaliQ40316.
    SMRiQ40316. Positions 5-326.
    ModBaseiSearch...
    MobiDBiSearch...

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    KEGGiag:AAB41550.

    Phylogenomic databases

    KOiK13265.

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-5044.

    Miscellaneous databases

    EvolutionaryTraceiQ40316.

    Family and domain databases

    Gene3Di3.40.50.720. 1 hit.
    InterProiIPR001509. Epimerase_deHydtase_N.
    IPR016040. NAD(P)-bd_dom.
    [Graphical view]
    PfamiPF01370. Epimerase. 1 hit.
    [Graphical view]
    SUPFAMiSSF51735. SSF51735. 1 hit.
    ProtoNetiSearch...

    Entry informationi

    Entry nameiVESTR_MEDSA
    AccessioniPrimary (citable) accession number: Q40316
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 16, 2013
    Last sequence update: November 1, 1996
    Last modified: December 9, 2015
    This is version 60 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Direct protein sequencing

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.