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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)DescriptionActionsGraphical viewLength
    Binding sitei37NADPSequence analysis1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Nucleotide bindingi12 – 18NADPSequence analysis7

    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)DescriptionActionsGraphical viewLength
    ChainiPRO_00004241981 – 326Vestitone reductaseAdd BLAST326

    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

    1326
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi7 – 12Combined sources6
    Helixi16 – 27Combined sources12
    Beta strandi31 – 35Combined sources5
    Helixi47 – 50Combined sources4
    Helixi55 – 58Combined sources4
    Beta strandi59 – 61Combined sources3
    Helixi69 – 72Combined sources4
    Helixi73 – 76Combined sources4
    Beta strandi80 – 84Combined sources5
    Helixi99 – 115Combined sources17
    Beta strandi123 – 129Combined sources7
    Helixi130 – 132Combined sources3
    Beta strandi136 – 138Combined sources3
    Beta strandi141 – 143Combined sources3
    Helixi151 – 157Combined sources7
    Helixi162 – 181Combined sources20
    Beta strandi186 – 191Combined sources6
    Beta strandi193 – 196Combined sources4
    Beta strandi200 – 202Combined sources3
    Helixi205 – 210Combined sources6
    Helixi212 – 215Combined sources4
    Helixi218 – 220Combined sources3
    Beta strandi223 – 230Combined sources8
    Helixi231 – 243Combined sources13
    Beta strandi249 – 252Combined sources4
    Beta strandi256 – 259Combined sources4
    Helixi260 – 270Combined sources11
    Turni279 – 284Combined sources6
    Helixi296 – 300Combined sources5
    Helixi309 – 322Combined sources14

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    2P4HX-ray1.40X5-326[»]
    ProteinModelPortaliQ40316.
    SMRiQ40316.
    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.
    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
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    2P4HX-ray1.40X5-326[»]
    ProteinModelPortaliQ40316.
    SMRiQ40316.
    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.
    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: November 30, 2016
    This is version 63 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.