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Protein

Inosine-5'-monophosphate dehydrogenase

Gene

impdh

Organism
Vigna unguiculata (Cowpea)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the conversion of inosine 5'-phosphate (IMP) to xanthosine 5'-phosphate (XMP), the first committed and rate-limiting step in the de novo synthesis of guanine nucleotides, and therefore plays an important role in the regulation of cell growth.UniRule annotation1 Publication

Catalytic activityi

Inosine 5'-phosphate + NAD+ + H2O = xanthosine 5'-phosphate + NADH.UniRule annotation

Cofactori

K(+)UniRule annotation

Enzyme regulationi

Mycophenolic acid (MPA) is a non-competitive inhibitor that prevents formation of the closed enzyme conformation by binding to the same site as the amobile flap. In contrast, mizoribine monophosphate (MZP) is a competitive inhibitor that induces the closed conformation. MPA is a potent inhibitor of mammalian IMPDHs but a poor inhibitor of the bacterial enzymes. MZP is a more potent inhibitor of bacterial IMPDH.UniRule annotation

Kineticsi

  1. KM=9.1 µM for Inosine 5'-phosphate1 Publication
  2. KM=18 µM for NAD+1 Publication
  3. KM=1.6 mM for K+1 Publication

    Pathway: XMP biosynthesis via de novo pathway

    This protein is involved in step 1 of the subpathway that synthesizes XMP from IMP.UniRule annotation
    Proteins known to be involved in this subpathway in this organism are:
    1. Inosine-5'-monophosphate dehydrogenase (impdh)
    This subpathway is part of the pathway XMP biosynthesis via de novo pathway, which is itself part of Purine metabolism.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes XMP from IMP, the pathway XMP biosynthesis via de novo pathway and in Purine metabolism.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi316 – 3161Potassium; via carbonyl oxygenUniRule annotation
    Metal bindingi318 – 3181Potassium; via carbonyl oxygenUniRule annotation
    Binding sitei319 – 3191IMPUniRule annotation
    Active sitei321 – 3211Thioimidate intermediateUniRule annotation
    Metal bindingi321 – 3211Potassium; via carbonyl oxygenUniRule annotation
    Binding sitei429 – 4291IMPUniRule annotation
    Metal bindingi488 – 4881Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation
    Metal bindingi489 – 4891Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation
    Metal bindingi490 – 4901Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi264 – 2663NADUniRule annotation
    Nucleotide bindingi314 – 3163NADUniRule annotation

    GO - Molecular functioni

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    GMP biosynthesis, Purine biosynthesis

    Keywords - Ligandi

    Metal-binding, NAD, Potassium

    Enzyme and pathway databases

    UniPathwayiUPA00601; UER00295.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Inosine-5'-monophosphate dehydrogenaseUniRule annotation (EC:1.1.1.205UniRule annotation)
    Short name:
    IMP dehydrogenaseUniRule annotation
    Short name:
    IMPDUniRule annotation
    Short name:
    IMPDHUniRule annotation
    Gene namesi
    Name:impdh
    OrganismiVigna unguiculata (Cowpea)
    Taxonomic identifieri3917 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsFabalesFabaceaePapilionoideaePhaseoleaeVigna

    Subcellular locationi

    • Cytoplasm UniRule annotation

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 502502Inosine-5'-monophosphate dehydrogenasePRO_0000415681Add
    BLAST

    Interactioni

    Subunit structurei

    Homotetramer.UniRule annotation1 Publication

    Structurei

    3D structure databases

    ProteinModelPortaliQ84XA3.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini168 – 22457CBSUniRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni354 – 3563IMP bindingUniRule annotation
    Regioni377 – 3782IMP bindingUniRule annotation
    Regioni401 – 4055IMP bindingUniRule annotation

    Sequence similaritiesi

    Belongs to the IMPDH/GMPR family.UniRule annotation
    Contains 1 CBS domain.UniRule annotation

    Keywords - Domaini

    CBS domain

    Family and domain databases

    Gene3Di3.20.20.70. 1 hit.
    HAMAPiMF_01964. IMPDH.
    InterProiIPR013785. Aldolase_TIM.
    IPR005990. IMP_DH.
    IPR015875. IMP_DH/GMP_Rdtase_CS.
    IPR001093. IMP_DH_GMPRt.
    [Graphical view]
    PANTHERiPTHR11911:SF6. PTHR11911:SF6. 1 hit.
    PfamiPF00478. IMPDH. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000130. IMPDH. 1 hit.
    TIGRFAMsiTIGR01302. IMP_dehydrog. 1 hit.
    PROSITEiPS00487. IMP_DH_GMP_RED. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q84XA3-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MDFTPPPIED GFTAEKLFSQ GFSYTYDDVI FLPHYIDFAA DAVDLSTRLT
    60 70 80 90 100
    RRLPLAVPLV ASPMDTVSES AMASAMASLG GIAIVHSNVP AAAQASLVRA
    110 120 130 140 150
    AKSRRVPILS EPAFAAPSAV IEHEDDFAAS PFLLVTDIGA AGGKLLGYVA
    160 170 180 190 200
    KRDWTNQKDK SLRVGDYMAP PPRRAPWNAD LNKIHEIMEN EKSGAVALER
    210 220 230 240 250
    DGEVVDLVVR EEVERVKGYP KLAAPATVGP DGEFMVGAAM GTREDDKERL
    260 270 280 290 300
    KHLVKAGVNV VVLDSSQGNS IYQLEMVKYV KSVYPELDVI GGNVVTMYQA
    310 320 330 340 350
    ENLIQAGVDG LRVGMGSGSI CTTQEVCAVG RGQATAVYKV SSIAYKSGVP
    360 370 380 390 400
    VIADGGISNS GHIVKALSLG ASTAMMGSFL AGSHEAPGAY VYQNGQRVKK
    410 420 430 440 450
    YRGMGSLEAM TKGSDARYLG DTAKLKIAQG VVGAVKDKGS VLNFIPYTLQ
    460 470 480 490 500
    AVRQGFQDIG ASSLQSAHDL LRSRVLRLEV RTGAAQVEGG VHGLVSYEKK

    YY
    Length:502
    Mass (Da):53,450
    Last modified:June 1, 2003 - v1
    Checksum:i61773EBE986FFD30
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AY193837 mRNA. Translation: AAO40253.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AY193837 mRNA. Translation: AAO40253.1.

    3D structure databases

    ProteinModelPortaliQ84XA3.
    ModBaseiSearch...
    MobiDBiSearch...

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Enzyme and pathway databases

    UniPathwayiUPA00601; UER00295.

    Family and domain databases

    Gene3Di3.20.20.70. 1 hit.
    HAMAPiMF_01964. IMPDH.
    InterProiIPR013785. Aldolase_TIM.
    IPR005990. IMP_DH.
    IPR015875. IMP_DH/GMP_Rdtase_CS.
    IPR001093. IMP_DH_GMPRt.
    [Graphical view]
    PANTHERiPTHR11911:SF6. PTHR11911:SF6. 1 hit.
    PfamiPF00478. IMPDH. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000130. IMPDH. 1 hit.
    TIGRFAMsiTIGR01302. IMP_dehydrog. 1 hit.
    PROSITEiPS00487. IMP_DH_GMP_RED. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    1. "Vuimpdh mRNA from cowpea encoding inosine monophosphate dehydrogenase."
      Mann A.J., Smith P.M.C., Bussell J.D.
      Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Root nodule.
    2. "Purification and properties of inosine monophosphate oxidoreductase from nitrogen-fixing nodules of cowpea (Vigna unguiculata L. Walp)."
      Atkins C.A., Shelp B.J., Storer P.J.
      Arch. Biochem. Biophys. 236:807-814(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.

    Entry informationi

    Entry nameiIMDH_VIGUN
    AccessioniPrimary (citable) accession number: Q84XA3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 22, 2012
    Last sequence update: June 1, 2003
    Last modified: January 7, 2015
    This is version 69 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    Miscellaneousi

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3

    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 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.