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Q84XA3

- IMDH_VIGUN

UniProt

Q84XA3 - IMDH_VIGUN

Protein

Inosine-5'-monophosphate dehydrogenase

Gene

impdh

Organism
Vigna unguiculata (Cowpea)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 66 (01 Oct 2014)
      Sequence version 1 (01 Jun 2003)
      Previous versions | rss
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    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.1 PublicationUniRule annotation

    Catalytic activityi

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

    Cofactori

    Potassium.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

    Pathwayi

    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

    1. IMP dehydrogenase activity Source: UniProtKB-HAMAP
    2. metal ion binding Source: UniProtKB-HAMAP
    3. nucleotide binding Source: UniProtKB-HAMAP

    GO - Biological processi

    1. GMP biosynthetic process Source: UniProtKB-HAMAP

    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

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

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

    Proteomic databases

    ProMEXiQ84XA3.

    Interactioni

    Subunit structurei

    Homotetramer.1 PublicationUniRule annotation

    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

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    MDFTPPPIED GFTAEKLFSQ GFSYTYDDVI FLPHYIDFAA DAVDLSTRLT    50
    RRLPLAVPLV ASPMDTVSES AMASAMASLG GIAIVHSNVP AAAQASLVRA 100
    AKSRRVPILS EPAFAAPSAV IEHEDDFAAS PFLLVTDIGA AGGKLLGYVA 150
    KRDWTNQKDK SLRVGDYMAP PPRRAPWNAD LNKIHEIMEN EKSGAVALER 200
    DGEVVDLVVR EEVERVKGYP KLAAPATVGP DGEFMVGAAM GTREDDKERL 250
    KHLVKAGVNV VVLDSSQGNS IYQLEMVKYV KSVYPELDVI GGNVVTMYQA 300
    ENLIQAGVDG LRVGMGSGSI CTTQEVCAVG RGQATAVYKV SSIAYKSGVP 350
    VIADGGISNS GHIVKALSLG ASTAMMGSFL AGSHEAPGAY VYQNGQRVKK 400
    YRGMGSLEAM TKGSDARYLG DTAKLKIAQG VVGAVKDKGS VLNFIPYTLQ 450
    AVRQGFQDIG ASSLQSAHDL LRSRVLRLEV RTGAAQVEGG VHGLVSYEKK 500
    YY 502
    Length:502
    Mass (Da):53,450
    Last modified:June 1, 2003 - v1
    Checksum:i61773EBE986FFD30
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY193837 mRNA. Translation: AAO40253.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY193837 mRNA. Translation: AAO40253.1 .

    3D structure databases

    ProteinModelPortali Q84XA3.
    ModBasei Search...
    MobiDBi Search...

    Proteomic databases

    ProMEXi Q84XA3.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    UniPathwayi UPA00601 ; UER00295 .

    Family and domain databases

    Gene3Di 3.20.20.70. 1 hit.
    HAMAPi MF_01964. IMPDH.
    InterProi IPR013785. Aldolase_TIM.
    IPR005990. IMP_DH.
    IPR015875. IMP_DH/GMP_Rdtase_CS.
    IPR001093. IMP_DH_GMPRt.
    [Graphical view ]
    PANTHERi PTHR11911:SF6. PTHR11911:SF6. 1 hit.
    Pfami PF00478. IMPDH. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000130. IMPDH. 1 hit.
    TIGRFAMsi TIGR01302. IMP_dehydrog. 1 hit.
    PROSITEi PS00487. IMP_DH_GMP_RED. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    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: October 1, 2014
    This is version 66 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