Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Inosine-5'-monophosphate dehydrogenase

Gene
N/A
Organism
Leishmania donovani
Status
Reviewed-Annotation score: -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. Potently inhibited by MPA. Inhibited by XMP and GMP.UniRule annotation1 Publication

Kineticsi

  1. KM=33 µM for Inosine 5'-phosphate1 Publication
  2. KM=390 µM for NAD+1 Publication

    Pathwayi: 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
    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)DescriptionActionsGraphical viewLength
    Metal bindingi322Potassium; via carbonyl oxygenUniRule annotation1
    Metal bindingi324Potassium; via carbonyl oxygenUniRule annotation1
    Binding sitei325IMPUniRule annotation1
    Active sitei327Thioimidate intermediateUniRule annotation1
    Metal bindingi327Potassium; via carbonyl oxygenUniRule annotation1
    Active sitei425Proton acceptorUniRule annotation1
    Binding sitei437IMPUniRule annotation1
    Metal bindingi496Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation1
    Metal bindingi497Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation1
    Metal bindingi498Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Nucleotide bindingi270 – 272NADUniRule annotation3
    Nucleotide bindingi320 – 322NADUniRule annotation3

    GO - Molecular functioni

    GO - Biological processi

    Keywordsi

    Molecular functionOxidoreductase
    Biological processGMP biosynthesis, Purine biosynthesis
    LigandMetal-binding, NAD, Potassium

    Enzyme and pathway databases

    BRENDAi1.1.1.205 2947
    SABIO-RKP21620
    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
    OrganismiLeishmania donovani
    Taxonomic identifieri5661 [NCBI]
    Taxonomic lineageiEukaryotaEuglenozoaKinetoplastidaTrypanosomatidaeLeishmaniinaeLeishmania

    Subcellular locationi

    • Glycosome UniRule annotation1 Publication

    GO - Cellular componenti

    Keywords - Cellular componenti

    Glycosome, Peroxisome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00000936751 – 514Inosine-5'-monophosphate dehydrogenaseAdd BLAST514

    Proteomic databases

    PRIDEiP21620

    Interactioni

    Subunit structurei

    Heterotetramer. Interacts with glycosomal protein sorting receptor PEX5.1 Publication

    Structurei

    3D structure databases

    ProteinModelPortaliP21620
    SMRiP21620
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Domaini112 – 171CBS 1UniRule annotationAdd BLAST60
    Domaini175 – 233CBS 2UniRule annotationAdd BLAST59

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni360 – 362IMP bindingUniRule annotation3
    Regioni383 – 384IMP bindingUniRule annotation2
    Regioni407 – 411IMP bindingUniRule annotation5

    Motif

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Motifi512 – 514Microbody targeting signalUniRule annotation3

    Sequence similaritiesi

    Belongs to the IMPDH/GMPR family.UniRule annotation

    Keywords - Domaini

    CBS domain, Repeat

    Phylogenomic databases

    eggNOGiKOG2550 Eukaryota
    COG0516 LUCA
    COG0517 LUCA
    KOiK00088

    Family and domain databases

    CDDicd00381 IMPDH, 1 hit
    HAMAPiMF_01964 IMPDH, 1 hit
    InterProiView protein in InterPro
    IPR000644 CBS_dom
    IPR005990 IMP_DH
    IPR015875 IMP_DH/GMP_Rdtase_CS
    IPR001093 IMP_DH_GMPRt
    PfamiView protein in Pfam
    PF00571 CBS, 2 hits
    PF00478 IMPDH, 1 hit
    PIRSFiPIRSF000130 IMPDH, 1 hit
    SMARTiView protein in SMART
    SM00116 CBS, 2 hits
    TIGRFAMsiTIGR01302 IMP_dehydrog, 1 hit
    PROSITEiView protein in PROSITE
    PS51371 CBS, 2 hits
    PS00487 IMP_DH_GMP_RED, 1 hit

    Sequencei

    Sequence statusi: Complete.

    P21620-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MATNNANYRI KTIKDGCTAE ELFRGDGLTY NDFIILPGFI DFGAADVNIS
    60 70 80 90 100
    GQFTKRIRLH IPIVSSPMDT ITENEMAKTM ALMGGVGVLH NNCTVERQVE
    110 120 130 140 150
    MVKSVKAYRN GFISKPKSVP PNTPISNIIR IKEEKGISGI LVTENGDPHG
    160 170 180 190 200
    KLLGIVCTKD IDYVKNKDTP VSAVMTRREK MTVERAPIQL EEAMDVLNRS
    210 220 230 240 250
    RYGYLPIVNE NDEVVNLCSR RDAVRARDYP HSTLDKSGRL ICAAATSTRP
    260 270 280 290 300
    EDKRRVAALA DVGVDVLVLD SSQGNTIYQI AFIKWVKSTY PHLEVVAGNV
    310 320 330 340 350
    VTQDQAKNLI DAGADGIRIG MGSGSICITQ EVLACGRPQG TAVYKVAQYC
    360 370 380 390 400
    ASRGVPCTAD GGLRQVGDIC KALAIGANCA MLGGMLSGTT ETPGEYFFKG
    410 420 430 440 450
    GVRLKVYRGM GSLEAMSQGK ESGKRYLSEN EAVQVAQGVS GNVVDKGSAA
    460 470 480 490 500
    KLIAYVSKGL QQSAQDIGEI SFDAIREKMY AGQVLFSRRS PTAQGEGGVH
    510
    SLHSYEKKLF AAKM
    Length:514
    Mass (Da):55,552
    Last modified:May 1, 1991 - v1
    Checksum:iE251FCC1362D60E5
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    M55667 Genomic DNA Translation: AAA29253.1
    PIRiA38668
    RefSeqiXP_003860332.1, XM_003860284.1

    Genome annotation databases

    GeneIDi13386143
    KEGGildo:LDBPK_191590

    Similar proteinsi

    Entry informationi

    Entry nameiIMDH_LEIDO
    AccessioniPrimary (citable) accession number: P21620
    Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 1, 1991
    Last sequence update: May 1, 1991
    Last modified: May 23, 2018
    This is version 113 of the entry and version 1 of the sequence. See complete history.
    Entry statusiReviewed (UniProtKB/Swiss-Prot)

    Cookie policy

    We would like to use anonymized google analytics cookies to gather statistics on how uniprot.org is used in aggregate. Learn more

    UniProt is an ELIXIR core data resource
    Main funding by: National Institutes of Health