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P21620

- IMDH_LEIDO

UniProt

P21620 - IMDH_LEIDO

Protein

Inosine-5'-monophosphate dehydrogenase

Gene
N/A
Organism
Leishmania donovani
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 96 (01 Oct 2014)
      Sequence version 1 (01 May 1991)
      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. Potently inhibited by MPA. Inhibited by XMP and GMP.1 PublicationUniRule annotation

    Kineticsi

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

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi322 – 3221Potassium; via carbonyl oxygenUniRule annotation
    Metal bindingi324 – 3241Potassium; via carbonyl oxygenUniRule annotation
    Binding sitei325 – 3251IMPUniRule annotation
    Active sitei327 – 3271Thioimidate intermediateUniRule annotation
    Metal bindingi327 – 3271Potassium; via carbonyl oxygenUniRule annotation
    Binding sitei437 – 4371IMPUniRule annotation
    Metal bindingi496 – 4961Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation
    Metal bindingi497 – 4971Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation
    Metal bindingi498 – 4981Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi270 – 2723NADUniRule annotation
    Nucleotide bindingi320 – 3223NADUniRule annotation

    GO - Molecular functioni

    1. adenyl nucleotide binding Source: InterPro
    2. IMP dehydrogenase activity Source: UniProtKB-HAMAP
    3. metal ion 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
    OrganismiLeishmania donovani
    Taxonomic identifieri5661 [NCBI]
    Taxonomic lineageiEukaryotaEuglenozoaKinetoplastidaTrypanosomatidaeLeishmaniinaeLeishmania

    Subcellular locationi

    Glycosome 1 PublicationUniRule annotation

    GO - Cellular componenti

    1. glycosome Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Glycosome, Peroxisome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 514514Inosine-5'-monophosphate dehydrogenasePRO_0000093675Add
    BLAST

    Interactioni

    Subunit structurei

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

    Structurei

    3D structure databases

    ProteinModelPortaliP21620.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini112 – 17160CBS 1UniRule annotationAdd
    BLAST
    Domaini175 – 23359CBS 2UniRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni360 – 3623IMP bindingUniRule annotation
    Regioni383 – 3842IMP bindingUniRule annotation
    Regioni407 – 4115IMP bindingUniRule annotation

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi512 – 5143Microbody targeting signalUniRule annotation

    Sequence similaritiesi

    Belongs to the IMPDH/GMPR family.UniRule annotation
    Contains 2 CBS domains.UniRule annotation

    Keywords - Domaini

    CBS domain, Repeat

    Phylogenomic databases

    KOiK00088.

    Family and domain databases

    Gene3Di3.20.20.70. 1 hit.
    HAMAPiMF_01964. IMPDH.
    InterProiIPR013785. Aldolase_TIM.
    IPR000644. CBS_dom.
    IPR005990. IMP_DH.
    IPR015875. IMP_DH/GMP_Rdtase_CS.
    IPR001093. IMP_DH_GMPRt.
    [Graphical view]
    PANTHERiPTHR11911:SF6. PTHR11911:SF6. 1 hit.
    PfamiPF00571. CBS. 2 hits.
    PF00478. IMPDH. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000130. IMPDH. 1 hit.
    SMARTiSM00116. CBS. 2 hits.
    [Graphical view]
    TIGRFAMsiTIGR01302. IMP_dehydrog. 1 hit.
    PROSITEiPS51371. CBS. 2 hits.
    PS00487. IMP_DH_GMP_RED. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P21620-1 [UniParc]FASTAAdd to Basket

    « Hide

    MATNNANYRI KTIKDGCTAE ELFRGDGLTY NDFIILPGFI DFGAADVNIS    50
    GQFTKRIRLH IPIVSSPMDT ITENEMAKTM ALMGGVGVLH NNCTVERQVE 100
    MVKSVKAYRN GFISKPKSVP PNTPISNIIR IKEEKGISGI LVTENGDPHG 150
    KLLGIVCTKD IDYVKNKDTP VSAVMTRREK MTVERAPIQL EEAMDVLNRS 200
    RYGYLPIVNE NDEVVNLCSR RDAVRARDYP HSTLDKSGRL ICAAATSTRP 250
    EDKRRVAALA DVGVDVLVLD SSQGNTIYQI AFIKWVKSTY PHLEVVAGNV 300
    VTQDQAKNLI DAGADGIRIG MGSGSICITQ EVLACGRPQG TAVYKVAQYC 350
    ASRGVPCTAD GGLRQVGDIC KALAIGANCA MLGGMLSGTT ETPGEYFFKG 400
    GVRLKVYRGM GSLEAMSQGK ESGKRYLSEN EAVQVAQGVS GNVVDKGSAA 450
    KLIAYVSKGL QQSAQDIGEI SFDAIREKMY AGQVLFSRRS PTAQGEGGVH 500
    SLHSYEKKLF AAKM 514
    Length:514
    Mass (Da):55,552
    Last modified:May 1, 1991 - v1
    Checksum:iE251FCC1362D60E5
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M55667 Genomic DNA. Translation: AAA29253.1.
    PIRiA38668.
    RefSeqiXP_003860332.1. XM_003860284.1.

    Genome annotation databases

    GeneIDi13386143.
    KEGGildo:LDBPK_191590.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M55667 Genomic DNA. Translation: AAA29253.1 .
    PIRi A38668.
    RefSeqi XP_003860332.1. XM_003860284.1.

    3D structure databases

    ProteinModelPortali P21620.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 13386143.
    KEGGi ldo:LDBPK_191590.

    Phylogenomic databases

    KOi K00088.

    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.
    IPR000644. CBS_dom.
    IPR005990. IMP_DH.
    IPR015875. IMP_DH/GMP_Rdtase_CS.
    IPR001093. IMP_DH_GMPRt.
    [Graphical view ]
    PANTHERi PTHR11911:SF6. PTHR11911:SF6. 1 hit.
    Pfami PF00571. CBS. 2 hits.
    PF00478. IMPDH. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000130. IMPDH. 1 hit.
    SMARTi SM00116. CBS. 2 hits.
    [Graphical view ]
    TIGRFAMsi TIGR01302. IMP_dehydrog. 1 hit.
    PROSITEi PS51371. CBS. 2 hits.
    PS00487. IMP_DH_GMP_RED. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Amplification and molecular cloning of the IMP dehydrogenase gene of Leishmania donovani."
      Wilson K.E., Collart F.R., Huberman E., Stringer J.R., Ullman B.
      J. Biol. Chem. 266:1665-1671(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Kinetic characterization of inosine monophosphate dehydrogenase of Leishmania donovani."
      Dobie F., Berg A., Boitz J.M., Jardim A.
      Mol. Biochem. Parasitol. 152:11-21(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, SUBCELLULAR LOCATION, INTERACTION WITH PEX5, SUBUNIT.

    Entry informationi

    Entry nameiIMDH_LEIDO
    AccessioniPrimary (citable) accession number: P21620
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 1, 1991
    Last sequence update: May 1, 1991
    Last modified: October 1, 2014
    This is version 96 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)

    Miscellaneousi

    Documents

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

    External Data

    Dasty 3