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P50098

- IMDH_TRYBB

UniProt

P50098 - IMDH_TRYBB

Protein

Inosine-5'-monophosphate dehydrogenase

Gene
N/A
Organism
Trypanosoma brucei brucei
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 88 (01 Oct 2014)
      Sequence version 1 (01 Oct 1996)
      Previous versions | rss
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    • Comment

    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 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

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi320 – 3201Potassium; via carbonyl oxygenUniRule annotation
    Metal bindingi322 – 3221Potassium; via carbonyl oxygenUniRule annotation
    Binding sitei323 – 3231IMPUniRule annotation
    Active sitei325 – 3251Thioimidate intermediateUniRule annotation
    Metal bindingi325 – 3251Potassium; via carbonyl oxygenUniRule annotation
    Binding sitei435 – 4351IMPUniRule annotation
    Metal bindingi494 – 4941Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation
    Metal bindingi495 – 4951Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi268 – 2703NADUniRule annotation
    Nucleotide bindingi318 – 3203NADUniRule 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
    OrganismiTrypanosoma brucei brucei
    Taxonomic identifieri5702 [NCBI]
    Taxonomic lineageiEukaryotaEuglenozoaKinetoplastidaTrypanosomatidaeTrypanosoma

    Subcellular locationi

    Glycosome UniRule 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 – 512512Inosine-5'-monophosphate dehydrogenasePRO_0000093677Add
    BLAST

    Interactioni

    Subunit structurei

    Homotetramer.UniRule annotation

    Structurei

    3D structure databases

    ProteinModelPortaliP50098.
    SMRiP50098. Positions 13-106.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini110 – 16960CBS 1UniRule annotationAdd
    BLAST
    Domaini173 – 23159CBS 2UniRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni358 – 3603IMP bindingUniRule annotation
    Regioni381 – 3822IMP bindingUniRule annotation
    Regioni405 – 4095IMP bindingUniRule annotation

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi510 – 5123Microbody targeting signalUniRule annotation

    Sequence similaritiesi

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

    Keywords - Domaini

    CBS domain, Repeat

    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.

    P50098-1 [UniParc]FASTAAdd to Basket

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    MENTNLRTKT LRDGTTAEEL FSQDGLSFND FIILPGFIDF DSSKVNVSGQ    50
    FTKNILLHLP LVSSPMDTVT ESSMARAMAL MGGIGVIHNN CTVEQQARMV 100
    RSVKLYRNGF IMKPKSVSPD VPVSTIRNIK SEKGISGILV TEGGKYDGKL 150
    LGIVCTKDID FVKDASAPVS QYMTRRENMT VERYPIKLEE AMDVLNRSRH 200
    GYLPVLNDKD EVVCLCSRRD AVRARDYPNS SLDRNGHLLC AAATSTREAD 250
    KGRVAALSEA GIDVLVLDSS QGNTIYQVSF IRWVKKTYPH LEVVAGNVVT 300
    QDQAKNLIDA GADSLRIGMG SGSICITQEV LACGRPQATA IYKVARYAAS 350
    RGVPCVADGG LRNVGDVCKA LAVGANVAML GSMIAGTSET PGEYFFKDGM 400
    RLKGYRGMGS IDAMLQGRES GKRYLSENET LQVAQGVAGA VLDKGSVLKL 450
    LAYIHKGLQQ SAQDIGEVSF DAIREKVYEG QVLFNRRTLT AQSEGAVHSL 500
    HHYERKLFAS KL 512
    Length:512
    Mass (Da):55,709
    Last modified:October 1, 1996 - v1
    Checksum:i1A86C46AE6445045
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M97794 Genomic DNA. Translation: AAB46420.1.
    PIRiA55407.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M97794 Genomic DNA. Translation: AAB46420.1 .
    PIRi A55407.

    3D structure databases

    ProteinModelPortali P50098.
    SMRi P50098. Positions 13-106.
    ModBasei Search...
    MobiDBi Search...

    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.
    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 of the inosinate dehydrogenase gene in Trypanosoma brucei gambiense due to an increase in chromosome copy number."
      Wilson K., Berens R.L., Sifri C.D., Ullman B.
      J. Biol. Chem. 269:28979-28987(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: Eatro 164 / ISTat 1.7.

    Entry informationi

    Entry nameiIMDH_TRYBB
    AccessioniPrimary (citable) accession number: P50098
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: October 1, 1996
    Last modified: October 1, 2014
    This is version 88 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