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P50095

- IMDH3_YEAST

UniProt

P50095 - IMDH3_YEAST

Protein

Inosine-5'-monophosphate dehydrogenase 3

Gene

IMD3

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 139 (01 Oct 2014)
      Sequence version 1 (01 Oct 1996)
      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.3 PublicationsUniRule 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=100 µM for Inosine 5'-phosphate1 Publication
    2. KM=314 µM for NAD+1 Publication

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi330 – 3301Potassium; via carbonyl oxygenUniRule annotation
    Metal bindingi332 – 3321Potassium; via carbonyl oxygenUniRule annotation
    Binding sitei333 – 3331IMPUniRule annotation
    Active sitei335 – 3351Thioimidate intermediateUniRule annotation
    Metal bindingi335 – 3351Potassium; via carbonyl oxygenUniRule annotation
    Binding sitei449 – 4491IMPUniRule annotation
    Metal bindingi508 – 5081Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation
    Metal bindingi509 – 5091Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation
    Metal bindingi510 – 5101Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi278 – 2803NADUniRule annotation
    Nucleotide bindingi328 – 3303NADUniRule annotation

    GO - Molecular functioni

    1. adenyl nucleotide binding Source: InterPro
    2. IMP dehydrogenase activity Source: SGD
    3. metal ion binding Source: UniProtKB-HAMAP
    4. protein binding Source: IntAct

    GO - Biological processi

    1. GMP biosynthetic process Source: UniProtKB-HAMAP
    2. GTP biosynthetic process Source: SGD

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    GMP biosynthesis, Purine biosynthesis

    Keywords - Ligandi

    Metal-binding, NAD, Potassium

    Enzyme and pathway databases

    BioCyciYEAST:YLR432W-MONOMER.
    SABIO-RKP50095.
    UniPathwayiUPA00601; UER00295.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Inosine-5'-monophosphate dehydrogenase 3UniRule annotation (EC:1.1.1.205UniRule annotation)
    Short name:
    IMP dehydrogenase 3UniRule annotation
    Short name:
    IMPD 3UniRule annotation
    Short name:
    IMPDH 3UniRule annotation
    Gene namesi
    Name:IMD3UniRule annotation
    Ordered Locus Names:YLR432W
    ORF Names:L9753.4
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome XII

    Organism-specific databases

    CYGDiYLR432w.
    SGDiS000004424. IMD3.

    Subcellular locationi

    Cytoplasm 1 PublicationUniRule annotation

    GO - Cellular componenti

    1. cytoplasm Source: SGD

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi253 – 2531A → S: Increases drug-resistance to MPA. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 523523Inosine-5'-monophosphate dehydrogenase 3PRO_0000093683Add
    BLAST

    Proteomic databases

    MaxQBiP50095.
    PaxDbiP50095.
    PeptideAtlasiP50095.

    Expressioni

    Gene expression databases

    GenevestigatoriP50095.

    Interactioni

    Subunit structurei

    Homotetramer. Seems to be able to form heterotetramers composed from more than 1 of the 3 IMPDH gene products (IMD2-4).1 PublicationUniRule annotation

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    IMD4P500946EBI-9190,EBI-9195

    Protein-protein interaction databases

    BioGridi31691. 127 interactions.
    DIPiDIP-1947N.
    IntActiP50095. 191 interactions.
    MINTiMINT-385605.
    STRINGi4932.YLR432W.

    Structurei

    3D structure databases

    ProteinModelPortaliP50095.
    SMRiP50095. Positions 3-521.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini121 – 18363CBS 1UniRule annotationAdd
    BLAST
    Domaini184 – 24057CBS 2UniRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni368 – 3703IMP bindingUniRule annotation
    Regioni391 – 3922IMP bindingUniRule annotation
    Regioni415 – 4195IMP bindingUniRule annotation

    Sequence similaritiesi

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

    Keywords - Domaini

    CBS domain, Repeat

    Phylogenomic databases

    eggNOGiCOG0517.
    GeneTreeiENSGT00530000062923.
    HOGENOMiHOG000165752.
    KOiK00088.
    OMAiSEMAIFM.
    OrthoDBiEOG793BHK.

    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.

    P50095-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAAVRDYKTA LEFAKSLPRL DGLSVQELMD SKTRGGLTYN DFLVLPGLVD    50
    FPSSEVSLQT KLTRNITLNT PFVSSPMDTV TESEMAIFMA LLGGIGFIHH 100
    NCTPEDQADM VRRVKNYENG FINNPIVISP TTTVGEAKSM KERFGFSGFP 150
    VTEDGKRNGK LMGIVTSRDI QFVEDNSLLV QDVMTKNPVT GAQGITLSEG 200
    NEILKKIKKG KLLIVDDNGN LVSMLSRTDL MKNQNYPLAS KSATTKQLLC 250
    GAAIGTIDAD KERLRLLVEA GLDVVILDSS QGNSIFQLNM IKWIKETFPD 300
    LEIIAGNVAT REQAANLIAA GADGLRIGMG SGSICITQEV MACGRPQGTA 350
    VYNVCEFANQ FGIPCMADGG VQNIGHITKA LALGSSTVMM GGMLAGTTES 400
    PGEYFYQDGK RLKAYRGMGS IDAMQKTGTK GNASTSRYFS ESDSVLVAQG 450
    VSGAVVDKGS IKKFIPYLYN GLQHSCQDIG YKSLTLLKEN VQSGKVRFEF 500
    RTASAQLEGG VHNLHSYEKR LHN 523
    Length:523
    Mass (Da):56,585
    Last modified:October 1, 1996 - v1
    Checksum:iA0C84C22527AAEA6
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U21094 Genomic DNA. Translation: AAB67516.1.
    BK006945 Genomic DNA. Translation: DAA09733.1.
    PIRiS59402.
    RefSeqiNP_013536.3. NM_001182320.3.

    Genome annotation databases

    EnsemblFungiiYLR432W; YLR432W; YLR432W.
    GeneIDi851152.
    KEGGisce:YLR432W.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U21094 Genomic DNA. Translation: AAB67516.1 .
    BK006945 Genomic DNA. Translation: DAA09733.1 .
    PIRi S59402.
    RefSeqi NP_013536.3. NM_001182320.3.

    3D structure databases

    ProteinModelPortali P50095.
    SMRi P50095. Positions 3-521.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 31691. 127 interactions.
    DIPi DIP-1947N.
    IntActi P50095. 191 interactions.
    MINTi MINT-385605.
    STRINGi 4932.YLR432W.

    Proteomic databases

    MaxQBi P50095.
    PaxDbi P50095.
    PeptideAtlasi P50095.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YLR432W ; YLR432W ; YLR432W .
    GeneIDi 851152.
    KEGGi sce:YLR432W.

    Organism-specific databases

    CYGDi YLR432w.
    SGDi S000004424. IMD3.

    Phylogenomic databases

    eggNOGi COG0517.
    GeneTreei ENSGT00530000062923.
    HOGENOMi HOG000165752.
    KOi K00088.
    OMAi SEMAIFM.
    OrthoDBi EOG793BHK.

    Enzyme and pathway databases

    UniPathwayi UPA00601 ; UER00295 .
    BioCyci YEAST:YLR432W-MONOMER.
    SABIO-RK P50095.

    Miscellaneous databases

    NextBioi 967930.

    Gene expression databases

    Genevestigatori P50095.

    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. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII."
      Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W., Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A., Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K., Heuss-Neitzel D., Hilbert H.
      , Hilger F., Kleine K., Koetter P., Louis E.J., Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S., Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D., Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M., Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P., Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M., Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K., Zollner A., Hani J., Hoheisel J.D.
      Nature 387:87-90(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    2. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    3. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    4. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    5. "Functional distinctions between IMP dehydrogenase genes in providing mycophenolate resistance and guanine prototrophy to yeast."
      Hyle J.W., Shaw R.J., Reines D.
      J. Biol. Chem. 278:28470-28478(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    6. "Detection of the mycophenolate-inhibited form of IMP dehydrogenase in vivo."
      McPhillips C.C., Hyle J.W., Reines D.
      Proc. Natl. Acad. Sci. U.S.A. 101:12171-12176(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES.
    7. "Dissection of the molecular basis of mycophenolate resistance in Saccharomyces cerevisiae."
      Jenks M.H., Reines D.
      Yeast 22:1181-1190(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF ALA-253.

    Entry informationi

    Entry nameiIMDH3_YEAST
    AccessioniPrimary (citable) accession number: P50095
    Secondary accession number(s): D6VZ67
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: October 1, 1996
    Last modified: October 1, 2014
    This is version 139 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Present with 26300 molecules/cell in log phase SD medium.1 Publication

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families
    3. Yeast
      Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
    4. Yeast chromosome XII
      Yeast (Saccharomyces cerevisiae) chromosome XII: entries and gene names

    External Data

    Dasty 3