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P50094

- IMDH4_YEAST

UniProt

P50094 - IMDH4_YEAST

Protein

Inosine-5'-monophosphate dehydrogenase 4

Gene

IMD4

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 134 (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.2 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

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi331 – 3311Potassium; via carbonyl oxygenUniRule annotation
    Metal bindingi333 – 3331Potassium; via carbonyl oxygenUniRule annotation
    Binding sitei334 – 3341IMPUniRule annotation
    Active sitei336 – 3361Thioimidate intermediateUniRule annotation
    Metal bindingi336 – 3361Potassium; via carbonyl oxygenUniRule annotation
    Binding sitei450 – 4501IMPUniRule annotation
    Metal bindingi509 – 5091Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation
    Metal bindingi510 – 5101Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation
    Metal bindingi511 – 5111Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi279 – 2813NADUniRule annotation
    Nucleotide bindingi329 – 3313NADUniRule 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

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    GMP biosynthesis, Purine biosynthesis

    Keywords - Ligandi

    Metal-binding, NAD, Potassium

    Enzyme and pathway databases

    BioCyciYEAST:YML056C-MONOMER.
    UniPathwayiUPA00601; UER00295.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Inosine-5'-monophosphate dehydrogenase 4UniRule annotation (EC:1.1.1.205UniRule annotation)
    Short name:
    IMP dehydrogenase 4UniRule annotation
    Short name:
    IMPD 4UniRule annotation
    Short name:
    IMPDH 4UniRule annotation
    Gene namesi
    Name:IMD4UniRule annotation
    Ordered Locus Names:YML056C
    ORF Names:YM9958.06C
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome XIII

    Organism-specific databases

    CYGDiYML056c.
    SGDiS000004520. IMD4.

    Subcellular locationi

    Cytoplasm 1 PublicationUniRule annotation

    GO - Cellular componenti

    1. cytoplasm Source: SGD

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 524524Inosine-5'-monophosphate dehydrogenase 4PRO_0000093684Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei125 – 1251Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP50094.
    PaxDbiP50094.
    PeptideAtlasiP50094.

    Expressioni

    Gene expression databases

    GenevestigatoriP50094.

    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
    IMD3P500956EBI-9195,EBI-9190

    Protein-protein interaction databases

    BioGridi35111. 85 interactions.
    DIPiDIP-6458N.
    IntActiP50094. 60 interactions.
    MINTiMINT-675699.
    STRINGi4932.YML056C.

    Structurei

    3D structure databases

    ProteinModelPortaliP50094.
    SMRiP50094. Positions 2-523.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini122 – 18362CBS 1UniRule annotationAdd
    BLAST
    Domaini185 – 24157CBS 2UniRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni369 – 3713IMP bindingUniRule annotation
    Regioni392 – 3932IMP bindingUniRule annotation
    Regioni416 – 4205IMP 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.
    OMAiYLIFLET.
    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.

    P50094-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSAAPLDYKK ALEHLKTYSS KDGLSVQELM DSTTRGGLTY NDFLVLPGLV    50
    NFPSSAVSLQ TKLTKKITLN TPFVSSPMDT VTEADMAIYM ALLGGIGFIH 100
    HNCTPKEQAS MVKKVKMFEN GFINSPIVIS PTTTVGEVKV MKRKFGFSGF 150
    PVTEDGKCPG KLVGLVTSRD IQFLEDDSLV VSEVMTKNPV TGIKGITLKE 200
    GNEILKQTKK GKLLIVDDNG NLVSMLSRAD LMKNQNYPLA SKSATTKQLL 250
    CGAAIGTIEA DKERLRLLVE AGLDVVILDS SQGNSVFQLN MIKWIKETFP 300
    DLEIIAGNVA TREQAANLIA AGADGLRIGM GSGSICITQE VMACGRPQGT 350
    AVYNVCQFAN QFGVPCMADG GVQNIGHITK ALALGSSTVM MGGMLAGTTE 400
    SPGEYFYKDG KRLKAYRGMG SIDAMQKTGN KGNASTSRYF SESDSVLVAQ 450
    GVSGAVVDKG SIKKFIPYLY NGLQHSCQDI GCESLTSLKE NVQNGEVRFE 500
    FRTASAQLEG GVHNLHSYEK RLYN 524
    Length:524
    Mass (Da):56,394
    Last modified:October 1, 1996 - v1
    Checksum:iA73D1E4EFE8AEAD9
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z46729 Genomic DNA. Translation: CAA86719.1.
    AY899250 mRNA. Translation: AAX83935.1.
    BK006946 Genomic DNA. Translation: DAA09842.1.
    PIRiS50890.
    RefSeqiNP_013656.1. NM_001182414.1.

    Genome annotation databases

    EnsemblFungiiYML056C; YML056C; YML056C.
    GeneIDi854948.
    KEGGisce:YML056C.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z46729 Genomic DNA. Translation: CAA86719.1 .
    AY899250 mRNA. Translation: AAX83935.1 .
    BK006946 Genomic DNA. Translation: DAA09842.1 .
    PIRi S50890.
    RefSeqi NP_013656.1. NM_001182414.1.

    3D structure databases

    ProteinModelPortali P50094.
    SMRi P50094. Positions 2-523.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 35111. 85 interactions.
    DIPi DIP-6458N.
    IntActi P50094. 60 interactions.
    MINTi MINT-675699.
    STRINGi 4932.YML056C.

    Proteomic databases

    MaxQBi P50094.
    PaxDbi P50094.
    PeptideAtlasi P50094.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YML056C ; YML056C ; YML056C .
    GeneIDi 854948.
    KEGGi sce:YML056C.

    Organism-specific databases

    CYGDi YML056c.
    SGDi S000004520. IMD4.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00601 ; UER00295 .
    BioCyci YEAST:YML056C-MONOMER.

    Miscellaneous databases

    NextBioi 978010.

    Gene expression databases

    Genevestigatori P50094.

    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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    2. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    3. "Mapping of transcription start sites in Saccharomyces cerevisiae using 5' SAGE."
      Zhang Z., Dietrich F.S.
      Nucleic Acids Res. 33:2838-2851(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-83.
      Strain: ATCC 208353 / W303-1A.
    4. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    5. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    6. "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.
    7. "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.
    8. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
      Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
      Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-125, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiIMDH4_YEAST
    AccessioniPrimary (citable) accession number: P50094
    Secondary accession number(s): D6VZB8, Q2VQW8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: October 1, 1996
    Last modified: October 1, 2014
    This is version 134 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 2970 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 XIII
      Yeast (Saccharomyces cerevisiae) chromosome XIII: entries and gene names

    External Data

    Dasty 3