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P0ADG7

- IMDH_ECOLI

UniProt

P0ADG7 - IMDH_ECOLI

Protein

Inosine-5'-monophosphate dehydrogenase

Gene

guaB

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 85 (01 Oct 2014)
      Sequence version 1 (06 Dec 2005)
      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. IMP dehydrogenase subunit of E.coli contains a cysteine at the IMP binding site and is inhibited in a simple competitive manner by GMP. It does not exhibit allosteric properties as does IMP dehydrogenase from B.subtilis or S.typhimurium.1 PublicationUniRule annotation

    Kineticsi

    1. KM=61 µM for Inosine 5'-phosphate1 Publication
    2. KM=2000 µM for NAD+1 Publication
    3. KM=2.8 mM for K+1 Publication

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei248 – 2481NADUniRule annotation
    Metal bindingi300 – 3001Potassium; via carbonyl oxygenUniRule annotation
    Metal bindingi302 – 3021Potassium; via carbonyl oxygenUniRule annotation
    Binding sitei303 – 3031IMPUniRule annotation
    Active sitei305 – 3051Thioimidate intermediateUniRule annotation
    Metal bindingi305 – 3051Potassium; via carbonyl oxygenUniRule annotation
    Binding sitei415 – 4151IMPUniRule annotation
    Metal bindingi469 – 4691Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation
    Metal bindingi470 – 4701Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation
    Metal bindingi471 – 4711Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi248 – 2503NADUniRule annotation
    Nucleotide bindingi298 – 3003NADUniRule annotation

    GO - Molecular functioni

    1. adenyl nucleotide binding Source: InterPro
    2. identical protein binding Source: EcoCyc
    3. IMP dehydrogenase activity Source: EcoCyc
    4. 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

    BioCyciEcoCyc:IMP-DEHYDROG-MONOMER.
    ECOL316407:JW5401-MONOMER.
    MetaCyc:IMP-DEHYDROG-MONOMER.
    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
    Gene namesi
    Name:guaBUniRule annotation
    Synonyms:guaR
    Ordered Locus Names:b2508, JW5401
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG10421. guaB.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: UniProtKB

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi13 – 131D → A: Causes a 38-fold increase in the value of Km for K(+). No change is observed in the value of Km for IMP. 1 Publication
    Mutagenesisi50 – 501D → A: Causes a 17-fold increase in the value of Km for K(+). 1 Publication
    Mutagenesisi54 – 541E → A: No effect. 1 Publication
    Mutagenesisi138 – 1381D → A: No effect. 1 Publication
    Mutagenesisi200 – 2001D → A: No effect. 1 Publication
    Mutagenesisi243 – 2431D → A: No effect. 1 Publication
    Mutagenesisi248 – 2481D → A: Causes a 130-fold decrease in the value of kcat. 1 Publication
    Mutagenesisi338 – 3381D → A: Decreases the value of kcat by 600-fold. Increases the value of Km for IMP by 12-fold. 1 Publication
    Mutagenesisi369 – 3691E → A: No effect. 1 Publication
    Mutagenesisi373 – 3731E → A: No effect. 1 Publication
    Mutagenesisi469 – 4691E → A: Increases the value of Km for K(+) by 17-fold. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 488488Inosine-5'-monophosphate dehydrogenasePRO_0000093695Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei267 – 2671N6-acetyllysine1 Publication
    Modified residuei428 – 4281N6-acetyllysine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    PaxDbiP0ADG7.
    PRIDEiP0ADG7.

    2D gel databases

    SWISS-2DPAGEP0ADG7.

    Expressioni

    Gene expression databases

    GenevestigatoriP0ADG7.

    Interactioni

    Subunit structurei

    Homotetramer.1 PublicationUniRule annotation

    Protein-protein interaction databases

    BioGridi851324. 1 interaction.
    DIPiDIP-36207N.
    IntActiP0ADG7. 1 interaction.
    MINTiMINT-1235980.
    STRINGi511145.b2508.

    Structurei

    3D structure databases

    ProteinModelPortaliP0ADG7.
    SMRiP0ADG7. Positions 1-487.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini93 – 14957CBS 1UniRule annotationAdd
    BLAST
    Domaini153 – 21462CBS 2UniRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni338 – 3403IMP bindingUniRule annotation
    Regioni361 – 3622IMP bindingUniRule annotation
    Regioni385 – 3895IMP bindingUniRule annotation

    Domaini

    The CBS domain of IMPDH is a negative trans-regulator of adenylate nucleotide synthesis, and this role is independent of the catalytic function of IMPDH in the de novo GMP biosynthesis. Deletion of the CBS domain derepresses the synthesis of AMP from IMP.2 Publications

    Sequence similaritiesi

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

    Keywords - Domaini

    CBS domain, Repeat

    Phylogenomic databases

    eggNOGiCOG0517.
    HOGENOMiHOG000165755.
    KOiK00088.
    OMAiHGHSKNI.
    OrthoDBiEOG6GTZPV.
    PhylomeDBiP0ADG7.

    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]
    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.

    P0ADG7-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLRIAKEALT FDDVLLVPAH STVLPNTADL STQLTKTIRL NIPMLSAAMD    50
    TVTEARLAIA LAQEGGIGFI HKNMSIERQA EEVRRVKKHE SGVVTDPQTV 100
    LPTTTLREVK ELTERNGFAG YPVVTEENEL VGIITGRDVR FVTDLNQPVS 150
    VYMTPKERLV TVREGEAREV VLAKMHEKRV EKALVVDDEF HLIGMITVKD 200
    FQKAERKPNA CKDEQGRLRV GAAVGAGAGN EERVDALVAA GVDVLLIDSS 250
    HGHSEGVLQR IRETRAKYPD LQIIGGNVAT AAGARALAEA GCSAVKVGIG 300
    PGSICTTRIV TGVGVPQITA VADAVEALEG TGIPVIADGG IRFSGDIAKA 350
    IAAGASAVMV GSMLAGTEES PGEIELYQGR SYKSYRGMGS LGAMSKGSSD 400
    RYFQSDNAAD KLVPEGIEGR VAYKGRLKEI IHQQMGGLRS CMGLTGCGTI 450
    DELRTKAEFV RISGAGIQES HVHDVTITKE SPNYRLGS 488
    Length:488
    Mass (Da):52,022
    Last modified:December 6, 2005 - v1
    Checksum:iB0FD0A786779C98E
    GO

    Sequence cautioni

    The sequence CAA26133.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti206 – 2061R → A in CAA26133. (PubMed:2860637)Curated
    Sequence conflicti206 – 2061R → A in AAB18618. (PubMed:2860637)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X02209 Genomic DNA. Translation: CAA26133.1. Different initiation.
    U00096 Genomic DNA. Translation: AAC75561.1.
    AP009048 Genomic DNA. Translation: BAA16395.2.
    M10101 Genomic DNA. Translation: AAB18618.1.
    PIRiC65027. DEECIP.
    RefSeqiNP_417003.1. NC_000913.3.
    YP_490736.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC75561; AAC75561; b2508.
    BAA16395; BAA16395; BAA16395.
    GeneIDi12934227.
    946985.
    KEGGiecj:Y75_p2461.
    eco:b2508.
    PATRICi32120407. VBIEscCol129921_2606.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X02209 Genomic DNA. Translation: CAA26133.1 . Different initiation.
    U00096 Genomic DNA. Translation: AAC75561.1 .
    AP009048 Genomic DNA. Translation: BAA16395.2 .
    M10101 Genomic DNA. Translation: AAB18618.1 .
    PIRi C65027. DEECIP.
    RefSeqi NP_417003.1. NC_000913.3.
    YP_490736.1. NC_007779.1.

    3D structure databases

    ProteinModelPortali P0ADG7.
    SMRi P0ADG7. Positions 1-487.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 851324. 1 interaction.
    DIPi DIP-36207N.
    IntActi P0ADG7. 1 interaction.
    MINTi MINT-1235980.
    STRINGi 511145.b2508.

    Chemistry

    BindingDBi P0ADG7.
    ChEMBLi CHEMBL3630.

    2D gel databases

    SWISS-2DPAGE P0ADG7.

    Proteomic databases

    PaxDbi P0ADG7.
    PRIDEi P0ADG7.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC75561 ; AAC75561 ; b2508 .
    BAA16395 ; BAA16395 ; BAA16395 .
    GeneIDi 12934227.
    946985.
    KEGGi ecj:Y75_p2461.
    eco:b2508.
    PATRICi 32120407. VBIEscCol129921_2606.

    Organism-specific databases

    EchoBASEi EB0416.
    EcoGenei EG10421. guaB.

    Phylogenomic databases

    eggNOGi COG0517.
    HOGENOMi HOG000165755.
    KOi K00088.
    OMAi HGHSKNI.
    OrthoDBi EOG6GTZPV.
    PhylomeDBi P0ADG7.

    Enzyme and pathway databases

    UniPathwayi UPA00601 ; UER00295 .
    BioCyci EcoCyc:IMP-DEHYDROG-MONOMER.
    ECOL316407:JW5401-MONOMER.
    MetaCyc:IMP-DEHYDROG-MONOMER.

    Miscellaneous databases

    PROi P0ADG7.

    Gene expression databases

    Genevestigatori P0ADG7.

    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 ]
    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. "Nucleotide sequence of the guaB locus encoding IMP dehydrogenase of Escherichia coli K12."
      Tiedeman A.A., Smith J.M.
      Nucleic Acids Res. 13:1303-1316(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: K12.
    2. "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12 genome corresponding to 50.0-68.8 min on the linkage map and analysis of its sequence features."
      Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T., Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K., Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T.
      , Oyama S., Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H., Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.
      DNA Res. 4:91-113(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    4. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
      Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
      Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    5. "Nucleotide sequence and organisation of the gua promoter region of Escherichia coli."
      Thomas M.S., Drabble W.T.
      Gene 36:45-53(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-96.
    6. "Regulation of the gua operon of Escherichia coli by the DnaA protein."
      Tesfa-Selase F., Drabble W.T.
      Mol. Gen. Genet. 231:256-264(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-90.
    7. "Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12."
      Link A.J., Robison K., Church G.M.
      Electrophoresis 18:1259-1313(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 1-12.
      Strain: K12 / EMG2.
    8. Frutiger S., Hughes G.J., Pasquali C., Hochstrasser D.F.
      Submitted (FEB-1996) to UniProtKB
      Cited for: PARTIAL PROTEIN SEQUENCE OF 1-11.
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    9. "Extraction of membrane proteins by differential solubilization for separation using two-dimensional gel electrophoresis."
      Molloy M.P., Herbert B.R., Walsh B.J., Tyler M.I., Traini M., Sanchez J.-C., Hochstrasser D.F., Williams K.L., Gooley A.A.
      Electrophoresis 19:837-844(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 1-5.
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    10. Cited for: PROTEIN SEQUENCE OF 1-4.
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    11. "The roles of conserved carboxylate residues in IMP dehydrogenase and identification of a transition state analog."
      Kerr K.M., Hedstrom L.
      Biochemistry 36:13365-13373(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, ENZYME REGULATION, MUTAGENESIS OF ASP-13; ASP-50; GLU-54; ASP-138; ASP-200; ASP-243; ASP-248; ASP-338; GLU-369; GLU-373 AND GLU-469.
      Strain: K12.
    12. "The CBS subdomain of inosine 5'-monophosphate dehydrogenase regulates purine nucleotide turnover."
      Pimkin M., Markham G.D.
      Mol. Microbiol. 68:342-359(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: DOMAIN CBS.
      Strain: K12 / BW25113.
    13. "A regulatory role of the Bateman domain of IMP dehydrogenase in adenylate nucleotide biosynthesis."
      Pimkin M., Pimkina J., Markham G.D.
      J. Biol. Chem. 284:7960-7969(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: DOMAIN CBS.
      Strain: K12 / BW25113.
    14. "Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli."
      Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F., Grishin N.V., Zhao Y.
      Mol. Cell. Proteomics 8:215-225(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-267 AND LYS-428, IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: K12 / JW1106 and K12 / MG1655 / ATCC 47076.

    Entry informationi

    Entry nameiIMDH_ECOLI
    AccessioniPrimary (citable) accession number: P0ADG7
    Secondary accession number(s): P06981, P76574, P78202
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1988
    Last sequence update: December 6, 2005
    Last modified: October 1, 2014
    This is version 85 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3