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Q9L6B7

- IMDH_PASMU

UniProt

Q9L6B7 - IMDH_PASMU

Protein

Inosine-5'-monophosphate dehydrogenase

Gene

guaB

Organism
Pasteurella multocida (strain Pm70)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 101 (01 Oct 2014)
      Sequence version 1 (01 Oct 2000)
      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.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
    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. 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

    BioCyciPMUL272843:GC8W-299-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
    Ordered Locus Names:PM0295
    OrganismiPasteurella multocida (strain Pm70)
    Taxonomic identifieri272843 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaePasteurella
    ProteomesiUP000000809: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 487487Inosine-5'-monophosphate dehydrogenasePRO_0000093703Add
    BLAST

    Proteomic databases

    PRIDEiQ9L6B7.

    Interactioni

    Subunit structurei

    Homotetramer.UniRule annotation

    Protein-protein interaction databases

    STRINGi272843.PM0295.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9L6B7.
    SMRiQ9L6B7. Positions 3-485.
    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

    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.

    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.

    Q9L6B7-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLRVIKEALT FDDVLLVPAH STVLPNTADL STQLTKTIRL NIPMLSAAMD    50
    TVTETKLAIS LAQEGGIGFI HKNMSIERQA ERVRKVKKFE SGIVSDPVTV 100
    SPTLSLAELS ELVKKNGFAS FPVVDDEKNL VGIITGRDTR FVTDLNKTVA 150
    DFMTPKARLV TVKRNASRDE IFGLMHTHRV EKVLVVSDDF KLKGMITLKD 200
    YQKSEQKPQA CKDEFGRLRV GAAVGAGPGN EERIDALVKA GVDVLLIDSS 250
    HGHSEGVLQR VRETRAKYPD LPIVAGNVAT AEGAIALADA GASAVKVGIG 300
    PGSICTTRIV TGVGVPQITA IADAAEALKD RGIPVIADGG IRFSGDISKA 350
    IAAGASCVMV GSMFAGTEEA PGEIELYQGR AFKSYRGMGS LGAMSKGSSD 400
    RYFQSDNAAD KLVPEGIEGR IPYKGFLKEI IHQQMGGLRS CMGLTGCATI 450
    DELRTKAQFV RISGAGIQES HVHDVTITKE APNYRMG 487
    Length:487
    Mass (Da):52,008
    Last modified:October 1, 2000 - v1
    Checksum:i0871DB08893B8FCA
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF237921 Genomic DNA. Translation: AAF68407.1.
    AE004439 Genomic DNA. Translation: AAK02379.1.
    RefSeqiNP_245232.1. NC_002663.1.
    WP_005725353.1. NC_002663.1.

    Genome annotation databases

    EnsemblBacteriaiAAK02379; AAK02379; PM0295.
    GeneIDi1243642.
    KEGGipmu:PM0295.
    PATRICi22869746. VBIPasMul88067_0305.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF237921 Genomic DNA. Translation: AAF68407.1 .
    AE004439 Genomic DNA. Translation: AAK02379.1 .
    RefSeqi NP_245232.1. NC_002663.1.
    WP_005725353.1. NC_002663.1.

    3D structure databases

    ProteinModelPortali Q9L6B7.
    SMRi Q9L6B7. Positions 3-485.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 272843.PM0295.

    Proteomic databases

    PRIDEi Q9L6B7.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAK02379 ; AAK02379 ; PM0295 .
    GeneIDi 1243642.
    KEGGi pmu:PM0295.
    PATRICi 22869746. VBIPasMul88067_0305.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00601 ; UER00295 .
    BioCyci PMUL272843:GC8W-299-MONOMER.

    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. "Identification of Pasteurella multocida virulence genes in a septicemic mouse model using signature-tagged mutagenesis."
      Fuller T.E., Kennedy M.J., Lowery D.E.
      Microb. Pathog. 29:25-38(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Pm70.

    Entry informationi

    Entry nameiIMDH_PASMU
    AccessioniPrimary (citable) accession number: Q9L6B7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 4, 2001
    Last sequence update: October 1, 2000
    Last modified: October 1, 2014
    This is version 101 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, Reference proteome

    Documents

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

    External Data

    Dasty 3