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Q8G3N6

- IMDH_BIFLO

UniProt

Q8G3N6 - IMDH_BIFLO

Protein

Inosine-5'-monophosphate dehydrogenase

Gene

guaB

Organism
Bifidobacterium longum (strain NCC 2705)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 84 (01 Oct 2014)
      Sequence version 1 (01 Mar 2003)
      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 sitei295 – 2951NADUniRule annotation
    Metal bindingi349 – 3491Potassium; via carbonyl oxygenUniRule annotation
    Metal bindingi351 – 3511Potassium; via carbonyl oxygenUniRule annotation
    Binding sitei352 – 3521IMPUniRule annotation
    Active sitei354 – 3541Thioimidate intermediateUniRule annotation
    Metal bindingi354 – 3541Potassium; via carbonyl oxygenUniRule annotation
    Binding sitei470 – 4701IMPUniRule annotation
    Metal bindingi524 – 5241Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation
    Metal bindingi525 – 5251Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation
    Metal bindingi526 – 5261Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi347 – 3493NADUniRule 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

    BioCyciBLON206672:GI1E-1707-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:BL1722
    OrganismiBifidobacterium longum (strain NCC 2705)
    Taxonomic identifieri206672 [NCBI]
    Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeBifidobacterialesBifidobacteriaceaeBifidobacterium
    ProteomesiUP000000439: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 545545Inosine-5'-monophosphate dehydrogenasePRO_0000415688Add
    BLAST

    Interactioni

    Subunit structurei

    Homotetramer.UniRule annotation

    Protein-protein interaction databases

    STRINGi206672.BL1722.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8G3N6.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini138 – 19457CBS 1UniRule annotationAdd
    BLAST
    Domaini201 – 25858CBS 2UniRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni387 – 3893IMP bindingUniRule annotation
    Regioni410 – 4112IMP bindingUniRule annotation
    Regioni434 – 4385IMP 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

    HOGENOMiHOG000165755.
    KOiK00088.
    OMAiFQADVRS.
    OrthoDBiEOG6GTZPV.
    PhylomeDBiQ8G3N6.

    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.

    Q8G3N6-1 [UniParc]FASTAAdd to Basket

    « Hide

    MRCRTRQRIS ERSQACVVKV SACSYSVCMA TNLDELNAQS AYAPLPPIFA    50
    KLGLAYDDVL LLPNETDVIP SEVDTSTHLT RKIVMKAPVL SAAMDTVTES 100
    EMAIAMARNG GIGVLHRNLS IDDQAAQVDV VKRSESGMIT DPLTVNPEVT 150
    LADLDKLCGK FHISGLPVVD KENKLVGIIT NRDMRFIASE DYDTLKVKDV 200
    MTKENLVTGP SNISKDDAHR LLAQHKVEKL PLVDEEGHLT GLITVKDFVK 250
    TEQYPDATKD EQGRLRVAAG VGFLGDAWQR ASALMEAGVD VLVVDTANGE 300
    ARLALDMISR LKHDSAFDGV QIIGGNVGTR SGAQAMIEAG ADAVKVGIGP 350
    GSICTTRIVA GVGVPQLTAV YEAAQACRAA GVPCIADGGI HYSGDIAKAL 400
    VAGASSVMLG GTLAGCEEAP GEKVLLHGKQ YKLYRGMGSL GAMAPRGKKS 450
    YSKDRYFQAD VTSSDKVVPE GVEGEVPYRG PLNAVLYQML GGLHQSMFYI 500
    GAHNIAEMPE RGKFIRITDA GLRESHPHDI VMTTEAPNYS GFHNN 545
    Length:545
    Mass (Da):58,263
    Last modified:March 1, 2003 - v1
    Checksum:iE56CD074DAF63CD3
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE014295 Genomic DNA. Translation: AAN25506.1.
    RefSeqiNP_696870.1. NC_004307.2.

    Genome annotation databases

    EnsemblBacteriaiAAN25506; AAN25506; BL1722.
    GeneIDi1021976.
    KEGGiblo:BL1722.
    PATRICi21120714. VBIBifLon107831_1776.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE014295 Genomic DNA. Translation: AAN25506.1 .
    RefSeqi NP_696870.1. NC_004307.2.

    3D structure databases

    ProteinModelPortali Q8G3N6.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 206672.BL1722.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAN25506 ; AAN25506 ; BL1722 .
    GeneIDi 1021976.
    KEGGi blo:BL1722.
    PATRICi 21120714. VBIBifLon107831_1776.

    Phylogenomic databases

    HOGENOMi HOG000165755.
    KOi K00088.
    OMAi FQADVRS.
    OrthoDBi EOG6GTZPV.
    PhylomeDBi Q8G3N6.

    Enzyme and pathway databases

    UniPathwayi UPA00601 ; UER00295 .
    BioCyci BLON206672:GI1E-1707-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 ]
    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 genome sequence of Bifidobacterium longum reflects its adaptation to the human gastrointestinal tract."
      Schell M.A., Karmirantzou M., Snel B., Vilanova D., Berger B., Pessi G., Zwahlen M.-C., Desiere F., Bork P., Delley M., Pridmore R.D., Arigoni F.
      Proc. Natl. Acad. Sci. U.S.A. 99:14422-14427(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: NCC 2705.

    Entry informationi

    Entry nameiIMDH_BIFLO
    AccessioniPrimary (citable) accession number: Q8G3N6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 22, 2012
    Last sequence update: March 1, 2003
    Last modified: October 1, 2014
    This is version 84 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