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P0DB89

- IMDH_STRPQ

UniProt

P0DB89 - IMDH_STRPQ

Protein

Inosine-5'-monophosphate dehydrogenase

Gene

guaB

Organism
Streptococcus pyogenes serotype M3 (strain SSI-1)
Status
Reviewed - Annotation score: 4 out of 5- Protein inferred from homologyi
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    • History
      Entry version 24 (01 Oct 2014)
      Sequence version 1 (27 Jul 2011)
      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 sitei253 – 2531NADUniRule annotation
    Metal bindingi305 – 3051Potassium; via carbonyl oxygenUniRule annotation
    Metal bindingi307 – 3071Potassium; via carbonyl oxygenUniRule annotation
    Binding sitei308 – 3081IMPUniRule annotation
    Active sitei310 – 3101Thioimidate intermediateUniRule annotation
    Metal bindingi310 – 3101Potassium; via carbonyl oxygenUniRule annotation
    Binding sitei421 – 4211IMPUniRule annotation
    Metal bindingi475 – 4751Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation
    Metal bindingi476 – 4761Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation
    Metal bindingi477 – 4771Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi303 – 3053NADUniRule 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

    BioCyciSPYO193567:GHDO-1920-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:impD
    Ordered Locus Names:SPs1853
    OrganismiStreptococcus pyogenes serotype M3 (strain SSI-1)
    Taxonomic identifieri193567 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeStreptococcus
    ProteomesiUP000002699: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 493492Inosine-5'-monophosphate dehydrogenasePRO_0000411382Add
    BLAST

    Proteomic databases

    PRIDEiP0DB89.

    Interactioni

    Subunit structurei

    Homotetramer.UniRule annotation

    Structurei

    3D structure databases

    ProteinModelPortaliP0DB89.
    SMRiP0DB89. Positions 2-491.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini97 – 15559CBS 1UniRule annotationAdd
    BLAST
    Domaini159 – 21961CBS 2UniRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni343 – 3453IMP bindingUniRule annotation
    Regioni366 – 3672IMP bindingUniRule annotation
    Regioni390 – 3945IMP 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.
    OMAiHAAKDEH.
    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]
    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.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P0DB89-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSNWDTKFLK KGYTFDDVLL IPAESHVLPN EVDLKTKLAD NLTLNIPIIT    50
    AAMDTVTGSK MAIAIARAGG LGVIHKNMSI TEQAEEVRKV KRSENGVIID 100
    PFFLTPEHKV SEAEELMQRY RISGVPIVET LANRKLVGII TNRDMRFISN 150
    YNAPISEHMT SEHLVTAAVG TDLETAERIL HEHRIEKLPL VDNSGRLSGL 200
    ITIKDIEKVI EFPHAAKDEF GRLLVAAAVG VTSDTFERAE ALFEAGADAI 250
    VIDTAHGHSA GVLRKIAEIR AHFPNRTLIA GNIATAEGAR ALYDAGVDVV 300
    KVGIGPGSIC TTRVVAGVGV PQVTAIYDAA AVAREYGKTI IADGGIKYSG 350
    DIVKALAAGG NAVMLGSMFA GTDEAPGETE IYQGRKFKTY RGMGSIAAMK 400
    KGSSDRYFQG SVNEANKLVP EGIEGRVAYK GAASDIVFQM LGGIRSGMGY 450
    VGAGDIQELH ENAQFVEMSG AGLIESHPHD VQITNEAPNY SVH 493
    Length:493
    Mass (Da):52,806
    Last modified:July 27, 2011 - v1
    Checksum:i429190D9B2A57B09
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BA000034 Genomic DNA. Translation: BAC64948.1.
    RefSeqiNP_803115.1. NC_004606.1.
    WP_011055116.1. NC_004606.1.

    Genome annotation databases

    EnsemblBacteriaiBAC64948; BAC64948; BAC64948.
    GeneIDi1066094.
    KEGGisps:SPs1853.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BA000034 Genomic DNA. Translation: BAC64948.1 .
    RefSeqi NP_803115.1. NC_004606.1.
    WP_011055116.1. NC_004606.1.

    3D structure databases

    ProteinModelPortali P0DB89.
    SMRi P0DB89. Positions 2-491.
    ModBasei Search...
    MobiDBi Search...

    Proteomic databases

    PRIDEi P0DB89.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai BAC64948 ; BAC64948 ; BAC64948 .
    GeneIDi 1066094.
    KEGGi sps:SPs1853.

    Phylogenomic databases

    HOGENOMi HOG000165755.
    KOi K00088.
    OMAi HAAKDEH.
    OrthoDBi EOG6GTZPV.

    Enzyme and pathway databases

    UniPathwayi UPA00601 ; UER00295 .
    BioCyci SPYO193567:GHDO-1920-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. "Genome sequence of an M3 strain of Streptococcus pyogenes reveals a large-scale genomic rearrangement in invasive strains and new insights into phage evolution."
      Nakagawa I., Kurokawa K., Yamashita A., Nakata M., Tomiyasu Y., Okahashi N., Kawabata S., Yamazaki K., Shiba T., Yasunaga T., Hayashi H., Hattori M., Hamada S.
      Genome Res. 13:1042-1055(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: SSI-1.

    Entry informationi

    Entry nameiIMDH_STRPQ
    AccessioniPrimary (citable) accession number: P0DB89
    Secondary accession number(s): Q8K5G1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 27, 2011
    Last sequence update: July 27, 2011
    Last modified: October 1, 2014
    This is version 24 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

    Documents

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

    External Data

    Dasty 3