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Q4L385

- IMDH_STAHJ

UniProt

Q4L385 - IMDH_STAHJ

Protein

Inosine-5'-monophosphate dehydrogenase

Gene

guaB

Organism
Staphylococcus haemolyticus (strain JCSC1435)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 71 (01 Oct 2014)
      Sequence version 1 (02 Aug 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.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 sitei250 – 2501NADUniRule annotation
    Metal bindingi302 – 3021Potassium; via carbonyl oxygenUniRule annotation
    Metal bindingi304 – 3041Potassium; via carbonyl oxygenUniRule annotation
    Binding sitei305 – 3051IMPUniRule annotation
    Active sitei307 – 3071Thioimidate intermediateUniRule annotation
    Metal bindingi307 – 3071Potassium; via carbonyl oxygenUniRule annotation
    Binding sitei417 – 4171IMPUniRule annotation
    Metal bindingi471 – 4711Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation
    Metal bindingi472 – 4721Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation
    Metal bindingi473 – 4731Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi300 – 3023NADUniRule 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

    BioCyciSHAE279808:GJX7-2658-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:SH2583
    OrganismiStaphylococcus haemolyticus (strain JCSC1435)
    Taxonomic identifieri279808 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcus
    ProteomesiUP000000543: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 488488Inosine-5'-monophosphate dehydrogenasePRO_0000287362Add
    BLAST

    Interactioni

    Subunit structurei

    Homotetramer.UniRule annotation

    Protein-protein interaction databases

    STRINGi279808.SH2583.

    Structurei

    3D structure databases

    ProteinModelPortaliQ4L385.
    SMRiQ4L385. Positions 2-487.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini95 – 15359CBS 1UniRule annotationAdd
    BLAST
    Domaini157 – 21357CBS 2UniRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni340 – 3423IMP bindingUniRule annotation
    Regioni363 – 3642IMP bindingUniRule annotation
    Regioni387 – 3915IMP 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.
    HOGENOMiHOG000165752.
    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.

    Q4L385-1 [UniParc]FASTAAdd to Basket

    « Hide

    MWENKFAKES LTFDDVLLIP AASDVLPNDA DLSVELSERI KLNIPVISAG    50
    MDTVTESKMA IAMARQGGLG VIHKNMGIEE QAEEVQKVKR SENGVITNPF 100
    YLTPDESVYE AEALMGKYRI SGVPIVSDKE SRELVGILTN RDLRFIEDFS 150
    IKISDVMTKE NLITAPVGTT LDEAETILQE HKIEKLPLVE NGRLEGLITI 200
    KDIEKVLEFP HAAKDAHGRL LAAAAIGTSK DTEIRAQKLV EAGVDALIID 250
    TAHGHSSGVI QEVKKMKEKY PEITIVAGNV ATAEATRALF EAGADVVKVG 300
    IGPGSICTTR VVAGVGVPQI TAIYDCATEA RKFGKAIIAD GGIKFSGDII 350
    KALAAGGHAV MLGSLLAGTE ESPGATEVFQ GRQYKVYRGM GSLGAMEKGS 400
    NDRYFQEDKT PRKFVPEGIE GRTAYKGPLQ DTIYQLMGGV RAGMGYTGSP 450
    DLKTLRDEAQ FTRMGPAGLA ESHPHNVQIT KESPNYSF 488
    Length:488
    Mass (Da):52,577
    Last modified:August 2, 2005 - v1
    Checksum:i2B088725A4CA337B
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AP006716 Genomic DNA. Translation: BAE05892.1.
    RefSeqiYP_254498.1. NC_007168.1.

    Genome annotation databases

    EnsemblBacteriaiBAE05892; BAE05892; SH2583.
    GeneIDi3482174.
    KEGGisha:SH2583.
    PATRICi19621259. VBIStaHae67511_2532.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AP006716 Genomic DNA. Translation: BAE05892.1 .
    RefSeqi YP_254498.1. NC_007168.1.

    3D structure databases

    ProteinModelPortali Q4L385.
    SMRi Q4L385. Positions 2-487.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 279808.SH2583.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai BAE05892 ; BAE05892 ; SH2583 .
    GeneIDi 3482174.
    KEGGi sha:SH2583.
    PATRICi 19621259. VBIStaHae67511_2532.

    Phylogenomic databases

    eggNOGi COG0517.
    HOGENOMi HOG000165752.
    KOi K00088.
    OMAi HGHSKNI.
    OrthoDBi EOG6GTZPV.

    Enzyme and pathway databases

    UniPathwayi UPA00601 ; UER00295 .
    BioCyci SHAE279808:GJX7-2658-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. "Whole-genome sequencing of Staphylococcus haemolyticus uncovers the extreme plasticity of its genome and the evolution of human-colonizing staphylococcal species."
      Takeuchi F., Watanabe S., Baba T., Yuzawa H., Ito T., Morimoto Y., Kuroda M., Cui L., Takahashi M., Ankai A., Baba S., Fukui S., Lee J.C., Hiramatsu K.
      J. Bacteriol. 187:7292-7308(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: JCSC1435.

    Entry informationi

    Entry nameiIMDH_STAHJ
    AccessioniPrimary (citable) accession number: Q4L385
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 15, 2007
    Last sequence update: August 2, 2005
    Last modified: October 1, 2014
    This is version 71 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