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Q8F4Q4

- IMDH_LEPIN

UniProt

Q8F4Q4 - IMDH_LEPIN

Protein

Inosine-5'-monophosphate dehydrogenase

Gene

guaB

Organism
Leptospira interrogans serogroup Icterohaemorrhagiae serovar Lai (strain 56601)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 83 (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 sitei267 – 2671NADUniRule annotation
    Metal bindingi319 – 3191Potassium; via carbonyl oxygenUniRule annotation
    Metal bindingi321 – 3211Potassium; via carbonyl oxygenUniRule annotation
    Binding sitei322 – 3221IMPUniRule annotation
    Active sitei324 – 3241Thioimidate intermediateUniRule annotation
    Metal bindingi324 – 3241Potassium; via carbonyl oxygenUniRule annotation
    Binding sitei432 – 4321IMPUniRule annotation
    Metal bindingi492 – 4921Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi317 – 3193NADUniRule 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

    BioCyciLINT189518:GJBB-1599-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:LA_1986
    OrganismiLeptospira interrogans serogroup Icterohaemorrhagiae serovar Lai (strain 56601)
    Taxonomic identifieri189518 [NCBI]
    Taxonomic lineageiBacteriaSpirochaetesSpirochaetalesLeptospiraceaeLeptospira
    ProteomesiUP000001408: Chromosome I

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 508508Inosine-5'-monophosphate dehydrogenasePRO_0000415689Add
    BLAST

    Interactioni

    Subunit structurei

    Homotetramer.UniRule annotation

    Protein-protein interaction databases

    STRINGi189518.LA1986.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8F4Q4.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini111 – 17060CBS 1UniRule annotationAdd
    BLAST
    Domaini174 – 23057CBS 2UniRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni357 – 3593IMP bindingUniRule annotation
    Regioni380 – 3812IMP bindingUniRule annotation
    Regioni404 – 4085IMP 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

    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]
    PANTHERiPTHR11911:SF6. PTHR11911:SF6. 1 hit.
    PfamiPF00571. CBS. 1 hit.
    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.

    Q8F4Q4-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSNQTYRDSE YLDGLSGEEL FNLQIGLTYR DFLVLPGFID FHPSEVELET    50
    RLTRNIKLKR PFISSPMDTV TESQMAIAQA LMGGIGIIHY NNTIEEQVAL 100
    VEKVKRFENG FITDPVILGP KNVIRDLDAI KERKGFTGIP VTEDGTRNSK 150
    LIGIVTNRDI DFEKNREITL DKVMTTNLIT GKEGITLQDA NEIIKKSKIG 200
    KLPIVDSQGK LVSLVSRSDL KKNKEFPDAS KDERKRLRCG AAVSTLLESR 250
    DRVAALYEAG VDVIIIDSAQ GNSNYQIEMI QFIKKEFKNL DIVAGNVVTR 300
    AQAENLIRAG ADGLRIGMGP GSICITQDTM AVGRAQATAI YQTAKHSAKY 350
    DVPVIADGGI SNIGDIANSL AIGASTCMMG FMFAGTTEAP GEYFYENGIR 400
    LKKYRGMASI EAMKAGGDKR YFNEGQKVKV AQGVSGSVVD RGSILNFIPY 450
    LSQGLRLSFQ DMGYKSIPEI HKALRDGKLR FERRSESAQA QGSVHGLYSF 500
    SAPTMRAE 508
    Length:508
    Mass (Da):55,881
    Last modified:March 1, 2003 - v1
    Checksum:i5D24AEC8D93512FA
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE010300 Genomic DNA. Translation: AAN49185.1.
    RefSeqiNP_712167.1. NC_004342.2.

    Genome annotation databases

    EnsemblBacteriaiAAN49185; AAN49185; LA_1986.
    GeneIDi1151329.
    KEGGilil:LA_1986.
    PATRICi22384813. VBILepInt91350_1979.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE010300 Genomic DNA. Translation: AAN49185.1 .
    RefSeqi NP_712167.1. NC_004342.2.

    3D structure databases

    ProteinModelPortali Q8F4Q4.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 189518.LA1986.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAN49185 ; AAN49185 ; LA_1986 .
    GeneIDi 1151329.
    KEGGi lil:LA_1986.
    PATRICi 22384813. VBILepInt91350_1979.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00601 ; UER00295 .
    BioCyci LINT189518:GJBB-1599-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. 1 hit.
    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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: 56601.

    Entry informationi

    Entry nameiIMDH_LEPIN
    AccessioniPrimary (citable) accession number: Q8F4Q4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 22, 2012
    Last sequence update: March 1, 2003
    Last modified: October 1, 2014
    This is version 83 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