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Q49729

- IMDH_MYCLE

UniProt

Q49729 - IMDH_MYCLE

Protein

Inosine-5'-monophosphate dehydrogenase

Gene

guaB

Organism
Mycobacterium leprae (strain TN)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 108 (01 Oct 2014)
      Sequence version 1 (01 Nov 1997)
      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 sitei283 – 2831NADUniRule annotation
    Metal bindingi336 – 3361Potassium; via carbonyl oxygenUniRule annotation
    Metal bindingi338 – 3381Potassium; via carbonyl oxygenUniRule annotation
    Binding sitei339 – 3391IMPUniRule annotation
    Active sitei341 – 3411Thioimidate intermediateUniRule annotation
    Metal bindingi341 – 3411Potassium; via carbonyl oxygenUniRule annotation
    Binding sitei458 – 4581IMPUniRule annotation
    Metal bindingi511 – 5111Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation
    Metal bindingi512 – 5121Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation
    Metal bindingi513 – 5131Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi334 – 3363NADUniRule 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

    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:ML0387
    ORF Names:B1620_C3_238
    OrganismiMycobacterium leprae (strain TN)
    Taxonomic identifieri272631 [NCBI]
    Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacterium
    ProteomesiUP000000806: Chromosome

    Organism-specific databases

    LepromaiML0387.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 529529Inosine-5'-monophosphate dehydrogenasePRO_0000093701Add
    BLAST

    Interactioni

    Subunit structurei

    Homotetramer.UniRule annotation

    Protein-protein interaction databases

    STRINGi272631.ML0387.

    Structurei

    3D structure databases

    ProteinModelPortaliQ49729.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini129 – 18557CBS 1UniRule annotationAdd
    BLAST
    Domaini189 – 24658CBS 2UniRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni374 – 3763IMP bindingUniRule annotation
    Regioni397 – 3982IMP bindingUniRule annotation
    Regioni421 – 4255IMP 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.

    Q49729-1 [UniParc]FASTAAdd to Basket

    « Hide

    MIRGMSNLKE SSDFVASSYV RLGGLMDDPA ATGGDNPHKV AMLGLTFDDV    50
    LLLPAASDVV PATADISSQL TKKIRLKVPL VSSAMDTVTE ARMAIAMARA 100
    GGMGVLHRNL PVGEQAGQVE TVKRSEAGMV TDPVTCRPDN TLAQVGALCA 150
    RFRISGLPVV DDSGALAGII TNRDMRFEVD QSKQVAEVMT KTPLITAAEG 200
    VSADAALGLL RRNKIEKLPV VDGHGRLTGL ITVKDFVKTE QHPLATKDND 250
    GRLLVGAAVG VGGDAWVRAM MLVDAGVDVL IVDTAHAHNR LVLDMVGKLK 300
    VEIGDRVQVI GGNVATRSAA AALVEAGADA VKVGVGPGST CTTRVVAGVG 350
    APQITAILEA VAACGPAGVP VIADGGLQYS GDIAKALAAG ASTTMLGSLL 400
    AGTAEAPGEL IFVNGKQFKS YRGMGSLGAM QGRGGDKSYS KDRYFADDAL 450
    SEDKLVPEGI EGRVPFRGPL SSVIHQLVGG LRAAMGYTGS PTIEVLQQAQ 500
    FVRITPAGLK ESHPHDVAMT VEAPNYYPR 529
    Length:529
    Mass (Da):54,814
    Last modified:November 1, 1997 - v1
    Checksum:i1565C62EC9529870
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U00015 Genomic DNA. Translation: AAC43232.1.
    AL583918 Genomic DNA. Translation: CAC29895.1.
    PIRiS72823.
    RefSeqiNP_301377.1. NC_002677.1.
    WP_010907701.1. NC_002677.1.

    Genome annotation databases

    EnsemblBacteriaiCAC29895; CAC29895; CAC29895.
    GeneIDi909092.
    KEGGimle:ML0387.
    PATRICi18051408. VBIMycLep78757_0653.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U00015 Genomic DNA. Translation: AAC43232.1 .
    AL583918 Genomic DNA. Translation: CAC29895.1 .
    PIRi S72823.
    RefSeqi NP_301377.1. NC_002677.1.
    WP_010907701.1. NC_002677.1.

    3D structure databases

    ProteinModelPortali Q49729.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 272631.ML0387.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAC29895 ; CAC29895 ; CAC29895 .
    GeneIDi 909092.
    KEGGi mle:ML0387.
    PATRICi 18051408. VBIMycLep78757_0653.

    Organism-specific databases

    Lepromai ML0387.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00601 ; UER00295 .

    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. Smith D.R., Robison K.
      Submitted (MAR-1994) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: TN.

    Entry informationi

    Entry nameiIMDH_MYCLE
    AccessioniPrimary (citable) accession number: Q49729
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: November 1, 1997
    Last modified: October 1, 2014
    This is version 108 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