Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Inosine-5'-monophosphate dehydrogenase

Gene

IMH3

Organism
Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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 annotation1 Publication

Catalytic activityi

Inosine 5'-phosphate + NAD+ + H2O = xanthosine 5'-phosphate + NADH.UniRule annotation

Cofactori

K+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. Also inhibited by ADP.UniRule annotation1 Publication

Kineticsi

  1. KM=60 µM for Inosine 5'-phosphate1 Publication
  2. KM=3500 µM for NAD+1 Publication

    Pathwayi: XMP biosynthesis via de novo pathway

    This protein is involved in step 1 of the subpathway that synthesizes XMP from IMP.UniRule annotation
    Proteins known to be involved in this subpathway in this organism are:
    1. Inosine-5'-monophosphate dehydrogenase (IMH3)
    This subpathway is part of the pathway XMP biosynthesis via de novo pathway, which is itself part of Purine metabolism.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes XMP from IMP, the pathway XMP biosynthesis via de novo pathway and in Purine metabolism.

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Metal bindingi328Potassium; via carbonyl oxygenUniRule annotation1
    Metal bindingi330Potassium; via carbonyl oxygenUniRule annotation1
    Binding sitei331IMPUniRule annotation1
    Active sitei333Thioimidate intermediateUniRule annotation1
    Metal bindingi333Potassium; via carbonyl oxygenUniRule annotation1
    Active sitei435Proton acceptorUniRule annotation1
    Binding sitei447IMPUniRule annotation1
    Metal bindingi506Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation1
    Metal bindingi507Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation1
    Metal bindingi508Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Nucleotide bindingi276 – 278NADUniRule annotation3
    Nucleotide bindingi326 – 328NADUniRule annotation3

    GO - Molecular functioni

    • IMP dehydrogenase activity Source: CGD
    • metal ion binding Source: UniProtKB-HAMAP
    • nucleotide binding Source: UniProtKB-HAMAP

    GO - Biological processi

    • cellular response to drug Source: CGD
    • cellular response to starvation Source: CGD
    • filamentous growth Source: CGD
    • filamentous growth of a population of unicellular organisms in response to biotic stimulus Source: CGD
    • filamentous growth of a population of unicellular organisms in response to starvation Source: CGD
    • GMP biosynthetic process Source: UniProtKB-HAMAP
    • induction by symbiont of host defense response Source: CGD
    Complete GO annotation...

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    GMP biosynthesis, Purine biosynthesis

    Keywords - Ligandi

    Metal-binding, NAD, Potassium

    Enzyme and pathway databases

    BRENDAi1.1.1.205. 1096.
    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:IMH3
    Synonyms:IMD3
    ORF Names:CaO19.18, CaO19.7689
    OrganismiCandida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
    Taxonomic identifieri237561 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesDebaryomycetaceaeCandida/Lodderomyces cladeCandida
    Proteomesi
    • UP000000559 Componenti: Unassembled WGS sequence

    Organism-specific databases

    CGDiCAL0000175344. IMH3.

    Subcellular locationi

    • Cytoplasm UniRule annotation

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi251A → T in MPA-resistant strain; decreases the K(M) values for both substrates. Decreases sensitivity to MPA 4-fold, but increases sensitivity to mizoribine monophosphate 40-fold. 1 Publication1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00004156841 – 521Inosine-5'-monophosphate dehydrogenaseAdd BLAST521

    Proteomic databases

    PRIDEiQ59Q46.

    Interactioni

    Subunit structurei

    Homotetramer.UniRule annotation

    Structurei

    3D structure databases

    ProteinModelPortaliQ59Q46.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Domaini119 – 178CBS 1UniRule annotationAdd BLAST60
    Domaini182 – 238CBS 2UniRule annotationAdd BLAST57

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni366 – 368IMP bindingUniRule annotation3
    Regioni389 – 390IMP bindingUniRule annotation2
    Regioni413 – 417IMP bindingUniRule annotation5

    Sequence similaritiesi

    Belongs to the IMPDH/GMPR family.UniRule annotation
    Contains 2 CBS domains.UniRule annotation

    Keywords - Domaini

    CBS domain, Repeat

    Phylogenomic databases

    InParanoidiQ59Q46.
    KOiK00088.
    OrthoDBiEOG092C1U8P.

    Family and domain databases

    CDDicd00381. IMPDH. 1 hit.
    Gene3Di3.20.20.70. 1 hit.
    HAMAPiMF_01964. IMPDH. 1 hit.
    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. 2 hits.
    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.

    Q59Q46-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MVFETSKATS YLKDYPKKDG LSVKELIDST NFGGLTYNDF LILPGLINFP
    60 70 80 90 100
    SSAVSLETKL TKKITLKSPF VSSPMDTVTE ENMAIHMALL GGIGIIHHNC
    110 120 130 140 150
    TSEEQAEMVR KVKKYENGFI NDPVVISPEV TVGEVKKMGE VLGFTSFPVT
    160 170 180 190 200
    ENGKVGGKLV GIITSRDIQF HEDNKSPVSE VMTKDLVVGK KGISLTDGNE
    210 220 230 240 250
    LLRSSKKGKL PIVDAEGNLV SLISRTDLQK NQDYPNASKS FHSKQLLCGA
    260 270 280 290 300
    AIGTIDADRE RLDKLVEAGL DVVVLDSSNG SSVFQLNMIK WIKEKYPELQ
    310 320 330 340 350
    VIAGNVVTRE QAALLIEAGA DALRIGMGSG SICITQEVMA CGRPQGTAVY
    360 370 380 390 400
    GVTEFANKFG VPCIADGGIG NIGHITKALA LGASCVMMGG LLAGTAETPG
    410 420 430 440 450
    DYFYRDGKRL KTYRGMGSID AMQQTNTNAN ASTSRYFSEA DKVLVAQGVS
    460 470 480 490 500
    GSVVDKGSIT KFVPYLYNGL QHSLQDIGIK SIDELRENVD NGEIRFEFRT
    510 520
    ASAQFEGGVH GLHSYEKRLH N
    Length:521
    Mass (Da):56,239
    Last modified:February 22, 2012 - v2
    Checksum:i5F1E52611B1E1418
    GO

    Sequence cautioni

    The sequence EAK92581 differs from that shown. Reason: Erroneous gene model prediction.Curated
    The sequence EAK92603 differs from that shown. Reason: Erroneous gene model prediction.Curated

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AY864854 Genomic DNA. Translation: AAW65379.1.
    AACQ01000181 Genomic DNA. Translation: EAK92581.1. Sequence problems.
    AACQ01000180 Genomic DNA. Translation: EAK92603.1. Sequence problems.
    RefSeqiXP_711803.1. XM_706711.1.
    XP_711825.1. XM_706733.1.

    Genome annotation databases

    EnsemblFungiiEAK92581; EAK92581; CaO19.7689.
    EAK92603; EAK92603; CaO19.18.
    GeneIDi3646555.
    3646575.
    KEGGical:CaO19.18.
    cal:CaO19.7689.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AY864854 Genomic DNA. Translation: AAW65379.1.
    AACQ01000181 Genomic DNA. Translation: EAK92581.1. Sequence problems.
    AACQ01000180 Genomic DNA. Translation: EAK92603.1. Sequence problems.
    RefSeqiXP_711803.1. XM_706711.1.
    XP_711825.1. XM_706733.1.

    3D structure databases

    ProteinModelPortaliQ59Q46.
    ModBaseiSearch...
    MobiDBiSearch...

    Proteomic databases

    PRIDEiQ59Q46.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblFungiiEAK92581; EAK92581; CaO19.7689.
    EAK92603; EAK92603; CaO19.18.
    GeneIDi3646555.
    3646575.
    KEGGical:CaO19.18.
    cal:CaO19.7689.

    Organism-specific databases

    CGDiCAL0000175344. IMH3.

    Phylogenomic databases

    InParanoidiQ59Q46.
    KOiK00088.
    OrthoDBiEOG092C1U8P.

    Enzyme and pathway databases

    UniPathwayiUPA00601; UER00295.
    BRENDAi1.1.1.205. 1096.

    Family and domain databases

    CDDicd00381. IMPDH. 1 hit.
    Gene3Di3.20.20.70. 1 hit.
    HAMAPiMF_01964. IMPDH. 1 hit.
    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. 2 hits.
    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]
    ProtoNetiSearch...

    Entry informationi

    Entry nameiIMDH_CANAL
    AccessioniPrimary (citable) accession number: Q59Q46
    Secondary accession number(s): Q5G1M4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 22, 2012
    Last sequence update: February 22, 2012
    Last modified: October 5, 2016
    This is version 85 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Candida albicans
      Candida albicans: entries and gene names
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. SIMILARITY comments
      Index of protein domains and families

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.