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Q12658

- IMDH_PNECA

UniProt

Q12658 - IMDH_PNECA

Protein

Inosine-5'-monophosphate dehydrogenase

Gene

GUA1

Organism
Pneumocystis carinii
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 85 (01 Oct 2014)
      Sequence version 2 (22 Feb 2012)
      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.2 PublicationsUniRule 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. MPA is a potent inhibitor in culture.1 PublicationUniRule annotation

    Kineticsi

    1. KM=21.7 µM for Inosine 5'-phosphate1 Publication
    2. KM=314 µM for NAD+1 Publication

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi333 – 3331Potassium; via carbonyl oxygenUniRule annotation
    Metal bindingi335 – 3351Potassium; via carbonyl oxygenUniRule annotation
    Binding sitei336 – 3361IMPUniRule annotation
    Active sitei338 – 3381Thioimidate intermediateUniRule annotation
    Metal bindingi338 – 3381Potassium; via carbonyl oxygenUniRule annotation
    Binding sitei455 – 4551IMPUniRule annotation
    Metal bindingi514 – 5141Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation
    Metal bindingi515 – 5151Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi281 – 2833NADUniRule annotation
    Nucleotide bindingi331 – 3333NADUniRule 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:GUA1
    OrganismiPneumocystis carinii
    Taxonomic identifieri4754 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaPneumocystidomycetesPneumocystidaceaePneumocystis

    Subcellular locationi

    Cytoplasm UniRule annotation

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 529529Inosine-5'-monophosphate dehydrogenasePRO_0000093679Add
    BLAST

    Post-translational modificationi

    The N-terminus is blocked.

    Interactioni

    Subunit structurei

    Homotetramer.UniRule annotation

    Structurei

    3D structure databases

    ProteinModelPortaliQ12658.
    SMRiQ12658. Positions 39-121, 238-528.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini124 – 18562CBS 1UniRule annotationAdd
    BLAST
    Domaini187 – 24357CBS 2UniRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni371 – 3733IMP bindingUniRule annotation
    Regioni394 – 3952IMP bindingUniRule annotation
    Regioni418 – 4225IMP bindingUniRule annotation

    Sequence similaritiesi

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

    Keywords - Domaini

    CBS domain, Repeat

    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]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q12658-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MGEDSYLCLS EEIKKKLEEY SEKDGYDLDS LICSRRHGGL TYNDIIILPG    50
    YIDFEVNSVS LESHITKKIV LKTPFMSSPM DTVTESDMAI NLALLGGIGV 100
    IHHNCTIEEQ TEMVRKVKKF ENGFITSPIV LSLNHRVRDV RRIKEELGFS 150
    GIPITDTGQL NGKLLGIVTS RDIQFHNNDE SFLSEVMTKD LVTGSEGIRL 200
    EEANEILRSC KKGKLPIVDK EGNLTALLSR SDLMKNLHFP LASKLPDSKQ 250
    LICAAAVGTR PDDRIRLKHL VEAGLDIVVL DSSQGNSIYQ INMIKWIKKE 300
    FPNLEVIAGN VVTREQAANL ISAGADALRV GMGSGSICIT QEIMAVGRPQ 350
    ATAVYAVSEF ASKFGVPTIA DGGIENIGHI TKALALGASA VMMGNLLAGT 400
    TESPGQYYYR DGQRLKSYRG MGSIDAMEHL SGKNKGDNAA SSRYFGEADT 450
    IRVAQGVSGS VIDKGSLHVY VPYLRTGLQH SLQDIGVQNL TELRKQVKEK 500
    NIRFEFRTVA SQLEGNVHGL DSYQKKLWS 529
    Length:529
    Mass (Da):58,066
    Last modified:February 22, 2012 - v2
    Checksum:i030573A8854ADB5A
    GO
    Isoform 2 (identifier: Q12658-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-75: Missing.

    Show »
    Length:454
    Mass (Da):49,483
    Checksum:i4B6A5AF9B4451210
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti187 – 1871M → I in AAA97462. (PubMed:8980752)Curated
    Sequence conflicti255 – 2551A → Q in AAA97462. (PubMed:8980752)Curated
    Sequence conflicti297 – 2971I → N in AAA97462. (PubMed:8980752)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 7575Missing in isoform 2. 2 PublicationsVSP_042318Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U42442 mRNA. Translation: AAA97462.1.
    AF196975 mRNA. Translation: AAF13230.1.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U42442 mRNA. Translation: AAA97462.1 .
    AF196975 mRNA. Translation: AAF13230.1 .

    3D structure databases

    ProteinModelPortali Q12658.
    SMRi Q12658. Positions 39-121, 238-528.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    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 ]
    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. "IMP dehydrogenase from Pneumocystis carinii as a potential drug target."
      O'Gara M.J., Lee C.H., Weinberg G.A., Nott J.M., Queener S.F.
      Antimicrob. Agents Chemother. 41:40-48(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), PROTEIN SEQUENCE OF 119-132; 172-186 AND 300-313, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION.
    2. "Differential splicing of Pneumocystis carinii f. sp. carinii inosine 5'-monophosphate dehydrogenase pre-mRNA."
      Ye D., Lee C.H., Queener S.F.
      Gene 263:151-158(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION.

    Entry informationi

    Entry nameiIMDH_PNECA
    AccessioniPrimary (citable) accession number: Q12658
    Secondary accession number(s): Q9UVL0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: February 22, 2012
    Last modified: October 1, 2014
    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

    Direct protein sequencing

    Documents

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

    External Data

    Dasty 3