P56088 · IMDH_HELPY

Function

function

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.

Catalytic activity

Cofactor

K+ (UniProtKB | Rhea| CHEBI:29103 )

Activity regulation

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.

Pathway

Purine metabolism; XMP biosynthesis via de novo pathway; XMP from IMP: step 1/1.

Features

Showing features for binding site, active site.

TypeIDPosition(s)Description
Binding site244NAD+ (UniProtKB | ChEBI)
Binding site293-295NAD+ (UniProtKB | ChEBI)
Binding site295K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners; in other chain
Binding site297K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners; in other chain
Binding site298IMP (UniProtKB | ChEBI)
Active site300Thioimidate intermediate
Binding site300K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners; in other chain
Binding site333-335IMP (UniProtKB | ChEBI)
Binding site356-357IMP (UniProtKB | ChEBI)
Binding site380-384IMP (UniProtKB | ChEBI)
Active site396Proton acceptor
Binding site410IMP (UniProtKB | ChEBI)
Binding site464K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners
Binding site465K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners
Binding site466K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners

GO annotations

AspectTerm
Molecular FunctionIMP dehydrogenase activity
Molecular Functionmetal ion binding
Molecular Functionnucleotide binding
Biological ProcessGMP biosynthetic process
Biological ProcessGTP biosynthetic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Inosine-5'-monophosphate dehydrogenase
  • EC number
  • Short names
    IMP dehydrogenase
    ; IMPD
    ; IMPDH

Gene names

    • Name
      guaB
    • Ordered locus names
      HP_0829

Organism names

Accessions

  • Primary accession
    P56088

Proteomes

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00000936981-481Inosine-5'-monophosphate dehydrogenase

Proteomic databases

Interaction

Subunit

Homotetramer.

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain92-148CBS 1
Domain152-209CBS 2

Sequence similarities

Belongs to the IMPDH/GMPR family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    481
  • Mass (Da)
    51,802
  • Last updated
    1997-11-01 v1
  • Checksum
    075A84B1F8AC9481
MRILQRALTFEDVLMVPRKSSVLPKDVSLKSRLTKNIRLNIPFISAAMDTVTEHKTAIAMARLGGIGIVHKNMDIQTQVKEITKVKKSESGVINDPIFIHAHRTLADAKVITDNYKISGVPVVDDKGLLIGILTNRDVRFETDLSKKVGDVMTKMPLVTAHVGISLDEASDLMHKHKIEKLPIVDKDNVLKGLITIKDIQKRIEYPEANKDDFGRLRVGAAIGVGQLDRAEMLVKAGVDALVLDSAHGHSANILHTLEEIKKSLVVDVIVGNVVTKEATSDLISAGADAIKVGIGPGSICTTRIVAGVGMPQVSAIDNCVEVASKFDIPVIADGGIRYSGDVAKALALGASSVMIGSLLAGTEESPGDFMIYQGRQYKSYRGMGSIGAMTKGSSDRYFQEGVASEKLVPEGIEGRVPYRGKVSDMIFQLVGGVRSSMGYQGAKNILELYQNAEFVEITSAGLKESHVHGVDITKEAPNYYG

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AE000511
EMBL· GenBank· DDBJ
AAD07879.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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