B6H451 · B6H451_PENRW

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.

Caution

Lacks conserved residue(s) required for the propagation of feature annotation.

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.

Type
IDPosition(s)Description
Binding site276-278NAD+ (UniProtKB | ChEBI)
Binding site326-328NAD+ (UniProtKB | ChEBI)
Binding site328K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners; in other chain
Binding site330K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners; in other chain
Binding site331IMP (UniProtKB | ChEBI)
Active site333Thioimidate intermediate
Binding site333K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners; in other chain
Binding site366-368IMP (UniProtKB | ChEBI)
Binding site389-390IMP (UniProtKB | ChEBI)
Active site439Proton acceptor
Binding site451IMP (UniProtKB | ChEBI)
Binding site506K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners

GO annotations

AspectTerm
Cellular Componentcytoplasm
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

    • ORF names
      Pc13g07630
      , PCH_Pc13g07630

Organism names

Accessions

  • Primary accession
    B6H451

Proteomes

Organism-specific databases

Subcellular Location

Keywords

Interaction

Subunit

Homotetramer.

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain, region.

Type
IDPosition(s)Description
Domain120-179CBS
Domain183-239CBS
Region506-525Disordered

Sequence similarities

Belongs to the IMPDH/GMPR family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    525
  • Mass (Da)
    55,770
  • Last updated
    2008-12-16 v1
  • Checksum
    32FB96F633F21DED
MVEVLDYTKALEVLKEYPGDGLHVDTLLDSDSHGALTYNDFLILPGSITFPASDVSLETKVTRRFTIKAPLLSSPMDTVTEHSMAIHMALLGGLGVIHNNCPPDEQAEMVRKVKRYENGFIQDPIVLSPETTVGEAKELKTKWGFGGFPVTEKGTLLSKLLGIVTSRDIQFHKNHEDPVTAVMMTDLVTAPAGTTLAEANEVLRSSKKGKLPIVDKDGSLISLLSRSDLMKNIHYPLASKLPSKQLLCAAAISTHDADKVRLEKLVDAGLDIVVVDSSQGHSIFQIAMIKYIKQTFPDIDVIGGNIVTREQAAALIAAGADGLRIGMGSGSACITQEVMAAGRPQAAAVRSVSAFAARFGVPTIADGGVQNLGHIVKGLALGASAVMMGSLLAGTTESPGEYFMSSEGQLVKAFRGMGSIAVMEDKSKSGAGNNAGASRYFSENDKVKVAQGVAGSVIDRGSITQYVPYLVAGVQHSLQDIGVQNLDALRDGVNNGTVRFEMRSASAQTEGNVHGLHTHEKKLYS

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AM920428
EMBL· GenBank· DDBJ
CAP91832.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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