Q2GHN8 · Q2GHN8_EHRCR

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 site247NAD+ (UniProtKB | ChEBI)
Binding site247-249NAD+ (UniProtKB | ChEBI)
Binding site297-299NAD+ (UniProtKB | ChEBI)
Binding site299K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners; in other chain
Binding site301K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners; in other chain
Binding site302IMP (UniProtKB | ChEBI)
Active site304Thioimidate intermediate
Binding site304K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners; in other chain
Binding site337-339IMP (UniProtKB | ChEBI)
Binding site360-361IMP (UniProtKB | ChEBI)
Binding site384-388IMP (UniProtKB | ChEBI)
Active site400Proton acceptor
Binding site412IMP (UniProtKB | ChEBI)
Binding site466K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners
Binding site467K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners
Binding site468K+ (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
      ECH_0224

Organism names

Accessions

  • Primary accession
    Q2GHN8

Proteomes

Interaction

Subunit

Homotetramer.

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain89-151CBS
Domain152-212CBS

Sequence similarities

Belongs to the IMPDH/GMPR family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    485
  • Mass (Da)
    52,197
  • Last updated
    2006-03-21 v1
  • Checksum
    83938A6F06AB35B0
MELSYAFDDILIIPSESDVLPSETNVKTYITNEIELRIPIISAAMDTVTEAKLAIALAQHGGIGCIHKNLPIDTQLLEVRKVKKYESWIVYNPIAVSPDDSLAVALSIMQEYSYSGIPVVTDTENGKLLVGILTNRDVRFVENKNCKVSDIMTKDHLITVPEGIERSDAIKLLHQYRKERLIVVDNNYCCVGLITVKDIEKFNQFPNSCKDSGARLRVAAAVGTGPKDGIERAEALIAEDVDIIVVDTAHGHSQKVLTTIKEIKTLFPYSQIIGGNIATAEGAHALIEAGVDAVKVGIGPGSICTTRIVTGVGVPQFSAILNVANACKNKKIKVIADGGIKYSGDIAKSIAAGADVVMIGSIFAGTDESPGEIIICNGRAYKSYRGMGSVGAMKRGSASRYFQENNHKFIPEGIEGRVPLKGPVAGVIHQLVGGLRSAMGYTGNRNISEMKTNCKFTSITSAGLRESHVHDVIITREASNYDPIS

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP000236
EMBL· GenBank· DDBJ
ABD44834.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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