A0A3N6PZJ2 · A0A3N6PZJ2_9BURK

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.
The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

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 site246NAD+ (UniProtKB | ChEBI)
Binding site246-248NAD+ (UniProtKB | ChEBI)
Binding site296-298NAD+ (UniProtKB | ChEBI)
Binding site298K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners; in other chain
Binding site300K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners; in other chain
Binding site301IMP (UniProtKB | ChEBI)
Active site303Thioimidate intermediate
Binding site303K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners; in other chain
Binding site336-338IMP (UniProtKB | ChEBI)
Binding site359-360IMP (UniProtKB | ChEBI)
Binding site383-387IMP (UniProtKB | ChEBI)
Active site399Proton acceptor
Binding site414IMP (UniProtKB | ChEBI)
Binding site468K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners
Binding site469K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners
Binding site470K+ (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

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
    • ORF names
      D1Y85_07500

Organism names

  • Taxonomic identifier
  • Strain
    • DHOA04
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Betaproteobacteria > Burkholderiales > Burkholderiaceae > Paraburkholderia

Accessions

  • Primary accession
    A0A3N6PZJ2

Proteomes

Interaction

Subunit

Homotetramer.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain92-150CBS
Domain151-212CBS

Sequence similarities

Belongs to the IMPDH/GMPR family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    486
  • Mass (Da)
    52,084
  • Last updated
    2019-02-13 v1
  • Checksum
    5FBD3BFC1C8E85EC
MRLIQKALTFDDVLLVPAFSDVLPRDTSLKTRLTRNISLNIPLVSAAMDTVTEGRLAIAMAQQGGVGIIHKNLTPAEQAREVAKVKRFESGVLRDPITIPPQMKVRDVIALSQQHGISGFPVVEGAQLIGIVTNRDLRFETRLDEPVRSIMTPRERLVTVKEGTPLYEAKALMHSHRLERVLVVNDAFELRGLMTVKDITKQTEHPAACKDEHGKLRAGAAVGVGPDNEERVELLVQAGVDVIVVDTAHGHSKGVLERVRWVKKNFPHVEVIGGNIATADAARALVEYGADGVKVGIGPGSICTTRIVAGVGVPQISAIANVSDALRGTGVPVVADGGVRYSGDVSKALAAGANAVMMGSMFAGTEESPGDVFLYQGRQYKSYRGMGSVGAMKDGAADRYFQDNSANIDKLVPEGIEGRVAYKGSVNAILFQLIGGVRASMGYCGCSTIDELHEKAAFVEITSAGMRESHVHDVQITKEAPNYHVD

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
RQIS01000004
EMBL· GenBank· DDBJ
RQH07940.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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