A0A2K2HCA2 · A0A2K2HCA2_9BACT

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 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 site415IMP (UniProtKB | ChEBI)
Binding site469K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners
Binding site470K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners
Binding site471K+ (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
      C2E25_04640

Organism names

  • Taxonomic identifier
  • Strain
    • HR-1
  • Taxonomic lineage
    Bacteria > Thermodesulfobacteriota > Desulfuromonadia > Desulfuromonadales > Geothermobacteraceae > Geothermobacter

Accessions

  • Primary accession
    A0A2K2HCA2

Proteomes

Interaction

Subunit

Homotetramer.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain94-151CBS
Domain153-210CBS

Sequence similarities

Belongs to the IMPDH/GMPR family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    489
  • Mass (Da)
    53,024
  • Last updated
    2018-03-28 v1
  • Checksum
    819501D4FD599B52
MLDPEVREGLTFDDVLLVPAHSEILPKEADISTWLTSTIRLNMPLLSAAMDTVTESRSAIIMAREGGMGIIHKNMTPKEQAVEVDQVKKSESGMIVDPITMEPEQKIFEALAVMKQYRISGVPVCKNGKLVGIMTNRDLRFETNLDQPIANVMTRDKLVTVPPGTTLEEAKQHLHAHRIEKLLVVDDNYTLKGLITIKDIEKVRKYPNSCKDDIGRLRVGAAIGVGPDREERLAELVAAGVDVVVIDTAHGHSQGVIDAVVDTRRQYPDLQLIAGNIATGTAAEVLIKAGVNAVKVGIGPGSICTTRVVAGVGVPQITAIADVSAVTRRHGVSMIADGGIKYSGELPKAIAAGADVIMIGSLFAGTEESPGETILYQGRTYKSYRGMGSLGAMKRGSKDRYFQGDVDNDVKLVPEGIEGRVPYRGPLSDNIHQLLGGLRAGMGYTGCRTIRELQEKGQFMRITNAGLRESHVHDVNITHEAPNYRIERN

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
PPFX01000007
EMBL· GenBank· DDBJ
PNU20883.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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