F9WXJ0 · F9WXJ0_ZYMTI

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.

TypeIDPosition(s)Description
Binding site297-299NAD+ (UniProtKB | ChEBI)
Binding site347-349NAD+ (UniProtKB | ChEBI)
Binding site349K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners; in other chain
Binding site351K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners; in other chain
Binding site352IMP (UniProtKB | ChEBI)
Active site354Thioimidate intermediate
Binding site354K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners; in other chain
Binding site387-389IMP (UniProtKB | ChEBI)
Binding site410-411IMP (UniProtKB | ChEBI)
Binding site435-439IMP (UniProtKB | ChEBI)
Active site467Proton acceptor
Binding site479IMP (UniProtKB | ChEBI)
Binding site534K+ (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
      MYCGRDRAFT_106783

Organism names

Accessions

  • Primary accession
    F9WXJ0

Proteomes

Organism-specific databases

Subcellular Location

Keywords

Interaction

Subunit

Homotetramer.

Protein-protein interaction databases

Family & Domains

Features

Showing features for compositional bias, region, domain.

TypeIDPosition(s)Description
Compositional bias1-25Polar residues
Region1-27Disordered
Domain140-199CBS
Domain203-259CBS

Sequence similarities

Belongs to the IMPDH/GMPR family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    553
  • Mass (Da)
    59,111
  • Last updated
    2011-10-19 v1
  • Checksum
    D5BA9C4BDDDE978F
MSANGNTDGDQLKKQMTNGQQSYEDPSRALEVLKTYRAKDGISVQELMDENKQGGLTYNDFLMLPGYIGFPAATVDLTSKLTRNITLKTPFTSSPMDTVTEHNMAIHMALLGGVGVVHHNCSVEEQAEMIRKVKRFENGFITDPIVISPETTVGEAIALKEQWGFGGFPVTESGQLRSKLIGIVTPRDTQFHSDHDAPVTDIMSRDLVTAPQNVSLSEANEILYKSKKGKLPIVDGQGNLISLLSRSDLMKNLNYPLATKVPGTKQLLAAAAIGTRENDKERLTALVEAGLDVVILDSSQGNSLYQISMIKWIKENYPKLDVIGGNVVTRDQAAALIAAGVDGLRIGMGAGSACITQEVMAVGRPQATSVFRVAEFAARFGIPCIADGGIQNVGHIVKSLALGASTVMMGGLLAATTESPGAYVVGPDGQLRKTYRGMGSIDAMEDKKAGGKGDKANNTAKNAGTARYFSEGDRLLVAQGVSGSVLDRGSVTKFLPYLMAGVQHSLQDVGIDSLLKLQEDVRAGDVRFEFRTASAQAEGNVHGMVGVEKKLYS

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias1-25Polar residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CM001196
EMBL· GenBank· DDBJ
EGP90873.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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