A0A1J9P938 · A0A1J9P938_9EURO

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.

Type
IDPosition(s)Description
Binding site296-298NAD+ (UniProtKB | ChEBI)
Binding site346-348NAD+ (UniProtKB | ChEBI)
Binding site348K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners; in other chain
Binding site350K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners; in other chain
Binding site351IMP (UniProtKB | ChEBI)
Active site353Thioimidate intermediate
Binding site353K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners; in other chain
Binding site386-388IMP (UniProtKB | ChEBI)
Binding site409-410IMP (UniProtKB | ChEBI)
Binding site434-438IMP (UniProtKB | ChEBI)
Active site464Proton acceptor
Binding site476IMP (UniProtKB | ChEBI)
Binding site531K+ (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
      AJ78_06481

Organism names

  • Taxonomic identifier
  • Strain
    • UAMH 9510
  • Taxonomic lineage
    Eukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Eurotiomycetes > Eurotiomycetidae > Onygenales > Ajellomycetaceae > Emergomyces

Accessions

  • Primary accession
    A0A1J9P938

Proteomes

Organism-specific databases

Subcellular Location

Keywords

Interaction

Subunit

Homotetramer.

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain139-198CBS
Domain202-258CBS

Sequence similarities

Belongs to the IMPDH/GMPR family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    550
  • Mass (Da)
    58,154
  • Last updated
    2017-02-15 v1
  • MD5 Checksum
    A9C86275DF6AC1D746C95CADF73A8098
MPISNGDASGSAFERFSGKAEFLDHTKALEILKSDYSGDGLDVNQLLDSEKRGALTYNDFLILPGYIGFPASDVTLESPVTKRITLKAPLLSSPMDTVTEHSMAIHMALLGGLGVIHHNCSAEDQANMVRKVKRYENGFISEPVVISPKTTVAEAKALKEKCGFGGFPVTENGTLSSKLIGMITSRDIQFHPTVEDPVTAVMTTDLVTAPSGTTLAEANEVLRSSKKGKLPIVDSEGNLVSLLSRSDLMKNLHYPLASKLPHSKQLICAAAIGTRPEDKERLHKLVEAGLDIVVLDSSQGNSMYQIEMIKYVKQTYPELDVIAGNVVTRDQAAALIAAGADGLRIGMGSGSACITQEVMAVGRPQAAAVRSVSQFAARFGVPCIADGGIQNIGHIVKGLAMGATTVMMGGLLAGTTESPGAYFVSREGQLVKAYRGMGSIDAMEDKKAGAGGDNGQASNAGTARYFSESDRLLVAQGVSGSVLDRGSVTKFVPYLIAGIQHSLQDIGVKSLKELHDGVAAGTVRFEVRSVSAQAEGNVHGLHSFDKKLYS

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
LGRN01000343
EMBL· GenBank· DDBJ
OJD13008.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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