A0AAP0G589 · A0AAP0G589_9ASPA

  • Protein
    Inosine-5'-monophosphate dehydrogenase
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    2/5

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 site264-266NAD+ (UniProtKB | ChEBI)
Binding site314-316NAD+ (UniProtKB | ChEBI)
Binding site316K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners; in other chain
Binding site318K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners; in other chain
Binding site319IMP (UniProtKB | ChEBI)
Active site321Thioimidate intermediate
Binding site321K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners; in other chain
Binding site354-356IMP (UniProtKB | ChEBI)
Binding site377-378IMP (UniProtKB | ChEBI)
Binding site401-405IMP (UniProtKB | ChEBI)
Active site417Proton acceptor
Binding site429IMP (UniProtKB | ChEBI)

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
      KSP39_PZI012728

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • Lor287
  • Taxonomic lineage
    Eukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > Liliopsida > Asparagales > Orchidaceae > Orchidoideae > Orchideae > Orchidinae > Platanthera

Accessions

  • Primary accession
    A0AAP0G589

Proteomes

Subcellular Location

Cytoplasm

Keywords

Interaction

Subunit

Homotetramer.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain23-492IMP dehydrogenase/GMP reductase

Sequence similarities

Belongs to the IMPDH/GMPR family.

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    502
  • Mass (Da)
    53,060
  • Last updated
    2024-10-02 v1
  • Checksum
    FA0BDFA42441F08E
MNGAAAAFDDGFTASRLFSQGFSYTYDDVIFLPHYIDFPADAVDLSTRLSRNHPLSIPCVASPMDTVSETSMAVAMASLGGAAIIHCNTIPARQAAIVRSAKSRRIPFASDPSFFAPSDFVSSAADFGSASFAIVTESGSSKSKPVGLISRSDWEALADEDYPVSKYMRQTPTSIPSNYDFEQVAAFLAGEGLELASLVGVDGEIIDLVCAEDVVRIRGFPKLGVPSLSPDGKFLVGAAIGTREEDKERLTHLVKAGVDVVVVDSSQGNSKYQMDMIKHAKNTYPSLDIIGGNVVTMAQTQNLIKVGVDGIRVGMGSGSICTTQEVCAVGRGQATAVYKVASFANDYDVPVIADGGISYSGHIVKALVLGASTVMMGSFLAGSHEAPGIYEYQDGHFVKKYRGMGSLEAMTKGSDARYLGDTLKLKVAQGVVGTVVDKGSLLKFIPYTMQAVKQGLQDLGASSLPIAHDLLRTDVLQLEVRTGAAQVEGGVHGLASYEKKAF

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
JBBWWQ010000010
EMBL· GenBank· DDBJ
KAK8937348.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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