A0A8B8UKT0 · A0A8B8UKT0_SACPA

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 site278-280NAD+ (UniProtKB | ChEBI)
Binding site328-330NAD+ (UniProtKB | ChEBI)
Binding site330K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners; in other chain
Binding site332K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners; in other chain
Binding site333IMP (UniProtKB | ChEBI)
Active site335Thioimidate intermediate
Binding site335K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners; in other chain
Binding site368-370IMP (UniProtKB | ChEBI)
Binding site391-392IMP (UniProtKB | ChEBI)
Binding site415-419IMP (UniProtKB | ChEBI)
Active site437Proton acceptor
Binding site449IMP (UniProtKB | ChEBI)
Binding site504K+ (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

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
      IMD
    • ORF names
      SPAR_A00010

Organism names

Accessions

  • Primary accession
    A0A8B8UKT0

Organism-specific databases

Subcellular Location

Keywords

Interaction

Subunit

Homotetramer.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain121-183CBS
Domain184-240CBS

Sequence similarities

Belongs to the IMPDH/GMPR family.

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    523
  • Mass (Da)
    56,499
  • Last updated
    2022-01-19 v1
  • Checksum
    CA58BE61E9A8D819
MAAIKDYETALQFAKSLPRLDGLSVQELMDSKIRGGLTYNDFLILPGLVDFASSEVSLQTKLTRNITLNIPLVSSPMDTVTESEMAIFMALSGGIGFIHHNCTPEDQADMVRRVKNYENGFINNPIVISPTTTVGEAKSMKKKYGFAGFPVTEDGKRNAKLVGVITSRDIQFVEDDSLLVQDVMTKNPVTGAQGITLSEGNEILKKIKKGRLLIVDEKGKLVSMLSRTDLMKNQNYPLASKSANTKQLLCGASIGTMDADKERLRLLVKAGLDVVILDSSQGNSIFQLNMLKWVKESFAGLEVIAGNVVTREQAANLIAAGADGLRIGMGTGSICITQEVMACGRPQGTAVYNVCEFANQFGVPCMADGGVQNIGHITKALALGSSTVMMGGMLAGTTESPGEYFYQDGKRLKAYRGMGSIDAMQKTGTKGNASTSRYFSEFDSVLVAQGVSGAVVDKGSIKKFIPYLYNGLQHSCQDIGCRSLTLLKKNVQSGKVRFEFRTASAQLEGGVNNLHSYEKRLHN

Sequence databases

Genome annotation databases

Similar Proteins

Disclaimer

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