A0A6I8P4R8 · A0A6I8P4R8_ORNAN

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. Could also have a single-stranded nucleic acid-binding activity and could play a role in RNA and/or DNA metabolism. It may also have a role in the development of malignancy and the growth progression of some tumors.

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 site325-327NAD+ (UniProtKB | ChEBI)
Binding site375-377NAD+ (UniProtKB | ChEBI)
Binding site377K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners; in other chain
Binding site379K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners; in other chain
Binding site380IMP (UniProtKB | ChEBI)
Active site382Thioimidate intermediate
Binding site382K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners; in other chain
Binding site415-417IMP (UniProtKB | ChEBI)
Binding site438-439IMP (UniProtKB | ChEBI)
Binding site462-466IMP (UniProtKB | ChEBI)
Active site480Proton acceptor
Binding site492IMP (UniProtKB | ChEBI)
Binding site547K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners

GO annotations

AspectTerm
Cellular Componentcytoplasm
Cellular Componentnucleus
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
      IMPDH1
    • Synonyms
      IMPDH

Organism names

Accessions

  • Primary accession
    A0A6I8P4R8

Proteomes

Subcellular Location

Keywords

Expression

Gene expression databases

Interaction

Subunit

Homotetramer.

Family & Domains

Features

Showing features for region, domain.

TypeIDPosition(s)Description
Region1-37Disordered
Domain165-224CBS
Domain230-288CBS

Sequence similarities

Belongs to the IMPDH/GMPR family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    565
  • Mass (Da)
    60,361
  • Last updated
    2020-08-12 v1
  • Checksum
    D74DAD8DC81350CA
MEGQGRGPAGGAGAAHPGPAPEPGAPQPPAHRTAGQRYSARLRSAGHEAESMADYLISGGTGYVPEDGLTAQQLFAIADGLTYNDFLILPGFIDFTADEVDLTSALTRKITLKTPLISSPMDTVTEADMAIAMALMGGIGFIHHNCTPEFQANEVRKVKKFEQGFITDPVVLSPSHTVGDVLEAKARHGFSGIPITETGTMGSKLVGIVTSRDIDFLAEKDHATYLSEVMTRRTELVVAPAGVTLKEANEILQRSKKGKLPIVNDSDELVAIIARTDLKKNRDYPLASKDAHKQLLCGAAVGTREDDKYRLDLLTQAGTDVIVLDSSQGNSVYQIAMVHYIKQKYPQLQVIGGNVVTAAQAKNLIDAGVDGLRVGMGCGSICITQEVMACGRPQGTAVYKVAEYARRFGVPVIADGGIQTVGHVVKALALGASTVMMGSLLAATTEAPGEYFFSDGVRLKKYRGMGSLDAMEKSSSSQKRYFSEGDKVKVAQGVSGSIQDKGSIQKFVPYLIAGIQHGCQDIGARSLSVLRSMMYSGELKFEKRTMSAQIEGGVHGLHSYEKRLY

Computationally mapped potential isoform sequences

There are 4 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
F6PLN7F6PLN7_ORNANIMPDH1571
A0A6I8PQP6A0A6I8PQP6_ORNANIMPDH1532
A0A6I8P9U5A0A6I8P9U5_ORNANIMPDH1489
F6PLM9F6PLM9_ORNANIMPDH1482

Keywords

Genome annotation databases

Similar Proteins

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