A0A5C6NCU4 · A0A5C6NCU4_9TELE

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 site374-376NAD+ (UniProtKB | ChEBI)
Binding site424-426NAD+ (UniProtKB | ChEBI)
Binding site426K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners; in other chain
Binding site428K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners; in other chain
Binding site429IMP (UniProtKB | ChEBI)
Active site431Thioimidate intermediate
Binding site431K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners; in other chain
Binding site464-466IMP (UniProtKB | ChEBI)
Binding site487-488IMP (UniProtKB | ChEBI)
Binding site511-515IMP (UniProtKB | ChEBI)
Active site529Proton acceptor
Binding site541IMP (UniProtKB | ChEBI)
Binding site596K+ (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
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

    • Name
      IMPDH
    • ORF names
      D4764_22G0003650

Organism names

  • Taxonomic identifier
  • Strain
    • HTHZ2018
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Actinopterygii > Neopterygii > Teleostei > Neoteleostei > Acanthomorphata > Eupercaria > Tetraodontiformes > Tetradontoidea > Tetraodontidae > Takifugu

Accessions

  • Primary accession
    A0A5C6NCU4

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Homotetramer.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain214-275CBS
Domain279-337CBS

Sequence similarities

Belongs to the IMPDH/GMPR family.

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    614
  • Mass (Da)
    66,366
  • Last updated
    2019-11-13 v1
  • Checksum
    15C02D289D1EE344
MEGYGYEHFGADGALESQQADYRRIVGEAQPPRTPASSRDHEHFVRQTSHGHGHETAAQRYSATRVQAGLGPESMADYLISGGTGYVPDDGLSAQQLFSIGDGLTYKSDQQCVVSDGHTAEELCSKGDGLTYNDFLILPGFIDFTADEVDLTSALTRKITLKTPLISSPMDTVTESAMAIAMALMGGIGIIHHNCTPEFQANEVRKVKRFEQGFITDPVVMSPRHTVKDVVEAKTRHGFSGIPITETGKMGSKLVGIVTSRDIDFLSEKDHNKPLEEAMTKREDLVVAPAGVTLKEANDILQRSKKGKLPIVNNNDELVAIIARTDLKKNRDYPLASKDSRKQLLCGAAIGTRDDDKYRLDLLVQAGVDMVVLDSSQGNSVFQIGMINYIKQKYGDLQVVGGNVVTAAQAKNLIDAGVDALRVGMGCGSICITQEVMACGRPQGTSVYKVAEYARRFGVPVIADGGIQTVGHVVKALSLGASTVMMGSLLAATTEAPGEYFFADGVRLKKYRGMGSLDAMEKSTSSQKRYFSEGDKVKVAQGVSGSVQDKGSIHKFVPYLIAGIQHGCQDIGAKSLSILRSMMYSGELKFEKRTMSAQVEGGVHGLHSYEKRLY

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
RHFK02000015
EMBL· GenBank· DDBJ
TWW64718.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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