A0A218P048 · A0A218P048_THECE

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 site248NAD+ (UniProtKB | ChEBI)
Binding site248-250NAD+ (UniProtKB | ChEBI)
Binding site295-297NAD+ (UniProtKB | ChEBI)
Binding site297K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners; in other chain
Binding site299K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners; in other chain
Binding site300IMP (UniProtKB | ChEBI)
Active site302Thioimidate intermediate
Binding site302K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners; in other chain
Binding site335-337IMP (UniProtKB | ChEBI)
Binding site358-359IMP (UniProtKB | ChEBI)
Binding site382-386IMP (UniProtKB | ChEBI)
Active site398Proton acceptor
Binding site413IMP (UniProtKB | ChEBI)
Binding site467K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners
Binding site468K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners
Binding site469K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners

GO annotations

AspectTerm
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
      guaB
    • ORF names
      A3L02_01325

Organism names

Accessions

  • Primary accession
    A0A218P048

Proteomes

Interaction

Subunit

Homotetramer.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain99-156CBS
Domain157-213CBS

Sequence similarities

Belongs to the IMPDH/GMPR family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    486
  • Mass (Da)
    52,078
  • Last updated
    2017-09-27 v1
  • Checksum
    3A207A9059B9BB4A
MGKFEHKLVNALRGYTFDDVLLIPQATEVEPKEVDVSTRITPNVKLNVPVLSAAMDTVTEWEMAVAMAREGGLGVIHRNMSVAEQVEMVRKVKRAERFIVEDVITVGPGETLDYALFLMERNDVDGLPVVDENGRIAGIITKEDIAAKEGSRVRDVMTGEVITVDENVSVEEALETMVSRRVSRLPVVDGDGKLVGIITMSDLTRRKKYRNAVRDANGDLIVAAAVGPFDIERAKALDRAGADVIVVDTAHAHNLKAIRAMKEIRKAVDADLIVGNVANPKAVDDLTFADAVKVGIGPGSICTTRVVAGVGVPQVTAIALVADRAGEYGLHVIADGGIRYSGDIVKAIAAGADAVMLGSLLAGTKEAPGKEVVINGRRYKTYRGMGSLGAMMKGGAERYYQKGHMKTGKFVPEGVEGVVPYRGSVGEVLYQLVGGLRSGMGYVGARNIAELKERGEFVIITQAGVRESHPHDITITNEAPNYPLGR

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP014854
EMBL· GenBank· DDBJ
ASI98301.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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