A0A6M8UH63 · A0A6M8UH63_9GAMM

  • Protein
    Inosine-5'-monophosphate dehydrogenase
  • Gene
    guaB
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    3/5

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.

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 site248-250NAD+ (UniProtKB | ChEBI)
Binding site298-300NAD+ (UniProtKB | ChEBI)
Binding site300K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners; in other chain
Binding site302K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners; in other chain
Binding site303IMP (UniProtKB | ChEBI)
Active site305Thioimidate intermediate
Binding site305K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners; in other chain
Binding site338-340IMP (UniProtKB | ChEBI)
Binding site361-362IMP (UniProtKB | ChEBI)
Binding site385-389IMP (UniProtKB | ChEBI)
Active site401Proton acceptor
Binding site415IMP (UniProtKB | ChEBI)
Binding site469K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners
Binding site470K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners
Binding site471K+ (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
      PMPD1_3288

Organism names

Accessions

  • Primary accession
    A0A6M8UH63

Proteomes

Interaction

Subunit

Homotetramer.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain93-149CBS
Domain153-214CBS

Sequence similarities

Belongs to the IMPDH/GMPR family.

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    488
  • Mass (Da)
    51,522
  • Last updated
    2020-10-07 v1
  • Checksum
    A30C91D11CEA1F97
MLRIAKEALTFDDVLLVPAHSTVLPNTADLSTQLTKSIRLNIPMLSAAMDTVTEANLAIALAQEGGLGFIHKNMSIERQADEVRKVKKHESGVVTDPQTVLPDTPLQEVKALTERNGFAGYPVVNSDNELVGIITGRDVRFVTDMSLPVSAVMTPKERLVTVKEGEARDIVLQKMHEKRVEKALVVDDSFHLLGMITVKDFQKAERKPHACKDEHGRLRVGAAVGAGAGNEERVDALVAAGVDVLLIDSSHGHSEGVLQRIRETRAKYPDLQIVGGNVATGAGALALVEAGVSAVKVGIGPGSICTTRIVTGVGVPQITAVSDAVAALEGTGIPVIADGGIRFSGDIAKAIAAGAACVMVGSMLAGTEESPGEIELYQGRAFKSYRGMGSLGAMSKGSSDRYFQTDNAADKLVPEGIEGRVAYKGRLKEIVHQQMGGLRSCMGLTGCGTIDALRTKAEFVRISGAGISESHVHDVTITKESPNYRMGS

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP054212
EMBL· GenBank· DDBJ
QKJ88211.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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