A0A2T9QCR3 · A0A2T9QCR3_SALET

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

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 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
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
      guaB
    • ORF names
      A8D33_04050
      , APX06_03970
      , BGP46_06405
      , C3N96_17580
      , CGD37_02160
      , D4F32_14070
      , DQ894_16280
      , E4904_05865
      , G3454_001398
      , G4A16_001960
      , G4Y54_000303

Organism names

  • Taxonomic identifier
  • Strains
    • 449466
    • 532482
    • 579255
    • 11-0573
    • 11-7712
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > Salmonella

Accessions

  • Primary accession
    A0A2T9QCR3

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)
    51,948
  • Last updated
    2018-07-18 v1
  • Checksum
    CDA4AE8D1B646010
MLRIAKEALTFDDVLLVPAHSTVLPNTADLSTQLTKTIRLNIPMLSAAMDTVTEARLAIALAQEGGIGFIHKNMSIERQAEEVRRVKKHESGVVTDPQTVLPTTTLHEVKALTERNGFAGYPVVTEDNELVGIITGRDVRFVTDLNQPVSVYMTPKERLVTVREGEAREVVLAKMHEKRVEKALVVDDNFHLLGMITVKDFQKAERKPNSCKDEQGRLRVGAAVGAGAGNEERVDALVAAGVDVLLIDSSHGHSEGVLQRIRETRAKYPDLQIIGGNVATGAGARALAEAGCSAVKVGIGPGSICTTRIVTGVGVPQITAVSDAVEALEGTGIPVIADGGIRFSGDIAKAIAAGASAVMVGSMLAGTEESPGEIELYQGRSYKSYRGMGSLGAMSKGSSDRYFQSDNAADKLVPEGIEGRVAYKGRLKEIIHQQMGGLRSCMGLTGCATIDELRTKAEFVRISGAGIQESHVHDVTITKESPNYRLGS

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AAHHQO010000019
EMBL· GenBank· DDBJ
EBW1954633.1
EMBL· GenBank· DDBJ
Genomic DNA
AAHKKG010000019
EMBL· GenBank· DDBJ
EBX1653771.1
EMBL· GenBank· DDBJ
Genomic DNA
AAHNXN010000016
EMBL· GenBank· DDBJ
EBY3765736.1
EMBL· GenBank· DDBJ
Genomic DNA
AAKIXF010000003
EMBL· GenBank· DDBJ
ECS2241214.1
EMBL· GenBank· DDBJ
Genomic DNA
AAKJYZ010000004
EMBL· GenBank· DDBJ
ECS5568834.1
EMBL· GenBank· DDBJ
Genomic DNA
AAKOHZ010000002
EMBL· GenBank· DDBJ
ECT9247402.1
EMBL· GenBank· DDBJ
Genomic DNA
AAKQSY010000003
EMBL· GenBank· DDBJ
ECU6928232.1
EMBL· GenBank· DDBJ
Genomic DNA
DAAROJ010000005
EMBL· GenBank· DDBJ
HAE3194288.1
EMBL· GenBank· DDBJ
Genomic DNA
DAARSL010000010
EMBL· GenBank· DDBJ
HAE3752207.1
EMBL· GenBank· DDBJ
Genomic DNA
DAATOQ010000002
EMBL· GenBank· DDBJ
HAE8893907.1
EMBL· GenBank· DDBJ
Genomic DNA
SRAQ01000003
EMBL· GenBank· DDBJ
KAA7286587.1
EMBL· GenBank· DDBJ
Genomic DNA

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