A0A1L8U1J3 · A0A1L8U1J3_ENTGA

  • 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.

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 site253NAD+ (UniProtKB | ChEBI)
Binding site253-255NAD+ (UniProtKB | ChEBI)
Binding site303-305NAD+ (UniProtKB | ChEBI)
Binding site305K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners; in other chain
Binding site307K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners; in other chain
Binding site308IMP (UniProtKB | ChEBI)
Active site310Thioimidate intermediate
Binding site310K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners; in other chain
Binding site343-345IMP (UniProtKB | ChEBI)
Binding site366-367IMP (UniProtKB | ChEBI)
Binding site390-394IMP (UniProtKB | ChEBI)
Active site406Proton acceptor
Binding site421IMP (UniProtKB | ChEBI)
Binding site475K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners
Binding site476K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners
Binding site477K+ (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
      EGM181_18125
      , HZY99_18410
      , NCTC12360_02233
      , P7E30_15335

Organism names

  • Taxonomic identifier
  • Organism
  • Strains
    • NCTC12360
    • EGM181
    • ENT
    • K69-2
  • Taxonomic lineage
    Bacteria > Bacillota > Bacilli > Lactobacillales > Enterococcaceae > Enterococcus

Accessions

  • Primary accession
    A0A1L8U1J3

Proteomes

Interaction

Subunit

Homotetramer.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain97-155CBS
Domain159-219CBS

Sequence similarities

Belongs to the IMPDH/GMPR family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    494
  • Mass (Da)
    52,732
  • Last updated
    2017-03-15 v1
  • Checksum
    0A44138FBC872E31
MSNWETKFVKKGLTFDDVLLIPAESHVLPNDVDMHVQLAKNITLNIPIMSASMDTVTDSKMAISMARQGGLGVIHKNMSIAAQADEVRKVKRSESGVIIDPFFLTPSHLVADAEHLMSKYRISGVPIVETMENRKLVGIITNRDMRFVTDYSIAISDVMTKEKLVTAPVGTSLKDAEKILQKHKIEKLPIVDDEGILSGLITIKDIEKVIEFPNAAKDTHGRLLVAAAVGVTSDTFERAQALLDAGADAIVIDTAHGHSAGVLRKISEIRAHFPEATLIAGNVATAEGTKALYDAGVDVVKVGIGPGSICTTRVVAGVGVPQLTAIYDAASVARQYGKAIIADGGIKYSGDIVKALAAGGHAVMLGSMLAGTDESPGEFEIYQGRRFKTYRGMGSLGAMEKGSSDRYFQGGVNEANKLVPEGIEGRVAYKGSVADILFQMIGGLKSGMGYVGAANLKQLRDEAQFIQMSGNGLKESHPHDVQITKEAPNYSVKS

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
JARPZN010000016
EMBL· GenBank· DDBJ
MDT2691550.1
EMBL· GenBank· DDBJ
Genomic DNA
JACBYD010000117
EMBL· GenBank· DDBJ
NYS84096.1
EMBL· GenBank· DDBJ
Genomic DNA
CP050485
EMBL· GenBank· DDBJ
QOG29036.1
EMBL· GenBank· DDBJ
Genomic DNA
UFYW01000001
EMBL· GenBank· DDBJ
STD83747.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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