Q03CJ2 · Q03CJ2_LACP3

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.

Type
IDPosition(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 site408Proton acceptor
Binding site423IMP (UniProtKB | ChEBI)
Binding site477K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners
Binding site478K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners
Binding site479K+ (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
    • Ordered locus names
      LSEI_0217

Organism names

Accessions

  • Primary accession
    Q03CJ2

Proteomes

PTM/Processing

Proteomic databases

Interaction

Subunit

Homotetramer.

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain97-157CBS
Domain159-216CBS

Sequence similarities

Belongs to the IMPDH/GMPR family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    495
  • Mass (Da)
    52,641
  • Last updated
    2006-11-14 v1
  • Checksum
    2A20BA7F023723F4
MSLWDTKFARRGFTFDDVLLIPAESHVLPHDVDLSVQLADNLKLNIPIISAGMDTVTESAMAIAMARQGGLGVIHKNMSIEAQADEVLKVKRSENGVIVDPFFLTADKPVSDAEDLMKKYRISGVPIVNNTTDRKLTGIITNRDLRYVDDKSVLIDTVMTKEGLVTAPAGTSIEDAEAILQSRKIEKLPLIDKEGRLSGLITIKDIEKVVEFPHAAKDAHGRLLVAAAVGVTSDTFDRAQALLDAGADAIVIDTAHGHSAGVIRKIKEIREQFPLATLIAGNVATAEATEALYDAGVDVVKVGIGPGSICTTRIVAGVGVPQLTAIYDAASVARKRGKTIIADGGIKYSGDIVKALAAGGNAVMLGSLLAGTDEAPGQFEIYQGRRFKTYRGMGSLGAMAQAHGSSDRYFQSGVNEANKLVPEGIEGRVAYKGSLGDVIFQMLGGIESGMGYVGAPNLQELQDNAQFIQITGAGLRESHPHDVQITREAPNYSVQ

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP000423
EMBL· GenBank· DDBJ
ABJ69080.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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