A1KU15 · A1KU15_NEIMF

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 site248NAD+ (UniProtKB | ChEBI)
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 site416IMP (UniProtKB | ChEBI)
Binding site470K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners
Binding site471K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners
Binding site472K+ (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
      NMC1103

Organism names

Accessions

  • Primary accession
    A1KU15

Proteomes

Interaction

Subunit

Homotetramer.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain92-149CBS
Domain153-214CBS

Sequence similarities

Belongs to the IMPDH/GMPR family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    487
  • Mass (Da)
    52,325
  • Last updated
    2007-02-06 v1
  • Checksum
    B494AF8D42A54F92
MRIVEKAYTFDDVLLVPAHSTVLPRDVKLQTKLTREITLNLPLLSAAMDTVTEARLAISMAQEGGIGIIHKNMPPEMQARAVSKVKRHESGVVKDPVTVAPTTLIREVLEMRAQRKRKMSGLPVVENGKVVGIVTNRDLRFENRVDLPVSAIMTPRERLVTVPEGTSIDEARELMHTHKVERVLVLNEKDELKGLITVKDILKTTEFPNANKDSEGRLRVGAAVGTGGDTEERVKALVEAGVDVIVVDTAHGHSQGVIDRVKWVKETYPHIQVIGGNIATAKAALDLVAAGADAVKVGIGPGSICTTRIVAGVGVPQLTAIHNVAEALKGTGVPLIADGGIRFSGDIAKALAAGAYSVMLGGMFAGTEEAPGEIELYQGRSYKSYRGMGSLGAMSQGSADRYFQDKTDSADKYVPEGIEGRVPYKGPIVNIIHQLTGGLRSSMGYLGCANIAEMHEKAEFVEITSAGMSESHVHDVQITKEAPNYHR

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AM421808
EMBL· GenBank· DDBJ
CAM10356.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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