A0A355Q2K0 · A0A355Q2K0_UNCDE

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.
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 site249NAD+ (UniProtKB | ChEBI)
Binding site249-251NAD+ (UniProtKB | ChEBI)
Binding site299-301NAD+ (UniProtKB | ChEBI)
Binding site301K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners; in other chain
Binding site303K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners; in other chain
Binding site304IMP (UniProtKB | ChEBI)
Active site306Thioimidate intermediate
Binding site306K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners; in other chain
Binding site339-341IMP (UniProtKB | ChEBI)
Binding site362-363IMP (UniProtKB | ChEBI)
Binding site386-390IMP (UniProtKB | ChEBI)
Active site402Proton 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
    • ORF names
      DDZ97_01295

Organism names

Accessions

  • Primary accession
    A0A355Q2K0

Proteomes

Interaction

Subunit

Homotetramer.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain94-149CBS
Domain153-212CBS

Sequence similarities

Belongs to the IMPDH/GMPR family.

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    491
  • Mass (Da)
    53,179
  • Last updated
    2018-11-07 v1
  • Checksum
    517FCAE4331004B6
MLQNRITEGLTFDDVLLVPAYSDILPHEVSVQTRLTRHLDCNIPLLSAAMDTVTEHQVAISMAQEGGLGVIHKNMSVEEQAAQVDRVKRSESGMISDPITVEPEQPLKDALQLMERYRISGVPVTRGTELVGILTNRDLRFETNLDQKVGSVMTSGRDRLVTVSPGIDLEEAKTLLHAHRIEKLLVVSEGYDLLGLITIKDIEKSRKYPNANKDDRGRLRVGAAVSTSRDLMERTAALISKGVDLVVLDTAHGHSSKVLQSIRELRETFPELEIVAGNIATASGCEALIKAGVDAVKIGIGPGSICTTRVVAGIGVPQITAISESASVARRYGIPVIADGGIKYSGDIVKALAAGADSVMIGSLFAGTAETPGQVILYQGRRYKLYRGMGSMGAMKEGSKDRYFQNNIEESKLVPEGIEGRVPFKGSLAEMVYQFVGGLRSGMGYTGCRNITELQEQAQFVRITSAGLRESHVHDVLITEEAPNYPISQVE

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
DNZT01000034
EMBL· GenBank· DDBJ
HBM51707.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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