A0AA35RHE1 · A0AA35RHE1_GEOBA

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 site284NAD+ (UniProtKB | ChEBI)
Binding site284-286NAD+ (UniProtKB | ChEBI)
Binding site334-336NAD+ (UniProtKB | ChEBI)
Binding site336K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners; in other chain
Binding site338K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners; in other chain
Binding site339IMP (UniProtKB | ChEBI)
Active site341Thioimidate intermediate
Binding site341K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners; in other chain
Binding site374-376IMP (UniProtKB | ChEBI)
Binding site397-398IMP (UniProtKB | ChEBI)
Binding site505K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners
Binding site506K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners
Binding site507K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners

GO annotations

AspectTerm
Cellular Componentcytoplasm
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

    • ORF names
      GBAR_LOCUS7427

Organism names

Accessions

  • Primary accession
    A0AA35RHE1

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Homotetramer.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain130-186CBS
Domain190-251CBS

Sequence similarities

Belongs to the IMPDH/GMPR family.

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    527
  • Mass (Da)
    56,880
  • Last updated
    2024-01-24 v1
  • Checksum
    9F93CD01AC115AC9
MGHRKRCYYTSFLNLSYPSQPAMKETILMETKISDVFPPRFAKEGLTFDDVLLIPAESDVLPDQVDTGTQLTRNLRLNIPICSAPMDTVTESILAIAIAREGGIGIIHYNCPIDEQVSEVDRVKRSESGMITAPITLTQDKTIRDALQITERYRIGGVPIVTEDGYLVGLITNRDLKYENNLELPVTARMTPGKELITASPGITLDKAKEVLHKSRKEKLPIVDEDFRLCGLITIKDIDKVQMFPQACKDTAGRLCVGAAVLPSTPLEHVDRLVAAGVDVLVLDTAHGHSKNVIRSTEYIKSHFPDVELVAGNVVTPEGTRSLIDAGADAVKVGVGPGSICTTRVVAGVSIPQITAIYDCAQEADKAGVPIIADGGIRYSGDIAKAIGAGASSVMIGSLLAGTDESPGDTVIYQGRTYKIHRGMGSLGALRKRSAQLSEESSEDISKLVPRGIEGRVPHKGKLSSFVYQLVGGIRSAMGYCGASDIEALRRDSQFVRMSSSGYRESHPHDIDITEEAPNYTVAHLSP

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CASHTH010001108
EMBL· GenBank· DDBJ
CAI8011525.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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