U9U2A7 · U9U2A7_RHIID
- ProteinInosine-5'-monophosphate dehydrogenase
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids549 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
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.
Catalytic activity
- IMP + NAD+ + H2O = XMP + NADH + H+
Cofactor
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 | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 299-301 | NAD+ (UniProtKB | ChEBI) | |||
Binding site | 350-352 | NAD+ (UniProtKB | ChEBI) | |||
Binding site | 352 | K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners; in other chain | |||
Binding site | 354 | K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners; in other chain | |||
Binding site | 355 | IMP (UniProtKB | ChEBI) | |||
Active site | 357 | Thioimidate intermediate | |||
Binding site | 357 | K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners; in other chain | |||
Binding site | 390-392 | IMP (UniProtKB | ChEBI) | |||
Binding site | 413-414 | IMP (UniProtKB | ChEBI) | |||
Binding site | 437-441 | IMP (UniProtKB | ChEBI) | |||
Active site | 463 | Proton acceptor | |||
Binding site | 475 | IMP (UniProtKB | ChEBI) | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | IMP dehydrogenase activity | |
Molecular Function | metal ion binding | |
Molecular Function | nucleotide binding | |
Biological Process | GMP biosynthetic process | |
Biological Process | GTP biosynthetic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameInosine-5'-monophosphate dehydrogenase
- EC number
- Short namesIMP dehydrogenase ; IMPD ; IMPDH
Gene names
Organism names
- Strains
- Taxonomic lineageEukaryota > Fungi > Fungi incertae sedis > Mucoromycota > Glomeromycotina > Glomeromycetes > Glomerales > Glomeraceae > Rhizophagus
Accessions
- Primary accessionU9U2A7
Proteomes
Organism-specific databases
Subcellular Location
Interaction
Structure
Family & Domains
Features
Showing features for region, domain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Region | 1-23 | Disordered | |||
Domain | 142-204 | CBS | |||
Domain | 205-261 | CBS | |||
Sequence similarities
Belongs to the IMPDH/GMPR family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length549
- Mass (Da)59,184
- Last updated2014-01-22 v1
- Checksum2D86C44B11D16FFF
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
KI282848 EMBL· GenBank· DDBJ | ESA14499.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AUPC02000146 EMBL· GenBank· DDBJ | POG68831.1 EMBL· GenBank· DDBJ | Genomic DNA |