Q2GHN8 · Q2GHN8_EHRCR
- ProteinInosine-5'-monophosphate dehydrogenase
- GeneguaB
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids485 (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 | 247 | NAD+ (UniProtKB | ChEBI) | |||
Binding site | 247-249 | NAD+ (UniProtKB | ChEBI) | |||
Binding site | 297-299 | NAD+ (UniProtKB | ChEBI) | |||
Binding site | 299 | K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners; in other chain | |||
Binding site | 301 | K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners; in other chain | |||
Binding site | 302 | IMP (UniProtKB | ChEBI) | |||
Active site | 304 | Thioimidate intermediate | |||
Binding site | 304 | K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners; in other chain | |||
Binding site | 337-339 | IMP (UniProtKB | ChEBI) | |||
Binding site | 360-361 | IMP (UniProtKB | ChEBI) | |||
Binding site | 384-388 | IMP (UniProtKB | ChEBI) | |||
Active site | 400 | Proton acceptor | |||
Binding site | 412 | IMP (UniProtKB | ChEBI) | |||
Binding site | 466 | K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners | |||
Binding site | 467 | K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners | |||
Binding site | 468 | K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners | |||
GO annotations
Aspect | Term | |
---|---|---|
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
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Alphaproteobacteria > Rickettsiales > Anaplasmataceae > Ehrlichia
Accessions
- Primary accessionQ2GHN8
Proteomes
Interaction
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Domain | 89-151 | CBS | |||
Domain | 152-212 | CBS | |||
Sequence similarities
Belongs to the IMPDH/GMPR family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length485
- Mass (Da)52,197
- Last updated2006-03-21 v1
- Checksum83938A6F06AB35B0
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP000236 EMBL· GenBank· DDBJ | ABD44834.1 EMBL· GenBank· DDBJ | Genomic DNA |