A0AAJ3UW33 · A0AAJ3UW33_9HYPH
- ProteinInosine-5'-monophosphate dehydrogenase
- GeneguaB
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids494 (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 | 252 | NAD+ (UniProtKB | ChEBI) | |||
Binding site | 252-254 | NAD+ (UniProtKB | ChEBI) | |||
Binding site | 302-304 | NAD+ (UniProtKB | ChEBI) | |||
Binding site | 304 | K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners; in other chain | |||
Binding site | 306 | K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners; in other chain | |||
Binding site | 307 | IMP (UniProtKB | ChEBI) | |||
Active site | 309 | Thioimidate intermediate | |||
Binding site | 309 | K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners; in other chain | |||
Binding site | 342-344 | IMP (UniProtKB | ChEBI) | |||
Binding site | 365-366 | IMP (UniProtKB | ChEBI) | |||
Binding site | 389-393 | IMP (UniProtKB | ChEBI) | |||
Active site | 405 | Proton acceptor | |||
Binding site | 420 | IMP (UniProtKB | ChEBI) | |||
Binding site | 474 | K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners | |||
Binding site | 475 | K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners | |||
Binding site | 476 | 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
- Organism
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Alphaproteobacteria > Hyphomicrobiales > Rhizobiaceae > Rhizobium/Agrobacterium group > Rhizobium
Accessions
- Primary accessionA0AAJ3UW33
Proteomes
Interaction
Subunit
Homotetramer.
Structure
Sequence
- Sequence statusComplete
- Length494
- Mass (Da)52,100
- Last updated2024-07-24 v1
- Checksum5224AF00282FDE55
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
NWSU01000026 EMBL· GenBank· DDBJ | PDS94545.1 EMBL· GenBank· DDBJ | Genomic DNA |