A0AAD0WG50 · A0AAD0WG50_RALSL
- ProteinInosine-5'-monophosphate dehydrogenase
- GeneguaB
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids487 (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 | 246 | NAD+ (UniProtKB | ChEBI) | |||
Binding site | 246-248 | NAD+ (UniProtKB | ChEBI) | |||
Binding site | 296-298 | NAD+ (UniProtKB | ChEBI) | |||
Binding site | 298 | K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners; in other chain | |||
Binding site | 300 | K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners; in other chain | |||
Binding site | 301 | IMP (UniProtKB | ChEBI) | |||
Active site | 303 | Thioimidate intermediate | |||
Binding site | 303 | K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners; in other chain | |||
Binding site | 336-338 | IMP (UniProtKB | ChEBI) | |||
Binding site | 359-360 | IMP (UniProtKB | ChEBI) | |||
Binding site | 383-387 | IMP (UniProtKB | ChEBI) | |||
Active site | 399 | Proton acceptor | |||
Binding site | 415 | IMP (UniProtKB | ChEBI) | |||
Binding site | 469 | K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners | |||
Binding site | 470 | K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners | |||
Binding site | 471 | 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 > Betaproteobacteria > Burkholderiales > Burkholderiaceae > Ralstonia > Ralstonia solanacearum species complex
Accessions
- Primary accessionA0AAD0WG50
Proteomes
Interaction
Subunit
Homotetramer.
Structure
Sequence
- Sequence statusComplete
- Length487
- Mass (Da)52,078
- Last updated2024-05-29 v1
- MD5 Checksum92CF48C71F78FD984FEFDE22B227D3F6
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP022759 EMBL· GenBank· DDBJ | AXV81693.1 EMBL· GenBank· DDBJ | Genomic DNA |