A0A2N7B7M3 · A0A2N7B7M3_9BACT
- ProteinInosine-5'-monophosphate dehydrogenase
- GeneguaB
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids489 (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 | 250 | NAD+ (UniProtKB | ChEBI) | |||
Binding site | 250-252 | NAD+ (UniProtKB | ChEBI) | |||
Binding site | 300-302 | NAD+ (UniProtKB | ChEBI) | |||
Binding site | 302 | K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners; in other chain | |||
Binding site | 304 | K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners; in other chain | |||
Binding site | 305 | IMP (UniProtKB | ChEBI) | |||
Active site | 307 | Thioimidate intermediate | |||
Binding site | 307 | K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners; in other chain | |||
Binding site | 340-342 | IMP (UniProtKB | ChEBI) | |||
Binding site | 363-364 | IMP (UniProtKB | ChEBI) | |||
Binding site | 387-391 | IMP (UniProtKB | ChEBI) | |||
Active site | 403 | Proton acceptor | |||
Binding site | 418 | IMP (UniProtKB | ChEBI) | |||
Binding site | 471 | K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners | |||
Binding site | 472 | K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners | |||
Binding site | 473 | 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 > Bacteroidota > Cytophagia > Cytophagales > Cytophagaceae > Siphonobacter
Accessions
- Primary accessionA0A2N7B7M3
Proteomes
Interaction
Subunit
Homotetramer.
Structure
Sequence
- Sequence statusComplete
- Length489
- Mass (Da)51,975
- Last updated2018-04-25 v1
- Checksum257BA05B6626818B
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
NJAG01000027 EMBL· GenBank· DDBJ | PMD93562.1 EMBL· GenBank· DDBJ | Genomic DNA |