A0A6M8UH63 · A0A6M8UH63_9GAMM
- ProteinInosine-5'-monophosphate dehydrogenase
- GeneguaB
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids488 (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
- H2O + IMP + NAD+ = H+ + NADH + XMP
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 | 248-250 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: DSS | ||||||
Binding site | 298-300 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: GIG | ||||||
Binding site | 300 | K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners; in other chain | ||||
Sequence: G | ||||||
Binding site | 302 | K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners; in other chain | ||||
Sequence: G | ||||||
Binding site | 303 | IMP (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Active site | 305 | Thioimidate intermediate | ||||
Sequence: C | ||||||
Binding site | 305 | K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners; in other chain | ||||
Sequence: C | ||||||
Binding site | 338-340 | IMP (UniProtKB | ChEBI) | ||||
Sequence: DGG | ||||||
Binding site | 361-362 | IMP (UniProtKB | ChEBI) | ||||
Sequence: GS | ||||||
Binding site | 385-389 | IMP (UniProtKB | ChEBI) | ||||
Sequence: YRGMG | ||||||
Active site | 401 | Proton acceptor | ||||
Sequence: R | ||||||
Binding site | 415 | IMP (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 469 | K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners | ||||
Sequence: E | ||||||
Binding site | 470 | K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners | ||||
Sequence: S | ||||||
Binding site | 471 | K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners | ||||
Sequence: H |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | IMP dehydrogenase activity | |
Molecular Function | metal ion binding | |
Molecular Function | nucleotide binding | |
Biological Process | GMP 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 > Gammaproteobacteria > Enterobacterales > Erwiniaceae
Accessions
- Primary accessionA0A6M8UH63
Proteomes
Interaction
Subunit
Homotetramer.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 93-149 | CBS | ||||
Sequence: VVTDPQTVLPDTPLQEVKALTERNGFAGYPVVNSDNELVGIITGRDVRFVTDMSLPV | ||||||
Domain | 153-214 | CBS | ||||
Sequence: MTPKERLVTVKEGEARDIVLQKMHEKRVEKALVVDDSFHLLGMITVKDFQKAERKPHACKDE |
Sequence similarities
Belongs to the IMPDH/GMPR family.
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusComplete
- Length488
- Mass (Da)51,522
- Last updated2020-10-07 v1
- ChecksumA30C91D11CEA1F97
Keywords
- Technical term