A0A317CPJ1 · A0A317CPJ1_9GAMM
- ProteinInosine-5'-monophosphate dehydrogenase
- GeneguaB
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids486 (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) | ||||
Sequence: D | ||||||
Binding site | 247-249 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: DTA | ||||||
Binding site | 297-299 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: GIG | ||||||
Binding site | 299 | K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners; in other chain | ||||
Sequence: G | ||||||
Binding site | 301 | K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners; in other chain | ||||
Sequence: G | ||||||
Binding site | 302 | IMP (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Active site | 304 | Thioimidate intermediate | ||||
Sequence: C | ||||||
Binding site | 304 | K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners; in other chain | ||||
Sequence: C | ||||||
Binding site | 337-339 | IMP (UniProtKB | ChEBI) | ||||
Sequence: DGG | ||||||
Binding site | 360-361 | IMP (UniProtKB | ChEBI) | ||||
Sequence: GS | ||||||
Binding site | 384-388 | IMP (UniProtKB | ChEBI) | ||||
Sequence: YRGMG | ||||||
Active site | 400 | 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 | |
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 > Gammaproteobacteria > Thiotrichales > Thiotrichaceae > Leucothrix
Accessions
- Primary accessionA0A317CPJ1
Proteomes
Interaction
Subunit
Homotetramer.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 92-148 | CBS | ||||
Sequence: IIKDPYTVTADTSVREVIELTAKRRISGVPVIAGDNDLVGIVTSRDLRFETNHDQPV | ||||||
Domain | 152-213 | CBS | ||||
Sequence: MTAKDKLITVKEGTEREEVLRLLHQNRIEKILVVDDSFKLRGLITVKDIQKSSDFPNACKDE |
Sequence similarities
Belongs to the IMPDH/GMPR family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length486
- Mass (Da)51,550
- Last updated2018-10-10 v1
- Checksum56E1EF465F4D1A1A
Keywords
- Technical term