A0A218P048 · A0A218P048_THECE
- ProteinInosine-5'-monophosphate dehydrogenase
- GeneguaB
- StatusUniProtKB unreviewed (TrEMBL)
- 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
- 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 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 248-250 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: DTA | ||||||
Binding site | 295-297 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: GIG | ||||||
Binding site | 297 | K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners; in other chain | ||||
Sequence: G | ||||||
Binding site | 299 | K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners; in other chain | ||||
Sequence: G | ||||||
Binding site | 300 | IMP (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Active site | 302 | Thioimidate intermediate | ||||
Sequence: C | ||||||
Binding site | 302 | K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners; in other chain | ||||
Sequence: C | ||||||
Binding site | 335-337 | IMP (UniProtKB | ChEBI) | ||||
Sequence: DGG | ||||||
Binding site | 358-359 | IMP (UniProtKB | ChEBI) | ||||
Sequence: GS | ||||||
Binding site | 382-386 | IMP (UniProtKB | ChEBI) | ||||
Sequence: YRGMG | ||||||
Active site | 398 | Proton acceptor | ||||
Sequence: R | ||||||
Binding site | 413 | IMP (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 467 | K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners | ||||
Sequence: E | ||||||
Binding site | 468 | K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners | ||||
Sequence: S | ||||||
Binding site | 469 | 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
- Strain
- Taxonomic lineageArchaea > Euryarchaeota > Thermococci > Thermococcales > Thermococcaceae > Thermococcus
Accessions
- Primary accessionA0A218P048
Proteomes
Interaction
Subunit
Homotetramer.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 99-156 | CBS | ||||
Sequence: IVEDVITVGPGETLDYALFLMERNDVDGLPVVDENGRIAGIITKEDIAAKEGSRVRDV | ||||||
Domain | 157-213 | CBS | ||||
Sequence: MTGEVITVDENVSVEEALETMVSRRVSRLPVVDGDGKLVGIITMSDLTRRKKYRNAV |
Sequence similarities
Belongs to the IMPDH/GMPR family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length486
- Mass (Da)52,078
- Last updated2017-09-27 v1
- Checksum3A207A9059B9BB4A
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP014854 EMBL· GenBank· DDBJ | ASI98301.1 EMBL· GenBank· DDBJ | Genomic DNA |