M7WKZ4 · M7WKZ4_RHOT1
- ProteinInosine-5'-monophosphate dehydrogenase
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids531 (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 | 278-280 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: DSS | ||||||
Binding site | 328-330 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: GMG | ||||||
Binding site | 330 | K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners; in other chain | ||||
Sequence: G | ||||||
Binding site | 332 | K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners; in other chain | ||||
Sequence: G | ||||||
Binding site | 333 | IMP (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Active site | 335 | Thioimidate intermediate | ||||
Sequence: C | ||||||
Binding site | 335 | K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners; in other chain | ||||
Sequence: C | ||||||
Binding site | 368-370 | IMP (UniProtKB | ChEBI) | ||||
Sequence: DGG | ||||||
Binding site | 391-392 | IMP (UniProtKB | ChEBI) | ||||
Sequence: GG | ||||||
Binding site | 415-419 | IMP (UniProtKB | ChEBI) | ||||
Sequence: YRGMG | ||||||
Active site | 445 | Proton acceptor | ||||
Sequence: R | ||||||
Binding site | 457 | IMP (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 512 | K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners | ||||
Sequence: S |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
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 lineageEukaryota > Fungi > Dikarya > Basidiomycota > Pucciniomycotina > Microbotryomycetes > Sporidiobolales > Sporidiobolaceae > Rhodotorula
Accessions
- Primary accessionM7WKZ4
Proteomes
Subcellular Location
Interaction
Subunit
Homotetramer.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 120-180 | CBS | ||||
Sequence: FITDPICLTPKNTVADVWAIKEKHGFCGIPITDSGKLGGKLLGIVTGRDIQFRPNSASLES | ||||||
Domain | 182-240 | CBS | ||||
Sequence: MTQGADLVTGPAGITLEQANDILRDSKKGKLPLVDKEGRLVALLARSDLLKNKDYPLAS |
Sequence similarities
Belongs to the IMPDH/GMPR family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length531
- Mass (Da)56,894
- Last updated2013-05-29 v1
- ChecksumB1C982E669A5544A
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
KB722679 EMBL· GenBank· DDBJ | EMS18515.1 EMBL· GenBank· DDBJ | Genomic DNA |