A0A1E4SV00 · A0A1E4SV00_9ASCO
- ProteinInosine-5'-monophosphate dehydrogenase
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids522 (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 | 277-279 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: DSS | ||||||
Binding site | 327-329 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: GMG | ||||||
Binding site | 329 | K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners; in other chain | ||||
Sequence: G | ||||||
Binding site | 331 | K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners; in other chain | ||||
Sequence: G | ||||||
Binding site | 332 | IMP (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Active site | 334 | Thioimidate intermediate | ||||
Sequence: C | ||||||
Binding site | 334 | K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners; in other chain | ||||
Sequence: C | ||||||
Binding site | 367-369 | IMP (UniProtKB | ChEBI) | ||||
Sequence: DGG | ||||||
Binding site | 390-391 | IMP (UniProtKB | ChEBI) | ||||
Sequence: GG | ||||||
Binding site | 414-418 | IMP (UniProtKB | ChEBI) | ||||
Sequence: YRGMG | ||||||
Active site | 436 | Proton acceptor | ||||
Sequence: R | ||||||
Binding site | 448 | IMP (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 503 | 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 |
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 > Ascomycota > Saccharomycotina > Saccharomycetes > Saccharomycetales > Pichiaceae > Ogataea > Ogataea/Candida clade
Accessions
- Primary accessionA0A1E4SV00
Proteomes
Subcellular Location
Interaction
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 120-181 | CBS | ||||
Sequence: FINDPIVISKEITVGQVKAMGEQFGFTSFPVTETGKVGGKLVGIVTSRDIQFHEDDSSSIAE | ||||||
Domain | 183-239 | CBS | ||||
Sequence: MTTDLVTGTAGVSLTDGNEILRKSKKGKLPIVDSEGNLVSMLSRTDLQKNLEFPHAS |
Sequence similarities
Belongs to the IMPDH/GMPR family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length522
- Mass (Da)56,018
- Last updated2017-01-18 v1
- Checksum791BE87EEE74C48F
Keywords
- Technical term