A0AAP0G589 · A0AAP0G589_9ASPA
- ProteinInosine-5'-monophosphate dehydrogenase
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids502 (go to sequence)
- Protein existenceInferred from homology
- Annotation score2/5
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 | 264-266 | NAD+ (UniProtKB | ChEBI) | |||
Binding site | 314-316 | NAD+ (UniProtKB | ChEBI) | |||
Binding site | 316 | K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners; in other chain | |||
Binding site | 318 | K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners; in other chain | |||
Binding site | 319 | IMP (UniProtKB | ChEBI) | |||
Active site | 321 | Thioimidate intermediate | |||
Binding site | 321 | K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners; in other chain | |||
Binding site | 354-356 | IMP (UniProtKB | ChEBI) | |||
Binding site | 377-378 | IMP (UniProtKB | ChEBI) | |||
Binding site | 401-405 | IMP (UniProtKB | ChEBI) | |||
Active site | 417 | Proton acceptor | |||
Binding site | 429 | IMP (UniProtKB | ChEBI) | |||
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 lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > Liliopsida > Asparagales > Orchidaceae > Orchidoideae > Orchideae > Orchidinae > Platanthera
Accessions
- Primary accessionA0AAP0G589
Proteomes
Subcellular Location
Interaction
Subunit
Homotetramer.
Structure
Sequence
- Sequence statusComplete
- Length502
- Mass (Da)53,060
- Last updated2024-10-02 v1
- ChecksumFA0BDFA42441F08E
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
JBBWWQ010000010 EMBL· GenBank· DDBJ | KAK8937348.1 EMBL· GenBank· DDBJ | Genomic DNA |