A0AA35XEV1 · A0AA35XEV1_GEOBA
- ProteinInosine-5'-monophosphate dehydrogenase
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids429 (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 | 190-192 | NAD+ (UniProtKB | ChEBI) | |||
Binding site | 240-242 | NAD+ (UniProtKB | ChEBI) | |||
Binding site | 242 | K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners; in other chain | |||
Binding site | 244 | K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners; in other chain | |||
Binding site | 245 | IMP (UniProtKB | ChEBI) | |||
Active site | 247 | Thioimidate intermediate | |||
Binding site | 247 | K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners; in other chain | |||
Binding site | 280-282 | IMP (UniProtKB | ChEBI) | |||
Binding site | 303-304 | IMP (UniProtKB | ChEBI) | |||
Binding site | 327-331 | IMP (UniProtKB | ChEBI) | |||
Active site | 344 | Proton acceptor | |||
Binding site | 356 | IMP (UniProtKB | ChEBI) | |||
Binding site | 411 | K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners | |||
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
- Taxonomic lineageEukaryota > Metazoa > Porifera > Demospongiae > Heteroscleromorpha > Tetractinellida > Astrophorina > Geodiidae > Geodia
Accessions
- Primary accessionA0AA35XEV1
Proteomes
Subcellular Location
Interaction
Subunit
Homotetramer.
Structure
Sequence
- Sequence statusComplete
- Length429
- Mass (Da)46,389
- Last updated2024-01-24 v1
- MD5 Checksum23C5B819455847A70CE9BA1309F7351F
Computationally mapped potential isoform sequences
There are 4 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0AA35U020 | A0AA35U020_GEOBA | GBAR_LOCUS30616 | 474 | ||
A0AA35TX97 | A0AA35TX97_GEOBA | GBAR_LOCUS30616 | 243 | ||
A0AA35U039 | A0AA35U039_GEOBA | GBAR_LOCUS30616 | 521 | ||
A0AA35XG45 | A0AA35XG45_GEOBA | GBAR_LOCUS30616 | 228 |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CASHTH010004335 EMBL· GenBank· DDBJ | CAI8056183.1 EMBL· GenBank· DDBJ | Genomic DNA |