A4V488 · A4V488_DROME
- ProteinInosine-5'-monophosphate dehydrogenase
- Generas
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids537 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
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 | 293-295 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: DSS | ||||||
Binding site | 343-345 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: GMG | ||||||
Binding site | 345 | K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners; in other chain | ||||
Sequence: G | ||||||
Binding site | 347 | K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners; in other chain | ||||
Sequence: G | ||||||
Binding site | 348 | IMP (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Active site | 350 | Thioimidate intermediate | ||||
Sequence: C | ||||||
Binding site | 350 | K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners; in other chain | ||||
Sequence: C | ||||||
Binding site | 383-385 | IMP (UniProtKB | ChEBI) | ||||
Sequence: DGG | ||||||
Binding site | 406-407 | IMP (UniProtKB | ChEBI) | ||||
Sequence: GS | ||||||
Binding site | 430-434 | IMP (UniProtKB | ChEBI) | ||||
Sequence: YRGMG | ||||||
Active site | 451 | Proton acceptor | ||||
Sequence: R | ||||||
Binding site | 464 | IMP (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 519 | 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 > Metazoa > Ecdysozoa > Arthropoda > Hexapoda > Insecta > Pterygota > Neoptera > Endopterygota > Diptera > Brachycera > Muscomorpha > Ephydroidea > Drosophilidae > Drosophila > Sophophora
Accessions
- Primary accessionA4V488
Proteomes
Organism-specific databases
Subcellular Location
Expression
Gene expression databases
Interaction
Subunit
Homotetramer.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 136-195 | CBS | ||||
Sequence: FMRDPSVMSPTNTVGDVLEARRKNGFTGYPVTENGKLGGKLLGMVTSRDIDFRENQPEVL | ||||||
Domain | 200-256 | CBS | ||||
Sequence: MTTELVTAPNGINLPTANAILEKSKKGKLPIVNQAGELVAMIARTDLKKARSYPNAS |
Sequence similarities
Belongs to the IMPDH/GMPR family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length537
- Mass (Da)57,829
- Last updated2007-05-29 v1
- ChecksumA5EAB41AEAA64EBD
Computationally mapped potential isoform sequences
There are 2 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
Q07152 | IMDH_DROME | ras | 537 | ||
A0A4D6K3W6 | A0A4D6K3W6_DROME | ras | 590 |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AE014298 EMBL· GenBank· DDBJ | AAN09265.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BT125958 EMBL· GenBank· DDBJ | ADX35937.1 EMBL· GenBank· DDBJ | mRNA | ||
AE014298 EMBL· GenBank· DDBJ | AGB95270.1 EMBL· GenBank· DDBJ | Genomic DNA |