Q07152 · IMDH_DROME
- ProteinInosine-5'-monophosphate dehydrogenase
- Generas
- StatusUniProtKB reviewed (Swiss-Prot)
- 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 | ||||||
Binding site | 464 | IMP (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 523 | K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners | ||||
Sequence: E | ||||||
Binding site | 524 | K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners | ||||
Sequence: G |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | IMP dehydrogenase activity | |
Molecular Function | metal ion binding | |
Molecular Function | nucleotide binding | |
Biological Process | axon guidance | |
Biological Process | GMP biosynthetic process | |
Biological Process | GTP biosynthetic process | |
Biological Process | purine nucleotide 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
- Alternative names
Gene names
Organism names
- Strains
- Taxonomic lineageEukaryota > Metazoa > Ecdysozoa > Arthropoda > Hexapoda > Insecta > Pterygota > Neoptera > Endopterygota > Diptera > Brachycera > Muscomorpha > Ephydroidea > Drosophilidae > Drosophila > Sophophora
Accessions
- Primary accessionQ07152
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000093678 | 1-537 | Inosine-5'-monophosphate dehydrogenase | |||
Sequence: MESTTKVKVNGFVESTSSSAAPAIQTKSTTGFDAELQDGLSCKELFQNGEGLTYNDFLILPGYIDFTAEEVDLSSPLTKSLTLRAPLVSSPMDTVTESEMAIAMALCGGIGIIHHNCTPEYQALEVHKVKKYKHGFMRDPSVMSPTNTVGDVLEARRKNGFTGYPVTENGKLGGKLLGMVTSRDIDFRENQPEVLLADIMTTELVTAPNGINLPTANAILEKSKKGKLPIVNQAGELVAMIARTDLKKARSYPNASKDSNKQLLVGAAIGTRSEDKARLALLVANGVDVIILDSSQGNSVYQVEMIKYIKETYPELQVIGGNVVTRAQAKNLIDAGVDGLRVGMGSGSICITQEVMACGCPQATAVYQVSTYARQFGVPVIADGGIQSIGHIVKAIALGASAVMMGSLLAGTSEAPGEYFFSDGVRLKKYRGMGSLEAMERGDAKGAAMSRYYHNEMDKMKVAQGVSGSIVDKGSVLRYLPYLECGLQHSCQDIGANSINKLRDMIYNGQLRFMKRTHSAQLEGNVHGLFSYEKRLF | ||||||
Modified residue | 28 | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Enriched in adult ovary and testis.
Developmental stage
Expressed both maternally and zygotically.
Gene expression databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 136-195 | CBS 1 | ||||
Sequence: FMRDPSVMSPTNTVGDVLEARRKNGFTGYPVTENGKLGGKLLGMVTSRDIDFRENQPEVL | ||||||
Domain | 200-256 | CBS 2 | ||||
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 updated1995-11-01 v1
- ChecksumA5EAB41AEAA64EBD
Computationally mapped potential isoform sequences
There are 2 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A4V488 | A4V488_DROME | ras | 537 | ||
A0A4D6K3W6 | A0A4D6K3W6_DROME | ras | 590 |
Sequence caution
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 38 | in Ref. 4; AAB35628 | ||||
Sequence: D → V | ||||||
Sequence conflict | 53 | in Ref. 4; AAB35628 | ||||
Sequence: T → P | ||||||
Sequence conflict | 99-102 | in Ref. 4; AAB35628 | ||||
Sequence: EMAI → RCH | ||||||
Sequence conflict | 184 | in Ref. 4; AAB35628 | ||||
Sequence: D → A | ||||||
Sequence conflict | 194 | in Ref. 4; AAB35628 | ||||
Sequence: V → S | ||||||
Sequence conflict | 216-217 | in Ref. 4; AAB35628 | ||||
Sequence: AN → EH | ||||||
Sequence conflict | 226-229 | in Ref. 4; AAB35628 | ||||
Sequence: GKLP → ATA | ||||||
Sequence conflict | 244 | in Ref. 4; AAB35628 | ||||
Sequence: T → A | ||||||
Sequence conflict | 261-262 | in Ref. 4; AAB35628 | ||||
Sequence: KQ → TR | ||||||
Sequence conflict | 265-266 | in Ref. 4; AAB35628 | ||||
Sequence: VG → CP | ||||||
Sequence conflict | 277-278 | in Ref. 4; AAB35628 | ||||
Sequence: AR → GCRA | ||||||
Sequence conflict | 284 | in Ref. 4; AAB35628 | ||||
Sequence: A → R | ||||||
Sequence conflict | 301 | in Ref. 4; AAB35628 | ||||
Sequence: Y → I | ||||||
Sequence conflict | 387-388 | in Ref. 4; AAB35628 | ||||
Sequence: QS → HA |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
L14847 EMBL· GenBank· DDBJ | AAA21831.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
L22608 EMBL· GenBank· DDBJ | AAA16839.1 EMBL· GenBank· DDBJ | mRNA | ||
S80430 EMBL· GenBank· DDBJ | AAB35628.1 EMBL· GenBank· DDBJ | mRNA | ||
AE014298 EMBL· GenBank· DDBJ | AAF46621.3 EMBL· GenBank· DDBJ | Genomic DNA | ||
AE014298 EMBL· GenBank· DDBJ | AAF46622.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY089553 EMBL· GenBank· DDBJ | AAL90291.1 EMBL· GenBank· DDBJ | mRNA | Frameshift |