A0A994J749 · A0A994J749_HUMAN
- ProteinInosine-5'-monophosphate dehydrogenase
- GeneIMPDH
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids1194 (go to sequence)
- Protein existenceInferred from homology
- Annotation score4/5
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. Could also have a single-stranded nucleic acid-binding activity and could play a role in RNA and/or DNA metabolism. It may also have a role in the development of malignancy and the growth progression of some tumors.
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 | 954-956 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: DSS | ||||||
Binding site | 1004-1006 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: GMG | ||||||
Binding site | 1006 | K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners; in other chain | ||||
Sequence: G | ||||||
Binding site | 1008 | K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners; in other chain | ||||
Sequence: G | ||||||
Binding site | 1009 | IMP (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Active site | 1011 | Thioimidate intermediate | ||||
Sequence: C | ||||||
Binding site | 1011 | K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners; in other chain | ||||
Sequence: C | ||||||
Binding site | 1044-1046 | IMP (UniProtKB | ChEBI) | ||||
Sequence: DGG | ||||||
Binding site | 1067-1068 | IMP (UniProtKB | ChEBI) | ||||
Sequence: GS | ||||||
Binding site | 1091-1095 | IMP (UniProtKB | ChEBI) | ||||
Sequence: YRGMG | ||||||
Active site | 1109 | Proton acceptor | ||||
Sequence: R | ||||||
Binding site | 1121 | IMP (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 1176 | K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners | ||||
Sequence: S |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Cellular Component | nucleus | |
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
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionA0A994J749
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Modified residue (large scale data) | 240 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 303 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 343 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 345 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 802 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 839 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 840 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1096 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1106 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1124 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1175 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1176 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1185 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1188 | PRIDE | Phosphoserine | ||||
Sequence: S |
Proteomic databases
Interaction
Subunit
Homotetramer.
Family & Domains
Features
Showing features for region, compositional bias, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 139-164 | Disordered | ||||
Sequence: IQGQAPQSAAPSIQTPSLQSPSPSQL | ||||||
Compositional bias | 212-227 | Polar residues | ||||
Sequence: QIQTVGALSPPPSQQG | ||||||
Region | 212-240 | Disordered | ||||
Sequence: QIQTVGALSPPPSQQGSPREGERRVGTAS | ||||||
Region | 413-441 | Disordered | ||||
Sequence: VHIWDPQQQPQQQTPQEQTPPPQQQQQQL | ||||||
Domain | 794-853 | CBS | ||||
Sequence: FITDPVVLSPKDRVRDVFEAKARHGFCGIPITDTGRMGSRLVGIISSRDIDFLKEEEHDC | ||||||
Domain | 859-917 | CBS | ||||
Sequence: MTKREDLVVAPAGITLKEANEILQRSKKGKLPIVNEDDELVAIIARTDLKKNRDYPLAS |
Sequence similarities
Belongs to the IMPDH/GMPR family.
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusComplete
- Length1,194
- Mass (Da)131,677
- Last updated2023-05-03 v1
- ChecksumE81F03706FC0BA48
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 212-227 | Polar residues | ||||
Sequence: QIQTVGALSPPPSQQG |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AC135506 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC137630 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. |