A0A3V2FYX1 · A0A3V2FYX1_SALET
- ProteinInosine-5'-monophosphate dehydrogenase
- GeneguaB
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids488 (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 | 248-250 | NAD+ (UniProtKB | ChEBI) | |||
Binding site | 298-300 | NAD+ (UniProtKB | ChEBI) | |||
Binding site | 300 | K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners; in other chain | |||
Binding site | 302 | K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners; in other chain | |||
Binding site | 303 | IMP (UniProtKB | ChEBI) | |||
Active site | 305 | Thioimidate intermediate | |||
Binding site | 305 | K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners; in other chain | |||
Binding site | 338-340 | IMP (UniProtKB | ChEBI) | |||
Binding site | 361-362 | IMP (UniProtKB | ChEBI) | |||
Binding site | 385-389 | IMP (UniProtKB | ChEBI) | |||
Active site | 401 | Proton acceptor | |||
Binding site | 415 | IMP (UniProtKB | ChEBI) | |||
Binding site | 469 | K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners | |||
Binding site | 470 | K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners | |||
Binding site | 471 | K+ (UniProtKB | ChEBI); ligand shared between two tetrameric partners | |||
GO annotations
Aspect | Term | |
---|---|---|
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
- Strains
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > Salmonella
Accessions
- Primary accessionA0A3V2FYX1
- Secondary accessions
Proteomes
Interaction
Subunit
Homotetramer.
Structure
Sequence
- Sequence statusComplete
- Length488
- Mass (Da)51,948
- Last updated2019-05-08 v1
- MD5 ChecksumA010555B6C67D0D5138C89FCF69FBAED
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AAHCWL010000018 EMBL· GenBank· DDBJ | EBU6916476.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AAHFAS010000043 EMBL· GenBank· DDBJ | EBV3763375.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AAHGTQ010000024 EMBL· GenBank· DDBJ | EBV9202405.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AAHIGD010000016 EMBL· GenBank· DDBJ | EBW4106222.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AAHIXO010000004 EMBL· GenBank· DDBJ | EBW6731915.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AAHKXZ010000016 EMBL· GenBank· DDBJ | EBX3356626.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AAHOXC010000030 EMBL· GenBank· DDBJ | EBY7387392.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AAHPAD010000018 EMBL· GenBank· DDBJ | EBY7628729.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AAHWIJ010000015 EMBL· GenBank· DDBJ | ECB0525233.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AAKLND010000012 EMBL· GenBank· DDBJ | ECT0410623.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AAKPQX010000003 EMBL· GenBank· DDBJ | ECU3482937.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AAKTKA010000011 EMBL· GenBank· DDBJ | ECV4805696.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AALIQJ010000062 EMBL· GenBank· DDBJ | EDA0177736.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AALLSV010000019 EMBL· GenBank· DDBJ | EDA9403651.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AALLTD010000023 EMBL· GenBank· DDBJ | EDA9439098.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AAMGJL010000004 EMBL· GenBank· DDBJ | EDH0978879.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AAMIHV010000017 EMBL· GenBank· DDBJ | EDH6430152.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
DAAMJL010000011 EMBL· GenBank· DDBJ | HAC6917711.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
DAARLP010000006 EMBL· GenBank· DDBJ | HAE2914081.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
DAARUC010000002 EMBL· GenBank· DDBJ | HAE3938501.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
DAARUZ010000002 EMBL· GenBank· DDBJ | HAE4047332.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
DAASLG010000005 EMBL· GenBank· DDBJ | HAE6000855.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
DAASLQ010000106 EMBL· GenBank· DDBJ | HAE6034264.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
DAASRW010000005 EMBL· GenBank· DDBJ | HAE6746838.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
DAATPN010000003 EMBL· GenBank· DDBJ | HAE9560983.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
DAAUAM010000001 EMBL· GenBank· DDBJ | HAF0860884.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
RSGD01000006 EMBL· GenBank· DDBJ | MID45405.1 EMBL· GenBank· DDBJ | Genomic DNA |