IMD3 (YLR432W) encodes an inosine-5'-monophosphate dehydrogenase (IMPDH; EC 1.1.1.205), one of three expressed IMPDH paralogs in S. cerevisiae together with IMD2 and IMD4 (IMD1 is a poorly expressed subtelomeric paralog). It catalyses the NAD+-dependent oxidation of IMP to XMP, the first committed and rate-limiting step in guanine nucleotide synthesis. Unlike IMD2, IMD3 is not the drug-inducible, mycophenolic acid-resistant paralog, and its loss does not cause drug sensitivity. Imd3 forms homotetramers and can form mixed tetramers with its close paralog Imd4. The enzyme is cytoplasmic; it has also been recovered in mRNP capture experiments.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0000166 nucleotide binding | IEA GO_REF:0000104 | KEEP AS NON CORE | Summary: IEA from HAMAP MF_03156. IMP and NAD+ are nucleotide substrates; true but subsumed by IMP dehydrogenase activity. Reason: Substrate/cofactor binding implied by the catalytic MF. Supporting Evidence: file:yeast/IMD3/IMD3-uniprot.txt Reaction=IMP + NAD(+) + H2O = XMP + NADH + H(+) |
| GO:0003729 mRNA binding | HDA PMID:23222640 Global analysis of yeast mRNPs. | KEEP AS NON CORE | Summary: HDA from global mRNP capture (Mitchell et al. 2013), which recovered all three IMPDHs among metabolic proteins bound to poly(A) RNA. IMPDH CBS domains bind nucleic acids in other species, but no specific mRNA-related role is established for IMD3. Reason: High-throughput mRNP capture; no defined RNA-related function. Supporting Evidence: PMID:23222640 Various metabolic proteins were observed (Imd2, Imd3, Imd4, Cys4, Cpr1) |
| GO:0003824 catalytic activity | IEA GO_REF:0000002 | TOO GENERAL | Summary: IEA from InterPro IPR001093 (IMPDH/GMPR). True but uninformative. Reason: Uninformative root MF. Supporting Evidence: file:yeast/IMD3/IMD3-uniprot.txt Reaction=IMP + NAD(+) + H2O = XMP + NADH + H(+) |
| GO:0003938 IMP dehydrogenase activity | IBA GO_REF:0000033 | ACCEPT | Summary: IBA from PANTHER PTN000226903 (IMPDH). IMD3 is one of the three expressed yeast IMPDH paralogs; core MF. Supporting Evidence: file:yeast/IMD3/IMD3-uniprot.txt Reaction=IMP + NAD(+) + H2O = XMP + NADH + H(+) file:yeast/IMD3/IMD3-uniprot.txt 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 |
| GO:0003938 IMP dehydrogenase activity | IEA GO_REF:0000120 | ACCEPT | Summary: IEA via RHEA:11708 / EC 1.1.1.205, InterPro IPR005990 and HAMAP MF_03156. Correct. Supporting Evidence: file:yeast/IMD3/IMD3-uniprot.txt Reaction=IMP + NAD(+) + H2O = XMP + NADH + H(+) |
| GO:0003938 IMP dehydrogenase activity | RCA GO_REF:0000123 | ACCEPT | Summary: RCA from YeastPathways DENOVOPURINE2-PWY (superpathway of purine nucleotides de novo biosynthesis II), assigning IMD3 (with Imd2/Imd4) to IMP + NAD+ -> XMP + NADH (EC 1.1.1.205). Correct. Supporting Evidence: file:yeast/IMD3/IMD3-uniprot.txt Reaction=IMP + NAD(+) + H2O = XMP + NADH + H(+) |
| GO:0003938 IMP dehydrogenase activity | RCA GO_REF:0000123 | ACCEPT | Summary: RCA from YeastPathways DENOVOPURINE3-PWY (de novo biosynthesis of purine nucleotides), assigning IMD3 (with Imd2/Imd4) to IMP + NAD+ -> XMP + NADH (EC 1.1.1.205). Correct. Supporting Evidence: file:yeast/IMD3/IMD3-uniprot.txt Reaction=IMP + NAD(+) + H2O = XMP + NADH + H(+) |
| GO:0003938 IMP dehydrogenase activity | RCA GO_REF:0000123 | ACCEPT | Summary: RCA from YeastPathways PRPP-PWY-1 (superpathway of histidine, purine, and pyrimidine biosynthesis), assigning IMD3 (with Imd2/Imd4) to IMP + NAD+ -> XMP + NADH (EC 1.1.1.205). Correct. Supporting Evidence: file:yeast/IMD3/IMD3-uniprot.txt Reaction=IMP + NAD(+) + H2O = XMP + NADH + H(+) |
| GO:0003938 IMP dehydrogenase activity | RCA GO_REF:0000123 | ACCEPT | Summary: RCA from YeastPathways PWY-6125 (superpathway of guanosine nucleotides de novo biosynthesis II), assigning IMD3 (with Imd2/Imd4) to IMP + NAD+ -> XMP + NADH (EC 1.1.1.205). Correct. Supporting Evidence: file:yeast/IMD3/IMD3-uniprot.txt Reaction=IMP + NAD(+) + H2O = XMP + NADH + H(+) |
| GO:0003938 IMP dehydrogenase activity | RCA GO_REF:0000123 | ACCEPT | Summary: RCA from YeastPathways PWY-7221 (guanosine ribonucleotides de novo biosynthesis), assigning IMD3 (with Imd2/Imd4) to IMP + NAD+ -> XMP + NADH (EC 1.1.1.205). Correct. Supporting Evidence: file:yeast/IMD3/IMD3-uniprot.txt Reaction=IMP + NAD(+) + H2O = XMP + NADH + H(+) |
| GO:0003938 IMP dehydrogenase activity | RCA GO_REF:0000123 | ACCEPT | Summary: RCA from YeastPathways PWY3O-285 (superpathway of purine biosynthesis and salvage pathways), assigning IMD3 (with Imd2/Imd4) to IMP + NAD+ -> XMP + NADH (EC 1.1.1.205). Correct. Supporting Evidence: file:yeast/IMD3/IMD3-uniprot.txt Reaction=IMP + NAD(+) + H2O = XMP + NADH + H(+) |
| GO:0003938 IMP dehydrogenase activity | TAS PMID:11441018 Regulation of an IMP dehydrogenase gene and its overexpressi... | ACCEPT | Summary: TAS (Shaw et al. 2001): IMD1-4 encode IMPDH family members; IMPDH is rate-limiting for GTP synthesis. Accept; IMD3 carries the conserved catalytic residues (Cys335 active site). Supporting Evidence: PMID:11441018 IMP dehydrogenase is a rate-limiting enzyme involved in the synthesis of GTP file:yeast/IMD3/IMD3-uniprot.txt 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 |
| GO:0005515 protein binding | IPI PMID:16429126 Proteome survey reveals modularity of the yeast cell machine... | REMOVE | Summary: IPI (PMID:16429126) with the splicing helicase Prp22 (P24384) from a proteomics interaction screen. No functional significance is established for an IMPDH-Prp22 interaction, and generic protein binding is uninformative. Reason: Bare protein binding from a high-throughput screen; no functional consequence established. Supporting Evidence: PMID:16429126 using affinity purification and mass spectrometry |
| GO:0005515 protein binding | IPI PMID:16429126 Proteome survey reveals modularity of the yeast cell machine... | REMOVE | Summary: IPI (PMID:16429126) for interaction with the paralog Imd4 (P50094). The interaction reflects mixed IMPDH paralog tetramers, a structural feature of the enzyme. Generic protein binding carries no functional information; removal does not dispute the interaction. Reason: Bare protein binding is uninformative; the Imd3-Imd4 interaction reflects IMPDH heterotetramer formation, already implicit in the subunit description. Supporting Evidence: PMID:16429126 using affinity purification and mass spectrometry file:yeast/IMD3/IMD3-uniprot.txt Seems to be able to form heterotetramers composed from more than 1 of the 3 IMPDH gene products (IMD2-4) |
| GO:0005515 protein binding | IPI PMID:18467557 An in vivo map of the yeast protein interactome. | REMOVE | Summary: IPI (PMID:18467557) for interaction with the paralog Imd4 (P50094). The interaction reflects mixed IMPDH paralog tetramers, a structural feature of the enzyme. Generic protein binding carries no functional information; removal does not dispute the interaction. Reason: Bare protein binding is uninformative; the Imd3-Imd4 interaction reflects IMPDH heterotetramer formation, already implicit in the subunit description. Supporting Evidence: PMID:18467557 by means of a protein-fragment complementation assay (PCA) file:yeast/IMD3/IMD3-uniprot.txt Seems to be able to form heterotetramers composed from more than 1 of the 3 IMPDH gene products (IMD2-4) |
| GO:0005515 protein binding | IPI PMID:18719252 High-quality binary protein interaction map of the yeast int... | REMOVE | Summary: IPI (PMID:18719252) for interaction with the paralog Imd4 (P50094). The interaction reflects mixed IMPDH paralog tetramers, a structural feature of the enzyme. Generic protein binding carries no functional information; removal does not dispute the interaction. Reason: Bare protein binding is uninformative; the Imd3-Imd4 interaction reflects IMPDH heterotetramer formation, already implicit in the subunit description. Supporting Evidence: PMID:18719252 high-throughput yeast two-hybrid (Y2H) screening provides high-quality binary interaction information file:yeast/IMD3/IMD3-uniprot.txt Seems to be able to form heterotetramers composed from more than 1 of the 3 IMPDH gene products (IMD2-4) |
| GO:0005515 protein binding | IPI PMID:31454312 The role of structural pleiotropy and regulatory evolution i... | REMOVE | Summary: IPI (PMID:31454312) for interaction with the paralog Imd4 (P50094). The interaction reflects mixed IMPDH paralog tetramers, a structural feature of the enzyme. Generic protein binding carries no functional information; removal does not dispute the interaction. Reason: Bare protein binding is uninformative; the Imd3-Imd4 interaction reflects IMPDH heterotetramer formation, already implicit in the subunit description. Supporting Evidence: PMID:31454312 The duplication of genes encoding homomeric proteins leads to the formation of homomers and heteromers of paralogs file:yeast/IMD3/IMD3-uniprot.txt Seems to be able to form heterotetramers composed from more than 1 of the 3 IMPDH gene products (IMD2-4) |
| GO:0005515 protein binding | IPI PMID:37070168 RNA-dependent interactome allows network-based assignment of... | REMOVE | Summary: IPI (PMID:37070168) with the splicing helicase Prp22 (P24384) from a proteomics interaction screen. No functional significance is established for an IMPDH-Prp22 interaction, and generic protein binding is uninformative. Reason: Bare protein binding from a high-throughput screen; no functional consequence established. Supporting Evidence: PMID:37070168 We used mass spectrometry-based quantitative proteomics to systematically identify protein-protein interactions (PPIs) and RNA-dependent interactions (RDIs) |
| GO:0005515 protein binding | IPI PMID:37968396 The social and structural architecture of the yeast protein ... | REMOVE | Summary: IPI (PMID:37968396) for interaction with the paralog Imd4 (P50094). The interaction reflects mixed IMPDH paralog tetramers, a structural feature of the enzyme. Generic protein binding carries no functional information; removal does not dispute the interaction. Reason: Bare protein binding is uninformative; the Imd3-Imd4 interaction reflects IMPDH heterotetramer formation, already implicit in the subunit description. Supporting Evidence: PMID:37968396 Here we develop a sensitive high-throughput method using highly reproducible affinity enrichment coupled to mass spectrometry file:yeast/IMD3/IMD3-uniprot.txt Seems to be able to form heterotetramers composed from more than 1 of the 3 IMPDH gene products (IMD2-4) |
| GO:0005737 cytoplasm | HDA PMID:11914276 Subcellular localization of the yeast proteome. | ACCEPT | Summary: HDA from the Kumar et al. 2002 epitope-tag immunolocalisation screen; cytoplasmic. Correct. Supporting Evidence: PMID:11914276 we have epitope-tagged 60% of the Saccharomyces cerevisiae proteome |
| GO:0005737 cytoplasm | HDA PMID:14562095 Global analysis of protein localization in budding yeast. | ACCEPT | Summary: HDA from the Huh et al. 2003 GFP screen: IMD3-GFP is cytoplasmic. Correct. Supporting Evidence: PMID:14562095 We classify these proteins, representing 75% of the yeast proteome, into 22 distinct subcellular localization categories file:yeast/IMD3/IMD3-uniprot.txt SUBCELLULAR LOCATION: Cytoplasm |
| GO:0005737 cytoplasm | IBA GO_REF:0000033 | ACCEPT | Summary: IBA (is_active_in cytoplasm) from PTN000226902. Correct. Supporting Evidence: file:yeast/IMD3/IMD3-uniprot.txt SUBCELLULAR LOCATION: Cytoplasm |
| GO:0005737 cytoplasm | IDA PMID:23222640 Global analysis of yeast mRNPs. | ACCEPT | Summary: IDA from the global mRNP study (Mitchell et al. 2013), which identified the IMPDHs among novel mRNA-binding proteins and imaged mRNA-binding proteins in the cytoplasm; the specific IMD3 image is not in the cached text, so defer to the curator. Consistent with GFP and HAMAP data. Supporting Evidence: PMID:23222640 Various metabolic proteins were observed (Imd2, Imd3, Imd4, Cys4, Cpr1) file:yeast/IMD3/IMD3-uniprot.txt SUBCELLULAR LOCATION: Cytoplasm |
| GO:0005737 cytoplasm | IEA GO_REF:0000120 | ACCEPT | Summary: IEA from UniProt subcellular location SL-0086 / HAMAP. Correct. Supporting Evidence: file:yeast/IMD3/IMD3-uniprot.txt SUBCELLULAR LOCATION: Cytoplasm |
| GO:0005829 cytosol | RCA GO_REF:0000123 | ACCEPT | Summary: RCA (is_active_in cytosol) from YeastPathways DENOVOPURINE2-PWY (superpathway of purine nucleotides de novo biosynthesis II). IMPDH is a soluble cytoplasmic enzyme; cytosol is appropriate. Supporting Evidence: file:yeast/IMD3/IMD3-uniprot.txt SUBCELLULAR LOCATION: Cytoplasm PMID:14562095 We classify these proteins, representing 75% of the yeast proteome, into 22 distinct subcellular localization categories |
| GO:0005829 cytosol | RCA GO_REF:0000123 | ACCEPT | Summary: RCA (is_active_in cytosol) from YeastPathways DENOVOPURINE3-PWY (de novo biosynthesis of purine nucleotides). IMPDH is a soluble cytoplasmic enzyme; cytosol is appropriate. Supporting Evidence: file:yeast/IMD3/IMD3-uniprot.txt SUBCELLULAR LOCATION: Cytoplasm PMID:14562095 We classify these proteins, representing 75% of the yeast proteome, into 22 distinct subcellular localization categories |
| GO:0005829 cytosol | RCA GO_REF:0000123 | ACCEPT | Summary: RCA (is_active_in cytosol) from YeastPathways PRPP-PWY-1 (superpathway of histidine, purine, and pyrimidine biosynthesis). IMPDH is a soluble cytoplasmic enzyme; cytosol is appropriate. Supporting Evidence: file:yeast/IMD3/IMD3-uniprot.txt SUBCELLULAR LOCATION: Cytoplasm PMID:14562095 We classify these proteins, representing 75% of the yeast proteome, into 22 distinct subcellular localization categories |
| GO:0005829 cytosol | RCA GO_REF:0000123 | ACCEPT | Summary: RCA (is_active_in cytosol) from YeastPathways PWY-6125 (superpathway of guanosine nucleotides de novo biosynthesis II). IMPDH is a soluble cytoplasmic enzyme; cytosol is appropriate. Supporting Evidence: file:yeast/IMD3/IMD3-uniprot.txt SUBCELLULAR LOCATION: Cytoplasm PMID:14562095 We classify these proteins, representing 75% of the yeast proteome, into 22 distinct subcellular localization categories |
| GO:0005829 cytosol | RCA GO_REF:0000123 | ACCEPT | Summary: RCA (is_active_in cytosol) from YeastPathways PWY-7221 (guanosine ribonucleotides de novo biosynthesis). IMPDH is a soluble cytoplasmic enzyme; cytosol is appropriate. Supporting Evidence: file:yeast/IMD3/IMD3-uniprot.txt SUBCELLULAR LOCATION: Cytoplasm PMID:14562095 We classify these proteins, representing 75% of the yeast proteome, into 22 distinct subcellular localization categories |
| GO:0005829 cytosol | RCA GO_REF:0000123 | ACCEPT | Summary: RCA (is_active_in cytosol) from YeastPathways PWY3O-285 (superpathway of purine biosynthesis and salvage pathways). IMPDH is a soluble cytoplasmic enzyme; cytosol is appropriate. Supporting Evidence: file:yeast/IMD3/IMD3-uniprot.txt SUBCELLULAR LOCATION: Cytoplasm PMID:14562095 We classify these proteins, representing 75% of the yeast proteome, into 22 distinct subcellular localization categories |
| GO:0005886 plasma membrane | HDA PMID:16622836 The plasma membrane proteome of Saccharomyces cerevisiae and... | MARK AS OVER ANNOTATED | Summary: HDA from a plasma membrane proteomics study (Delom et al. 2006). IMPDH is a soluble cytoplasmic enzyme without membrane-targeting features; abundant metabolic enzymes commonly contaminate stripped membrane fractions. Not a functional location. Reason: Soluble cytoplasmic enzyme detected in a membrane proteomics fraction; likely contamination. Supporting Evidence: PMID:16622836 Proteins from a stripped plasma membrane fraction were solubilized file:yeast/IMD3/IMD3-uniprot.txt SUBCELLULAR LOCATION: Cytoplasm |
| GO:0006164 purine nucleotide biosynthetic process | IEA GO_REF:0000002 | ACCEPT | Summary: IEA from InterPro IPR005990. Correct general BP. Supporting Evidence: file:yeast/IMD3/IMD3-uniprot.txt 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 |
| GO:0006164 purine nucleotide biosynthetic process | RCA GO_REF:0000123 | ACCEPT | Summary: RCA from YeastPathways DENOVOPURINE2-PWY (superpathway of purine nucleotides de novo biosynthesis II). IMP -> XMP is the committed step of guanine nucleotide synthesis; correct. Supporting Evidence: file:yeast/IMD3/IMD3-uniprot.txt 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 |
| GO:0006164 purine nucleotide biosynthetic process | RCA GO_REF:0000123 | ACCEPT | Summary: RCA from YeastPathways DENOVOPURINE3-PWY (de novo biosynthesis of purine nucleotides). IMP -> XMP is the committed step of guanine nucleotide synthesis; correct. Supporting Evidence: file:yeast/IMD3/IMD3-uniprot.txt 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 |
| GO:0006177 GMP biosynthetic process | IEA GO_REF:0000104 | ACCEPT | Summary: IEA from HAMAP MF_03156. Correct; 'de novo GMP biosynthetic process' is more precise. Supporting Evidence: file:yeast/IMD3/IMD3-uniprot.txt 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 |
| GO:0006183 GTP biosynthetic process | IBA GO_REF:0000033 | ACCEPT | Summary: IBA from PTN000226903. IMPDH is rate-limiting for guanine nucleotide (GTP) synthesis; correct, acting through GMP. Supporting Evidence: PMID:11441018 IMP dehydrogenase is a rate-limiting enzyme involved in the synthesis of GTP |
| GO:0006183 GTP biosynthetic process | TAS PMID:11441018 Regulation of an IMP dehydrogenase gene and its overexpressi... | ACCEPT | Summary: TAS (Shaw et al. 2001): IMPDH is the rate-limiting enzyme for GTP synthesis. Correct. Supporting Evidence: PMID:11441018 IMP dehydrogenase is a rate-limiting enzyme involved in the synthesis of GTP |
| GO:0009165 nucleotide biosynthetic process | RCA GO_REF:0000123 | TOO GENERAL | Summary: RCA from YeastPathways superpathway PRPP-PWY-1 (superpathway of histidine, purine, and pyrimidine biosynthesis). True but uninformative. Reason: True but very general parent from a superpathway. Supporting Evidence: file:yeast/IMD3/IMD3-uniprot.txt 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 |
| GO:0016491 oxidoreductase activity | IEA GO_REF:0000002 | TOO GENERAL | Summary: IEA from InterPro IPR015875 (IMPDH/GMPR conserved site). True but uninformative. Reason: Uninformative parent of the core MF. Supporting Evidence: file:yeast/IMD3/IMD3-uniprot.txt Reaction=IMP + NAD(+) + H2O = XMP + NADH + H(+) |
| GO:0042802 identical protein binding | IPI PMID:18467557 An in vivo map of the yeast protein interactome. | KEEP AS NON CORE | Summary: IPI (PMID:18467557) for Imd3 self-interaction, consistent with the IMPDH homotetramer. Correct but structural rather than functional. Reason: Self-association reflects homotetramer assembly, a structural property of IMPDH. Supporting Evidence: PMID:18467557 by means of a protein-fragment complementation assay (PCA) file:yeast/IMD3/IMD3-uniprot.txt Seems to be able to form heterotetramers composed from more than 1 of the 3 IMPDH gene products (IMD2-4) |
| GO:0042802 identical protein binding | IPI PMID:18719252 High-quality binary protein interaction map of the yeast int... | KEEP AS NON CORE | Summary: IPI (PMID:18719252) for Imd3 self-interaction, consistent with the IMPDH homotetramer. Correct but structural rather than functional. Reason: Self-association reflects homotetramer assembly, a structural property of IMPDH. Supporting Evidence: PMID:18719252 high-throughput yeast two-hybrid (Y2H) screening provides high-quality binary interaction information file:yeast/IMD3/IMD3-uniprot.txt Seems to be able to form heterotetramers composed from more than 1 of the 3 IMPDH gene products (IMD2-4) |
| GO:0042802 identical protein binding | IPI PMID:31454312 The role of structural pleiotropy and regulatory evolution i... | KEEP AS NON CORE | Summary: IPI (PMID:31454312) for Imd3 self-interaction, consistent with the IMPDH homotetramer. Correct but structural rather than functional. Reason: Self-association reflects homotetramer assembly, a structural property of IMPDH. Supporting Evidence: PMID:31454312 The duplication of genes encoding homomeric proteins leads to the formation of homomers and heteromers of paralogs file:yeast/IMD3/IMD3-uniprot.txt Seems to be able to form heterotetramers composed from more than 1 of the 3 IMPDH gene products (IMD2-4) |
| GO:0043101 purine-containing compound salvage | RCA GO_REF:0000123 | KEEP AS NON CORE | Summary: RCA from YeastPathways PWY3O-285 (superpathway of purine biosynthesis and salvage pathways). IMP produced by hypoxanthine salvage (Hpt1) or from adenine (Apt1/Amd1) reaches guanine nucleotides only via IMPDH, so IMPDH acts downstream of these salvage routes; guanine salvage by Hpt1 produces GMP directly. Non-core. Reason: IMPDH routes salvaged IMP to guanine nucleotides, but guanine salvage itself bypasses it. Supporting Evidence: file:yeast/IMD3/IMD3-uniprot.txt 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 |
| GO:0046872 metal ion binding | IEA GO_REF:0000104 | KEEP AS NON CORE | Summary: IEA from HAMAP MF_03156: IMPDHs bind a monovalent K+ activator at the subunit interface. Correct but secondary to the catalytic MF. Reason: Cofactor binding; correct but secondary. Supporting Evidence: file:yeast/IMD3/IMD3-uniprot.txt Name=K(+) |
| GO:0106387 'de novo' GMP biosynthetic process | RCA GO_REF:0000123 | ACCEPT | Summary: RCA from YeastPathways PWY-6125 (superpathway of guanosine nucleotides de novo biosynthesis II). IMP -> XMP is the first committed step of GMP synthesis via IMP; the most precise BP. Core BP. Supporting Evidence: file:yeast/IMD3/IMD3-uniprot.txt 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 PMID:11441018 IMP dehydrogenase is a rate-limiting enzyme involved in the synthesis of GTP |
| GO:0106387 'de novo' GMP biosynthetic process | RCA GO_REF:0000123 | ACCEPT | Summary: RCA from YeastPathways PWY-7221 (guanosine ribonucleotides de novo biosynthesis). IMP -> XMP is the first committed step of GMP synthesis via IMP; the most precise BP. Core BP. Supporting Evidence: file:yeast/IMD3/IMD3-uniprot.txt 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 PMID:11441018 IMP dehydrogenase is a rate-limiting enzyme involved in the synthesis of GTP |
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Download this section (compressed HTML)Q: Do Imd3-Imd4 heterotetramers differ in kinetics or regulation from homotetramers, and is this why the paralog heteromer is retained?
Experiment: Measure IMPDH activity and guanine nucleotide pools in imd3, imd4 and imd3 imd4 strains with and without IMD2 induction to define each paralog's contribution.
Inosine monophosphate dehydrogenase; catalyzes the rate-limiting step in the de novo synthesis of GTP; member of a four-gene family in S. cerevisiae, constitutively expressed; IMD3 has a paralog, IMD4, that arose from the whole genome duplication
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