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IPR001093 is a IMP dehydrogenase/GMP reductase.
<p>Synonym(s): Inosine-5'-monophosphate dehydrogenase, Inosinic acid dehydrogenase; Synonym(s): Guanosine 5'-monophosphate oxidoreductase <p>This entry contains two related enzymes: IMP dehydrogenase and GMP reductase. These enzymes adopt a TIM barrel structure.</p> <p>IMP dehydrogenase ([ec:1.1.1.205]) (IMPDH) catalyses the rate-limiting reaction of<i>de novo</i>GTP biosynthesis, the NAD-dependent reduction of IMP into XMP [[cite:PUB00002466]]. <reaction> Inosine 5-phosphate + NAD<sup>+</sup>+ H<sub>2</sub>O = xanthosine 5-phosphate + NADH </reaction> IMP dehydrogenase is associated with cell proliferation and is a possible target for cancer chemotherapy. Mammalian and bacterial IMPDHs are tetramers of identical chains. There are two IMP dehydrogenase isozymes in humans [[cite:PUB00002609]]. IMP dehydrogenase nearly always contains a long insertion that has two CBS domains within it.</p> <p>GMP reductase ([ec:1.7.1.7]) catalyses the irreversible and NADPH-dependent reductive deamination of GMP into IMP [[cite:PUB00000471]]. <reaction> NADPH + guanosine 5-phosphate = NADP<sup>+</sup>+ inosine 5-phosphate + NH<sub>3</sub> </reaction> It converts nucleobase, nucleoside and nucleotide derivatives of G to A nucleotides, and maintains intracellular balance of A and G nucleotides.</p>
This description is obtained from EB-eye REST.
GO predictions are based solely on the InterPro-to-GO mappings published by EMBL-EBI, which are in turn based on the mapping of predicted domains to the InterPro dataset. The InterPro-to-GO mapping was last updated on , while the GO metadata was last updated on .
| GO term | Namespace | Name | Definition | Relationships |
|---|---|---|---|---|
| Molecular function | Catalytic activity | Catalysis of a biochemical reaction at physiological temperatures. In biologically catalyzed reactions, the reactants are known as substrates, and the catalysts are naturally occurring macromolecular substances known as enzymes. Enzymes possess specific binding sites for substrates, and are usually composed wholly or largely of protein, but RNA that has catalytic activity (ribozyme) is often also regarded as enzymatic. | ||
| Biological process | Oxidation-reduction process | A metabolic process that results in the removal or addition of one or more electrons to or from a substance, with or without the concomitant removal or addition of a proton or protons. |
| Transcript | Name | Description | Predicted domains | Domain count |
|---|---|---|---|---|
| – | PREDICTED: inosine-5'-monophosphate dehydrogenase-like [Cicer arietinum] gi|502107091|ref|XP_004493154.1| | 19 | ||
| – | Inosine-5'-monophosphate dehydrogenase; TAIR: AT1G16350.1 Aldolase-type TIM barrel family protein; Swiss-Prot: sp|Q84XA3|IMDH_VIGUN Inosine-5'-monophosphate dehydrogenase; TrEMBL-Plants: tr|G7KZG9|G7KZG9_MEDTR Inosine-5'-monophosphate dehydrogenase; Found in the gene: LotjaGi3g1v0440200 | 18 |
A list of co-occurring predicted domains within the L. japonicus gene space:
| Predicted domain | Source | Observations | Saturation (%) |
|---|---|---|---|
| cd04601 | CDD | 1 | 50.00 |