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IPR011342 is a Shikimate dehydrogenase.
<p>The shikimate pathway links the metabolism of carbohydrates to the biosynthesis of aromatic compounds and is essential for the biosynthesis of aromatic amino acids and other aromatic compounds in bacteria, eukaryotic microorganisms and plants [[cite:PUB00014334]]. It is a seven-step pathway which converts phosphoenolpyruvate and erythrose 4-phosphate to chorismate, the common precursor for the synthesis of folic acid, ubiquinone, vitamins E and K, and aromatic amino acids. Since this pathway is absent in metazoans, which must therefore obtain the essential amino acids phenylalanine and tryptophan from their diet, the enzymes in this pathway are important targets for the development of novel herbicides and antimicrobial compounds.</p> <p>This entry represents shikimate 5-dehydrogenases from prokaryotes and functionally equivalent C-terminal domains from larger, multifunctional proteins, the majority of which have an N-terminal quinate dehydrogenase domain. These multifunctional proteins occur in plants, chlamydiae, planctomycetes and a limited number of marine proteobacteria. Shikimate 5-dehydrogenase catalyses the fourth step of the shikimate pathway, which is the NADP-dependent reduction of 3-dehydroshikimate to shikimate [[cite:PUB00028041]].</p> <p>Structural studies suggests that some shikimate dehydrogenases are monmers while others form homodimers [[cite:PUB00028042], [cite:PUB00028043]]. Each shikimate dehydrogenase monomer forms a compact two-domain α/β sandwich with a deep interdomain cleft. The N-terminal substrate-binding domain forms a three layer α-β-α sandwich, while the C-terminal NADP-binding domain forms a nearly typical Rossman fold. The active site is thought to be located within the interdomain cleft, with substrate binding causing a conformational change which closes the active site cleft, forming a productive active site.</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 | Shikimate 3-dehydrogenase (NADP+) activity | Catalysis of the reaction: shikimate + NADP+ = 3-dehydroshikimate + NADPH + H+. | ||
| Biological process | Shikimate metabolic process | The chemical reactions and pathways involving shikimate, (3R,4S,5R)--3,4,5-trihydroxycyclohex-1-ene-1-carboxylate, the anion of shikimic acid. It is an important intermediate in the biosynthesis of aromatic amino acids. | ||
| Molecular function | NADP binding | Interacting selectively and non-covalently with nicotinamide-adenine dinucleotide phosphate, a coenzyme involved in many redox and biosynthetic reactions; binding may be to either the oxidized form, NADP+, or the reduced form, NADPH. | ||
| 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: bifunctional 3-dehydroquinate dehydratase/shikimate dehydrogenase, chloroplastic-like isoform X1 [Cicer arietinum] gi|502079645|ref|XP_004486324.1| | 24 | ||
| – | Shikimate dehydrogenase (NADP(+)); TAIR: AT3G06350.1 dehydroquinate dehydratase, putative / shikimate dehydrogenase; Swiss-Prot: sp|Q9SQT8|DHQSD_ARATH Bifunctional 3-dehydroquinate dehydratase/shikimate dehydrogenase, chloroplastic; TrEMBL-Plants: tr|A0A0S3T202|A0A0S3T202_PHAAN Uncharacterized protein; Found in the gene: LotjaGi4g1v0050500 | 26 |
A list of co-occurring predicted domains within the L. japonicus gene space:
| Predicted domain | Source | Observations | Saturation (%) |
|---|---|---|---|
| cd01065 | CDD | 1 | 50.00 |