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IPR018528 is a Prephenate dehydratase, conserved site.
<p>Prephenate dehydratase ([ec:4.2.1.51], PDT) catalyses the decarboxylation of prephenate to phenylpyruvate. In microorganisms it is part of the terminal pathway of phenylalanine biosynthesis. In some bacteria such as Escherichia coli PDT is part of a bifunctional enzyme (P-protein) that also catalyses the transformation of chorismate into prephenate (chorismate mutase, [interpro:IPR002701], [ec:5.4.99.5]) while in other bacteria it is a monofunctional enzyme. In the archaea Archaeoglobus fulgidus is part of a trifunctional enzyme [[cite:PUB00070219]]. The sequence of monofunctional PDT aligns well with the C-terminal part of P-proteins [[cite:PUB00003018]].</p> <p>This entry represents two conserved regions. The first contains a conserved threonine which appears to be essential for the activity of the enzyme in E. coli [[cite:PUB00011056]]. The second region is located in the regulatory (Phe binding) region in the part C-terminal to PDT and this includes a conserved glutamate.</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 | Prephenate dehydratase activity | Catalysis of the reaction: prephenate = phenylpyruvate + H2O + CO2. | ||
Biological process | L-phenylalanine biosynthetic process | The chemical reactions and pathways resulting in the formation of L-phenylalanine, the L-enantiomer of 2-amino-3-phenylpropanoic acid, i.e. (2S)-2-amino-3-phenylpropanoic acid. |
Transcript | Name | Description | Predicted domains | Domain count |
---|---|---|---|---|
– | PREDICTED: arogenate dehydratase/prephenate dehydratase 2, chloroplastic-like [Glycine max] gi|356539096|ref|XP_003538036.1| | 16 | ||
– | PREDICTED: arogenate dehydratase/prephenate dehydratase 1, chloroplastic-like [Glycine max] gi|356563073|ref|XP_003549790.1| | 17 | ||
– | Arogenate dehydratase; TAIR: AT3G07630.1 arogenate dehydratase 2; Swiss-Prot: sp|Q9SSE7|AROD2_ARATH Arogenate dehydratase/prephenate dehydratase 2, chloroplastic; TrEMBL-Plants: tr|I1LKB8|I1LKB8_SOYBN Arogenate dehydratase; Found in the gene: LotjaGi2g1v0364500 | 17 | ||
– | Arogenate dehydratase; TAIR: AT1G08250.1 arogenate dehydratase 6; Swiss-Prot: sp|Q9SGD6|AROD6_ARATH Arogenate dehydratase/prephenate dehydratase 6, chloroplastic; TrEMBL-Plants: tr|I1MS62|I1MS62_SOYBN Arogenate dehydratase; Found in the gene: LotjaGi3g1v0173200 | 16 | ||
– | Arogenate dehydratase; TAIR: AT1G11790.1 arogenate dehydratase 1; Swiss-Prot: sp|Q9SA96|AROD1_ARATH Arogenate dehydratase/prephenate dehydratase 1, chloroplastic; TrEMBL-Plants: tr|A0A151RMQ8|A0A151RMQ8_CAJCA Uncharacterized protein; Found in the gene: LotjaGi3g1v0187700 | 21 | ||
– | Arogenate dehydratase; TAIR: AT1G11790.1 arogenate dehydratase 1; Swiss-Prot: sp|Q9SA96|AROD1_ARATH Arogenate dehydratase/prephenate dehydratase 1, chloroplastic; TrEMBL-Plants: tr|A0A151RMQ8|A0A151RMQ8_CAJCA Uncharacterized protein; Found in the gene: LotjaGi3g1v0187700 | 21 | ||
– | Arogenate dehydratase; TAIR: AT1G08250.1 arogenate dehydratase 6; Swiss-Prot: sp|Q9SGD6|AROD6_ARATH Arogenate dehydratase/prephenate dehydratase 6, chloroplastic; TrEMBL-Plants: tr|I1LRC6|I1LRC6_SOYBN Arogenate dehydratase; Found in the gene: LotjaGi3g1v0480500 | 16 | ||
– | Arogenate dehydratase; TAIR: AT1G11790.1 arogenate dehydratase 1; Swiss-Prot: sp|Q9SA96|AROD1_ARATH Arogenate dehydratase/prephenate dehydratase 1, chloroplastic; TrEMBL-Plants: tr|I1MR49|I1MR49_SOYBN Arogenate dehydratase; Found in the gene: LotjaGi4g1v0013900 | 17 |
A list of co-occurring predicted domains within the L. japonicus gene space:
Predicted domain | Source | Observations | Saturation (%) |
---|---|---|---|
mobidb-lite | MobiDBLite | 1 | 12.50 |