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IPR011817 is a Uridylate kinase.
<p>Uridylate kinases (also known as UMP kinases) are key enzymes in the synthesis of nucleoside triphosphates. They catalyse the reversible transfer of the gamma-phosphoryl group from an ATP donor to UMP, yielding UDP, which is the starting point for the synthesis of all other pyrimidine nucleotides. The eukaryotic enzyme has a dual specificity, phosphorylating both UMP and CMP, while the bacterial enzyme is specific to UMP. The bacterial enzyme shows no sequence similarity to the eukaryotic enzyme or other nucleoside monophosphate kinases, but rather appears to be part of the amino acid kinase family. It is dependent on magnesium for activity and is activated by GTP and repressed by UTP [[cite:PUB00042653], [cite:PUB00042654]]. In many bacterial genomes, the gene tends to be located immediately downstream of elongation factor T and upstream of ribosome recycling factor. A related protein family, believed to be equivalent in function is found in the archaea and in spirochetes.</p> <p>Structurally, the bacterial and archaeal proteins are homohexamers centred around a hollow nucleus and organised as a trimer of dimers [[cite:PUB00039683], [cite:PUB00039689]]. Each monomer within the protein forms the amino acid kinase fold and can be divided into an N-terminal region which binds UMP and mediates intersubunit interactions within the dimer, and a C-terminal region which binds ATP and contains a mobile loop covering the active site. Inhibition of enzyme activity by UTP appears to be due to competition for the binding site for UMP, not allosteric inhibition as was previously suspected.</p> <p>This entry represents both the bacterial and archaeal enzymes.</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 |
|---|---|---|---|---|
| Biological process | Pyrimidine nucleotide biosynthetic process | The chemical reactions and pathways resulting in the formation of a pyrimidine nucleotide, a compound consisting of nucleoside (a pyrimidine base linked to a deoxyribose or ribose sugar) esterified with a phosphate group at either the 3' or 5'-hydroxyl group of the sugar. | ||
| Molecular function | Uridylate kinase activity | Catalysis of the reaction: ATP + (d)UMP = ADP + (d)UDP. |
| Transcript | Name | Description | Predicted domains | Domain count |
|---|---|---|---|---|
| – | PREDICTED: uridylate kinase-like [Glycine max] gi|356512819|ref|XP_003525113.1| | 18 | ||
| – | Uridylate kinase; TAIR: AT3G10030.1 aspartate/glutamate/uridylate kinase family protein; Swiss-Prot: sp|Q7VD61|PYRH_PROMA Uridylate kinase; TrEMBL-Plants: tr|V7BJN9|V7BJN9_PHAVU Uncharacterized protein; Found in the gene: LotjaGi5g1v0089900 | 15 |
A list of co-occurring predicted domains within the L. japonicus gene space:
| Predicted domain | Source | Observations | Saturation (%) |
|---|---|---|---|
| mobidb-lite | MobiDBLite | 1 | 50.00 |