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IPR025777 is a GMP synthetase ATP pyrophosphatase domain.
<p>Guanosine 5'-monophosphate synthetase (GMPS) is a widespread enzyme seen in all domains of life. GMPS is required for the final step of the de novo synthesis of guanine nucleotides, converting xanthosine 5'-monophosphate (XMP) into guanosine 5'-monophosphate (GMP), a precursor of DNA and RNA. GMPS consists of two catalytic units, glutamine amidotransferase (GATase) and ATP pyrophosphatase (ATP-PPase). GATase hydrolyzes glutamine to yield glutamate and ammonia, while ATP-PPase utilises ammonia to convert adenyl xanthosine 5'-monophosphate (adenyl-XMP) into GMP. The two catalytic units are either encoded by a single gene (two-domain type) in eucaryotes, bacteria, and some archaea, or encoded by two separate genes (two-subunit type) in other archaea. In two-domain-type GMPS, the GATase domain is located in the N-terminal half, and the ATP-PPase domain is located in the C-terminal half; in two-subunit-type GMPS, these two units exist as separate polypeptides. ATP-PPase consists of two domains (N-domain and C-domain). The N-domain contains an ATP-binding platform called P-loop, whereas the C-domain contains the XMP-binding site and also contributes to homodimerisation [[cite:PUB00003933], [cite:PUB00057998], [cite:PUB00057178]].</p> <p>The GMP synthetase ATP-PPase ATP-binding domain is a twisted, five-stranded parallel β-sheet sandwiched between helical layers. It contains a glycine rich ATP-binding motif called the "P-loop motif" located after the first β-strand [[cite:PUB00003933], [cite:PUB00057178]].</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 | ATP binding | Interacting selectively and non-covalently with ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. | ||
| Molecular function | Pyrophosphatase activity | Catalysis of the hydrolysis of a pyrophosphate bond between two phosphate groups, leaving one phosphate on each of the two fragments. |
| Transcript | Name | Description | Predicted domains | Domain count |
|---|---|---|---|---|
| – | PREDICTED: GMP synthase [glutamine]-hydrolyzing] gi|502139270|ref|XP_004503710.1| | 26 | ||
| – | GMP synthase [glutamine]-hydrolyzing] protein; TAIR: AT1G63660.1 GMP synthase (glutamine-hydrolyzing), putative / glutamine amidotransferase; Swiss-Prot: sp|Q89N53|GUAA_BRADU GMP synthase [glutamine]-hydrolyzing]; TrEMBL-Plants: tr|A0A0L9VPW7|A0A0L9VPW7_PHAAN Uncharacterized protein; Found in the gene: LotjaGi4g1v0426900 | 26 |
A list of co-occurring predicted domains within the L. japonicus gene space:
| Predicted domain | Source | Observations | Saturation (%) |
|---|---|---|---|
| cd01997 | CDD | 1 | 50.00 |