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UniProt functional annotation for P28650 | ||
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| UniProt code: P28650. |
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| Organism: | |
Mus musculus (Mouse). |
| Taxonomy: | |
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; Murinae; Mus; Mus. |
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| Function: | |
Component of the purine nucleotide cycle (PNC), which interconverts IMP and AMP to regulate the nucleotide levels in various tissues, and which contributes to glycolysis and ammoniagenesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000269|PubMed:12482871}. |
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| Catalytic activity: | |
Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2- dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000255|HAMAP- Rule:MF_03126}; |
| Cofactor: | |
Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Note=Binds 1 Mg(2+) ion per subunit.; |
| Activity regulation: | |
Weakly inhibited by AMP non-competitively to all substrates. Inhibited by IMP non-competitively with respect to GTP. Inhibited by fructose 1,6-bisphosphate competitively with respect to IMP. |
| Biophysicochemical properties: | |
Kinetic parameters: KM=12 uM for GTP {ECO:0000269|PubMed:12482871}; KM=45 uM for IMP {ECO:0000269|PubMed:12482871}; KM=140 uM for L-aspartate {ECO:0000269|PubMed:12482871}; pH dependence: Optimum pH is 6.6-6.9. {ECO:0000269|PubMed:12482871}; |
| Pathway: | |
Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. {ECO:0000255|HAMAP-Rule:MF_03126}. |
| Subunit: | |
Homodimer. {ECO:0000255|HAMAP-Rule:MF_03126, ECO:0000269|PubMed:12004071}. |
| Subcellular location: | |
Cytoplasm. Membrane; Peripheral membrane protein. Note=Partially associated with particulate fractions. |
| Tissue specificity: | |
High levels in muscle. |
| Similarity: | |
Belongs to the adenylosuccinate synthetase family. {ECO:0000255|HAMAP-Rule:MF_03126}. |
Annotations taken from UniProtKB at the EBI.