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UniProt functional annotation for P30870 | ||
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| UniProt code: P30870. |
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| Organism: | |
Escherichia coli (strain K12). |
| Taxonomy: | |
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia. |
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| Function: | |
Involved in the regulation of glutamine synthetase GlnA, a key enzyme in the process to assimilate ammonia (PubMed:8412694). When cellular nitrogen levels are high, the C-terminal adenylyl transferase inactivates GlnA by covalent transfer of an adenylyl group from ATP to 'Tyr-398' of GlnA, thus reducing its activity (PubMed:4920894, PubMed:9312015). Conversely, when nitrogen levels are low, the N- terminal adenylyl removase (AR) activates GlnA by removing the adenylyl group by phosphorolysis, increasing its activity (PubMed:4893578, PubMed:4920873, PubMed:4934180, PubMed:9312015, PubMed:14766310). The regulatory region of GlnE binds the signal transduction protein PII (GlnB) which indicates the nitrogen status of the cell (PubMed:8412694). {ECO:0000269|PubMed:14766310, ECO:0000269|PubMed:4867671, ECO:0000269|PubMed:4893578, ECO:0000269|PubMed:4920873, ECO:0000269|PubMed:4920894, ECO:0000269|PubMed:4934180, ECO:0000269|PubMed:8412694, ECO:0000269|PubMed:9312015}. |
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| Catalytic activity: | |
Reaction=[glutamine synthetase]-O(4)-(5'-adenylyl)-L-tyrosine + phosphate = [glutamine synthetase]-L-tyrosine + ADP; Xref=Rhea:RHEA:43716, Rhea:RHEA-COMP:10660, Rhea:RHEA-COMP:10661, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858, ChEBI:CHEBI:83624, ChEBI:CHEBI:456216; EC=2.7.7.89; Evidence={ECO:0000269|PubMed:4934180, ECO:0000305|PubMed:14766310, ECO:0000305|PubMed:4893578, ECO:0000305|PubMed:4920873, ECO:0000305|PubMed:9312015}; |
| Catalytic activity: | |
Reaction=[glutamine synthetase]-L-tyrosine + ATP = [glutamine synthetase]-O(4)-(5'-adenylyl)-L-tyrosine + diphosphate; Xref=Rhea:RHEA:18589, Rhea:RHEA-COMP:10660, Rhea:RHEA-COMP:10661, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:46858, ChEBI:CHEBI:83624; EC=2.7.7.42; Evidence={ECO:0000269|PubMed:4920894, ECO:0000305|PubMed:9312015}; |
| Cofactor: | |
Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:4867671, ECO:0000269|PubMed:4893578, ECO:0000269|PubMed:4920894, ECO:0000269|PubMed:4934180}; Note=Can also use Mn(2+). {ECO:0000269|PubMed:4867671, ECO:0000269|PubMed:4893578, ECO:0000269|PubMed:4920894, ECO:0000269|PubMed:4934180}; |
| Activity regulation: | |
The adenylation activity is stimulated by glutamine and PII (GlnB), and inhibited by 2-oxoglutarate (PubMed:4867671, PubMed:4920894, PubMed:33597, PubMed:9312015). Deadenylation activity is stimulated by PII-UMP (GlnB-UMP) and 2- oxoglutarate, and inhibited by glutamine (PubMed:4893578, PubMed:4934180, PubMed:33597, PubMed:9312015, PubMed:14766310). {ECO:0000269|PubMed:14766310, ECO:0000269|PubMed:33597, ECO:0000269|PubMed:4867671, ECO:0000269|PubMed:4893578, ECO:0000269|PubMed:4920894, ECO:0000269|PubMed:4934180, ECO:0000269|PubMed:9312015}. |
| Biophysicochemical properties: | |
Kinetic parameters: KM=4 uM for adenylyl {ECO:0000269|PubMed:4893578}; KM=5 uM for [L-glutamate:ammonia ligase (ADP-forming)] {ECO:0000269|PubMed:4920894}; KM=150 uM for ATP {ECO:0000269|PubMed:4920894}; pH dependence: Optimum pH is between 7.3 and 7.6 (PubMed:4893578, PubMed:4920894). The enzyme is stable between pH 4 and 9 (PubMed:4920894). {ECO:0000269|PubMed:4893578, ECO:0000269|PubMed:4920894}; |
| Subunit: | |
Monomer. {ECO:0000269|PubMed:4920894}. |
| Similarity: | |
Belongs to the GlnE family. {ECO:0000305}. |
Annotations taken from UniProtKB at the EBI.