UniProt functional annotation for P0A1P6

UniProt code: P0A1P6.

Organism: Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
Taxonomy: Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Salmonella.
 
Function: Catalyzes the ATP-dependent biosynthesis of glutamine from glutamate and ammonia. {ECO:0000269|PubMed:7727369}.
 
Catalytic activity: Reaction=ATP + L-glutamate + NH4(+) = ADP + H(+) + L-glutamine + phosphate; Xref=Rhea:RHEA:16169, ChEBI:CHEBI:15378, ChEBI:CHEBI:28938, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:58359, ChEBI:CHEBI:456216; EC=6.3.1.2; Evidence={ECO:0000305|PubMed:7727369};
Cofactor: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:11329256, ECO:0000269|PubMed:2572586, ECO:0000269|PubMed:7727369, ECO:0000269|PubMed:8099447}; Note=Binds 2 Mn(2+) ions per subunit. {ECO:0000269|PubMed:11329256, ECO:0000269|PubMed:2572586, ECO:0000269|PubMed:7727369, ECO:0000269|PubMed:8099447};
Activity regulation: When cellular nitrogen levels are high, the C- terminal adenylyl transferase (AT) of GlnE inhibits GlnA by covalent transfer of an adenylyl group from ATP to Tyr-398. Conversely, when nitrogen levels are low, the N-terminal adenylyl removase (AR) of GlnE activates GlnA by removing the adenylyl group by phosphorolysis. The fully adenylated enzyme complex is inactive. {ECO:0000250|UniProtKB:Q3V5W6}.
Biophysicochemical properties: Kinetic parameters: KM=0.58 mM for ATP {ECO:0000269|PubMed:7727369};
Subunit: Oligomer of 12 subunits arranged in the form of two hexameric ring. {ECO:0000269|PubMed:11329256, ECO:0000269|PubMed:2572586, ECO:0000269|PubMed:7727369, ECO:0000269|PubMed:8099447}.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P9WN39}.
Similarity: Belongs to the glutamine synthetase family. {ECO:0000305}.

Annotations taken from UniProtKB at the EBI.