UniProt functional annotation for P22106



	UniProt functional annotation for P22106

UniProt code: P22106.

Organism: Escherichia coli (strain K12).

Taxonomy: Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia.

Function: Catalyzes the ATP-dependent conversion of aspartate into asparagine, using glutamine as a source of nitrogen. Can also use ammonia as the nitrogen source in vitro, albeit with lower efficiency. As nucleotide substrates, ATP and dATP are utilized at a similar rate in both the glutamine- and ammonia-dependent reactions, whereas GTP utilization is only 15% that of ATP, and CTP, UTP, ITP and XTP are very poor or not substrates. Also exhibits glutaminase activity. {ECO:0000269|PubMed:20853825, ECO:0000269|PubMed:6102982, ECO:0000269|PubMed:7907328}.

Catalytic activity: Reaction=ATP + H2O + L-aspartate + L-glutamine = AMP + diphosphate + H(+) + L-asparagine + L-glutamate; Xref=Rhea:RHEA:12228, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, ChEBI:CHEBI:29991, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:58048, ChEBI:CHEBI:58359, ChEBI:CHEBI:456215; EC=6.3.5.4; Evidence={ECO:0000269|PubMed:20853825, ECO:0000269|PubMed:7907328};

Activity regulation: Glutamine-dependent asparagine synthesis activity can be inhibited by aspartic acid analogs (such as a sulfinate derivative and (2S,3R)-2-amino-3-methylsuccinate) in vitro; the inhibition is competitive with respect to aspartate. {ECO:0000269|PubMed:8691431}.

Biophysicochemical properties: Kinetic parameters: KM=17 mM for ammonia {ECO:0000269|PubMed:12706338, ECO:0000269|PubMed:7907328}; KM=0.53 mM for aspartate (when assaying the ammonia-dependent synthetase reaction) {ECO:0000269|PubMed:12706338, ECO:0000269|PubMed:7907328}; KM=0.85 mM for aspartate (when assaying the glutamine-dependent synthetase reaction) {ECO:0000269|PubMed:12706338, ECO:0000269|PubMed:7907328}; KM=0.26 mM for ATP (when assaying the glutamine-dependent synthetase reaction) {ECO:0000269|PubMed:12706338, ECO:0000269|PubMed:7907328}; KM=0.66 mM for glutamine (when assaying the glutamine-dependent synthetase reaction) {ECO:0000269|PubMed:12706338, ECO:0000269|PubMed:7907328}; pH dependence: Optimum pH is 6.5-8. {ECO:0000269|PubMed:7907328};

Pathway: Amino-acid biosynthesis; L-asparagine biosynthesis; L- asparagine from L-aspartate (L-Gln route): step 1/1.

Subunit: Homodimer. {ECO:0000269|PubMed:10587437}.

Similarity: Belongs to the asparagine synthetase family. {ECO:0000305}.

Annotations taken from UniProtKB at the EBI.


Organism:		Escherichia coli (strain K12).
Taxonomy:		Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia.



Function:		Catalyzes the ATP-dependent conversion of aspartate into asparagine, using glutamine as a source of nitrogen. Can also use ammonia as the nitrogen source in vitro, albeit with lower efficiency. As nucleotide substrates, ATP and dATP are utilized at a similar rate in both the glutamine- and ammonia-dependent reactions, whereas GTP utilization is only 15% that of ATP, and CTP, UTP, ITP and XTP are very poor or not substrates. Also exhibits glutaminase activity. {ECO:0000269\|PubMed:20853825, ECO:0000269\|PubMed:6102982, ECO:0000269\|PubMed:7907328}.


Catalytic activity:		Reaction=ATP + H2O + L-aspartate + L-glutamine = AMP + diphosphate + H(+) + L-asparagine + L-glutamate; Xref=Rhea:RHEA:12228, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, ChEBI:CHEBI:29991, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:58048, ChEBI:CHEBI:58359, ChEBI:CHEBI:456215; EC=6.3.5.4; Evidence={ECO:0000269\|PubMed:20853825, ECO:0000269\|PubMed:7907328};
Activity regulation:		Glutamine-dependent asparagine synthesis activity can be inhibited by aspartic acid analogs (such as a sulfinate derivative and (2S,3R)-2-amino-3-methylsuccinate) in vitro; the inhibition is competitive with respect to aspartate. {ECO:0000269\|PubMed:8691431}.
Biophysicochemical properties:		Kinetic parameters: KM=17 mM for ammonia {ECO:0000269\|PubMed:12706338, ECO:0000269\|PubMed:7907328}; KM=0.53 mM for aspartate (when assaying the ammonia-dependent synthetase reaction) {ECO:0000269\|PubMed:12706338, ECO:0000269\|PubMed:7907328}; KM=0.85 mM for aspartate (when assaying the glutamine-dependent synthetase reaction) {ECO:0000269\|PubMed:12706338, ECO:0000269\|PubMed:7907328}; KM=0.26 mM for ATP (when assaying the glutamine-dependent synthetase reaction) {ECO:0000269\|PubMed:12706338, ECO:0000269\|PubMed:7907328}; KM=0.66 mM for glutamine (when assaying the glutamine-dependent synthetase reaction) {ECO:0000269\|PubMed:12706338, ECO:0000269\|PubMed:7907328}; pH dependence: Optimum pH is 6.5-8. {ECO:0000269\|PubMed:7907328};
Pathway:		Amino-acid biosynthesis; L-asparagine biosynthesis; L- asparagine from L-aspartate (L-Gln route): step 1/1.
Subunit:		Homodimer. {ECO:0000269\|PubMed:10587437}.
Similarity:		Belongs to the asparagine synthetase family. {ECO:0000305}.