SitesBLAST

P12425 Glutamine synthetase; GS; Glutamate--ammonia ligase; Glutamine synthetase I alpha; GSI alpha; EC 6.3.1.2 from Bacillus subtilis (strain 168) (see 5 papers)
34% identity, 99% coverage: 3:449/453 of query aligns to 2:440/444 of P12425

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G59 (= G60) mutation to R: Unable to form stable complex with TnrA. In the presence of glutamine, this mutant derepresses amtB-lacZ fusion and glnRA-lacZ fusion.
R62 (≠ K64) Important for inhibition by glutamine; mutation to A: Highly resistant to inhibition by glutamine and AMP. Regulation by TnrA and GlnR is abolished. Only small differences (less than 2-fold) in its steady-state kinetic constants compared with the wild-type. Similar sensitivity to Met-Sox that compared to the wild-ytpe.
E132 (= E129) binding Mg(2+)
E134 (= E131) binding Mg(2+)
E189 (= E189) binding Mg(2+)
V190 (≠ D190) mutation to A: Unable to form stable complex with TnrA. In the presence of glutamine, this mutant partially relieves expression of the glnRA-lacZ fusion, but has no effect on the TnrA-dependent regulation of amtB-lacZ fusion. Resistant to inhibition by MetSox.
E196 (= E196) binding Mg(2+)
G241 (= G241) binding L-glutamate
H245 (= H245) binding Mg(2+)
G302 (≠ Q308) mutation to E: Unable to form stable complex with TnrA. In the presence of glutamine, amtB-lacZ fusion is only 4-fold regulated by TnrA, whereas glnRA-lacZ fusion is derepressed. This mutant retains enzymatic specific activity with a 2-fold decrease of the affinity for glutamate and glutamine compared to the wild-type. Slightly less sensitive to inhibition by glutamine.
E304 (≠ D310) mutation to A: Highly resistant to Met-Sox inhibition. 8- and 2-fold increase of the affinity for glutamate and ATP, respectively. Strong decrease of the affinity for ammonium.
P306 (= P318) mutation to H: Unable to form stable complex with TnrA. In the presence of glutamine, this mutant completely derepresses glnRA-lacZ fusion, whereas amtB-lacZ fusion expression is only partially derepresses.
E333 (= E342) binding Mg(2+)
E424 (= E433) mutation to K: Unable to form stable complex with TnrA. In the presence of glutamine, this mutant derepresses amtB-lacZ fusion and glnRA-lacZ fusion. Although it is defective in regulation, this mutant retains enzymatic specific activity and similar affinity for ATP, glutamate and glutamine compared to the wild-type. Slightly less sensitive to inhibition by glutamine.

Sites not aligning to the query:

1 modified: Initiator methionine, Removed

4lnkA B. Subtilis glutamine synthetase structures reveal large active site conformational changes and basis for isoenzyme specific regulation: structure of gs-glutamate-amppcp complex (see paper)
33% identity, 100% coverage: 3:453/453 of query aligns to 1:443/443 of 4lnkA

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active site: D52 (≠ T54), E131 (= E129), E133 (= E131), E188 (= E189), E195 (= E196), H244 (= H245), R315 (= R328), E332 (= E342), R334 (= R344)
binding adenosine-5'-diphosphate: K43 (≠ Q45), M50 (≠ L52), F198 (= F199), Y200 (= Y201), N246 (= N247), S248 (= S249), S324 (≠ G337), S328 (vs. gap), R330 (= R340)
binding glutamic acid: E133 (= E131), E188 (= E189),