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)
31% identity, 98% coverage: 10:451/451 of query aligns to 7:444/444 of P12425

query
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P12425

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G59 (≠ S66) 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 (≠ V69) 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 (= E140) binding Mg(2+)
E134 (= E142) binding Mg(2+)
E189 (= E194) binding Mg(2+)
V190 (≠ S195) 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 (= E201) binding Mg(2+)
G241 (= G246) binding L-glutamate
H245 (= H250) binding Mg(2+)
G302 (≠ H307) 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 (≠ W309) 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 (≠ G311) 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 (= E340) binding Mg(2+)
E424 (= E431) 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)
31% identity, 98% coverage: 10:451/451 of query aligns to 6:443/443 of 4lnkA

query
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4lnkA

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active site: D52 (≠ T56), E131 (= E140), E133 (= E142), E188 (= E194), E195 (= E201), H244 (= H250), R315 (= R321), E332 (= E340), R334 (≠ K342)
binding adenosine-5'-diphosphate: K43 (≠ E47), M50 (≠ S54), F198 (≠ I204), Y200 (= Y206), N246 (≠ H252), S248 (= S254), S324 (≠ N330), S328 (≠ P336), R330 (≠ H338)
binding glutamic acid: E133 (= E142), E188 (= E194), V189 (≠ S195), N239 (≠ A245), G240 (= G246), G242 (= G248), E303 (≠ W309)
binding magnesium ion: E131 (= E140), E188 (= E194), E195 (= E201), H244 (= H250), E332 (= E340)

4lniA B. Subtilis glutamine synthetase structures reveal large active site conformational changes and basis for isoenzyme specific regulation: structure of the transition state complex (see paper)
31% identity, 98% coverage: 10:451/451 of query aligns to 6:443/443 of 4lniA

query
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4lniA

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