SitesBLAST
Comparing WP_085122690.1 NCBI__GCF_900177295.1:WP_085122690.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 20 (the maximum) hits to proteins with known functional sites (download)
7tdpA Structure of paenibacillus polymyxa gs bound to met-sox-p-adp (transition state complex) to 1.98 angstom (see paper)
33% identity, 99% coverage: 7:444/444 of query aligns to 9:439/439 of 7tdpA
- binding adenosine-5'-diphosphate: N123 (vs. gap), G125 (≠ S140), E127 (= E142), E179 (≠ I189), D193 (≠ N203), Y196 (≠ P206), N242 (≠ H252), S244 (= S254), R316 (= R328), R326 (≠ H338)
- binding magnesium ion: E127 (= E142), E127 (= E142), E129 (= E144), E184 (= E194), E191 (= E201), E191 (= E201), H240 (= H250), E328 (= E340)
- binding l-methionine-s-sulfoximine phosphate: E127 (= E142), E129 (= E144), E184 (= E194), E191 (= E201), G236 (= G246), H240 (= H250), R293 (= R305), E299 (≠ F311), R311 (= R323), R330 (= R342)
7tfaB Glutamine synthetase (see paper)
33% identity, 99% coverage: 7:444/444 of query aligns to 9:441/441 of 7tfaB
- binding glutamine: E131 (= E144), Y153 (≠ H161), E186 (= E194), G238 (= G246), H242 (= H250), R295 (= R305), E301 (≠ F311)
- binding magnesium ion: E129 (= E142), E131 (= E144), E186 (= E194), E193 (= E201), H242 (= H250), E330 (= E340)
- binding : Y58 (≠ T71), R60 (≠ L73), V187 (≠ Y195), N237 (≠ A245), G299 (≠ H309), Y300 (≠ T310), R313 (= R323), M424 (≠ R427)
8oooA Glutamine synthetase from methanothermococcus thermolithotrophicus in complex with 2-oxoglutarate and mgatp at 2.15 a resolution (see paper)
31% identity, 98% coverage: 8:443/444 of query aligns to 3:447/447 of 8oooA
- binding 2-oxoglutaric acid: F17 (= F22), R19 (= R24), A33 (≠ L38), R87 (≠ K97), V93 (≠ T100), P170 (vs. gap), R173 (vs. gap), R174 (vs. gap), S190 (≠ H191)
- binding adenosine-5'-triphosphate: E136 (= E142), E188 (≠ I189), F203 (≠ Y204), K204 (≠ G205), F205 (≠ P206), H251 (= H252), S253 (= S254), R325 (= R328), R335 (≠ H338)
8ooqB Glutamine synthetase from Methanothermococcus thermolithotrophicus (see paper)
31% identity, 98% coverage: 8:443/444 of query aligns to 2:446/446 of 8ooqB
- binding 2-oxoglutaric acid: F16 (= F22), R18 (= R24), A32 (≠ L38), R86 (≠ K97), V92 (≠ T100), P169 (vs. gap), R172 (vs. gap), R173 (vs. gap), S189 (≠ H191)
- binding magnesium ion: E137 (= E144), E192 (= E194), E199 (= E201)
7tf6A Glutamine synthetase (see paper)
32% identity, 96% coverage: 17:444/444 of query aligns to 13:438/438 of 7tf6A
- binding glutamine: E128 (= E144), E183 (= E194), G235 (= G246), H239 (= H250), R292 (= R305), E298 (≠ F311)
- binding magnesium ion: E126 (= E142), E128 (= E144), E183 (= E194), E190 (= E201), H239 (= H250), E327 (= E340)
- binding : F58 (≠ T71), R60 (≠ L73), G232 (= G243), N234 (≠ A245), G296 (≠ H309), Y297 (≠ T310), R310 (= R323), Y367 (≠ S379), Y421 (≠ R427), Q433 (≠ E439), Q437 (≠ L443)
7tdvC Glutamine synthetase (see paper)
32% identity, 97% coverage: 15:444/444 of query aligns to 12:443/443 of 7tdvC
- binding adenosine-5'-diphosphate: G129 (≠ S140), E131 (= E142), E183 (≠ I189), D197 (≠ N203), F198 (≠ Y204), K199 (≠ G205), Y200 (≠ P206), N246 (≠ H252), V247 (≠ I253), S248 (= S254), R320 (= R328), S328 (≠ G336), R330 (≠ H338)
- binding magnesium ion: E131 (= E142), E131 (= E142), E133 (= E144), E188 (= E194), E195 (= E201), E195 (= E201), H244 (= H250), E332 (= E340)
- binding l-methionine-s-sulfoximine phosphate: E131 (= E142), E133 (= E144), E188 (= E194), E195 (= E201), G240 (= G246), H244 (= H250), R297 (= R305), E303 (≠ F311), R315 (= R323)
4s0rD Structure of gs-tnra complex (see paper)
31% identity, 98% coverage: 10:444/444 of query aligns to 10:447/447 of 4s0rD
- active site: D56 (≠ Y55), E135 (= E142), E137 (= E144), E192 (= E194), E199 (= E201), H248 (= H250), R319 (= R323), E336 (= E340), R338 (= R342)
- binding glutamine: E137 (= E144), E192 (= E194), R301 (= R305), E307 (≠ F311)
- binding magnesium ion: I66 (≠ N74), E135 (= E142), E135 (= E142), E199 (= E201), H248 (= H250), H248 (= H250), E336 (= E340), H419 (≠ L416)
- binding : F63 (≠ T71), V64 (≠ G72), R65 (≠ L73), I66 (≠ N74), D161 (≠ F163), G241 (= G243), V242 (≠ R244), N243 (≠ A245), G305 (≠ H309), Y306 (≠ T310), Y376 (vs. gap), I426 (≠ A423), M430 (≠ R427)
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: 10:444/444 of query aligns to 7:444/444 of P12425
- G59 (= G70) 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 (≠ L73) 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 (= E142) binding Mg(2+)
- E134 (= E144) binding Mg(2+)
- E189 (= E194) binding Mg(2+)
- V190 (≠ Y195) 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 (≠ H309) 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 (≠ F311) 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 (= P313) 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 (= E424) 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: 10:444/444 of query aligns to 6:443/443 of 4lnkA
- active site: D52 (≠ Y55), E131 (= E142), E133 (= E144), E188 (= E194), E195 (= E201), H244 (= H250), R315 (= R323), E332 (= E340), R334 (= R342)
- binding adenosine-5'-diphosphate: K43 (≠ G46), M50 (≠ N53), F198 (≠ Y204), Y200 (≠ P206), N246 (≠ H252), S248 (= S254), S324 (≠ T332), S328 (≠ G336), R330 (≠ H338)
- binding glutamic acid: E133 (= E144), E188 (= E194), V189 (≠ Y195), N239 (≠ A245), G240 (= G246), G242 (= G248), E303 (≠ F311)
- binding magnesium ion: E131 (= E142), 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: 10:444/444 of query aligns to 6:443/443 of 4lniA