SitesBLAST
Comparing WP_076581084.1 NCBI__GCF_001971705.1:WP_076581084.1 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)
8ooxB Glutamine synthetase (see paper)
54% identity, 98% coverage: 10:451/451 of query aligns to 3:438/438 of 8ooxB
7tdpA Structure of paenibacillus polymyxa gs bound to met-sox-p-adp (transition state complex) to 1.98 angstom (see paper)
56% identity, 96% coverage: 18:451/451 of query aligns to 12:439/439 of 7tdpA
- binding adenosine-5'-diphosphate: N123 (= N133), G125 (≠ A135), E127 (= E137), E179 (= E189), D193 (≠ N203), Y196 (= Y206), N242 (≠ H252), S244 (= S254), R316 (= R327), R326 (= R338)
- binding magnesium ion: E127 (= E137), E127 (= E137), E129 (= E139), E184 (= E194), E191 (= E201), E191 (= E201), H240 (= H250), E328 (= E340)
- binding l-methionine-s-sulfoximine phosphate: E127 (= E137), E129 (= E139), E184 (= E194), E191 (= E201), G236 (= G246), H240 (= H250), R293 (= R304), E299 (= E310), R311 (= R322), R330 (= R342)
7tfaB Glutamine synthetase (see paper)
56% identity, 96% coverage: 18:451/451 of query aligns to 12:441/441 of 7tfaB
- binding glutamine: E131 (= E139), Y153 (= Y161), E186 (= E194), G238 (= G246), H242 (= H250), R295 (= R304), E301 (= E310)
- binding magnesium ion: E129 (= E137), E131 (= E139), E186 (= E194), E193 (= E201), H242 (= H250), E330 (= E340)
- binding : Y58 (≠ F64), R60 (= R66), V187 (= V195), N237 (= N245), G299 (= G308), Y300 (= Y309), R313 (= R322), M424 (≠ E434)
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)
55% identity, 96% coverage: 17:451/451 of query aligns to 13:444/444 of P12425
- G59 (= G63) 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 (= R66) 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 (= E137) binding Mg(2+)
- E134 (= E139) binding Mg(2+)
- E189 (= E194) binding Mg(2+)
- V190 (= V195) 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 (= G308) 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 (= E310) 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 (= P312) 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
4s0rD Structure of gs-tnra complex (see paper)
55% identity, 96% coverage: 17:451/451 of query aligns to 16:447/447 of 4s0rD
- active site: D56 (= D57), E135 (= E137), E137 (= E139), E192 (= E194), E199 (= E201), H248 (= H250), R319 (= R322), E336 (= E340), R338 (= R342)
- binding glutamine: E137 (= E139), E192 (= E194), R301 (= R304), E307 (= E310)
- binding magnesium ion: I66 (= I67), E135 (= E137), E135 (= E137), E199 (= E201), H248 (= H250), H248 (= H250), E336 (= E340), H419 (≠ K423)
- binding : F63 (= F64), V64 (= V65), R65 (= R66), I66 (= I67), D161 (= D163), G241 (≠ E243), V242 (≠ I244), N243 (= N245), G305 (= G308), Y306 (= Y309), Y376 (= Y380), I426 (≠ Q430), M430 (≠ E434)
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)
55% identity, 96% coverage: 17:451/451 of query aligns to 12:443/443 of 4lnkA
- active site: D52 (= D57), E131 (= E137), E133 (= E139), E188 (= E194), E195 (= E201), H244 (= H250), R315 (= R322), E332 (= E340), R334 (= R342)
- binding adenosine-5'-diphosphate: K43 (= K48), M50 (≠ Y55), F198 (= F204), Y200 (= Y206), N246 (≠ H252), S248 (= S254), S324 (≠ A331), S328 (≠ A336), R330 (= R338)
- binding glutamic acid: E133 (= E139), E188 (= E194), V189 (= V195), N239 (= N245), G240 (= G246), G242 (= G248), E303 (= E310)
- binding magnesium ion: E131 (= E137), 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)
55% identity, 96% coverage: 17:451/451 of query aligns to 12:443/443 of 4lniA
- active site: D52 (= D57), E131 (= E137), E133 (= E139), E188 (= E194), E195 (= E201), H244 (= H250), R315 (= R322), E332 (= E340), R334 (= R342)
- binding adenosine-5'-diphosphate: E131 (= E137), E183 (= E189), D197 (≠ N203), Y200 (= Y206), N246 (≠ H252), S248 (= S254), R320 (= R327), R330 (= R338)
- binding magnesium ion: E131 (= E137), E131 (= E137), E133 (= E139), E188 (= E194), E195 (= E201), E195 (= E201), H244 (= H250), E332 (= E340)
- binding l-methionine-s-sulfoximine phosphate: E133 (= E139), E188 (= E194), H244 (= H250), R297 (= R304), E303 (= E310), R315 (= R322), R334 (= R342)
7tdvC Glutamine synthetase (see paper)
55% identity, 96% coverage: 17:451/451 of query aligns to 12:443/443 of 7tdvC
- binding adenosine-5'-diphosphate: G129 (≠ A135), E131 (= E137), E183 (= E189), D197 (≠ N203), F198 (= F204), K199 (≠ E205), Y200 (= Y206), N246 (≠ H252), V247 (≠ I253), S248 (= S254), R320 (= R327), S328 (≠ A336), R330 (= R338)
- binding magnesium ion: E131 (= E137), E131 (= E137), E133 (= E139), E188 (= E194), E195 (= E201), E195 (= E201), H244 (= H250), E332 (= E340)
- binding l-methionine-s-sulfoximine phosphate: E131 (= E137), E133 (= E139), E188 (= E194), E195 (= E201), G240 (= G246), H244 (= H250), R297 (= R304), E303 (= E310), R315 (= R322)
7tf6A Glutamine synthetase (see paper)
55% identity, 96% coverage: 18:451/451 of query aligns to 12:438/438 of 7tf6A
- binding glutamine: E128 (= E139), E183 (= E194), G235 (= G246), H239 (= H250), R292 (= R304), E298 (= E310)
- binding magnesium ion: E126 (= E137), E128 (= E139), E183 (= E194), E190 (= E201), H239 (= H250), E327 (= E340)
- binding : F58 (= F64), R60 (= R66), G232 (≠ E243), N234 (= N245), G296 (= G308), Y297 (= Y309), R310 (= R322), Y367 (= Y380), Y421 (≠ E434), Q433 (≠ R446), Q437 (≠ T450)
8ufjB Glutamine synthetase (see paper)
54% identity, 97% coverage: 13:451/451 of query aligns to 10:444/444 of 8ufjB