SitesBLAST

Comparing WP_099618753.1 NCBI__GCF_002744735.1:WP_099618753.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.

Found 20 (the maximum) hits to proteins with known functional sites

7cqwA Gmas/adp complex-conformation 1 (see paper)
40% identity, 98% coverage: 1:444/452 of query aligns to 1:423/430 of 7cqwA

• binding adenosine-5'-diphosphate: Y174 (= Y184), Y191 (= Y201), H237 (≠ N247), L238 (≠ M248), S239 (= S249), R317 (= R332), R323 (= R339)

7cquA Gmas/adp/metsox-p complex (see paper)
40% identity, 95% coverage: 16:444/452 of query aligns to 9:422/429 of 7cquA

• binding adenosine-5'-diphosphate: E121 (= E129), Y173 (= Y184), N187 (≠ D198), W188 (≠ F199), D189 (≠ K200), Y190 (= Y201), H236 (≠ N247), L237 (≠ M248), S238 (= S249), R316 (= R332), R322 (= R339)
• binding magnesium ion: E121 (= E129), E121 (= E129), E123 (= E131), E178 (= E189), E185 (= E196), E185 (= E196), H234 (= H245), E324 (= E341)
• binding l-methionine-s-sulfoximine phosphate: E121 (= E129), E123 (= E131), E178 (= E189), E185 (= E196), T229 (= T240), G230 (= G241), H234 (= H245), R287 (= R303), W299 (= W315), R311 (= R327), R326 (= R343)

7cqqA Gmas in complex with amppnp and metsox (see paper)
40% identity, 95% coverage: 16:444/452 of query aligns to 9:422/429 of 7cqqA

• binding phosphoaminophosphonic acid-adenylate ester: E121 (= E129), Y173 (= Y184), E185 (= E196), N187 (≠ D198), D189 (≠ K200), Y190 (= Y201), H234 (= H245), H236 (≠ N247), S238 (= S249), R311 (= R327), R316 (= R332), R322 (= R339), E324 (= E341)
• binding magnesium ion: E121 (= E129), E121 (= E129), E123 (= E131), E178 (= E189), E185 (= E196), E185 (= E196), H234 (= H245), E324 (= E341)
• binding (2s)-2-amino-4-(methylsulfonimidoyl)butanoic acid: E123 (= E131), E178 (= E189), T229 (= T240), H234 (= H245), R287 (= R303), W299 (= W315), R311 (= R327), R326 (= R343)

7cqnA Gmas in complex with amppcp (see paper)
40% identity, 95% coverage: 16:444/452 of query aligns to 9:422/429 of 7cqnA

• binding phosphomethylphosphonic acid adenylate ester: G45 (≠ L52), D61 (≠ E69), E121 (= E129), Y173 (= Y184), Q174 (≠ S185), W188 (≠ F199), D189 (≠ K200), Y190 (= Y201), H236 (≠ N247), S238 (= S249), R311 (= R327), R316 (= R332), R322 (= R339)

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)
37% identity, 99% coverage: 6:452/452 of query aligns to 5:444/444 of P12425

• 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 (≠ Q63) 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 (≠ S313) 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 (≠ W315) 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 (= P317) 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 (= E341) binding Mg(2+)
• E424 (= E432) 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)
37% identity, 99% coverage: 6:452/452 of query aligns to 4:443/443 of 4lnkA

• active site: D52 (≠ T54), E131 (= E129), E133 (= E131), E188 (= E189), E195 (= E196), H244 (= H245), R315 (= R327), E332 (= E341), R334 (= R343)
• binding adenosine-5'-diphosphate: K43 (≠ Q45), M50 (≠ L52), F198 (= F199), Y200 (= Y201), N246 (= N247), S248 (= S249), S324 (vs. gap), S328 (≠ G337), R330 (= R339)
• binding glutamic acid: E133 (= E131), E188 (= E189), V189 (≠ D190), N239 (≠ T240), G240 (= G241), G242 (= G243), E303 (≠ W315)
• binding magnesium ion: E131 (= E129), E188 (= E189), E195 (= E196), H244 (= H245), E332 (= E341)

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)
37% identity, 99% coverage: 6:452/452 of query aligns to 4:443/443 of 4lniA

• active site: D52 (≠ T54), E131 (= E129), E133 (= E131), E188 (= E189), E195 (= E196), H244 (= H245), R315 (= R327), E332 (= E341), R334 (= R343)
• binding adenosine-5'-diphosphate: E131 (= E129), E183 (≠ Y184), D197 (= D198), Y200 (= Y201), N246 (= N247), S248 (= S249), R320 (= R332), R330 (= R339)
• binding magnesium ion: E131 (= E129), E131 (= E129), E133 (= E131), E188 (= E189), E195 (= E196), E195 (= E196), H244 (= H245), E332 (= E341)
• binding l-methionine-s-sulfoximine phosphate: E133 (= E131), E188 (= E189), H244 (= H245), R297 (= R303), E303 (≠ W315), R315 (= R327), R334 (= R343)

4s0rD Structure of gs-tnra complex (see paper)
37% identity, 99% coverage: 6:452/452 of query aligns to 8:447/447 of 4s0rD

• active site: D56 (≠ T54), E135 (= E129), E137 (= E131), E192 (= E189), E199 (= E196), H248 (= H245), R319 (= R327), E336 (= E341), R338 (= R343)
• binding glutamine: E137 (= E131), E192 (= E189), R301 (= R303), E307 (≠ W315)
• binding magnesium ion: I66 (= I65), E135 (= E129), E135 (= E129), E199 (= E196), H248 (= H245), H248 (= H245), E336 (= E341), H419 (≠ S424)
• binding : F63 (≠ V61), V64 (≠ P62), R65 (≠ Q63), I66 (= I65), D161 (≠ C156), G241 (≠ D238), V242 (≠ R239), N243 (≠ T240), G305 (≠ S313), Y306 (≠ T314), Y376 (= Y381), I426 (≠ G431), M430 (≠ S435)

7tdpA Structure of paenibacillus polymyxa gs bound to met-sox-p-adp (transition state complex) to 1.98 angstom (see paper)
36% identity, 99% coverage: 6:452/452 of query aligns to 3:439/439 of 7tdpA

• binding adenosine-5'-diphosphate: N123 (= N125), G125 (= G127), E127 (= E129), E179 (≠ Y184), D193 (= D198), Y196 (= Y201), N242 (= N247), S244 (= S249), R316 (= R332), R326 (= R339)
• binding magnesium ion: E127 (= E129), E127 (= E129), E129 (= E131), E184 (= E189), E191 (= E196), E191 (= E196), H240 (= H245), E328 (= E341)
• binding l-methionine-s-sulfoximine phosphate: E127 (= E129), E129 (= E131), E184 (= E189), E191 (= E196), G236 (= G241), H240 (= H245), R293 (= R303), E299 (≠ W315), R311 (= R327), R330 (= R343)

7tf6A Glutamine synthetase (see paper)
35% identity, 99% coverage: 6:452/452 of query aligns to 3:438/438 of 7tf6A