SitesBLAST
Comparing PfGW456L13_2714 FitnessBrowser__pseudo13_GW456_L13:PfGW456L13_2714 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)
5dm3C Crystal structure of glutamine synthetase from chromohalobacter salexigens dsm 3043(csal_0679, target efi-550015) with bound adp
53% identity, 98% coverage: 7:455/457 of query aligns to 1:396/396 of 5dm3C
- active site: E115 (= E144), E117 (= E146), E162 (= E207), E169 (= E214), H218 (= H263), R286 (= R336), E303 (= E353), R305 (= R355)
- binding adenosine-5'-diphosphate: R173 (= R218), C174 (≠ Y219), H220 (= H265), S222 (= S267), R301 (= R351)
5dm3A Crystal structure of glutamine synthetase from chromohalobacter salexigens dsm 3043(csal_0679, target efi-550015) with bound adp
51% identity, 98% coverage: 6:455/457 of query aligns to 2:374/374 of 5dm3A
- active site: E107 (= E144), E109 (= E146), E146 (= E207), E150 (= E214), H199 (= H263), R265 (= R336), E282 (= E353), R284 (= R355)
- binding adenosine-5'-diphosphate: I103 (≠ M140), E141 (= E202), R154 (= R218), C155 (≠ Y219), H201 (= H265), S203 (= S267), R280 (= R351)
7tdpA Structure of paenibacillus polymyxa gs bound to met-sox-p-adp (transition state complex) to 1.98 angstom (see paper)
32% identity, 81% coverage: 81:449/457 of query aligns to 64:431/439 of 7tdpA
- binding adenosine-5'-diphosphate: N123 (vs. gap), G125 (≠ A142), E127 (= E144), E179 (= E202), D193 (≠ N216), Y196 (= Y219), N242 (≠ H265), S244 (= S267), R316 (= R341), R326 (= R351)
- binding magnesium ion: E127 (= E144), E127 (= E144), E129 (= E146), E184 (= E207), E191 (= E214), E191 (= E214), H240 (= H263), E328 (= E353)
- binding l-methionine-s-sulfoximine phosphate: E127 (= E144), E129 (= E146), E184 (= E207), E191 (= E214), G236 (= G259), H240 (= H263), R293 (= R318), E299 (≠ F324), R311 (= R336), R330 (= R355)
7tfaB Glutamine synthetase (see paper)
32% identity, 81% coverage: 81:449/457 of query aligns to 64:433/441 of 7tfaB
- binding glutamine: E131 (= E146), Y153 (≠ H170), E186 (= E207), G238 (= G259), H242 (= H263), R295 (= R318), E301 (≠ F324)
- binding magnesium ion: E129 (= E144), E131 (= E146), E186 (= E207), E193 (= E214), H242 (= H263), E330 (= E353)
- binding : V187 (≠ W208), N237 (≠ A258), G299 (= G322), Y300 (≠ T323), R313 (= R336), M424 (≠ E440)
Sites not aligning to the query:
7tf6A Glutamine synthetase (see paper)
31% identity, 82% coverage: 82:457/457 of query aligns to 65:438/438 of 7tf6A
- binding glutamine: E128 (= E146), E183 (= E207), G235 (= G259), H239 (= H263), R292 (= R318), E298 (≠ F324)
- binding magnesium ion: E126 (= E144), E128 (= E146), E183 (= E207), E190 (= E214), H239 (= H263), E327 (= E353)
- binding : G232 (≠ D256), N234 (≠ A258), G296 (= G322), Y297 (≠ T323), R310 (= R336), Y367 (= Y393), Y421 (≠ E440), Q433 (≠ R452), Q437 (≠ R456)
Sites not aligning to the query:
7tdvC Glutamine synthetase (see paper)
30% identity, 82% coverage: 82:457/457 of query aligns to 66:443/443 of 7tdvC
- binding adenosine-5'-diphosphate: G129 (≠ A142), E131 (= E144), E183 (= E202), D197 (≠ N216), F198 (≠ I217), K199 (≠ R218), Y200 (= Y219), N246 (≠ H265), V247 (≠ N266), S248 (= S267), R320 (= R341), S328 (≠ A349), R330 (= R351)
- binding magnesium ion: E131 (= E144), E131 (= E144), E133 (= E146), E188 (= E207), E195 (= E214), E195 (= E214), H244 (= H263), E332 (= E353)
- binding l-methionine-s-sulfoximine phosphate: E131 (= E144), E133 (= E146), E188 (= E207), E195 (= E214), G240 (= G259), H244 (= H263), R297 (= R318), E303 (≠ F324), R315 (= R336)
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)
30% identity, 82% coverage: 82:457/457 of query aligns to 66:443/443 of 4lnkA
- active site: E131 (= E144), E133 (= E146), E188 (= E207), E195 (= E214), H244 (= H263), R315 (= R336), E332 (= E353), R334 (= R355)
- binding adenosine-5'-diphosphate: F198 (≠ I217), Y200 (= Y219), N246 (≠ H265), S248 (= S267), S324 (≠ E345), S328 (≠ A349), R330 (= R351)
- binding glutamic acid: E133 (= E146), E188 (= E207), V189 (≠ W208), N239 (≠ A258), G240 (= G259), G242 (≠ S261), E303 (≠ F324)
- binding magnesium ion: E131 (= E144), E188 (= E207), E195 (= E214), H244 (= H263), E332 (= E353)
Sites not aligning to the query:
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)
30% identity, 82% coverage: 82:457/457 of query aligns to 66:443/443 of 4lniA
- active site: E131 (= E144), E133 (= E146), E188 (= E207), E195 (= E214), H244 (= H263), R315 (= R336), E332 (= E353), R334 (= R355)
- binding adenosine-5'-diphosphate: E131 (= E144), E183 (= E202), D197 (≠ N216), Y200 (= Y219), N246 (≠ H265), S248 (= S267), R320 (= R341), R330 (= R351)
- binding magnesium ion: E131 (= E144), E131 (= E144), E133 (= E146), E188 (= E207), E195 (= E214), E195 (= E214), H244 (= H263), E332 (= E353)
- binding l-methionine-s-sulfoximine phosphate: E133 (= E146), E188 (= E207), H244 (= H263), R297 (= R318), E303 (≠ F324), R315 (= R336), R334 (= R355)
Sites not aligning to the query:
4s0rD Structure of gs-tnra complex (see paper)
30% identity, 82% coverage: 82:457/457 of query aligns to 70:447/447 of 4s0rD
- active site: E135 (= E144), E137 (= E146), E192 (= E207), E199 (= E214), H248 (= H263), R319 (= R336), E336 (= E353), R338 (= R355)
- binding glutamine: E137 (= E146), E192 (= E207), R301 (= R318), E307 (≠ F324)
- binding magnesium ion: E135 (= E144), E135 (= E144), E199 (= E214), H248 (= H263), H248 (= H263), E336 (= E353), H419 (= H429)
- binding : D161 (≠ N176), G241 (≠ D256), V242 (≠ A257), N243 (≠ A258), G305 (= G322), Y306 (≠ T323), Y376 (= Y393), I426 (≠ W436), M430 (≠ E440)
Sites not aligning to the query:
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)
30% identity, 82% coverage: 82:457/457 of query aligns to 67:444/444 of P12425
- E132 (= E144) binding
- E134 (= E146) binding
- E189 (= E207) binding
- V190 (≠ W208) 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 (= E214) binding
- G241 (= G259) binding
- H245 (= H263) binding
- G302 (= G322) 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 (≠ F324) 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 (= P326) 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 (= E353) binding
- E424 (= E437) 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
- 59 G→R: Unable to form stable complex with TnrA. In the presence of glutamine, this mutant derepresses amtB-lacZ fusion and glnRA-lacZ fusion.
- 62 Important for inhibition by glutamine; R→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.
A0R083 Glutamine synthetase; GS; Glutamate--ammonia ligase; Glutamine synthetase I alpha; GSI alpha; EC 6.3.1.2 from Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis) (see paper)
30% identity, 81% coverage: 82:451/457 of query aligns to 66:441/446 of A0R083