SitesBLAST
Comparing Ac3H11_1551 FitnessBrowser__acidovorax_3H11:Ac3H11_1551 to proteins with known functional sites using BLASTp with E ≤ 0.001.
Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures
Found 20 (the maximum) hits to proteins with known functional sites (download)
7cqwA Gmas/adp complex-conformation 1 (see paper)
44% identity, 90% coverage: 4:395/435 of query aligns to 13:392/430 of 7cqwA
7cquA Gmas/adp/metsox-p complex (see paper)
44% identity, 90% coverage: 4:395/435 of query aligns to 12:391/429 of 7cquA
- binding adenosine-5'-diphosphate: E121 (= E115), Y173 (= Y171), N187 (= N185), W188 (≠ F186), D189 (≠ T187), Y190 (= Y188), H236 (= H234), L237 (≠ M235), S238 (= S236), R316 (= R317), R322 (= R322)
- binding magnesium ion: E121 (= E115), E121 (= E115), E123 (= E117), E178 (= E176), E185 (= E183), E185 (= E183), H234 (= H232), E324 (= E324)
- binding l-methionine-s-sulfoximine phosphate: E121 (= E115), E123 (= E117), E178 (= E176), E185 (= E183), T229 (≠ S227), G230 (= G228), H234 (= H232), R287 (= R288), W299 (= W300), R311 (= R312), R326 (= R326)
7cqqA Gmas in complex with amppnp and metsox (see paper)
44% identity, 90% coverage: 4:395/435 of query aligns to 12:391/429 of 7cqqA
- binding phosphoaminophosphonic acid-adenylate ester: E121 (= E115), Y173 (= Y171), E185 (= E183), N187 (= N185), D189 (≠ T187), Y190 (= Y188), H234 (= H232), H236 (= H234), S238 (= S236), R311 (= R312), R316 (= R317), R322 (= R322), E324 (= E324)
- binding magnesium ion: E121 (= E115), E121 (= E115), E123 (= E117), E178 (= E176), E185 (= E183), E185 (= E183), H234 (= H232), E324 (= E324)
- binding (2s)-2-amino-4-(methylsulfonimidoyl)butanoic acid: E123 (= E117), E178 (= E176), T229 (≠ S227), H234 (= H232), R287 (= R288), W299 (= W300), R311 (= R312), R326 (= R326)
7cqnA Gmas in complex with amppcp (see paper)
44% identity, 90% coverage: 4:395/435 of query aligns to 12:391/429 of 7cqnA
- binding phosphomethylphosphonic acid adenylate ester: G45 (= G37), D61 (≠ E54), E121 (= E115), Y173 (= Y171), Q174 (= Q172), W188 (≠ F186), D189 (≠ T187), Y190 (= Y188), H236 (= H234), S238 (= S236), R311 (= R312), R316 (= R317), R322 (= R322)
8oooA Glutamine synthetase from methanothermococcus thermolithotrophicus in complex with 2-oxoglutarate and mgatp at 2.15 a resolution (see paper)
37% identity, 97% coverage: 10:432/435 of query aligns to 21:445/447 of 8oooA
- binding 2-oxoglutaric acid: A33 (≠ L22), R87 (≠ M70), V93 (≠ T73), P170 (≠ S153), R173 (≠ L156), R174 (≠ M157), S190 (≠ I173)
- binding adenosine-5'-triphosphate: E136 (= E115), E188 (≠ Y171), F203 (= F186), K204 (≠ T187), F205 (≠ Y188), H251 (= H234), S253 (= S236), R325 (= R317), R335 (= R322)
Sites not aligning to the query:
8ooqB Glutamine synthetase from Methanothermococcus thermolithotrophicus (see paper)
37% identity, 97% coverage: 10:432/435 of query aligns to 20:444/446 of 8ooqB
Sites not aligning to the query:
8tfkA Glutamine synthetase (see paper)
35% identity, 97% coverage: 9:432/435 of query aligns to 20:437/440 of 8tfkA
- binding adenosine-5'-diphosphate: E128 (= E115), D194 (≠ N185), F195 (= F186), F197 (≠ Y188), N243 (≠ H234), R312 (= R312), R317 (= R317), G325 (= G320), R327 (= R322)
- binding magnesium ion: E128 (= E115), E128 (= E115), E130 (= E117), E185 (= E176), E192 (= E183), E192 (= E183), H241 (= H232), E329 (= E324)
- binding l-methionine-s-sulfoximine phosphate: E128 (= E115), E130 (= E117), E185 (= E176), E192 (= E183), G237 (= G228), H241 (= H232), R294 (= R288), E300 (≠ S294), R312 (= R312), R331 (= R326)
8ufjB Glutamine synthetase (see paper)
35% identity, 97% coverage: 9:432/435 of query aligns to 24:441/444 of 8ufjB
7tf6A Glutamine synthetase (see paper)
35% identity, 98% coverage: 6:432/435 of query aligns to 18:435/438 of 7tf6A
- binding glutamine: E128 (= E117), E183 (= E176), G235 (= G228), H239 (= H232), R292 (= R288), E298 (≠ S294)
- binding magnesium ion: E126 (= E115), E128 (= E117), E183 (= E176), E190 (= E183), H239 (= H232), E327 (= E324)
- binding : F58 (≠ M46), R60 (≠ M48), G232 (≠ E225), N234 (≠ S227), G296 (≠ S292), Y297 (≠ G293), R310 (= R312), Y367 (= Y364), Y421 (≠ E418), Q433 (≠ R430)
Sites not aligning to the query:
7tdvC Glutamine synthetase (see paper)
35% identity, 98% coverage: 6:432/435 of query aligns to 19:440/443 of 7tdvC
- binding adenosine-5'-diphosphate: G129 (= G113), E131 (= E115), E183 (≠ Y171), D197 (≠ N185), F198 (= F186), K199 (≠ T187), Y200 (= Y188), N246 (≠ H234), V247 (≠ M235), S248 (= S236), R320 (= R317), S328 (vs. gap), R330 (vs. gap)
- binding magnesium ion: E131 (= E115), E131 (= E115), E133 (= E117), E188 (= E176), E195 (= E183), E195 (= E183), H244 (= H232), E332 (= E324)
- binding l-methionine-s-sulfoximine phosphate: E131 (= E115), E133 (= E117), E188 (= E176), E195 (= E183), G240 (= G228), H244 (= H232), R297 (= R288), E303 (≠ S294), R315 (= R312)
7tdpA Structure of paenibacillus polymyxa gs bound to met-sox-p-adp (transition state complex) to 1.98 angstom (see paper)
35% identity, 98% coverage: 10:435/435 of query aligns to 22:439/439 of 7tdpA
- binding adenosine-5'-diphosphate: N123 (≠ F111), G125 (= G113), E127 (= E115), E179 (≠ Y171), D193 (≠ N185), Y196 (= Y188), N242 (≠ H234), S244 (= S236), R316 (= R317), R326 (vs. gap)
- binding magnesium ion: E127 (= E115), E127 (= E115), E129 (= E117), E184 (= E176), E191 (= E183), E191 (= E183), H240 (= H232), E328 (= E324)
- binding l-methionine-s-sulfoximine phosphate: E127 (= E115), E129 (= E117), E184 (= E176), E191 (= E183), G236 (= G228), H240 (= H232), R293 (= R288), E299 (≠ S294), R311 (= R312), R330 (= R326)
7tf9S L. Monocytogenes gs(14)-q-glnr peptide (see paper)
35% identity, 98% coverage: 10:435/435 of query aligns to 23:443/443 of 7tf9S
- binding glutamine: E133 (= E117), Y155 (≠ L139), E188 (= E176), G240 (= G228), G242 (= G230), R297 (= R288), E303 (≠ S294)
- binding magnesium ion: E131 (= E115), E133 (= E117), E188 (= E176), E195 (= E183), H244 (= H232), E332 (= E324)
- binding : F59 (≠ M46), V60 (≠ G47), E418 (≠ A410), I422 (≠ A414), M426 (≠ E418)
7tenA Glutamine synthetase (see paper)
35% identity, 98% coverage: 10:435/435 of query aligns to 22:442/442 of 7tenA
- binding adenosine-5'-diphosphate: G128 (= G113), E130 (= E115), E182 (≠ Y171), D196 (≠ N185), F197 (= F186), K198 (≠ T187), Y199 (= Y188), N245 (≠ H234), S247 (= S236), R319 (= R317), S327 (vs. gap), R329 (vs. gap)
- binding l-methionine-s-sulfoximine phosphate: E130 (= E115), E132 (= E117), E187 (= E176), E194 (= E183), N238 (≠ S227), G239 (= G228), H243 (= H232), R296 (= R288), E302 (≠ S294), R314 (= R312), R333 (= R326)
7tfaB Glutamine synthetase (see paper)
35% identity, 98% coverage: 10:435/435 of query aligns to 22:441/441 of 7tfaB
- binding glutamine: E131 (= E117), Y153 (= Y144), E186 (= E176), G238 (= G228), H242 (= H232), R295 (= R288), E301 (≠ S294)
- binding magnesium ion: E129 (= E115), E131 (= E117), E186 (= E176), E193 (= E183), H242 (= H232), E330 (= E324)
- binding : Y58 (≠ M46), R60 (≠ M48), V187 (≠ D177), N237 (≠ S227), G299 (≠ S292), Y300 (≠ G293), R313 (= R312), M424 (≠ E418)
8oozA Glutamine synthetase (see paper)
34% identity, 98% coverage: 10:435/435 of query aligns to 21:430/430 of 8oozA
- binding adenosine-5'-triphosphate: G117 (= G113), E170 (≠ Y171), F185 (= F186), K186 (≠ T187), Y187 (= Y188), N233 (≠ H234), S235 (= S236), S315 (≠ G320), R317 (= R322)
- binding magnesium ion: E119 (= E115), H231 (= H232), E319 (= E324)
8ooxB Glutamine synthetase (see paper)
35% identity, 98% coverage: 10:435/435 of query aligns to 21:438/438 of 8ooxB
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)
33% identity, 98% coverage: 6:432/435 of query aligns to 19:440/443 of 4lnkA
- active site: D52 (≠ A39), E131 (= E115), E133 (= E117), E188 (= E176), E195 (= E183), H244 (= H232), R315 (= R312), E332 (= E324), R334 (= R326)
- binding adenosine-5'-diphosphate: K43 (≠ M30), M50 (≠ G37), F198 (= F186), Y200 (= Y188), N246 (≠ H234), S248 (= S236), S324 (≠ G321), S328 (vs. gap), R330 (vs. gap)
- binding glutamic acid: E133 (= E117), E188 (= E176), V189 (≠ D177), N239 (≠ S227), G240 (= G228), G242 (= G230), E303 (≠ S294)
- binding magnesium ion: E131 (= E115), E188 (= E176), E195 (= E183), H244 (= H232), E332 (= E324)
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)
33% identity, 98% coverage: 6:432/435 of query aligns to 19:440/443 of 4lniA
- active site: D52 (≠ A39), E131 (= E115), E133 (= E117), E188 (= E176), E195 (= E183), H244 (= H232), R315 (= R312), E332 (= E324), R334 (= R326)
- binding adenosine-5'-diphosphate: E131 (= E115), E183 (≠ Y171), D197 (≠ N185), Y200 (= Y188), N246 (≠ H234), S248 (= S236), R320 (= R317), R330 (vs. gap)
- binding magnesium ion: E131 (= E115), E131 (= E115), E133 (= E117), E188 (= E176), E195 (= E183), E195 (= E183), H244 (= H232), E332 (= E324)
- binding l-methionine-s-sulfoximine phosphate: E133 (= E117), E188 (= E176), H244 (= H232), R297 (= R288), E303 (≠ S294), R315 (= R312), R334 (= R326)
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)
33% identity, 98% coverage: 6:432/435 of query aligns to 20:441/444 of P12425
- G59 (= G45) 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 (≠ M48) 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 (= E115) binding
- E134 (= E117) binding
- E189 (= E176) binding
- V190 (≠ D177) 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 (= E183) binding
- G241 (= G228) binding
- H245 (= H232) binding
- G302 (≠ S292) 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 (≠ S294) 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 (= P302) 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 (= E324) binding
- E424 (= E415) 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)
33% identity, 98% coverage: 6:432/435 of query aligns to 23:444/447 of 4s0rD
- active site: D56 (≠ A39), E135 (= E115), E137 (= E117), E192 (= E176), E199 (= E183), H248 (= H232), R319 (= R312), E336 (= E324), R338 (= R326)
- binding glutamine: E137 (= E117), E192 (= E176), R301 (= R288), E307 (≠ S294)
- binding magnesium ion: I66 (≠ G49), E135 (= E115), E135 (= E115), E199 (= E183), H248 (= H232), H248 (= H232), E336 (= E324), H419 (≠ E407)
- binding : F63 (≠ M46), V64 (≠ G47), R65 (≠ M48), I66 (≠ G49), D161 (= D145), G241 (≠ E225), V242 (≠ R226), N243 (≠ S227), G305 (≠ S292), Y306 (≠ G293), Y376 (= Y364), I426 (≠ A414), M430 (≠ E418)
Query Sequence
>Ac3H11_1551 FitnessBrowser__acidovorax_3H11:Ac3H11_1551
MAEFDYYLAQFVDIHGRPKAKLVPAKHKDMIFGAGAGFAGFAIAGMGMGPNGREFMAVGD
RDSIRPVPWMGSTASVTCEGYVDGKPHALDPRVILKKALAKFRETTGLEFFTGLEPEFFL
LKAGAAAGSWVVATESESLDKPCYDFRHLSSVSDFLMELRAALEEAGIDVYQIDHEDANG
QFEMNFTYADALKTADNLTYFKMAAQAIAKKHGMLCSFMPKPFAERSGSGLHMHMSAGGE
FCDNAFEDKTDPREMDLSPMAYQFLGGLMANAAALTAIAAPCVNSYKRLVKSGSRSGATW
APINIAYGNNNRTALVRVPGGRLELRLPDAAANPYLLTAAVIYAGLDGIERELEPGQPVN
DNLYVLSVADLAALGIKCLPTSLPDALDELDASEVMRRGLGEAFIAEYLAVKRAECDELV
LEISKAEFTRYVDFF
Or try a new SitesBLAST search
SitesBLAST's Database
SitesBLAST's database includes
(1) SwissProt
entries with experimentally-supported functional features;
and (2) protein structures with bound ligands, from the
BioLip database.
by Morgan Price,
Arkin group
Lawrence Berkeley National Laboratory