SitesBLAST
Comparing SMc01594 FitnessBrowser__Smeli:SMc01594 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)
5dm3C Crystal structure of glutamine synthetase from chromohalobacter salexigens dsm 3043(csal_0679, target efi-550015) with bound adp
58% identity, 99% coverage: 4:452/454 of query aligns to 1:396/396 of 5dm3C
- active site: E115 (= E141), E117 (= E143), E162 (= E204), E169 (= E211), H218 (= H260), R286 (= R333), E303 (= E350), R305 (= R352)
- binding adenosine-5'-diphosphate: R173 (= R215), C174 (≠ Y216), H220 (= H262), S222 (= S264), R301 (= R348)
5dm3A Crystal structure of glutamine synthetase from chromohalobacter salexigens dsm 3043(csal_0679, target efi-550015) with bound adp
54% identity, 99% coverage: 2:452/454 of query aligns to 1:374/374 of 5dm3A
- active site: E107 (= E141), E109 (= E143), E146 (= E204), E150 (= E211), H199 (= H260), R265 (= R333), E282 (= E350), R284 (= R352)
- binding adenosine-5'-diphosphate: I103 (≠ Y137), E141 (= E199), R154 (= R215), C155 (≠ Y216), H201 (= H262), S203 (= S264), R280 (= R348)
8tfkA Glutamine synthetase (see paper)
34% identity, 82% coverage: 79:449/454 of query aligns to 64:435/440 of 8tfkA
- binding adenosine-5'-diphosphate: E128 (= E141), D194 (≠ N213), F195 (≠ V214), F197 (≠ Y216), N243 (≠ H262), R312 (= R333), R317 (= R338), G325 (≠ A346), R327 (= R348)
- binding magnesium ion: E128 (= E141), E128 (= E141), E130 (= E143), E185 (= E204), E192 (= E211), E192 (= E211), H241 (= H260), E329 (= E350)
- binding l-methionine-s-sulfoximine phosphate: E128 (= E141), E130 (= E143), E185 (= E204), E192 (= E211), G237 (= G256), H241 (= H260), R294 (= R315), E300 (≠ F321), R312 (= R333), R331 (= R352)
8ufjB Glutamine synthetase (see paper)
34% identity, 82% coverage: 79:449/454 of query aligns to 68:439/444 of 8ufjB
8ooqB Glutamine synthetase from Methanothermococcus thermolithotrophicus (see paper)
32% identity, 81% coverage: 79:448/454 of query aligns to 70:441/446 of 8ooqB
Sites not aligning to the query:
8oooA Glutamine synthetase from methanothermococcus thermolithotrophicus in complex with 2-oxoglutarate and mgatp at 2.15 a resolution (see paper)
32% identity, 81% coverage: 79:448/454 of query aligns to 71:442/447 of 8oooA
- binding 2-oxoglutaric acid: R87 (≠ L95), V93 (≠ T98), P170 (≠ E181), R173 (≠ M184), R174 (= R185), S190 (= S201)
- binding adenosine-5'-triphosphate: E136 (= E141), E188 (= E199), F203 (≠ V214), K204 (≠ R215), F205 (≠ Y216), H251 (= H262), S253 (= S264), R325 (= R338), R335 (= R348)
Sites not aligning to the query:
8oozA Glutamine synthetase (see paper)
33% identity, 82% coverage: 79:449/454 of query aligns to 58:425/430 of 8oozA
- binding adenosine-5'-triphosphate: G117 (≠ A139), E170 (= E199), F185 (≠ V214), K186 (≠ R215), Y187 (= Y216), N233 (≠ H262), S235 (= S264), S315 (≠ A346), R317 (= R348)
- binding magnesium ion: E119 (= E141), H231 (= H260), E319 (= E350)
7tdpA Structure of paenibacillus polymyxa gs bound to met-sox-p-adp (transition state complex) to 1.98 angstom (see paper)
33% identity, 81% coverage: 78:446/454 of query aligns to 64:431/439 of 7tdpA
- binding adenosine-5'-diphosphate: N123 (vs. gap), G125 (≠ A139), E127 (= E141), E179 (= E199), D193 (≠ N213), Y196 (= Y216), N242 (≠ H262), S244 (= S264), R316 (= R338), R326 (= R348)
- binding magnesium ion: E127 (= E141), E127 (= E141), E129 (= E143), E184 (= E204), E191 (= E211), E191 (= E211), H240 (= H260), E328 (= E350)
- binding l-methionine-s-sulfoximine phosphate: E127 (= E141), E129 (= E143), E184 (= E204), E191 (= E211), G236 (= G256), H240 (= H260), R293 (= R315), E299 (≠ F321), R311 (= R333), R330 (= R352)
8ooxB Glutamine synthetase (see paper)
33% identity, 82% coverage: 79:449/454 of query aligns to 64:433/438 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, 81% coverage: 79:446/454 of query aligns to 66:435/443 of 4lnkA
- active site: E131 (= E141), E133 (= E143), E188 (= E204), E195 (= E211), H244 (= H260), R315 (= R333), E332 (= E350), R334 (= R352)
- binding adenosine-5'-diphosphate: F198 (≠ V214), Y200 (= Y216), N246 (≠ H262), S248 (= S264), S324 (≠ E342), S328 (≠ A346), R330 (= R348)
- binding glutamic acid: E133 (= E143), E188 (= E204), V189 (≠ A205), N239 (≠ A255), G240 (= G256), G242 (≠ S258), E303 (≠ F321)
- binding magnesium ion: E131 (= E141), E188 (= E204), E195 (= E211), H244 (= H260), E332 (= E350)
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)
33% identity, 81% coverage: 79:446/454 of query aligns to 66:435/443 of 4lniA
- active site: E131 (= E141), E133 (= E143), E188 (= E204), E195 (= E211), H244 (= H260), R315 (= R333), E332 (= E350), R334 (= R352)
- binding adenosine-5'-diphosphate: E131 (= E141), E183 (= E199), D197 (≠ N213), Y200 (= Y216), N246 (≠ H262), S248 (= S264), R320 (= R338), R330 (= R348)
- binding magnesium ion: E131 (= E141), E131 (= E141), E133 (= E143), E188 (= E204), E195 (= E211), E195 (= E211), H244 (= H260), E332 (= E350)
- binding l-methionine-s-sulfoximine phosphate: E133 (= E143), E188 (= E204), H244 (= H260), R297 (= R315), E303 (≠ F321), R315 (= R333), R334 (= R352)
Sites not aligning to the query:
4s0rD Structure of gs-tnra complex (see paper)
33% identity, 81% coverage: 79:446/454 of query aligns to 70:439/447 of 4s0rD
- active site: E135 (= E141), E137 (= E143), E192 (= E204), E199 (= E211), H248 (= H260), R319 (= R333), E336 (= E350), R338 (= R352)
- binding glutamine: E137 (= E143), E192 (= E204), R301 (= R315), E307 (≠ F321)
- binding magnesium ion: E135 (= E141), E135 (= E141), E199 (= E211), H248 (= H260), H248 (= H260), E336 (= E350), H419 (= H426)
- binding : D161 (≠ H173), G241 (≠ S253), V242 (≠ A254), N243 (≠ A255), G305 (= G319), Y306 (≠ T320), Y376 (= Y390), I426 (≠ W433), M430 (≠ E437)
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)
33% identity, 81% coverage: 79:446/454 of query aligns to 67:436/444 of P12425
- E132 (= E141) binding
- E134 (= E143) binding
- E189 (= E204) binding
- V190 (≠ A205) 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 (= E211) binding
- G241 (= G256) binding
- H245 (= H260) binding
- G302 (= G319) 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 (≠ F321) 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 (= P323) 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 (= E350) binding
- E424 (= E434) 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.
7tfaB Glutamine synthetase (see paper)
32% identity, 81% coverage: 78:446/454 of query aligns to 64:433/441 of 7tfaB
- binding glutamine: E131 (= E143), Y153 (= Y168), E186 (= E204), G238 (= G256), H242 (= H260), R295 (= R315), E301 (≠ F321)
- binding magnesium ion: E129 (= E141), E131 (= E143), E186 (= E204), E193 (= E211), H242 (= H260), E330 (= E350)
- binding : V187 (≠ A205), N237 (≠ A255), G299 (= G319), Y300 (≠ T320), R313 (= R333), M424 (≠ E437)
Sites not aligning to the query:
4acfA Crystal structure of mycobacterium tuberculosis glutamine synthetase in complex with imidazopyridine inhibitor ((4-(6-bromo-3- (butylamino)imidazo(1,2-a)pyridin-2-yl)phenoxy) acetic acid) and l- methionine-s-sulfoximine phosphate.
34% identity, 73% coverage: 79:409/454 of query aligns to 65:424/475 of 4acfA
- active site: E130 (= E141), E132 (= E143), E216 (= E204), E224 (= E211), H273 (= H260), R344 (= R333), E363 (= E350), R365 (= R352)
- binding {4-[6-bromo-3-(butylamino)imidazo[1,2-a]pyridin-2-yl]phenoxy}acetic acid: Y126 (= Y137), F229 (≠ Y216), H275 (= H262), Q276 (= Q263), W279 (= W266), N356 (≠ G343), K358 (= K345), R361 (= R348)
- binding magnesium ion: E130 (= E141), E130 (= E141), E132 (= E143), E216 (= E204), E224 (= E211), E224 (= E211), H273 (= H260), E363 (= E350)
- binding l-methionine-s-sulfoximine phosphate: E130 (= E141), E132 (= E143), E216 (= E204), E224 (= E211), G269 (= G256), H273 (= H260), R326 (= R315), E332 (≠ F321), R344 (= R333), R365 (= R352)
Sites not aligning to the query:
3zxvA Crystal structure of mycobacterium tuberculosis glutamine synthetase in complex with tri-substituted imidazole inhibitor (4-(2-tert-butyl- 4-(6-methoxynaphthalen-2-yl)-1h-imidazol-5-yl)pyridin-2-amine) and l- methionine-s-sulfoximine phosphate (see paper)
34% identity, 73% coverage: 79:409/454 of query aligns to 65:424/475 of 3zxvA
- active site: E130 (= E141), E132 (= E143), E216 (= E204), E224 (= E211), H273 (= H260), R344 (= R333), E363 (= E350), R365 (= R352)
- binding magnesium ion: E130 (= E141), E130 (= E141), E132 (= E143), E216 (= E204), E224 (= E211), E224 (= E211), H273 (= H260), E363 (= E350)
- binding 4-(2-tert-butyl-4-(6-methoxynaphthalen-2-yl)-3h-imidazol-4-yl)pyridin-2-amine: Y126 (= Y137), G128 (≠ A139), F229 (≠ Y216), H275 (= H262), S277 (= S264), K358 (= K345), R361 (= R348)
- binding l-methionine-s-sulfoximine phosphate: E130 (= E141), E132 (= E143), E216 (= E204), E224 (= E211), G269 (= G256), H273 (= H260), R326 (= R315), E332 (≠ F321), R344 (= R333), R365 (= R352)
Sites not aligning to the query:
3zxrA Crystal structure of mycobacterium tuberculosis glutamine synthetase in complex with tri-substituted imidazole inhibitor (3-(2-tert-butyl- 5-(pyridin-4-yl)-1h-imidazol-4-yl)quinoline) and l-methionine-s- sulfoximine phosphate. (see paper)
34% identity, 73% coverage: 79:409/454 of query aligns to 65:424/475 of 3zxrA
- active site: E130 (= E141), E132 (= E143), E216 (= E204), E224 (= E211), H273 (= H260), R344 (= R333), E363 (= E350), R365 (= R352)
- binding 3-(2-tert-butyl-5-(pyridin-4-yl)-1h-imidazol-4-yl)quinoline: G128 (≠ A139), F229 (≠ Y216), H275 (= H262), S277 (= S264), R361 (= R348)
- binding magnesium ion: E130 (= E141), E130 (= E141), E132 (= E143), E216 (= E204), E224 (= E211), E224 (= E211), H273 (= H260), E363 (= E350)
- binding l-methionine-s-sulfoximine phosphate: E130 (= E141), E132 (= E143), E216 (= E204), E224 (= E211), H273 (= H260), R326 (= R315), E332 (≠ F321), R344 (= R333), R365 (= R352)
Sites not aligning to the query:
2bvcA Crystal structure of mycobacterium tuberculosis glutamine synthetase in complex with a transition state mimic (see paper)
34% identity, 73% coverage: 79:409/454 of query aligns to 65:424/475 of 2bvcA
- active site: E130 (= E141), E132 (= E143), E216 (= E204), E224 (= E211), H273 (= H260), R344 (= R333), E363 (= E350), R365 (= R352)
- binding adenosine-5'-diphosphate: E130 (= E141), E211 (= E199), K212 (≠ N200), N226 (= N213), F229 (≠ Y216), H275 (= H262), S277 (= S264), R344 (= R333), R349 (= R338), R361 (= R348), E363 (= E350)
- binding magnesium ion: E130 (= E141), E130 (= E141), E132 (= E143), E216 (= E204), E224 (= E211), E224 (= E211), H273 (= H260), E363 (= E350)
- binding l-methionine-s-sulfoximine phosphate: E130 (= E141), E132 (= E143), E216 (= E204), E224 (= E211), G269 (= G256), H273 (= H260), R326 (= R315), E332 (≠ F321), R344 (= R333), R365 (= R352)
Sites not aligning to the query:
1htoA Crystallographic structure of a relaxed glutamine synthetase from mycobacterium tuberculosis (see paper)
34% identity, 73% coverage: 79:409/454 of query aligns to 67:426/477 of 1htoA
- active site: E132 (= E141), E134 (= E143), E218 (= E204), E226 (= E211), H275 (= H260), R346 (= R333), E365 (= E350), R367 (= R352)
- binding adenosine monophosphate: Y128 (= Y137), G130 (≠ A139), E132 (= E141), F231 (≠ Y216), H277 (= H262), S279 (= S264), R363 (= R348)
- binding manganese (ii) ion: E132 (= E141), H275 (= H260), E365 (= E350)
Sites not aligning to the query:
2whiA Crystal structure of mycobacterium tuberculosis glutamine synthetase in complex with a purine analogue inhibitor and l-methionine-s- sulfoximine phosphate. (see paper)
34% identity, 73% coverage: 79:409/454 of query aligns to 66:425/476 of 2whiA
- active site: E131 (= E141), E133 (= E143), E217 (= E204), E225 (= E211), H274 (= H260), R345 (= R333), E364 (= E350), R366 (= R352)
- binding 1-(3,4-dichlorobenzyl)-3,7-dimethyl-8-morpholin-4-yl-3,7-dihydro-1H-purine-2,6-dione: Y127 (= Y137), G129 (≠ A139), F230 (≠ Y216), H276 (= H262), S278 (= S264), W280 (= W266), K359 (= K345), R362 (= R348)
- binding magnesium ion: E131 (= E141), E131 (= E141), E133 (= E143), E217 (= E204), E225 (= E211), E225 (= E211), H274 (= H260), E364 (= E350)
- binding l-methionine-s-sulfoximine phosphate: E131 (= E141), E133 (= E143), E217 (= E204), E225 (= E211), G270 (= G256), H274 (= H260), R327 (= R315), E333 (≠ F321), R345 (= R333), R366 (= R352)
- binding phosphate ion: E131 (= E141), R350 (= R338), E364 (= E350)
Sites not aligning to the query:
Query Sequence
>SMc01594 FitnessBrowser__Smeli:SMc01594
MSYSFEELKEDVAAGRIDTVLACQVDMQGRLMGKRFHAEYFVESAWKETHSCNYLLATDM
EMETVPGYKATSWEKGYGDYTMKPDLSTLRRIPWLEGTALVLCDMLDHDTHAEVPHSPRA
ILKKQVARLEAMGFKAYMASELEFFLFDQSYDDARLSGYRDLQLASGYNEDYHIFQTTKE
EDVMRAIRNGLQGAGIPVENSKGEASAGQEEINVRYADALTMADRHAIIKNGCKEIAWQR
GKAITFLAKWNYSAAGSSSHIHQSLWSKDGETPLFFDKNGQYGMSELMRHYVAGQLAHAS
EVTYFLAPYINSYKRFMAGTFAPTKAIWSKDNRTAGYRLCGEGSKAIRIECRVGGSDLNP
YLAFAALIAAGIAGIENKMELEAPFVGDAYQGKEVREIPHTLREAGEALSGSKMLRAAFG
EEVVDHYVHAAEWEQQEYDRRVTDWEVARGFERA
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