SitesBLAST
Comparing WP_012041189.1 NCBI__GCF_000015165.1:WP_012041189.1 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)
8wwvA Glutamine synthetase
46% identity, 100% coverage: 3:479/479 of query aligns to 2:490/490 of 8wwvA
- binding adenosine-5'-diphosphate: G155 (= G157), E157 (= E159), R224 (= R226), F239 (≠ L241), D240 (≠ Q242), V241 (≠ P243), H288 (= H290), S290 (= S292), R374 (= R375), E376 (= E377)
- binding magnesium ion: E157 (= E159), E236 (= E238)
- binding manganese (ii) ion: E157 (= E159), E159 (= E161), E229 (= E231), E236 (= E238), H286 (= H288), E376 (= E377)
- binding l-methionine-s-sulfoximine phosphate: E157 (= E159), E159 (= E161), E229 (= E231), E236 (= E238), A282 (≠ S284), H286 (= H288), R340 (= R341), K358 (≠ R359)
8wwuB Glutamine synthetase
46% identity, 100% coverage: 3:479/479 of query aligns to 4:492/492 of 8wwuB
- binding phosphoaminophosphonic acid-adenylate ester: G157 (= G157), E159 (= E159), R226 (= R226), F241 (≠ L241), V243 (≠ P243), H290 (= H290), S292 (= S292), K360 (≠ R359), R365 (= R364), R376 (= R375)
- binding magnesium ion: E159 (= E159), E238 (= E238)
- binding manganese (ii) ion: E159 (= E159), E161 (= E161), E231 (= E231), E238 (= E238), H288 (= H288), E378 (= E377)
8tfkA Glutamine synthetase (see paper)
31% identity, 95% coverage: 25:479/479 of query aligns to 10:440/440 of 8tfkA
- binding adenosine-5'-diphosphate: E128 (= E159), D194 (≠ V240), F195 (≠ L241), F197 (≠ P243), N243 (≠ H290), R312 (= R359), R317 (= R364), G325 (≠ A373), R327 (= R375)
- binding magnesium ion: E128 (= E159), E128 (= E159), E130 (= E161), E185 (= E231), E192 (= E238), E192 (= E238), H241 (= H288), E329 (= E377)
- binding l-methionine-s-sulfoximine phosphate: E128 (= E159), E130 (= E161), E185 (= E231), E192 (= E238), G237 (≠ S284), H241 (= H288), R294 (= R341), E300 (≠ L347), R312 (= R359), R331 (= R379)
8ufjB Glutamine synthetase (see paper)
31% identity, 95% coverage: 25:479/479 of query aligns to 14:444/444 of 8ufjB
7tdpA Structure of paenibacillus polymyxa gs bound to met-sox-p-adp (transition state complex) to 1.98 angstom (see paper)
32% identity, 95% coverage: 23:479/479 of query aligns to 9:439/439 of 7tdpA
- binding adenosine-5'-diphosphate: N123 (≠ K155), G125 (= G157), E127 (= E159), E179 (≠ R226), D193 (≠ V240), Y196 (≠ P243), N242 (≠ H290), S244 (= S292), R316 (= R364), R326 (= R375)
- binding magnesium ion: E127 (= E159), E127 (= E159), E129 (= E161), E184 (= E231), E191 (= E238), E191 (= E238), H240 (= H288), E328 (= E377)
- binding l-methionine-s-sulfoximine phosphate: E127 (= E159), E129 (= E161), E184 (= E231), E191 (= E238), G236 (≠ S284), H240 (= H288), R293 (= R341), E299 (≠ L347), R311 (= R359), R330 (= R379)
7tfaB Glutamine synthetase (see paper)
31% identity, 95% coverage: 23:479/479 of query aligns to 9:441/441 of 7tfaB
- binding glutamine: E131 (= E161), Y153 (= Y198), E186 (= E231), G238 (≠ S284), H242 (= H288), R295 (= R341), E301 (≠ L347)
- binding magnesium ion: E129 (= E159), E131 (= E161), E186 (= E231), E193 (= E238), H242 (= H288), E330 (= E377)
- binding : Y58 (≠ G87), R60 (≠ G89), V187 (≠ Y232), N237 (≠ M283), G299 (≠ Y345), Y300 (≠ S346), R313 (= R359), M424 (≠ R462)
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)
29% identity, 96% coverage: 21:479/479 of query aligns to 8:443/443 of 4lnkA
- active site: D52 (≠ P80), E131 (= E159), E133 (= E161), E188 (= E231), E195 (= E238), H244 (= H288), R315 (= R359), E332 (= E377), R334 (= R379)
- binding adenosine-5'-diphosphate: K43 (= K71), M50 (≠ V78), F198 (≠ L241), Y200 (≠ P243), N246 (≠ H290), S248 (= S292), S324 (≠ G368), S328 (≠ A373), R330 (= R375)
- binding glutamic acid: E133 (= E161), E188 (= E231), V189 (≠ Y232), N239 (≠ M283), G240 (≠ S284), G242 (= G286), E303 (≠ L347)
- binding magnesium ion: E131 (= E159), E188 (= E231), E195 (= E238), H244 (= H288), E332 (= E377)
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)
29% identity, 96% coverage: 21:479/479 of query aligns to 8:443/443 of 4lniA
- active site: D52 (≠ P80), E131 (= E159), E133 (= E161), E188 (= E231), E195 (= E238), H244 (= H288), R315 (= R359), E332 (= E377), R334 (= R379)
- binding adenosine-5'-diphosphate: E131 (= E159), E183 (≠ R226), D197 (≠ V240), Y200 (≠ P243), N246 (≠ H290), S248 (= S292), R320 (= R364), R330 (= R375)
- binding magnesium ion: E131 (= E159), E131 (= E159), E133 (= E161), E188 (= E231), E195 (= E238), E195 (= E238), H244 (= H288), E332 (= E377)
- binding l-methionine-s-sulfoximine phosphate: E133 (= E161), E188 (= E231), H244 (= H288), R297 (= R341), E303 (≠ L347), R315 (= R359), R334 (= R379)
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)
29% identity, 96% coverage: 21:479/479 of query aligns to 9:444/444 of P12425
- G59 (= G86) 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 (≠ G89) 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 (= E159) binding Mg(2+)
- E134 (= E161) binding Mg(2+)
- E189 (= E231) binding Mg(2+)
- V190 (≠ Y232) 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 (= E238) binding Mg(2+)
- G241 (≠ S284) binding L-glutamate
- H245 (= H288) binding Mg(2+)
- G302 (≠ Y345) 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 (≠ L347) 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 (= P349) 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 (= E377) binding Mg(2+)
- E424 (= E459) 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)
29% identity, 96% coverage: 21:479/479 of query aligns to 12:447/447 of 4s0rD
- active site: D56 (≠ P80), E135 (= E159), E137 (= E161), E192 (= E231), E199 (= E238), H248 (= H288), R319 (= R359), E336 (= E377), R338 (= R379)
- binding glutamine: E137 (= E161), E192 (= E231), R301 (= R341), E307 (≠ L347)
- binding magnesium ion: I66 (≠ M90), E135 (= E159), E135 (= E159), E199 (= E238), H248 (= H288), H248 (= H288), E336 (= E377), H419 (≠ Y451)
- binding : F63 (≠ G87), V64 (≠ F88), R65 (≠ G89), I66 (≠ M90), D161 (≠ G184), G241 (≠ N281), V242 (= V282), N243 (≠ M283), G305 (≠ Y345), Y306 (≠ S346), Y376 (vs. gap), I426 (≠ A458), M430 (≠ R462)
8oozA Glutamine synthetase (see paper)
28% identity, 95% coverage: 23:479/479 of query aligns to 8:430/430 of 8oozA
- binding adenosine-5'-triphosphate: G117 (= G157), E170 (≠ R226), F185 (≠ L241), K186 (≠ Q242), Y187 (≠ P243), N233 (≠ H290), S235 (= S292), S315 (≠ A373), R317 (= R375)
- binding magnesium ion: E119 (= E159), H231 (= H288), E319 (= E377)
8ooqB Glutamine synthetase from Methanothermococcus thermolithotrophicus (see paper)
29% identity, 94% coverage: 28:478/479 of query aligns to 12:446/446 of 8ooqB
- binding 2-oxoglutaric acid: F16 (≠ T32), R18 (= R34), A32 (= A48), R86 (≠ A114), V92 (≠ T117), P169 (≠ Q208), R172 (≠ L211), R173 (≠ E212), S189 (≠ I228)
- binding magnesium ion: E137 (= E161), E192 (= E231), E199 (= E238)
8oooA Glutamine synthetase from methanothermococcus thermolithotrophicus in complex with 2-oxoglutarate and mgatp at 2.15 a resolution (see paper)
29% identity, 94% coverage: 28:478/479 of query aligns to 13:447/447 of 8oooA
- binding 2-oxoglutaric acid: F17 (≠ T32), R19 (= R34), A33 (= A48), R87 (≠ A114), V93 (≠ T117), P170 (≠ Q208), R173 (≠ L211), R174 (≠ E212), S190 (≠ I228)
- binding adenosine-5'-triphosphate: E136 (= E159), E188 (≠ R226), F203 (≠ L241), K204 (≠ Q242), F205 (≠ P243), H251 (= H290), S253 (= S292), R325 (= R364), R335 (= R375)
7tenA Glutamine synthetase (see paper)
29% identity, 95% coverage: 23:479/479 of query aligns to 9:442/442 of 7tenA
- binding adenosine-5'-diphosphate: G128 (= G157), E130 (= E159), E182 (≠ R226), D196 (≠ V240), F197 (≠ L241), K198 (≠ Q242), Y199 (≠ P243), N245 (≠ H290), S247 (= S292), R319 (= R364), S327 (≠ A373), R329 (= R375)
- binding l-methionine-s-sulfoximine phosphate: E130 (= E159), E132 (= E161), E187 (= E231), E194 (= E238), N238 (≠ M283), G239 (≠ S284), H243 (= H288), R296 (= R341), E302 (≠ L347), R314 (= R359), R333 (= R379)
7tf9S L. Monocytogenes gs(14)-q-glnr peptide (see paper)
29% identity, 95% coverage: 23:479/479 of query aligns to 10:443/443 of 7tf9S
- binding glutamine: E133 (= E161), Y155 (= Y198), E188 (= E231), G240 (≠ S284), G242 (= G286), R297 (= R341), E303 (≠ L347)
- binding magnesium ion: E131 (= E159), E133 (= E161), E188 (= E231), E195 (= E238), H244 (= H288), E332 (= E377)
- binding : F59 (≠ G87), V60 (≠ F88), E418 (≠ F454), I422 (≠ A458), M426 (≠ R462)
8ooxB Glutamine synthetase (see paper)
29% identity, 95% coverage: 23:479/479 of query aligns to 8:438/438 of 8ooxB
5dm3C Crystal structure of glutamine synthetase from chromohalobacter salexigens dsm 3043(csal_0679, target efi-550015) with bound adp
33% identity, 79% coverage: 100:477/479 of query aligns to 55:396/396 of 5dm3C
- active site: E115 (= E159), E117 (= E161), E162 (= E231), E169 (= E238), H218 (= H288), R286 (= R359), E303 (= E377), R305 (= R379)
- binding adenosine-5'-diphosphate: R173 (≠ Q242), C174 (≠ P243), H220 (= H290), S222 (= S292), R301 (= R375)
7tdvC Glutamine synthetase (see paper)
28% identity, 96% coverage: 21:479/479 of query aligns to 8:443/443 of 7tdvC
- binding adenosine-5'-diphosphate: G129 (= G157), E131 (= E159), E183 (≠ R226), D197 (≠ V240), F198 (≠ L241), K199 (≠ Q242), Y200 (≠ P243), N246 (≠ H290), V247 (≠ Q291), S248 (= S292), R320 (= R364), S328 (≠ A373), R330 (= R375)
- binding magnesium ion: E131 (= E159), E131 (= E159), E133 (= E161), E188 (= E231), E195 (= E238), E195 (= E238), H244 (= H288), E332 (= E377)
- binding l-methionine-s-sulfoximine phosphate: E131 (= E159), E133 (= E161), E188 (= E231), E195 (= E238), G240 (≠ S284), H244 (= H288), R297 (= R341), E303 (≠ L347), R315 (= R359)
5dm3A Crystal structure of glutamine synthetase from chromohalobacter salexigens dsm 3043(csal_0679, target efi-550015) with bound adp
32% identity, 80% coverage: 97:477/479 of query aligns to 48:374/374 of 5dm3A
- active site: E107 (= E159), E109 (= E161), E146 (≠ P234), E150 (= E238), H199 (= H288), R265 (= R359), E282 (= E377), R284 (= R379)
- binding adenosine-5'-diphosphate: I103 (≠ K155), E141 (= E229), R154 (≠ Q242), C155 (≠ P243), H201 (= H290), S203 (= S292), R280 (= R375)
7tf6A Glutamine synthetase (see paper)
28% identity, 96% coverage: 21:479/479 of query aligns to 7:438/438 of 7tf6A
- binding glutamine: E128 (= E161), E183 (= E231), G235 (≠ S284), H239 (= H288), R292 (= R341), E298 (≠ L347)
- binding magnesium ion: E126 (= E159), E128 (= E161), E183 (= E231), E190 (= E238), H239 (= H288), E327 (= E377)
- binding : F58 (≠ G87), R60 (≠ G89), G232 (≠ N281), N234 (≠ M283), G296 (≠ Y345), Y297 (≠ S346), R310 (= R359), Y367 (= Y416), Y421 (≠ R462), Q433 (≠ E474), Q437 (≠ M478)
Query Sequence
>WP_012041189.1 NCBI__GCF_000015165.1:WP_012041189.1
MSFVQKHQLWSAEQTEAALRMRRIAEEQGLKTIRFSFPDQHGILRGKALAVDAALSSLED
GCSITTTLLAKDTSHRTVFPVFTAGGGFGMSEMQGGSDALMVADPTTFRVLPWAPGTGWV
LCDLYFANGAPVPFATRNLYRSALAALDQRGYQFKAGLEVECHIFKVEDPRLAPGDAGSP
GQPGVPPTVSLLTQGYQYLTEQRFDQMQPALETIRANLTALGLPLRSIELEYGPSQCEFV
LQPGIGMEPADTMVLFRSAVKQIAQRHGYHATFMCRPRIPNVMSSGWHLHQSLVARDGSN
AFMTSETDGLSALGRHYMAGLLAHARAAAVFSTPTINGYRRYRAYSLAPDRAIWGRDNRG
VMIRVLGGPGDRATRLENRIGEPAANPYLYMASQIAAGLDGVDRKLDPGPSADVPYETKA
SLLPKSLHEAVDALKADAFFRNAFGATFIDYYTFIKTAEIDRFNAEVSDWEQREYFEMF
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