SitesBLAST
Comparing WP_015934113.1 NCBI__GCF_000022085.1:WP_015934113.1 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)
8wwuB Glutamine synthetase
44% identity, 100% coverage: 3:478/478 of query aligns to 4:492/492 of 8wwuB
- binding phosphoaminophosphonic acid-adenylate ester: G157 (= G157), E159 (= E159), R226 (= R223), F241 (= F238), V243 (≠ P240), H290 (= H287), S292 (= S289), K360 (≠ R358), R365 (= R363), R376 (= R374)
- binding magnesium ion: E159 (= E159), E238 (= E235)
- binding manganese (ii) ion: E159 (= E159), E161 (= E161), E231 (= E228), E238 (= E235), H288 (= H285), E378 (= E376)
8wwvA Glutamine synthetase
44% identity, 100% coverage: 3:478/478 of query aligns to 2:490/490 of 8wwvA
- binding adenosine-5'-diphosphate: G155 (= G157), E157 (= E159), R224 (= R223), F239 (= F238), D240 (≠ Q239), V241 (≠ P240), H288 (= H287), S290 (= S289), R374 (= R374), E376 (= E376)
- binding magnesium ion: E157 (= E159), E236 (= E235)
- binding manganese (ii) ion: E157 (= E159), E159 (= E161), E229 (= E228), E236 (= E235), H286 (= H285), E376 (= E376)
- binding l-methionine-s-sulfoximine phosphate: E157 (= E159), E159 (= E161), E229 (= E228), E236 (= E235), A282 (≠ S281), H286 (= H285), R340 (= R340), K358 (≠ R358)
8ooqB Glutamine synthetase from Methanothermococcus thermolithotrophicus (see paper)
32% identity, 80% coverage: 97:477/478 of query aligns to 69:446/446 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, 80% coverage: 97:477/478 of query aligns to 70:447/447 of 8oooA
- binding 2-oxoglutaric acid: R87 (≠ A114), V93 (≠ T117), P170 (vs. gap), R173 (= R212), R174 (≠ K213), S190 (≠ I225)
- binding adenosine-5'-triphosphate: E136 (= E159), E188 (≠ R223), F203 (= F238), K204 (≠ Q239), F205 (≠ P240), H251 (= H287), S253 (= S289), R325 (= R363), R335 (= R374)
Sites not aligning to the query:
8tfkA Glutamine synthetase (see paper)
29% identity, 96% coverage: 20:478/478 of query aligns to 5:440/440 of 8tfkA
- binding adenosine-5'-diphosphate: E128 (= E159), D194 (≠ T237), F195 (= F238), F197 (≠ P240), N243 (≠ H287), R312 (= R358), R317 (= R363), G325 (≠ A372), R327 (= R374)
- binding magnesium ion: E128 (= E159), E128 (= E159), E130 (= E161), E185 (= E228), E192 (= E235), E192 (= E235), H241 (= H285), E329 (= E376)
- binding l-methionine-s-sulfoximine phosphate: E128 (= E159), E130 (= E161), E185 (= E228), E192 (= E235), G237 (≠ S281), H241 (= H285), R294 (= R340), E300 (≠ L346), R312 (= R358), R331 (= R378)
7tenA Glutamine synthetase (see paper)
30% identity, 96% coverage: 19:478/478 of query aligns to 5:442/442 of 7tenA
- binding adenosine-5'-diphosphate: G128 (= G157), E130 (= E159), E182 (≠ R223), D196 (≠ T237), F197 (= F238), K198 (≠ Q239), Y199 (≠ P240), N245 (≠ H287), S247 (= S289), R319 (= R363), S327 (≠ A372), R329 (= R374)
- binding l-methionine-s-sulfoximine phosphate: E130 (= E159), E132 (= E161), E187 (= E228), E194 (= E235), N238 (≠ V280), G239 (≠ S281), H243 (= H285), R296 (= R340), E302 (≠ L346), R314 (= R358), R333 (= R378)
7tf9S L. Monocytogenes gs(14)-q-glnr peptide (see paper)
30% identity, 96% coverage: 19:478/478 of query aligns to 6:443/443 of 7tf9S
- binding glutamine: E133 (= E161), Y155 (= Y193), E188 (= E228), G240 (≠ S281), G242 (= G283), R297 (= R340), E303 (≠ L346)
- binding magnesium ion: E131 (= E159), E133 (= E161), E188 (= E228), E195 (= E235), H244 (= H285), E332 (= E376)
- binding : F59 (≠ G87), V60 (≠ F88), E418 (≠ H453), I422 (≠ A457), M426 (≠ R461)
8ufjB Glutamine synthetase (see paper)
29% identity, 97% coverage: 14:478/478 of query aligns to 3:444/444 of 8ufjB
7tdpA Structure of paenibacillus polymyxa gs bound to met-sox-p-adp (transition state complex) to 1.98 angstom (see paper)
29% identity, 96% coverage: 20:478/478 of query aligns to 6:439/439 of 7tdpA
- binding adenosine-5'-diphosphate: N123 (vs. gap), G125 (= G157), E127 (= E159), E179 (≠ R223), D193 (≠ T237), Y196 (≠ P240), N242 (≠ H287), S244 (= S289), R316 (= R363), R326 (= R374)
- binding magnesium ion: E127 (= E159), E127 (= E159), E129 (= E161), E184 (= E228), E191 (= E235), E191 (= E235), H240 (= H285), E328 (= E376)
- binding l-methionine-s-sulfoximine phosphate: E127 (= E159), E129 (= E161), E184 (= E228), E191 (= E235), G236 (≠ S281), H240 (= H285), R293 (= R340), E299 (≠ L346), R311 (= R358), R330 (= R378)
8oozA Glutamine synthetase (see paper)
30% identity, 93% coverage: 33:478/478 of query aligns to 18:430/430 of 8oozA
- binding adenosine-5'-triphosphate: G117 (= G157), E170 (≠ R223), F185 (= F238), K186 (≠ Q239), Y187 (≠ P240), N233 (≠ H287), S235 (= S289), S315 (≠ A372), R317 (= R374)
- binding magnesium ion: E119 (= E159), H231 (= H285), E319 (= E376)
8ooxB Glutamine synthetase (see paper)
30% identity, 93% coverage: 33:478/478 of query aligns to 18:438/438 of 8ooxB
7tfaB Glutamine synthetase (see paper)
29% identity, 96% coverage: 20:478/478 of query aligns to 6:441/441 of 7tfaB
- binding glutamine: E131 (= E161), Y153 (= Y193), E186 (= E228), G238 (≠ S281), H242 (= H285), R295 (= R340), E301 (≠ L346)
- binding magnesium ion: E129 (= E159), E131 (= E161), E186 (= E228), E193 (= E235), H242 (= H285), E330 (= E376)
- binding : Y58 (≠ G87), R60 (≠ G89), V187 (≠ Y229), N237 (≠ V280), G299 (≠ Y344), Y300 (≠ S345), R313 (= R358), M424 (≠ R461)
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)
28% identity, 95% coverage: 19:474/478 of query aligns to 7:440/444 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 (= E228) binding Mg(2+)
- V190 (≠ Y229) 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 (= E235) binding Mg(2+)
- G241 (≠ S281) binding L-glutamate
- H245 (= H285) binding Mg(2+)
- G302 (≠ Y344) 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 (≠ L346) 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 (= P348) 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 (= E376) binding Mg(2+)
- E424 (= E458) 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)
28% identity, 95% coverage: 19:474/478 of query aligns to 6:439/443 of 4lnkA
- active site: D52 (≠ P80), E131 (= E159), E133 (= E161), E188 (= E228), E195 (= E235), H244 (= H285), R315 (= R358), E332 (= E376), R334 (= R378)
- binding adenosine-5'-diphosphate: K43 (= K56), M50 (≠ V78), F198 (= F238), Y200 (≠ P240), N246 (≠ H287), S248 (= S289), S324 (≠ G367), S328 (≠ A372), R330 (= R374)
- binding glutamic acid: E133 (= E161), E188 (= E228), V189 (≠ Y229), N239 (≠ V280), G240 (≠ S281), G242 (= G283), E303 (≠ L346)
- binding magnesium ion: E131 (= E159), E188 (= E228), E195 (= E235), H244 (= H285), E332 (= E376)
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)
28% identity, 95% coverage: 19:474/478 of query aligns to 6:439/443 of 4lniA
- active site: D52 (≠ P80), E131 (= E159), E133 (= E161), E188 (= E228), E195 (= E235), H244 (= H285), R315 (= R358), E332 (= E376), R334 (= R378)
- binding adenosine-5'-diphosphate: E131 (= E159), E183 (≠ R223), D197 (≠ T237), Y200 (≠ P240), N246 (≠ H287), S248 (= S289), R320 (= R363), R330 (= R374)
- binding magnesium ion: E131 (= E159), E131 (= E159), E133 (= E161), E188 (= E228), E195 (= E235), E195 (= E235), H244 (= H285), E332 (= E376)
- binding l-methionine-s-sulfoximine phosphate: E133 (= E161), E188 (= E228), H244 (= H285), R297 (= R340), E303 (≠ L346), R315 (= R358), R334 (= R378)
4s0rD Structure of gs-tnra complex (see paper)
28% identity, 95% coverage: 19:474/478 of query aligns to 10:443/447 of 4s0rD
- active site: D56 (≠ P80), E135 (= E159), E137 (= E161), E192 (= E228), E199 (= E235), H248 (= H285), R319 (= R358), E336 (= E376), R338 (= R378)
- binding glutamine: E137 (= E161), E192 (= E228), R301 (= R340), E307 (≠ L346)
- binding magnesium ion: I66 (≠ M90), E135 (= E159), E135 (= E159), E199 (= E235), H248 (= H285), H248 (= H285), E336 (= E376), H419 (≠ Y450)
- binding : F63 (≠ G87), V64 (≠ F88), R65 (≠ G89), I66 (≠ M90), D161 (≠ Q203), G241 (≠ N278), V242 (= V279), N243 (≠ V280), G305 (≠ Y344), Y306 (≠ S345), Y376 (vs. gap), I426 (≠ A457), M430 (≠ R461)
7cqwA Gmas/adp complex-conformation 1 (see paper)
33% identity, 85% coverage: 70:476/478 of query aligns to 29:429/430 of 7cqwA
7cquA Gmas/adp/metsox-p complex (see paper)
32% identity, 85% coverage: 70:476/478 of query aligns to 28:428/429 of 7cquA
- binding adenosine-5'-diphosphate: E121 (= E159), Y173 (≠ R223), N187 (≠ T237), W188 (≠ F238), D189 (≠ Q239), Y190 (≠ P240), H236 (= H287), L237 (≠ Q288), S238 (= S289), R316 (= R363), R322 (= R374)
- binding magnesium ion: E121 (= E159), E121 (= E159), E123 (= E161), E178 (= E228), E185 (= E235), E185 (= E235), H234 (= H285), E324 (= E376)
- binding l-methionine-s-sulfoximine phosphate: E121 (= E159), E123 (= E161), E178 (= E228), E185 (= E235), T229 (≠ V280), G230 (≠ S281), H234 (= H285), R287 (= R340), W299 (≠ L346), R311 (= R358), R326 (= R378)
7cqqA Gmas in complex with amppnp and metsox (see paper)
32% identity, 85% coverage: 70:476/478 of query aligns to 28:428/429 of 7cqqA
- binding phosphoaminophosphonic acid-adenylate ester: E121 (= E159), Y173 (≠ R223), E185 (= E235), N187 (≠ T237), D189 (≠ Q239), Y190 (≠ P240), H234 (= H285), H236 (= H287), S238 (= S289), R311 (= R358), R316 (= R363), R322 (= R374), E324 (= E376)
- binding magnesium ion: E121 (= E159), E121 (= E159), E123 (= E161), E178 (= E228), E185 (= E235), E185 (= E235), H234 (= H285), E324 (= E376)
- binding (2s)-2-amino-4-(methylsulfonimidoyl)butanoic acid: E123 (= E161), E178 (= E228), T229 (≠ V280), H234 (= H285), R287 (= R340), W299 (≠ L346), R311 (= R358), R326 (= R378)
7cqnA Gmas in complex with amppcp (see paper)
32% identity, 85% coverage: 70:476/478 of query aligns to 28:428/429 of 7cqnA
- binding phosphomethylphosphonic acid adenylate ester: G45 (= G87), D61 (= D98), E121 (= E159), Y173 (≠ R223), Q174 (≠ S224), W188 (≠ F238), D189 (≠ Q239), Y190 (≠ P240), H236 (= H287), S238 (= S289), R311 (= R358), R316 (= R363), R322 (= R374)
Query Sequence
>WP_015934113.1 NCBI__GCF_000022085.1:WP_015934113.1
MTFVQDHGLWTDAQADAARDVRERCDPERIDTVRLSFPDQHGILRGKTLVASEAVKALTG
GCAITTTMLAKDTSHRTVFPVFTAGGGFGMREMEGAADVVMVPDPTTFRTLPWAPRTGWL
LCDLYFQDGRPVPFATRGIYRSVLDRLSERSLEYVAGLEVEFHVFKLDDPRMAPADAGQP
GEPPSVSLISHGYQYLTEQRYDQVEPILEILRKDVLALGLPLRSIEVEYGPSQCEFTFQP
TAGAVPADLMVLFRSAVKQTCRRHGYHATFMCRPRIPNVVSSGWHLHQSLRDARTGANAF
VPGDGSQPLSGFGMGFLGGLLAHARAATVFTTPTINGYKRYRSYSLAPDRAVWGRDNRGV
MIRVLGGPGDPATRLENRVGEPAANPYLYMAAQVLAGLDGADRNLDPGPSADTPYEAEAD
LLPTSLREAVFALREDPFFRGALGESFVDYYTHIKNAEIERFQSEITEWEQREYFEIF
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