SitesBLAST
Comparing WP_011976260.1 NCBI__GCF_000017145.1:WP_011976260.1 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
57% 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
53% 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 (≠ F137), 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
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:
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:
8oozA Glutamine synthetase (see paper)
32% 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)
8ooxB Glutamine synthetase (see paper)
32% identity, 82% coverage: 79:449/454 of query aligns to 64:433/438 of 8ooxB
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: 79:446/454 of query aligns to 65:431/439 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)
A0R079 Glutamine synthetase; GS; Glutamate--ammonia ligase; Glutamine synthetase I beta; GSI beta; EC 6.3.1.2 from Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis) (see paper)
33% identity, 73% coverage: 79:409/454 of query aligns to 68:430/478 of A0R079
Sites not aligning to the query:
- 14 modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
7tfaB Glutamine synthetase (see paper)
32% identity, 81% coverage: 79:446/454 of query aligns to 65:433/441 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:
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)
32% identity, 81% coverage: 79:446/454 of query aligns to 67:436/444 of P12425
- E132 (= E141) binding Mg(2+)
- E134 (= E143) binding Mg(2+)
- E189 (= E204) binding Mg(2+)
- 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 Mg(2+)
- G241 (= G256) binding L-glutamate
- H245 (= H260) binding Mg(2+)
- 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 Mg(2+)
- 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.
4s0rD Structure of gs-tnra complex (see paper)
32% 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:
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)
32% 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)
32% 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:
7tdvC Glutamine synthetase (see paper)
30% identity, 81% coverage: 79:446/454 of query aligns to 66:435/443 of 7tdvC
- binding adenosine-5'-diphosphate: G129 (≠ A139), E131 (= E141), E183 (= E199), D197 (≠ N213), F198 (≠ V214), K199 (≠ R215), Y200 (= Y216), N246 (≠ H262), V247 (≠ Q263), S248 (= S264), R320 (= R338), S328 (≠ A346), 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: E131 (= E141), E133 (= E143), E188 (= E204), E195 (= E211), G240 (= G256), H244 (= H260), R297 (= R315), E303 (≠ F321), R315 (= R333)
7tf6A Glutamine synthetase (see paper)
30% identity, 81% coverage: 79:446/454 of query aligns to 65:430/438 of 7tf6A
- binding glutamine: E128 (= E143), E183 (= E204), G235 (= G256), H239 (= H260), R292 (= R315), E298 (≠ F321)
- binding magnesium ion: E126 (= E141), E128 (= E143), E183 (= E204), E190 (= E211), H239 (= H260), E327 (= E350)
- binding : G232 (≠ S253), N234 (≠ A255), G296 (= G319), Y297 (≠ T320), R310 (= R333), Y367 (= Y390), Y421 (≠ E437)
Sites not aligning to the query:
7tenA Glutamine synthetase (see paper)
31% identity, 81% coverage: 79:446/454 of query aligns to 65:434/442 of 7tenA
- binding adenosine-5'-diphosphate: G128 (≠ A139), E130 (= E141), E182 (= E199), D196 (≠ N213), F197 (≠ V214), K198 (≠ R215), Y199 (= Y216), N245 (≠ H262), S247 (= S264), R319 (= R338), S327 (≠ A346), R329 (= R348)
- binding l-methionine-s-sulfoximine phosphate: E130 (= E141), E132 (= E143), E187 (= E204), E194 (= E211), N238 (≠ A255), G239 (= G256), H243 (= H260), R296 (= R315), E302 (≠ F321), R314 (= R333), R333 (= R352)
7tf9S L. Monocytogenes gs(14)-q-glnr peptide (see paper)
31% identity, 81% coverage: 79:446/454 of query aligns to 66:435/443 of 7tf9S
- binding glutamine: E133 (= E143), Y155 (= Y168), E188 (= E204), G240 (= G256), G242 (≠ S258), R297 (= R315), E303 (≠ F321)
- binding magnesium ion: E131 (= E141), E133 (= E143), E188 (= E204), E195 (= E211), H244 (= H260), E332 (= E350)
- binding : E418 (≠ H429), I422 (≠ W433), M426 (≠ E437)
Sites not aligning to the query:
4xycA Nanomolar inhibitors of mycobacterium tuberculosis glutamine synthetase 1: synthesis, biological evaluation and x-ray crystallographic studies (see paper)
32% identity, 77% coverage: 60:409/454 of query aligns to 29:415/466 of 4xycA
- active site: D51 (vs. gap), E121 (= E141), E123 (= E143), E207 (= E204), E215 (= E211), H264 (= H260), R335 (= R333), E354 (= E350), R356 (= R352)
- binding 9-phenyl-4H-imidazo[1,2-a]indeno[1,2-e]pyrazin-4-one: Y117 (≠ F137), F220 (≠ Y216), H266 (= H262), S268 (= S264), W270 (= W266), K349 (= K345), A350 (= A346), R352 (= R348)
Query Sequence
>WP_011976260.1 NCBI__GCF_000017145.1:WP_011976260.1
MSYSFDELKEDVAEGRIDTVLACQVDMQGRLMGKRFHAEYFVESAWKETHSCNYLLATDM
EMETVPGYKATSWDKGYGDYTMKPDLSTLRRIPWLDGTALVLCDMLDHHTHAEVPHSPRA
ILKAQVSRLEAMGFKAFMASELEFFLFDQSYDDARLSGYRDLQLASGYNEDYHIFQTTKE
EDVMRAIRNGLQGAGIPVENSKGEASAGQEEINVRYAEAVTMADRHAIIKNGCKEIAWQR
GKAITFLAKWNYSAAGSSSHIHQSLWSKDGEKPLFFDKDGQYGMSDLMRHYVAGQLAHAS
EVTYFLAPYINSYKRFMAGTFAPTKAIWSKDNRTAGYRLCGEGSKAIRIECRVGGSDLNP
YLAFAALIAAGISGIENKMELEAPFVGDAYHGKDVREVPHTLRAATEALSGSKLLRAAFG
EEVIDHYVHAAEWEQQEYDRRVTDWEVARGFERA
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