SitesBLAST
Comparing 208921 MicrobesOnline__882:208921 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)
7tfaB Glutamine synthetase (see paper)
50% identity, 97% coverage: 12:446/447 of query aligns to 5:440/441 of 7tfaB
- binding glutamine: E131 (= E138), Y153 (= Y156), E186 (= E189), N237 (= N240), G238 (= G241), S239 (= S242), G240 (= G243), H242 (= H245), R295 (= R298), E301 (= E304)
- binding magnesium ion: E129 (= E136), E131 (= E138), E186 (= E189), E193 (= E196), H242 (= H245), E330 (= E336)
- binding : Y58 (≠ F65), R60 (= R67), V187 (= V190), G235 (= G238), N237 (= N240), G299 (= G302), Y300 (= Y303), R313 (= R316), I420 (= I426), M424 (≠ D430), W432 (≠ F438), Q436 (≠ R442)
7tdpA Structure of paenibacillus polymyxa gs bound to met-sox-p-adp (transition state complex) to 1.98 angstom (see paper)
50% identity, 97% coverage: 12:446/447 of query aligns to 5:438/439 of 7tdpA
- binding adenosine-5'-diphosphate: N123 (≠ Y132), V124 (= V133), G125 (= G134), E127 (= E136), E179 (= E184), E191 (= E196), D193 (= D198), F194 (≠ L199), K195 (≠ R200), Y196 (= Y201), N242 (≠ H247), Q243 (= Q248), S244 (= S249), R311 (= R316), R316 (= R321), L323 (≠ A331), S324 (≠ A332), T325 (= T333), R326 (= R334), E328 (= E336)
- binding magnesium ion: E127 (= E136), E127 (= E136), E129 (= E138), E184 (= E189), E191 (= E196), E191 (= E196), D193 (= D198), H240 (= H245), E328 (= E336)
- binding l-methionine-s-sulfoximine phosphate: E127 (= E136), E129 (= E138), E184 (= E189), E191 (= E196), N235 (= N240), G236 (= G241), G238 (= G243), H240 (= H245), R293 (= R298), E299 (= E304), A300 (= A305), R311 (= R316), R330 (= R338)
A0R083 Glutamine synthetase; GS; Glutamate--ammonia ligase; Glutamine synthetase I alpha; GSI alpha; EC 6.3.1.2 from Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis) (see paper)
51% identity, 97% coverage: 14:446/447 of query aligns to 8:446/446 of A0R083
- K363 (≠ N363) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
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)
49% identity, 97% coverage: 12:444/447 of query aligns to 6:440/443 of 4lnkA
- active site: D52 (= D58), E131 (= E136), E133 (= E138), E188 (= E189), E195 (= E196), H244 (= H245), R315 (= R316), E332 (= E336), R334 (= R338)
- binding adenosine-5'-diphosphate: K43 (≠ A49), M50 (≠ G56), N127 (≠ Y132), G129 (= G134), E131 (= E136), F198 (≠ L199), K199 (≠ R200), Y200 (= Y201), N246 (≠ H247), L247 (≠ Q248), S248 (= S249), F250 (= F251), S324 (≠ G328), I327 (≠ A331), S328 (≠ A332), R330 (= R334)
- binding glutamic acid: E133 (= E138), Y155 (= Y156), E188 (= E189), V189 (= V190), N239 (= N240), G240 (= G241), G242 (= G243), H244 (= H245), R297 (= R298), E303 (= E304), R334 (= R338)
- binding magnesium ion: E131 (= E136), E188 (= E189), E195 (= E196), H244 (= H245), E332 (= E336)
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)
49% identity, 97% coverage: 12:444/447 of query aligns to 6:440/443 of 4lniA
- active site: D52 (= D58), E131 (= E136), E133 (= E138), E188 (= E189), E195 (= E196), H244 (= H245), R315 (= R316), E332 (= E336), R334 (= R338)
- binding adenosine-5'-diphosphate: N127 (≠ Y132), G129 (= G134), E131 (= E136), E183 (= E184), D197 (= D198), F198 (≠ L199), K199 (≠ R200), Y200 (= Y201), N246 (≠ H247), S248 (= S249), R315 (= R316), R320 (= R321), I327 (≠ A331), S328 (≠ A332), R330 (= R334), E332 (= E336)
- binding magnesium ion: E131 (= E136), E131 (= E136), E133 (= E138), E188 (= E189), E195 (= E196), E195 (= E196), H244 (= H245), E332 (= E336)
- binding l-methionine-s-sulfoximine phosphate: E131 (= E136), E133 (= E138), Y155 (= Y156), E188 (= E189), E195 (= E196), G240 (= G241), G242 (= G243), H244 (= H245), R297 (= R298), Y302 (= Y303), E303 (= E304), A304 (= A305), R315 (= R316), R334 (= R338)
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)
49% identity, 97% coverage: 12:444/447 of query aligns to 7:441/444 of P12425
- G59 (= G64) 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 (= R67) 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 (= E136) binding
- E134 (= E138) binding
- E189 (= E189) binding
- V190 (= V190) 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 (= E196) binding
- G241 (= G241) binding
- H245 (= H245) binding
- G302 (= G302) 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 (= E304) 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 (= P306) 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 (= E336) binding
- E424 (= E427) 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)
49% identity, 97% coverage: 12:444/447 of query aligns to 10:444/447 of 4s0rD
- active site: D56 (= D58), E135 (= E136), E137 (= E138), E192 (= E189), E199 (= E196), H248 (= H245), R319 (= R316), E336 (= E336), R338 (= R338)
- binding glutamine: E137 (= E138), E192 (= E189), E199 (= E196), G244 (= G241), G246 (= G243), R301 (= R298), Y306 (= Y303), E307 (= E304), A308 (= A305)
- binding magnesium ion: I66 (= I68), E135 (= E136), E135 (= E136), E199 (= E196), H248 (= H245), H248 (= H245), E336 (= E336), K403 (≠ R403), S404 (≠ N404), H419 (≠ N419)
- binding : F63 (= F65), V64 (≠ T66), R65 (= R67), I66 (= I68), D161 (= D158), V193 (= V190), A194 (= A191), P195 (= P192), G241 (= G238), V242 (≠ E239), N243 (= N240), G305 (= G302), Y306 (= Y303), R319 (= R316), N374 (= N374), Y376 (≠ F376), M378 (= M378), I426 (= I426), M430 (≠ D430), Q442 (≠ R442)
Sites not aligning to the query:
P9WN37 Glutamine synthetase; GS; Glutamate--ammonia ligase; Glutamine synthetase I alpha; GSI alpha; EC 6.3.1.2 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see paper)
50% identity, 97% coverage: 14:446/447 of query aligns to 8:446/446 of P9WN37
- K363 (≠ N363) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
7tdvC Glutamine synthetase (see paper)
49% identity, 97% coverage: 12:444/447 of query aligns to 6:440/443 of 7tdvC
- binding adenosine-5'-diphosphate: N127 (≠ Y132), G129 (= G134), P130 (= P135), E131 (= E136), E183 (= E184), E195 (= E196), D197 (= D198), F198 (≠ L199), K199 (≠ R200), Y200 (= Y201), N246 (≠ H247), V247 (≠ Q248), S248 (= S249), R315 (= R316), R320 (= R321), L327 (≠ A331), S328 (≠ A332), T329 (= T333), R330 (= R334), E332 (= E336)
- binding magnesium ion: E131 (= E136), E131 (= E136), E133 (= E138), E188 (= E189), E195 (= E196), E195 (= E196), D197 (= D198), H244 (= H245), D259 (= D260), E268 (≠ H269), E332 (= E336)
- binding l-methionine-s-sulfoximine phosphate: E131 (= E136), E133 (= E138), E188 (= E189), Q193 (= Q194), E195 (= E196), G240 (= G241), G242 (= G243), H244 (= H245), R297 (= R298), Y302 (= Y303), E303 (= E304), A304 (= A305), R315 (= R316), R334 (= R338)
7tf6A Glutamine synthetase (see paper)
49% identity, 97% coverage: 12:444/447 of query aligns to 5:435/438 of 7tf6A