SitesBLAST
Comparing WP_029329000.1 NCBI__GCF_000224785.1:WP_029329000.1 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)
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)
78% identity, 99% coverage: 7:445/445 of query aligns to 6:444/444 of P12425
- G59 (= G60) 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 (= R63) 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 (= E133) binding Mg(2+)
- E134 (= E135) binding Mg(2+)
- E189 (= E190) binding Mg(2+)
- V190 (= V191) 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 (= E197) binding Mg(2+)
- G241 (= G242) binding L-glutamate
- H245 (= H246) binding Mg(2+)
- G302 (= G303) 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 (= E305) 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 (= P307) 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 (= E334) binding Mg(2+)
- E424 (= E425) 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)
78% identity, 99% coverage: 7:445/445 of query aligns to 5:443/443 of 4lnkA
- active site: D52 (= D54), E131 (= E133), E133 (= E135), E188 (= E190), E195 (= E197), H244 (= H246), R315 (= R317), E332 (= E334), R334 (= R336)
- binding adenosine-5'-diphosphate: K43 (= K45), M50 (= M52), F198 (= F200), Y200 (= Y202), N246 (= N248), S248 (= S250), S324 (= S326), S328 (= S330), R330 (= R332)
- binding glutamic acid: E133 (= E135), E188 (= E190), V189 (= V191), N239 (= N241), G240 (= G242), G242 (= G244), E303 (= E305)
- binding magnesium ion: E131 (= E133), E188 (= E190), E195 (= E197), H244 (= H246), E332 (= E334)
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)
78% identity, 99% coverage: 7:445/445 of query aligns to 5:443/443 of 4lniA
- active site: D52 (= D54), E131 (= E133), E133 (= E135), E188 (= E190), E195 (= E197), H244 (= H246), R315 (= R317), E332 (= E334), R334 (= R336)
- binding adenosine-5'-diphosphate: E131 (= E133), E183 (= E185), D197 (= D199), Y200 (= Y202), N246 (= N248), S248 (= S250), R320 (= R322), R330 (= R332)
- binding magnesium ion: E131 (= E133), E131 (= E133), E133 (= E135), E188 (= E190), E195 (= E197), E195 (= E197), H244 (= H246), E332 (= E334)
- binding l-methionine-s-sulfoximine phosphate: E133 (= E135), E188 (= E190), H244 (= H246), R297 (= R299), E303 (= E305), R315 (= R317), R334 (= R336)
4s0rD Structure of gs-tnra complex (see paper)
78% identity, 99% coverage: 7:445/445 of query aligns to 9:447/447 of 4s0rD
- active site: D56 (= D54), E135 (= E133), E137 (= E135), E192 (= E190), E199 (= E197), H248 (= H246), R319 (= R317), E336 (= E334), R338 (= R336)
- binding glutamine: E137 (= E135), E192 (= E190), R301 (= R299), E307 (= E305)
- binding magnesium ion: I66 (= I64), E135 (= E133), E135 (= E133), E199 (= E197), H248 (= H246), H248 (= H246), E336 (= E334), H419 (= H417)
- binding : F63 (= F61), V64 (= V62), R65 (= R63), I66 (= I64), D161 (= D159), G241 (= G239), V242 (= V240), N243 (= N241), G305 (= G303), Y306 (= Y304), Y376 (= Y374), I426 (= I424), M430 (= M428)
7tf9S L. Monocytogenes gs(14)-q-glnr peptide (see paper)
75% identity, 99% coverage: 7:445/445 of query aligns to 5:443/443 of 7tf9S
- binding glutamine: E133 (= E135), Y155 (= Y157), E188 (= E190), G240 (= G242), G242 (= G244), R297 (= R299), E303 (= E305)
- binding magnesium ion: E131 (= E133), E133 (= E135), E188 (= E190), E195 (= E197), H244 (= H246), E332 (= E334)
- binding : F59 (= F61), V60 (= V62), E418 (= E420), I422 (= I424), M426 (= M428)
7tenA Glutamine synthetase (see paper)
75% identity, 99% coverage: 7:445/445 of query aligns to 4:442/442 of 7tenA
- binding adenosine-5'-diphosphate: G128 (= G131), E130 (= E133), E182 (= E185), D196 (= D199), F197 (= F200), K198 (= K201), Y199 (= Y202), N245 (= N248), S247 (= S250), R319 (= R322), S327 (= S330), R329 (= R332)
- binding l-methionine-s-sulfoximine phosphate: E130 (= E133), E132 (= E135), E187 (= E190), E194 (= E197), N238 (= N241), G239 (= G242), H243 (= H246), R296 (= R299), E302 (= E305), R314 (= R317), R333 (= R336)
7tdvC Glutamine synthetase (see paper)
74% identity, 99% coverage: 7:445/445 of query aligns to 5:443/443 of 7tdvC
- binding adenosine-5'-diphosphate: G129 (= G131), E131 (= E133), E183 (= E185), D197 (= D199), F198 (= F200), K199 (= K201), Y200 (= Y202), N246 (= N248), V247 (≠ M249), S248 (= S250), R320 (= R322), S328 (= S330), R330 (= R332)
- binding magnesium ion: E131 (= E133), E131 (= E133), E133 (= E135), E188 (= E190), E195 (= E197), E195 (= E197), H244 (= H246), E332 (= E334)
- binding l-methionine-s-sulfoximine phosphate: E131 (= E133), E133 (= E135), E188 (= E190), E195 (= E197), G240 (= G242), H244 (= H246), R297 (= R299), E303 (= E305), R315 (= R317)
7tf6A Glutamine synthetase (see paper)
73% identity, 99% coverage: 7:445/445 of query aligns to 4:438/438 of 7tf6A
- binding glutamine: E128 (= E135), E183 (= E190), G235 (= G242), H239 (= H246), R292 (= R299), E298 (= E305)
- binding magnesium ion: E126 (= E133), E128 (= E135), E183 (= E190), E190 (= E197), H239 (= H246), E327 (= E334)
- binding : F58 (= F61), R60 (= R63), G232 (= G239), N234 (= N241), G296 (= G303), Y297 (= Y304), R310 (= R317), Y367 (= Y374), Y421 (≠ M428), Q433 (= Q440), Q437 (≠ S444)
7tfaB Glutamine synthetase (see paper)
72% identity, 99% coverage: 6:445/445 of query aligns to 3:441/441 of 7tfaB
- binding glutamine: E131 (= E135), Y153 (= Y157), E186 (= E190), G238 (= G242), H242 (= H246), R295 (= R299), E301 (= E305)
- binding magnesium ion: E129 (= E133), E131 (= E135), E186 (= E190), E193 (= E197), H242 (= H246), E330 (= E334)
- binding : Y58 (≠ F61), R60 (= R63), V187 (= V191), N237 (= N241), G299 (= G303), Y300 (= Y304), R313 (= R317), M424 (= M428)
7tdpA Structure of paenibacillus polymyxa gs bound to met-sox-p-adp (transition state complex) to 1.98 angstom (see paper)
72% identity, 99% coverage: 6:445/445 of query aligns to 3:439/439 of 7tdpA