SitesBLAST
Comparing GFF2319 FitnessBrowser__psRCH2:GFF2319 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)
7cqwA Gmas/adp complex-conformation 1 (see paper)
42% identity, 98% coverage: 9:451/454 of query aligns to 1:428/430 of 7cqwA
7cquA Gmas/adp/metsox-p complex (see paper)
42% identity, 97% coverage: 11:451/454 of query aligns to 2:427/429 of 7cquA
- binding adenosine-5'-diphosphate: E121 (= E131), Y173 (= Y186), N187 (≠ D200), W188 (≠ F201), D189 (≠ K202), Y190 (= Y203), H236 (≠ N249), L237 (≠ M250), S238 (= S251), R316 (= R334), R322 (= R341)
- binding magnesium ion: E121 (= E131), E121 (= E131), E123 (= E133), E178 (= E191), E185 (= E198), E185 (= E198), H234 (= H247), E324 (= E343)
- binding l-methionine-s-sulfoximine phosphate: E121 (= E131), E123 (= E133), E178 (= E191), E185 (= E198), T229 (= T242), G230 (= G243), H234 (= H247), R287 (= R305), W299 (= W317), R311 (= R329), R326 (= R345)
7cqqA Gmas in complex with amppnp and metsox (see paper)
42% identity, 97% coverage: 11:451/454 of query aligns to 2:427/429 of 7cqqA
- binding phosphoaminophosphonic acid-adenylate ester: E121 (= E131), Y173 (= Y186), E185 (= E198), N187 (≠ D200), D189 (≠ K202), Y190 (= Y203), H234 (= H247), H236 (≠ N249), S238 (= S251), R311 (= R329), R316 (= R334), R322 (= R341), E324 (= E343)
- binding magnesium ion: E121 (= E131), E121 (= E131), E123 (= E133), E178 (= E191), E185 (= E198), E185 (= E198), H234 (= H247), E324 (= E343)
- binding (2s)-2-amino-4-(methylsulfonimidoyl)butanoic acid: E123 (= E133), E178 (= E191), T229 (= T242), H234 (= H247), R287 (= R305), W299 (= W317), R311 (= R329), R326 (= R345)
7cqnA Gmas in complex with amppcp (see paper)
42% identity, 97% coverage: 11:451/454 of query aligns to 2:427/429 of 7cqnA
- binding phosphomethylphosphonic acid adenylate ester: G45 (≠ L54), D61 (≠ E71), E121 (= E131), Y173 (= Y186), Q174 (≠ S187), W188 (≠ F201), D189 (≠ K202), Y190 (= Y203), H236 (≠ N249), S238 (= S251), R311 (= R329), R316 (= R334), R322 (= R341)
8ooxB Glutamine synthetase (see paper)
36% identity, 99% coverage: 7:454/454 of query aligns to 1:438/438 of 8ooxB
8oozA Glutamine synthetase (see paper)
35% identity, 99% coverage: 7:454/454 of query aligns to 1:430/430 of 8oozA
- binding adenosine-5'-triphosphate: G117 (= G129), E170 (≠ Y186), F185 (= F201), K186 (= K202), Y187 (= Y203), N233 (= N249), S235 (= S251), S315 (≠ G339), R317 (= R341)
- binding magnesium ion: E119 (= E131), H231 (= H247), E319 (= E343)
7tdpA Structure of paenibacillus polymyxa gs bound to met-sox-p-adp (transition state complex) to 1.98 angstom (see paper)
36% identity, 98% coverage: 10:454/454 of query aligns to 5:439/439 of 7tdpA
- binding adenosine-5'-diphosphate: N123 (= N127), G125 (= G129), E127 (= E131), E179 (≠ Y186), D193 (= D200), Y196 (= Y203), N242 (= N249), S244 (= S251), R316 (= R334), R326 (= R341)
- binding magnesium ion: E127 (= E131), E127 (= E131), E129 (= E133), E184 (= E191), E191 (= E198), E191 (= E198), H240 (= H247), E328 (= E343)
- binding l-methionine-s-sulfoximine phosphate: E127 (= E131), E129 (= E133), E184 (= E191), E191 (= E198), G236 (= G243), H240 (= H247), R293 (= R305), E299 (≠ W317), R311 (= R329), R330 (= R345)
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)
36% identity, 97% coverage: 10:451/454 of query aligns to 7:441/444 of P12425
- G59 (= G62) 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 (≠ Q65) 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 (= E131) binding
- E134 (= E133) binding
- E189 (= E191) binding
- V190 (≠ D192) 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 (= E198) binding
- G241 (= G243) binding
- H245 (= H247) binding
- G302 (≠ S315) 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 (≠ W317) 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 (= P319) 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 (= E343) binding
- 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
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)
36% identity, 97% coverage: 10:451/454 of query aligns to 6:440/443 of 4lnkA
- active site: D52 (≠ T56), E131 (= E131), E133 (= E133), E188 (= E191), E195 (= E198), H244 (= H247), R315 (= R329), E332 (= E343), R334 (= R345)
- binding adenosine-5'-diphosphate: K43 (≠ Q47), M50 (≠ L54), F198 (= F201), Y200 (= Y203), N246 (= N249), S248 (= S251), S324 (≠ Q338), S328 (≠ G339), R330 (= R341)
- binding glutamic acid: E133 (= E133), E188 (= E191), V189 (≠ D192), N239 (≠ T242), G240 (= G243), G242 (= G245), E303 (≠ W317)
- binding magnesium ion: E131 (= E131), E188 (= E191), E195 (= E198), H244 (= H247), E332 (= E343)
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)
36% identity, 97% coverage: 10:451/454 of query aligns to 6:440/443 of 4lniA
- active site: D52 (≠ T56), E131 (= E131), E133 (= E133), E188 (= E191), E195 (= E198), H244 (= H247), R315 (= R329), E332 (= E343), R334 (= R345)
- binding adenosine-5'-diphosphate: E131 (= E131), E183 (≠ Y186), D197 (= D200), Y200 (= Y203), N246 (= N249), S248 (= S251), R320 (= R334), R330 (= R341)
- binding magnesium ion: E131 (= E131), E131 (= E131), E133 (= E133), E188 (= E191), E195 (= E198), E195 (= E198), H244 (= H247), E332 (= E343)
- binding l-methionine-s-sulfoximine phosphate: E133 (= E133), E188 (= E191), H244 (= H247), R297 (= R305), E303 (≠ W317), R315 (= R329), R334 (= R345)
4s0rD Structure of gs-tnra complex (see paper)
36% identity, 97% coverage: 10:451/454 of query aligns to 10:444/447 of 4s0rD
- active site: D56 (≠ T56), E135 (= E131), E137 (= E133), E192 (= E191), E199 (= E198), H248 (= H247), R319 (= R329), E336 (= E343), R338 (= R345)
- binding glutamine: E137 (= E133), E192 (= E191), R301 (= R305), E307 (≠ W317)
- binding magnesium ion: I66 (= I67), E135 (= E131), E135 (= E131), E199 (= E198), H248 (= H247), H248 (= H247), E336 (= E343), H419 (≠ A426)
- binding : F63 (≠ V63), V64 (≠ P64), R65 (≠ Q65), I66 (= I67), D161 (= D160), G241 (≠ N240), V242 (≠ R241), N243 (≠ T242), G305 (≠ S315), Y306 (≠ T316), Y376 (= Y383), I426 (≠ D433), M430 (≠ A437)
7tf6A Glutamine synthetase (see paper)
36% identity, 98% coverage: 10:452/454 of query aligns to 5:436/438 of 7tf6A
- binding glutamine: E128 (= E133), E183 (= E191), G235 (= G243), H239 (= H247), R292 (= R305), E298 (≠ W317)
- binding magnesium ion: E126 (= E131), E128 (= E133), E183 (= E191), E190 (= E198), H239 (= H247), E327 (= E343)
- binding : F58 (≠ V63), R60 (≠ Q65), G232 (≠ N240), N234 (≠ T242), G296 (≠ S315), Y297 (≠ T316), R310 (= R329), Y367 (= Y383), Y421 (≠ A437), Q433 (≠ R449)
Sites not aligning to the query:
7tdvC Glutamine synthetase (see paper)
36% identity, 98% coverage: 10:452/454 of query aligns to 6:441/443 of 7tdvC
- binding adenosine-5'-diphosphate: G129 (= G129), E131 (= E131), E183 (≠ Y186), D197 (= D200), F198 (= F201), K199 (= K202), Y200 (= Y203), N246 (= N249), V247 (≠ M250), S248 (= S251), R320 (= R334), S328 (≠ G339), R330 (= R341)
- binding magnesium ion: E131 (= E131), E131 (= E131), E133 (= E133), E188 (= E191), E195 (= E198), E195 (= E198), H244 (= H247), E332 (= E343)
- binding l-methionine-s-sulfoximine phosphate: E131 (= E131), E133 (= E133), E188 (= E191), E195 (= E198), G240 (= G243), H244 (= H247), R297 (= R305), E303 (≠ W317), R315 (= R329)
7tfaB Glutamine synthetase (see paper)
36% identity, 98% coverage: 10:454/454 of query aligns to 5:441/441 of 7tfaB
- binding glutamine: E131 (= E133), Y153 (≠ C158), E186 (= E191), G238 (= G243), H242 (= H247), R295 (= R305), E301 (≠ W317)
- binding magnesium ion: E129 (= E131), E131 (= E133), E186 (= E191), E193 (= E198), H242 (= H247), E330 (= E343)
- binding : Y58 (≠ V63), R60 (≠ Q65), V187 (≠ D192), N237 (≠ T242), G299 (≠ S315), Y300 (≠ T316), R313 (= R329), M424 (≠ A437)
7tf9S L. Monocytogenes gs(14)-q-glnr peptide (see paper)
36% identity, 96% coverage: 18:454/454 of query aligns to 14:443/443 of 7tf9S
- binding glutamine: E133 (= E133), Y155 (≠ C158), E188 (= E191), G240 (= G243), G242 (= G245), R297 (= R305), E303 (≠ W317)
- binding magnesium ion: E131 (= E131), E133 (= E133), E188 (= E191), E195 (= E198), H244 (= H247), E332 (= E343)
- binding : F59 (≠ V63), V60 (≠ P64), E418 (≠ D429), I422 (≠ D433), M426 (≠ A437)
7tenA Glutamine synthetase (see paper)
36% identity, 96% coverage: 18:454/454 of query aligns to 13:442/442 of 7tenA
- binding adenosine-5'-diphosphate: G128 (= G129), E130 (= E131), E182 (≠ Y186), D196 (= D200), F197 (= F201), K198 (= K202), Y199 (= Y203), N245 (= N249), S247 (= S251), R319 (= R334), S327 (≠ G339), R329 (= R341)
- binding l-methionine-s-sulfoximine phosphate: E130 (= E131), E132 (= E133), E187 (= E191), E194 (= E198), N238 (≠ T242), G239 (= G243), H243 (= H247), R296 (= R305), E302 (≠ W317), R314 (= R329), R333 (= R345)
8oooA Glutamine synthetase from methanothermococcus thermolithotrophicus in complex with 2-oxoglutarate and mgatp at 2.15 a resolution (see paper)
36% identity, 98% coverage: 7:453/454 of query aligns to 1:447/447 of 8oooA
- binding 2-oxoglutaric acid: F17 (≠ Y23), R19 (≠ M25), A33 (≠ F39), R87 (vs. gap), V93 (≠ L90), P170 (= P169), R173 (≠ V171), R174 (≠ D172), S190 (≠ F188)
- binding adenosine-5'-triphosphate: E136 (= E131), E188 (≠ Y186), F203 (= F201), K204 (= K202), F205 (≠ Y203), H251 (≠ N249), S253 (= S251), R325 (= R334), R335 (= R341)
8tfkA Glutamine synthetase (see paper)
33% identity, 98% coverage: 7:451/454 of query aligns to 1:437/440 of 8tfkA
- binding adenosine-5'-diphosphate: E128 (= E131), D194 (= D200), F195 (= F201), F197 (≠ Y203), N243 (= N249), R312 (= R329), R317 (= R334), G325 (= G339), R327 (= R341)
- binding magnesium ion: E128 (= E131), E128 (= E131), E130 (= E133), E185 (= E191), E192 (= E198), E192 (= E198), H241 (= H247), E329 (= E343)
- binding l-methionine-s-sulfoximine phosphate: E128 (= E131), E130 (= E133), E185 (= E191), E192 (= E198), G237 (= G243), H241 (= H247), R294 (= R305), E300 (≠ W317), R312 (= R329), R331 (= R345)
8ufjB Glutamine synthetase (see paper)
33% identity, 99% coverage: 7:454/454 of query aligns to 5:444/444 of 8ufjB
8ooqB Glutamine synthetase from Methanothermococcus thermolithotrophicus (see paper)
36% identity, 98% coverage: 8:453/454 of query aligns to 1:446/446 of 8ooqB
- binding 2-oxoglutaric acid: F16 (≠ Y23), R18 (≠ M25), A32 (≠ F39), R86 (vs. gap), V92 (≠ L90), P169 (= P169), R172 (≠ V171), R173 (≠ D172), S189 (≠ F188)
- binding magnesium ion: E137 (= E133), E192 (= E191), E199 (= E198)
Query Sequence
>GFF2319 FitnessBrowser__psRCH2:GFF2319
MTSFPLSSVEELKQQLQDKGVKYAMASYVDIHGVIKGKFVPIAHLGQMLRGSELYTGAAL
DGVPQEISDNEVAAMPDPATGTQCSWNRDLAWFASDLYLDGKPFEACSRGILKRQTEAAA
ELGYTFNLGIETEFFLFKDTPDGGFAPISERDDMAKPCYDPRLLMDNLPIVDELVQAMNE
MGWGVYSFDHEDANGQFETDFKYTDALGMADRFVFFRMMANEIARKHGAFATFMPKPSAN
RTGSGAHYNMSLADIETGKNLFEVDGEDTYGCGVTPLAYHFIAGVLKHAKAICAVIAPTV
NSYKRLIRKGAMSGSTWAPVFCCYGNNNRTNMLRIPSQGARVECRAADIGCNPYLGAAMI
LAAGLEGIRDELDPGQPHRENMYHYSEQEVVQMGIETLPRTLSEAIDAFEADPLSRQVFG
DAMYQAFVDFKRDEWNAYHTHVSDWEIQRYLKFF
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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