SitesBLAST
Comparing GFF1137 FitnessBrowser__Phaeo:GFF1137 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)
P78061 Gamma-glutamylputrescine synthetase PuuA; Gamma-Glu-Put synthetase; Glutamate--putrescine ligase; EC 6.3.1.11 from Escherichia coli (strain K12) (see paper)
34% identity, 95% coverage: 24:451/452 of query aligns to 40:471/472 of P78061
- H282 (= H262) mutation to N: Activity is impaired to 9% of wild-type.
- R357 (= R338) mutation to Q: Activity is impaired to 3% of wild-type.
7tf9S L. Monocytogenes gs(14)-q-glnr peptide (see paper)
30% identity, 93% coverage: 28:449/452 of query aligns to 24:440/443 of 7tf9S
- binding glutamine: E133 (= E143), Y155 (≠ A173), E188 (= E206), N239 (≠ P257), G240 (= G258), S241 (= S259), G242 (≠ A260), H244 (= H262), R297 (= R315), E303 (≠ A321)
- binding magnesium ion: E131 (= E141), E133 (= E143), E188 (= E206), E195 (= E213), H244 (= H262), E332 (= E350)
- binding : F59 (≠ W75), V60 (≠ I76), R61 (vs. gap), I62 (vs. gap), E418 (≠ I427), I422 (≠ A431), D425 (= D434), M426 (≠ E435)
7tenA Glutamine synthetase (see paper)
30% identity, 93% coverage: 28:449/452 of query aligns to 23:439/442 of 7tenA
- binding adenosine-5'-diphosphate: G128 (≠ A139), P129 (= P140), E130 (= E141), E182 (≠ D201), E194 (= E213), D196 (≠ N215), F197 (≠ L216), K198 (≠ R217), Y199 (≠ H218), N245 (≠ H264), S247 (= S266), R314 (= R333), R319 (= R338), L326 (≠ E345), S327 (≠ A346), T328 (≠ R347), R329 (= R348), E331 (= E350)
- binding l-methionine-s-sulfoximine phosphate: E130 (= E141), E132 (= E143), E187 (= E206), E194 (= E213), N238 (≠ P257), G239 (= G258), G241 (≠ A260), H243 (= H262), R296 (= R315), Y301 (≠ Q320), E302 (≠ A321), R314 (= R333), R333 (= R352)
4s0rD Structure of gs-tnra complex (see paper)
29% identity, 93% coverage: 28:449/452 of query aligns to 28:444/447 of 4s0rD
- active site: D56 (≠ E68), E135 (= E141), E137 (= E143), E192 (= E206), E199 (= E213), H248 (= H262), R319 (= R333), E336 (= E350), R338 (= R352)
- binding glutamine: E137 (= E143), E192 (= E206), E199 (= E213), G244 (= G258), G246 (≠ A260), R301 (= R315), Y306 (≠ Q320), E307 (≠ A321), A308 (= A322)
- binding magnesium ion: I66 (vs. gap), E135 (= E141), E135 (= E141), E199 (= E213), H248 (= H262), H248 (= H262), E336 (= E350), K403 (≠ E408), S404 (≠ E409), H419 (≠ V424)
- binding : F63 (≠ W75), V64 (≠ I76), R65 (vs. gap), I66 (vs. gap), D161 (≠ S175), V193 (≠ G207), A194 (≠ G208), P195 (≠ A209), G241 (≠ D255), V242 (≠ E256), N243 (≠ P257), G305 (≠ E319), Y306 (≠ Q320), R319 (= R333), N374 (≠ D388), Y376 (= Y390), M378 (vs. gap), I426 (≠ A431), M430 (≠ E435), Q442 (≠ H447)
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)
29% identity, 93% coverage: 28:449/452 of query aligns to 24:440/443 of 4lnkA
- active site: D52 (≠ E68), E131 (= E141), E133 (= E143), E188 (= E206), E195 (= E213), H244 (= H262), R315 (= R333), E332 (= E350), R334 (= R352)
- binding adenosine-5'-diphosphate: K43 (= K47), M50 (≠ F58), N127 (vs. gap), G129 (≠ A139), E131 (= E141), F198 (≠ L216), K199 (≠ R217), Y200 (≠ H218), N246 (≠ H264), L247 (≠ H265), S248 (= S266), F250 (≠ M270), S324 (= S342), I327 (≠ E345), S328 (≠ A346), R330 (= R348)
- binding glutamic acid: E133 (= E143), Y155 (≠ A169), E188 (= E206), V189 (≠ G207), N239 (≠ P257), G240 (= G258), G242 (≠ A260), H244 (= H262), R297 (= R315), E303 (≠ A321), R334 (= R352)
- binding magnesium ion: E131 (= E141), E188 (= E206), E195 (= E213), H244 (= H262), E332 (= E350)
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)
29% identity, 93% coverage: 28:449/452 of query aligns to 24:440/443 of 4lniA
- active site: D52 (≠ E68), E131 (= E141), E133 (= E143), E188 (= E206), E195 (= E213), H244 (= H262), R315 (= R333), E332 (= E350), R334 (= R352)
- binding adenosine-5'-diphosphate: N127 (vs. gap), G129 (≠ A139), E131 (= E141), E183 (≠ D201), D197 (≠ N215), F198 (≠ L216), K199 (≠ R217), Y200 (≠ H218), N246 (≠ H264), S248 (= S266), R315 (= R333), R320 (= R338), I327 (≠ E345), S328 (≠ A346), R330 (= R348), E332 (= E350)
- binding magnesium ion: E131 (= E141), E131 (= E141), E133 (= E143), E188 (= E206), E195 (= E213), E195 (= E213), H244 (= H262), E332 (= E350)
- binding l-methionine-s-sulfoximine phosphate: E131 (= E141), E133 (= E143), Y155 (≠ A169), E188 (= E206), E195 (= E213), G240 (= G258), G242 (≠ A260), H244 (= H262), R297 (= R315), Y302 (≠ Q320), E303 (≠ A321), A304 (= A322), R315 (= R333), R334 (= R352)
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)
29% identity, 93% coverage: 28:449/452 of query aligns to 25:441/444 of P12425
- G59 (= G74) 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 (vs. gap) 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 (= E141) binding
- E134 (= E143) binding
- E189 (= E206) binding
- V190 (≠ G207) 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 (= E213) binding
- G241 (= G258) binding
- H245 (= H262) binding
- G302 (≠ E319) 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 (≠ A321) 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
- E424 (= E432) 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
5dm3C Crystal structure of glutamine synthetase from chromohalobacter salexigens dsm 3043(csal_0679, target efi-550015) with bound adp
29% identity, 96% coverage: 13:444/452 of query aligns to 6:390/396 of 5dm3C
- active site: E115 (= E141), E117 (= E143), E162 (= E206), E169 (= E213), H218 (= H262), R286 (= R333), E303 (= E350), R305 (= R352)
- binding adenosine-5'-diphosphate: T46 (≠ F51), H47 (= H52), I111 (≠ V137), A113 (= A139), E157 (≠ D201), R173 (= R217), C174 (≠ H218), H220 (= H264), Q221 (≠ H265), S222 (= S266), W224 (≠ M270), A299 (= A346), R301 (= R348)
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)
31% identity, 83% coverage: 76:449/452 of query aligns to 63:444/446 of A0R083
- K363 (≠ N377) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
7tfaB Glutamine synthetase (see paper)
28% identity, 93% coverage: 28:449/452 of query aligns to 23:438/441 of 7tfaB