SitesBLAST
Comparing SMc01973 FitnessBrowser__Smeli:SMc01973 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)
38% identity, 97% coverage: 12:453/455 of query aligns to 28:470/472 of P78061
- H282 (= H264) mutation to N: Activity is impaired to 9% of wild-type.
- R357 (= R339) mutation to Q: Activity is impaired to 3% of wild-type.
7tenA Glutamine synthetase (see paper)
30% identity, 98% coverage: 9:454/455 of query aligns to 6:441/442 of 7tenA
- binding adenosine-5'-diphosphate: G128 (≠ A142), E130 (= E144), E182 (≠ D202), D196 (≠ N216), F197 (≠ L217), K198 (≠ L218), Y199 (≠ H219), N245 (≠ H266), S247 (= S268), R319 (= R339), S327 (≠ A347), R329 (= R349)
- binding l-methionine-s-sulfoximine phosphate: E130 (= E144), E132 (= E146), E187 (= E207), E194 (= E214), N238 (≠ S259), G239 (= G260), H243 (= H264), R296 (= R316), E302 (≠ H322), R314 (= R334), R333 (= R353)
7tf9S L. Monocytogenes gs(14)-q-glnr peptide (see paper)
30% identity, 98% coverage: 9:454/455 of query aligns to 7:442/443 of 7tf9S
- binding glutamine: E133 (= E146), Y155 (≠ F186), E188 (= E207), G240 (= G260), G242 (= G262), R297 (= R316), E303 (≠ H322)
- binding magnesium ion: E131 (= E144), E133 (= E146), E188 (= E207), E195 (= E214), H244 (= H264), E332 (= E351)
- binding : F59 (≠ E67), V60 (≠ D68), E418 (≠ A430), I422 (≠ Q434), M426 (≠ G438)
8ooqB Glutamine synthetase from Methanothermococcus thermolithotrophicus (see paper)
30% identity, 91% coverage: 42:454/455 of query aligns to 42:446/446 of 8ooqB
Sites not aligning to the query:
8oooA Glutamine synthetase from methanothermococcus thermolithotrophicus in complex with 2-oxoglutarate and mgatp at 2.15 a resolution (see paper)
30% identity, 91% coverage: 42:454/455 of query aligns to 43:447/447 of 8oooA
- binding 2-oxoglutaric acid: R87 (≠ N96), V93 (≠ S102), P170 (≠ G184), R173 (≠ F187), R174 (≠ S188), S190 (≠ A204)
- binding adenosine-5'-triphosphate: E136 (= E144), E188 (≠ D202), F203 (≠ L217), K204 (≠ H219), F205 (≠ S220), H251 (= H266), S253 (= S268), R325 (= R339), R335 (= R349)
Sites not aligning to the query:
8oozA Glutamine synthetase (see paper)
30% identity, 99% coverage: 5:453/455 of query aligns to 1:428/430 of 8oozA
- binding adenosine-5'-triphosphate: G117 (≠ A142), E170 (≠ D202), F185 (≠ L217), K186 (≠ L218), Y187 (≠ H219), N233 (≠ H266), S235 (= S268), S315 (≠ A347), R317 (= R349)
- binding magnesium ion: E119 (= E144), H231 (= H264), E319 (= E351)
4s0rD Structure of gs-tnra complex (see paper)
29% identity, 95% coverage: 21:452/455 of query aligns to 21:444/447 of 4s0rD
- active site: D56 (≠ V60), E135 (= E144), E137 (= E146), E192 (= E207), E199 (= E214), H248 (= H264), R319 (= R334), E336 (= E351), R338 (= R353)
- binding glutamine: E137 (= E146), E192 (= E207), R301 (= R316), E307 (≠ H322)
- binding magnesium ion: I66 (= I70), E135 (= E144), E135 (= E144), E199 (= E214), H248 (= H264), H248 (= H264), E336 (= E351), H419 (≠ M427)
- binding : F63 (≠ E67), V64 (≠ D68), R65 (≠ I69), I66 (= I70), D161 (vs. gap), G241 (≠ T257), V242 (≠ R258), N243 (≠ S259), G305 (≠ D320), Y306 (≠ T321), Y376 (= Y391), I426 (≠ Q434), M430 (≠ G438)
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, 95% coverage: 21:452/455 of query aligns to 17:440/443 of 4lnkA
- active site: D52 (≠ V60), E131 (= E144), E133 (= E146), E188 (= E207), E195 (= E214), H244 (= H264), R315 (= R334), E332 (= E351), R334 (= R353)
- binding adenosine-5'-diphosphate: K43 (≠ G51), M50 (≠ S58), F198 (≠ L217), Y200 (≠ H219), N246 (≠ H266), S248 (= S268), S324 (≠ G343), S328 (≠ A347), R330 (= R349)
- binding glutamic acid: E133 (= E146), E188 (= E207), V189 (≠ N208), N239 (≠ S259), G240 (= G260), G242 (= G262), E303 (≠ H322)
- binding magnesium ion: E131 (= E144), E188 (= E207), E195 (= E214), H244 (= H264), E332 (= E351)
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, 95% coverage: 21:452/455 of query aligns to 17:440/443 of 4lniA
- active site: D52 (≠ V60), E131 (= E144), E133 (= E146), E188 (= E207), E195 (= E214), H244 (= H264), R315 (= R334), E332 (= E351), R334 (= R353)
- binding adenosine-5'-diphosphate: E131 (= E144), E183 (≠ D202), D197 (≠ N216), Y200 (≠ H219), N246 (≠ H266), S248 (= S268), R320 (= R339), R330 (= R349)
- binding magnesium ion: E131 (= E144), E131 (= E144), E133 (= E146), E188 (= E207), E195 (= E214), E195 (= E214), H244 (= H264), E332 (= E351)
- binding l-methionine-s-sulfoximine phosphate: E133 (= E146), E188 (= E207), H244 (= H264), R297 (= R316), E303 (≠ H322), R315 (= R334), R334 (= R353)
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, 95% coverage: 21:452/455 of query aligns to 18:441/444 of P12425
- G59 (= G66) 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 (≠ I69) 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 (= E144) binding
- E134 (= E146) binding
- E189 (= E207) binding
- V190 (≠ N208) 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 (= E214) binding
- G241 (= G260) binding
- H245 (= H264) binding
- G302 (≠ D320) 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 (≠ H322) 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 (= P324) 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 (= E351) binding
- E424 (= E435) 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
8ooxB Glutamine synthetase (see paper)
30% identity, 99% coverage: 5:453/455 of query aligns to 1:436/438 of 8ooxB
7tdpA Structure of paenibacillus polymyxa gs bound to met-sox-p-adp (transition state complex) to 1.98 angstom (see paper)
30% identity, 95% coverage: 24:454/455 of query aligns to 19:438/439 of 7tdpA
- binding adenosine-5'-diphosphate: N123 (vs. gap), G125 (≠ A142), E127 (= E144), E179 (≠ D202), D193 (≠ N216), Y196 (≠ H219), N242 (≠ H266), S244 (= S268), R316 (= R339), R326 (= R349)
- binding magnesium ion: E127 (= E144), E127 (= E144), E129 (= E146), E184 (= E207), E191 (= E214), E191 (= E214), H240 (= H264), E328 (= E351)
- binding l-methionine-s-sulfoximine phosphate: E127 (= E144), E129 (= E146), E184 (= E207), E191 (= E214), G236 (= G260), H240 (= H264), R293 (= R316), E299 (≠ H322), R311 (= R334), R330 (= R353)
7tfaB Glutamine synthetase (see paper)
29% identity, 95% coverage: 24:454/455 of query aligns to 19:440/441 of 7tfaB
- binding glutamine: E131 (= E146), Y153 (≠ F186), E186 (= E207), G238 (= G260), H242 (= H264), R295 (= R316), E301 (≠ H322)
- binding magnesium ion: E129 (= E144), E131 (= E146), E186 (= E207), E193 (= E214), H242 (= H264), E330 (= E351)
- binding : Y58 (≠ E67), R60 (≠ I69), V187 (≠ N208), N237 (≠ S259), G299 (≠ D320), Y300 (≠ T321), R313 (= R334), M424 (≠ G438)
7tdvC Glutamine synthetase (see paper)
29% identity, 95% coverage: 21:453/455 of query aligns to 17:441/443 of 7tdvC
- binding adenosine-5'-diphosphate: G129 (≠ A142), E131 (= E144), E183 (≠ D202), D197 (≠ N216), F198 (≠ L217), K199 (≠ L218), Y200 (≠ H219), N246 (≠ H266), V247 (≠ F267), S248 (= S268), R320 (= R339), S328 (≠ A347), R330 (= R349)
- binding magnesium ion: E131 (= E144), E131 (= E144), E133 (= E146), E188 (= E207), E195 (= E214), E195 (= E214), H244 (= H264), E332 (= E351)
- binding l-methionine-s-sulfoximine phosphate: E131 (= E144), E133 (= E146), E188 (= E207), E195 (= E214), G240 (= G260), H244 (= H264), R297 (= R316), E303 (≠ H322), R315 (= R334)
7tf6A Glutamine synthetase (see paper)
28% identity, 95% coverage: 21:453/455 of query aligns to 16:436/438 of 7tf6A
- binding glutamine: E128 (= E146), E183 (= E207), G235 (= G260), H239 (= H264), R292 (= R316), E298 (≠ H322)
- binding magnesium ion: E126 (= E144), E128 (= E146), E183 (= E207), E190 (= E214), H239 (= H264), E327 (= E351)
- binding : F58 (≠ E67), R60 (≠ I69), G232 (≠ T257), N234 (≠ S259), G296 (≠ D320), Y297 (≠ T321), R310 (= R334), Y367 (= Y391), Y421 (≠ G438), Q433 (≠ A450)
Sites not aligning to the query:
8tfkA Glutamine synthetase (see paper)
28% identity, 96% coverage: 21:455/455 of query aligns to 15:440/440 of 8tfkA
- binding adenosine-5'-diphosphate: E128 (= E144), D194 (≠ N216), F195 (≠ L217), F197 (≠ H219), N243 (≠ H266), R312 (= R334), R317 (= R339), G325 (≠ A347), R327 (= R349)
- binding magnesium ion: E128 (= E144), E128 (= E144), E130 (= E146), E185 (= E207), E192 (= E214), E192 (= E214), H241 (= H264), E329 (= E351)
- binding l-methionine-s-sulfoximine phosphate: E128 (= E144), E130 (= E146), E185 (= E207), E192 (= E214), G237 (= G260), H241 (= H264), R294 (= R316), E300 (≠ H322), R312 (= R334), R331 (= R353)
8ufjB Glutamine synthetase (see paper)
28% identity, 96% coverage: 21:455/455 of query aligns to 19:444/444 of 8ufjB
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)
32% identity, 75% coverage: 113:454/455 of query aligns to 101:446/446 of P9WN37
- K363 (vs. gap) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
7cquA Gmas/adp/metsox-p complex (see paper)
31% identity, 95% coverage: 21:454/455 of query aligns to 12:429/429 of 7cquA
- binding adenosine-5'-diphosphate: E121 (= E144), Y173 (≠ A195), N187 (= N216), W188 (≠ L217), D189 (≠ L218), Y190 (≠ H219), H236 (= H266), L237 (≠ F267), S238 (= S268), R316 (= R339), R322 (= R349)
- binding magnesium ion: E121 (= E144), E121 (= E144), E123 (= E146), E178 (= E207), E185 (= E214), E185 (= E214), H234 (= H264), E324 (= E351)
- binding l-methionine-s-sulfoximine phosphate: E121 (= E144), E123 (= E146), E178 (= E207), E185 (= E214), T229 (≠ S259), G230 (= G260), H234 (= H264), R287 (= R316), W299 (≠ H322), R311 (= R334), R326 (= R353)
7cqqA Gmas in complex with amppnp and metsox (see paper)
31% identity, 95% coverage: 21:454/455 of query aligns to 12:429/429 of 7cqqA
- binding phosphoaminophosphonic acid-adenylate ester: E121 (= E144), Y173 (≠ A195), E185 (= E214), N187 (= N216), D189 (≠ L218), Y190 (≠ H219), H234 (= H264), H236 (= H266), S238 (= S268), R311 (= R334), R316 (= R339), R322 (= R349), E324 (= E351)
- binding magnesium ion: E121 (= E144), E121 (= E144), E123 (= E146), E178 (= E207), E185 (= E214), E185 (= E214), H234 (= H264), E324 (= E351)
- binding (2s)-2-amino-4-(methylsulfonimidoyl)butanoic acid: E123 (= E146), E178 (= E207), T229 (≠ S259), H234 (= H264), R287 (= R316), W299 (≠ H322), R311 (= R334), R326 (= R353)
Query Sequence
>SMc01973 FitnessBrowser__Smeli:SMc01973
MSIDADDPEVFQSWLEQNGPIESIQAVICDLNGIMRGKRVPVEQARKVLGGGIRMPLSIV
GVDVWGEDIIGSAQVFATGDRDGICGVTGRGALPVNWTSRPSALVPLWLFVENGRPFLAD
PRQALAAIMREYRELGLRPVVATELEFYLIDPEPDSAVPPISPYTGKRLDSDAILSIDEL
DDFGEFFSDVYRECARQNVPADAAIAENGIGQFEINLLHSDDPLKAADDAIFFKRIVKGV
ARKHGLAATFMAKPYGTRSGNGMHVHFSLLDEEGNNVFDDGSDEGSAVLKHAVAGLLRGM
AETTLMFAPHFNSYRRLRPDTHAPTSISWGYENRTSAIRIPGGNPAARRIEHRVAGADAN
PYLVIAAILGAALVGIRNKWKPPVPVEGRAYAAEKLPKIPADWGQAVDAFEAGPIAAEIF
DPVLRSMLIACKRQEIAGFAEQVTDYEFSAYLEIV
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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