SitesBLAST
Comparing WP_011876163.1 NCBI__GCF_000016205.1:WP_011876163.1 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)
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)
31% identity, 97% coverage: 9:455/459 of query aligns to 4:439/443 of 4lnkA
- active site: D52 (vs. gap), E131 (= E145), E133 (= E147), E188 (= E208), E195 (= E215), H244 (= H264), R315 (= R336), E332 (= E353), R334 (= R355)
- binding adenosine-5'-diphosphate: K43 (≠ S48), M50 (≠ G55), F198 (≠ L218), Y200 (≠ L220), N246 (≠ H266), S248 (= S268), S324 (≠ G345), S328 (= S349), R330 (= R351)
- binding glutamic acid: E133 (= E147), E188 (= E208), V189 (≠ A209), N239 (≠ P259), G240 (= G260), G242 (= G262), E303 (≠ W324)
- binding magnesium ion: E131 (= E145), E188 (= E208), E195 (= E215), H244 (= H264), E332 (= E353)
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)
31% identity, 97% coverage: 9:455/459 of query aligns to 4:439/443 of 4lniA
- active site: D52 (vs. gap), E131 (= E145), E133 (= E147), E188 (= E208), E195 (= E215), H244 (= H264), R315 (= R336), E332 (= E353), R334 (= R355)
- binding adenosine-5'-diphosphate: E131 (= E145), E183 (= E203), D197 (≠ A217), Y200 (≠ L220), N246 (≠ H266), S248 (= S268), R320 (= R341), R330 (= R351)
- binding magnesium ion: E131 (= E145), E131 (= E145), E133 (= E147), E188 (= E208), E195 (= E215), E195 (= E215), H244 (= H264), E332 (= E353)
- binding l-methionine-s-sulfoximine phosphate: E133 (= E147), E188 (= E208), H244 (= H264), R297 (= R318), E303 (≠ W324), R315 (= R336), R334 (= R355)
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)
31% identity, 97% coverage: 9:455/459 of query aligns to 5:440/444 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 (≠ K75) 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 (= E145) binding Mg(2+)
- E134 (= E147) binding Mg(2+)
- E189 (= E208) binding Mg(2+)
- V190 (≠ A209) 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 (= E215) binding Mg(2+)
- G241 (= G260) binding L-glutamate
- H245 (= H264) binding Mg(2+)
- G302 (= G322) 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 (≠ W324) 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 (= P326) 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 (= E353) binding Mg(2+)
- E424 (= E439) 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)
31% identity, 97% coverage: 9:455/459 of query aligns to 8:443/447 of 4s0rD
- active site: D56 (vs. gap), E135 (= E145), E137 (= E147), E192 (= E208), E199 (= E215), H248 (= H264), R319 (= R336), E336 (= E353), R338 (= R355)
- binding glutamine: E137 (= E147), E192 (= E208), R301 (= R318), E307 (≠ W324)
- binding magnesium ion: I66 (= I76), E135 (= E145), E135 (= E145), E199 (= E215), H248 (= H264), H248 (= H264), E336 (= E353), H419 (= H431)
- binding : F63 (≠ W63), V64 (≠ C74), R65 (≠ K75), I66 (= I76), D161 (vs. gap), G241 (≠ E257), V242 (≠ M258), N243 (≠ P259), G305 (= G322), Y306 (= Y323), Y376 (= Y393), I426 (≠ W438), M430 (≠ E442)
5dm3C Crystal structure of glutamine synthetase from chromohalobacter salexigens dsm 3043(csal_0679, target efi-550015) with bound adp
29% identity, 97% coverage: 12:457/459 of query aligns to 4:396/396 of 5dm3C
- active site: E115 (= E145), E117 (= E147), E162 (= E208), E169 (= E215), H218 (= H264), R286 (= R336), E303 (= E353), R305 (= R355)
- binding adenosine-5'-diphosphate: R173 (≠ S219), C174 (≠ L220), H220 (= H266), S222 (= S268), R301 (= R351)
8ufjB Glutamine synthetase (see paper)
28% identity, 98% coverage: 9:459/459 of query aligns to 6:444/444 of 8ufjB
P78061 Gamma-glutamylputrescine synthetase PuuA; Gamma-Glu-Put synthetase; Glutamate--putrescine ligase; EC 6.3.1.11 from Escherichia coli (strain K12) (see paper)
30% identity, 94% coverage: 24:453/459 of query aligns to 39:466/472 of P78061
- H282 (= H264) mutation to N: Activity is impaired to 9% of wild-type.
- R357 (= R341) mutation to Q: Activity is impaired to 3% of wild-type.
8tfkA Glutamine synthetase (see paper)
28% identity, 98% coverage: 9:459/459 of query aligns to 2:440/440 of 8tfkA
- binding adenosine-5'-diphosphate: E128 (= E145), D194 (≠ A217), F195 (≠ L218), F197 (≠ L220), N243 (≠ H266), R312 (= R336), R317 (= R341), G325 (≠ S349), R327 (= R351)
- binding magnesium ion: E128 (= E145), E128 (= E145), E130 (= E147), E185 (= E208), E192 (= E215), E192 (= E215), H241 (= H264), E329 (= E353)
- binding l-methionine-s-sulfoximine phosphate: E128 (= E145), E130 (= E147), E185 (= E208), E192 (= E215), G237 (= G260), H241 (= H264), R294 (= R318), E300 (≠ W324), R312 (= R336), R331 (= R355)
7tdpA Structure of paenibacillus polymyxa gs bound to met-sox-p-adp (transition state complex) to 1.98 angstom (see paper)
30% identity, 98% coverage: 9:458/459 of query aligns to 3:438/439 of 7tdpA
- binding adenosine-5'-diphosphate: N123 (≠ S142), G125 (= G143), E127 (= E145), E179 (= E203), D193 (≠ A217), Y196 (≠ L220), N242 (≠ H266), S244 (= S268), R316 (= R341), R326 (= R351)
- binding magnesium ion: E127 (= E145), E127 (= E145), E129 (= E147), E184 (= E208), E191 (= E215), E191 (= E215), H240 (= H264), E328 (= E353)
- binding l-methionine-s-sulfoximine phosphate: E127 (= E145), E129 (= E147), E184 (= E208), E191 (= E215), G236 (= G260), H240 (= H264), R293 (= R318), E299 (≠ W324), R311 (= R336), R330 (= R355)
7tfaB Glutamine synthetase (see paper)
29% identity, 98% coverage: 9:458/459 of query aligns to 3:440/441 of 7tfaB
- binding glutamine: E131 (= E147), Y153 (= Y163), E186 (= E208), G238 (= G260), H242 (= H264), R295 (= R318), E301 (≠ W324)
- binding magnesium ion: E129 (= E145), E131 (= E147), E186 (= E208), E193 (= E215), H242 (= H264), E330 (= E353)
- binding : Y58 (= Y85), R60 (= R91), V187 (≠ A209), N237 (≠ P259), G299 (= G322), Y300 (= Y323), R313 (= R336), M424 (≠ E442)
8oozA Glutamine synthetase (see paper)
28% identity, 97% coverage: 15:457/459 of query aligns to 8:428/430 of 8oozA
- binding adenosine-5'-triphosphate: G117 (= G143), E170 (= E203), F185 (≠ L218), K186 (≠ S219), Y187 (≠ L220), N233 (≠ H266), S235 (= S268), S315 (= S349), R317 (= R351)
- binding magnesium ion: E119 (= E145), H231 (= H264), E319 (= E353)
7tenA Glutamine synthetase (see paper)
32% identity, 73% coverage: 122:458/459 of query aligns to 106:441/442 of 7tenA
- binding adenosine-5'-diphosphate: G128 (= G143), E130 (= E145), E182 (= E203), D196 (≠ A217), F197 (≠ L218), K198 (≠ S219), Y199 (≠ L220), N245 (≠ H266), S247 (= S268), R319 (= R341), S327 (= S349), R329 (= R351)
- binding l-methionine-s-sulfoximine phosphate: E130 (= E145), E132 (= E147), E187 (= E208), E194 (= E215), N238 (≠ P259), G239 (= G260), H243 (= H264), R296 (= R318), E302 (≠ W324), R314 (= R336), R333 (= R355)
7tf9S L. Monocytogenes gs(14)-q-glnr peptide (see paper)
32% identity, 73% coverage: 122:458/459 of query aligns to 107:442/443 of 7tf9S
- binding glutamine: E133 (= E147), Y155 (= Y163), E188 (= E208), G240 (= G260), G242 (= G262), R297 (= R318), E303 (≠ W324)
- binding magnesium ion: E131 (= E145), E133 (= E147), E188 (= E208), E195 (= E215), H244 (= H264), E332 (= E353)
- binding : E418 (≠ S434), I422 (≠ W438), M426 (≠ E442)
Sites not aligning to the query:
8ooxB Glutamine synthetase (see paper)
28% identity, 97% coverage: 15:457/459 of query aligns to 8:436/438 of 8ooxB
8oooA Glutamine synthetase from methanothermococcus thermolithotrophicus in complex with 2-oxoglutarate and mgatp at 2.15 a resolution (see paper)
29% identity, 73% coverage: 122:458/459 of query aligns to 112:447/447 of 8oooA
- binding 2-oxoglutaric acid: P170 (≠ S173), R173 (≠ F188), R174 (≠ Q189), S190 (≠ L205)
- binding adenosine-5'-triphosphate: E136 (= E145), E188 (= E203), F203 (≠ L218), K204 (≠ S219), F205 (≠ L220), H251 (= H266), S253 (= S268), R325 (= R341), R335 (= R351)
Sites not aligning to the query:
8ooqB Glutamine synthetase from Methanothermococcus thermolithotrophicus (see paper)
29% identity, 73% coverage: 122:458/459 of query aligns to 111:446/446 of 8ooqB
Sites not aligning to the query:
5dm3A Crystal structure of glutamine synthetase from chromohalobacter salexigens dsm 3043(csal_0679, target efi-550015) with bound adp
32% identity, 73% coverage: 122:457/459 of query aligns to 84:374/374 of 5dm3A
- active site: E107 (= E145), E109 (= E147), E146 (≠ K211), E150 (= E215), H199 (= H264), R265 (= R336), E282 (= E353), R284 (= R355)
- binding adenosine-5'-diphosphate: I103 (≠ V141), E141 (= E203), R154 (≠ S219), C155 (≠ L220), H201 (= H266), S203 (= S268), R280 (= R351)
7tdvC Glutamine synthetase (see paper)
28% identity, 98% coverage: 9:457/459 of query aligns to 4:441/443 of 7tdvC
- binding adenosine-5'-diphosphate: G129 (= G143), E131 (= E145), E183 (= E203), D197 (≠ A217), F198 (≠ L218), K199 (≠ S219), Y200 (≠ L220), N246 (≠ H266), V247 (≠ L267), S248 (= S268), R320 (= R341), S328 (= S349), R330 (= R351)
- binding magnesium ion: E131 (= E145), E131 (= E145), E133 (= E147), E188 (= E208), E195 (= E215), E195 (= E215), H244 (= H264), E332 (= E353)
- binding l-methionine-s-sulfoximine phosphate: E131 (= E145), E133 (= E147), E188 (= E208), E195 (= E215), G240 (= G260), H244 (= H264), R297 (= R318), E303 (≠ W324), R315 (= R336)
7tf6A Glutamine synthetase (see paper)
28% identity, 98% coverage: 9:457/459 of query aligns to 3:436/438 of 7tf6A
- binding glutamine: E128 (= E147), E183 (= E208), G235 (= G260), H239 (= H264), R292 (= R318), E298 (≠ W324)
- binding magnesium ion: E126 (= E145), E128 (= E147), E183 (= E208), E190 (= E215), H239 (= H264), E327 (= E353)
- binding : F58 (≠ W63), R60 (≠ K75), G232 (≠ E257), N234 (≠ P259), G296 (= G322), Y297 (= Y323), R310 (= R336), Y367 (= Y393), Y421 (≠ E442), Q433 (≠ R454)
Sites not aligning to the query:
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)
29% identity, 97% coverage: 15:458/459 of query aligns to 10:446/446 of A0R083
- K363 (≠ H380) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
Query Sequence
>WP_011876163.1 NCBI__GCF_000016205.1:WP_011876163.1
MMQARDVKTAADARKIVEERGLTHVEVAVTDLDGVLRGKYLSRDKFFSALENSFGFCSVL
FGWDCNDELYDEACKIEYTGWHNGYRDDEVRVIPESCRELPHKNSLLFLAEAHSEHGARV
CPRNLLSRVLARADELGFSVVSGFEYEFYGFNETPQSAAEKGYRDLKLLTPTSCGYSVLR
AAVQSELFQDLLKIGQVMDFPIEGLHTEAGKGAMEAALSLDTGIGSADKAVLFKTFSKAV
AQQRDITLSFMAKYSMEMPGCGGHIHLSLKDKDGKPVFFDAAQAHQMSKTMRHFIAGQQL
LMPEFLAMVAPTVNAYSRLVPGYWAPTSATWGVDNRTCALRVVGGSPKSKRIEYRVTSAD
TNPYLVQAAVLASGLWGIEHELEPTPPSTGNAYVQKVSGELTLPRTLAEAAGRLRSSRAA
RDCFGDAFVDHFASTREWEDREYRRHVSDWELKRYFEII
Or try a new SitesBLAST search
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