SitesBLAST
Comparing WP_041950361.1 NCBI__GCF_000015565.1:WP_041950361.1 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)
8tfbA Glutamine synthetase (see paper)
29% identity, 98% coverage: 9:453/453 of query aligns to 9:443/443 of 8tfbA
8s59O Glutamine synthetase
29% identity, 98% coverage: 9:453/453 of query aligns to 12:446/446 of 8s59O
8tfkA Glutamine synthetase (see paper)
29% identity, 98% coverage: 9:453/453 of query aligns to 6:440/440 of 8tfkA
- binding adenosine-5'-diphosphate: E128 (= E141), D194 (≠ A213), F195 (≠ I214), F197 (= F216), N243 (≠ H262), R312 (= R331), R317 (= R336), G325 (≠ A344), R327 (= R346)
- binding magnesium ion: E128 (= E141), E128 (= E141), E130 (= E143), E185 (= E204), E192 (= E211), E192 (= E211), H241 (= H260), E329 (= E348)
- binding l-methionine-s-sulfoximine phosphate: E128 (= E141), E130 (= E143), E185 (= E204), E192 (= E211), G237 (= G256), H241 (= H260), R294 (= R313), E300 (≠ W319), R312 (= R331), R331 (= R350)
5dm3C Crystal structure of glutamine synthetase from chromohalobacter salexigens dsm 3043(csal_0679, target efi-550015) with bound adp
31% identity, 97% coverage: 14:451/453 of query aligns to 9:396/396 of 5dm3C
- active site: E115 (= E141), E117 (= E143), E162 (= E204), E169 (= E211), H218 (= H260), R286 (= R331), E303 (= E348), R305 (= R350)
- binding adenosine-5'-diphosphate: R173 (≠ S215), C174 (≠ F216), H220 (= H262), S222 (= S264), R301 (= R346)
7tdpA Structure of paenibacillus polymyxa gs bound to met-sox-p-adp (transition state complex) to 1.98 angstom (see paper)
33% identity, 79% coverage: 94:452/453 of query aligns to 79:438/439 of 7tdpA
- binding adenosine-5'-diphosphate: N123 (vs. gap), G125 (= G139), E127 (= E141), E179 (= E199), D193 (≠ A213), Y196 (≠ F216), N242 (≠ H262), S244 (= S264), R316 (= R336), R326 (= R346)
- binding magnesium ion: E127 (= E141), E127 (= E141), E129 (= E143), E184 (= E204), E191 (= E211), E191 (= E211), H240 (= H260), E328 (= E348)
- binding l-methionine-s-sulfoximine phosphate: E127 (= E141), E129 (= E143), E184 (= E204), E191 (= E211), G236 (= G256), H240 (= H260), R293 (= R313), E299 (≠ W319), R311 (= R331), R330 (= R350)
7tfaB Glutamine synthetase (see paper)
33% identity, 79% coverage: 94:452/453 of query aligns to 79:440/441 of 7tfaB
- binding glutamine: E131 (= E143), Y153 (≠ M169), E186 (= E204), G238 (= G256), H242 (= H260), R295 (= R313), E301 (≠ W319)
- binding magnesium ion: E129 (= E141), E131 (= E143), E186 (= E204), E193 (= E211), H242 (= H260), E330 (= E348)
- binding : V187 (≠ T205), N237 (≠ P255), G299 (= G317), Y300 (≠ F318), R313 (= R331), M424 (≠ Q436)
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, 95% coverage: 21:452/453 of query aligns to 20:446/446 of A0R083
- K363 (≠ Q375) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
5dm3A Crystal structure of glutamine synthetase from chromohalobacter salexigens dsm 3043(csal_0679, target efi-550015) with bound adp
30% identity, 97% coverage: 14:451/453 of query aligns to 11:374/374 of 5dm3A
- active site: E107 (= E141), E109 (= E143), E146 (≠ P207), E150 (= E211), H199 (= H260), R265 (= R331), E282 (= E348), R284 (= R350)
- binding adenosine-5'-diphosphate: I103 (≠ L137), E141 (= E199), R154 (≠ S215), C155 (≠ F216), H201 (= H262), S203 (= S264), R280 (= R346)
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)
29% identity, 95% coverage: 21:452/453 of query aligns to 20:446/446 of P9WN37
- K363 (≠ Q375) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
8oozA Glutamine synthetase (see paper)
30% identity, 82% coverage: 80:451/453 of query aligns to 58:428/430 of 8oozA
- binding adenosine-5'-triphosphate: G117 (= G139), E170 (= E199), F185 (≠ I214), K186 (≠ S215), Y187 (≠ F216), N233 (≠ H262), S235 (= S264), S315 (≠ A344), R317 (= R346)
- binding magnesium ion: E119 (= E141), H231 (= H260), E319 (= E348)
8ooxB Glutamine synthetase (see paper)
30% identity, 82% coverage: 80:451/453 of query aligns to 64:436/438 of 8ooxB
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)
30% identity, 82% coverage: 80:450/453 of query aligns to 67:441/444 of P12425
- E132 (= E141) binding Mg(2+)
- E134 (= E143) binding Mg(2+)
- E189 (= E204) binding Mg(2+)
- V190 (≠ T205) 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 (= E211) binding Mg(2+)
- G241 (= G256) binding L-glutamate
- H245 (= H260) binding Mg(2+)
- G302 (= G317) 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 (≠ W319) 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 (= P321) 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 (= E348) binding Mg(2+)
- E424 (= E433) 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
- 59 G→R: Unable to form stable complex with TnrA. In the presence of glutamine, this mutant derepresses amtB-lacZ fusion and glnRA-lacZ fusion.
- 62 Important for inhibition by glutamine; R→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.
4s0rD Structure of gs-tnra complex (see paper)
30% identity, 82% coverage: 80:450/453 of query aligns to 70:444/447 of 4s0rD
- active site: E135 (= E141), E137 (= E143), E192 (= E204), E199 (= E211), H248 (= H260), R319 (= R331), E336 (= E348), R338 (= R350)
- binding glutamine: E137 (= E143), E192 (= E204), R301 (= R313), E307 (≠ W319)
- binding magnesium ion: E135 (= E141), E135 (= E141), E199 (= E211), H248 (= H260), H248 (= H260), E336 (= E348), H419 (= H425)
- binding : D161 (≠ N185), G241 (≠ A253), V242 (≠ L254), N243 (≠ P255), G305 (= G317), Y306 (≠ F318), Y376 (vs. gap), I426 (≠ W432), M430 (≠ Q436)
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)
30% identity, 82% coverage: 80:450/453 of query aligns to 66:440/443 of 4lnkA
- active site: E131 (= E141), E133 (= E143), E188 (= E204), E195 (= E211), H244 (= H260), R315 (= R331), E332 (= E348), R334 (= R350)
- binding adenosine-5'-diphosphate: F198 (≠ I214), Y200 (≠ F216), N246 (≠ H262), S248 (= S264), S324 (≠ G340), S328 (≠ A344), R330 (= R346)
- binding glutamic acid: E133 (= E143), E188 (= E204), V189 (≠ T205), N239 (≠ P255), G240 (= G256), G242 (≠ S258), E303 (≠ W319)
- binding magnesium ion: E131 (= E141), E188 (= E204), E195 (= E211), H244 (= H260), E332 (= E348)
Sites not aligning to the query:
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)
30% identity, 82% coverage: 80:450/453 of query aligns to 66:440/443 of 4lniA
- active site: E131 (= E141), E133 (= E143), E188 (= E204), E195 (= E211), H244 (= H260), R315 (= R331), E332 (= E348), R334 (= R350)
- binding adenosine-5'-diphosphate: E131 (= E141), E183 (= E199), D197 (≠ A213), Y200 (≠ F216), N246 (≠ H262), S248 (= S264), R320 (= R336), R330 (= R346)
- binding magnesium ion: E131 (= E141), E131 (= E141), E133 (= E143), E188 (= E204), E195 (= E211), E195 (= E211), H244 (= H260), E332 (= E348)
- binding l-methionine-s-sulfoximine phosphate: E133 (= E143), E188 (= E204), H244 (= H260), R297 (= R313), E303 (≠ W319), R315 (= R331), R334 (= R350)
Sites not aligning to the query:
8ooqB Glutamine synthetase from Methanothermococcus thermolithotrophicus (see paper)
31% identity, 82% coverage: 80:452/453 of query aligns to 70:446/446 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)
31% identity, 82% coverage: 80:452/453 of query aligns to 71:447/447 of 8oooA
- binding 2-oxoglutaric acid: R87 (vs. gap), V93 (= V99), P170 (= P181), R173 (≠ F184), R174 (≠ N185), S190 (≠ L201)
- binding adenosine-5'-triphosphate: E136 (= E141), E188 (= E199), F203 (≠ I214), K204 (≠ S215), F205 (= F216), H251 (= H262), S253 (= S264), R325 (= R336), R335 (= R346)
Sites not aligning to the query:
7tf9S L. Monocytogenes gs(14)-q-glnr peptide (see paper)
29% identity, 97% coverage: 13:452/453 of query aligns to 12:442/443 of 7tf9S
- binding glutamine: E133 (= E143), Y155 (≠ P162), E188 (= E204), G240 (= G256), G242 (≠ S258), R297 (= R313), E303 (≠ W319)
- binding magnesium ion: E131 (= E141), E133 (= E143), E188 (= E204), E195 (= E211), H244 (= H260), E332 (= E348)
- binding : F59 (≠ W74), V60 (vs. gap), E418 (≠ A428), I422 (≠ W432), M426 (≠ Q436)
7tenA Glutamine synthetase (see paper)
29% identity, 97% coverage: 13:452/453 of query aligns to 11:441/442 of 7tenA
- binding adenosine-5'-diphosphate: G128 (= G139), E130 (= E141), E182 (= E199), D196 (≠ A213), F197 (≠ I214), K198 (≠ S215), Y199 (≠ F216), N245 (≠ H262), S247 (= S264), R319 (= R336), S327 (≠ A344), R329 (= R346)
- binding l-methionine-s-sulfoximine phosphate: E130 (= E141), E132 (= E143), E187 (= E204), E194 (= E211), N238 (≠ P255), G239 (= G256), H243 (= H260), R296 (= R313), E302 (≠ W319), R314 (= R331), R333 (= R350)
8wwvA Glutamine synthetase (see paper)
28% identity, 98% coverage: 10:453/453 of query aligns to 20:490/490 of 8wwvA
- binding adenosine-5'-diphosphate: G155 (= G139), E157 (= E141), R224 (≠ E199), F239 (≠ I214), D240 (≠ S215), V241 (≠ F216), H288 (= H262), S290 (= S264), R374 (= R346), E376 (= E348)
- binding magnesium ion: E157 (= E141), E236 (= E211)
- binding manganese (ii) ion: E157 (= E141), E159 (= E143), E229 (= E204), E236 (= E211), H286 (= H260), E376 (= E348)
- binding l-methionine-s-sulfoximine phosphate: E157 (= E141), E159 (= E143), E229 (= E204), E236 (= E211), A282 (vs. gap), H286 (= H260), R340 (= R313), K358 (≠ R331)
Query Sequence
>WP_041950361.1 NCBI__GCF_000015565.1:WP_041950361.1
MAHPPLHPAVAAALESGSTKVKVAVSDVDGILRGKYLHRDKFKSAAESGFSFCDVVLGWD
AHDHCYDNTRLTGWQHGYPDALVRIDPGTARQVPWDRQVPFFLGEFVNPDGSPHALCPRQ
TLKRVLKRAEKLGFTVLAGMEFEWFNFKESAQSWAAKQGVGPEPITPGMFGYSLLRMADN
PGFFNALMDEMAAFDVPIEGLHTETGPGVYEAAISFSEALAQADRAILFKTGAREIGKRF
GIMPSFMAKWNQALPGCSGHIHQSLSDGQRNLFFDASSERKMSPLFESYLAGQIGFLMEF
APLFWPTINSYKRLVDGFWAPVKPSWGMDNRTASFRVIAGSPKATRLETRCPGADINPYL
ALAAVIAAGLHGVEQGLKLSAPPITGTNQGAENVARAPRTLIETTRVLQHSRVAHDWLGD
AFVEHFAATREWEWRQWLDGVTDWELKRYLEIV
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