SitesBLAST
Comparing WP_011023309.1 NCBI__GCF_000007345.1:WP_011023309.1 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)
3ng0A Crystal structure of glutamine synthetase from synechocystis sp. Pcc 6803
26% identity, 89% coverage: 25:475/506 of query aligns to 2:441/465 of 3ng0A
- active site: D51 (= D76), E130 (= E147), E132 (≠ Q149), E213 (= E210), E221 (= E225), H270 (= H274), R340 (= R342), E359 (= E382), R361 (= R384)
- binding phosphoaminophosphonic acid-adenylate ester: Y126 (≠ K143), E130 (= E147), K209 (≠ Y206), I224 (≠ F228), F226 (≠ T230), H272 (= H276), S274 (≠ K278), R340 (= R342), R345 (= R347), R357 (≠ T380)
- binding manganese (ii) ion: E130 (= E147), E132 (≠ Q149), E213 (= E210), E221 (= E225), H270 (= H274), E359 (= E382), R361 (= R384)
8ooxB Glutamine synthetase (see paper)
26% identity, 85% coverage: 26:453/506 of query aligns to 3:395/438 of 8ooxB
P77961 Glutamine synthetase; GS; Glutamate--ammonia ligase; Glutamine synthetase I beta; GSI beta; EC 6.3.1.2 from Synechocystis sp. (strain ATCC 27184 / PCC 6803 / Kazusa)
26% identity, 89% coverage: 25:475/506 of query aligns to 4:449/473 of P77961
- E134 (≠ Q149) binding Mg(2+)
- E215 (= E210) binding Mg(2+)
- E223 (= E225) binding Mg(2+)
- E361 (= E382) binding Mn(2+)
7tdpA Structure of paenibacillus polymyxa gs bound to met-sox-p-adp (transition state complex) to 1.98 angstom (see paper)
27% identity, 91% coverage: 24:483/506 of query aligns to 2:419/439 of 7tdpA
- binding adenosine-5'-diphosphate: N123 (≠ A150), G125 (= G152), E127 (= E153), E179 (≠ K205), D193 (≠ E227), Y196 (≠ T230), N242 (≠ H276), S244 (≠ K278), R316 (= R347), R326 (≠ T380)
- binding magnesium ion: E127 (= E153), E127 (= E153), E129 (= E155), E184 (= E210), E191 (= E225), E191 (= E225), H240 (= H274), E328 (= E382)
- binding l-methionine-s-sulfoximine phosphate: E127 (= E153), E129 (= E155), E184 (= E210), E191 (= E225), G236 (= G270), H240 (= H274), R293 (= R324), E299 (= E330), R311 (= R342), R330 (= R384)
7tfaB Glutamine synthetase (see paper)
27% identity, 91% coverage: 24:483/506 of query aligns to 2:421/441 of 7tfaB
- binding glutamine: E131 (= E155), Y153 (= Y177), E186 (= E210), G238 (= G270), H242 (= H274), R295 (= R324), E301 (= E330)
- binding magnesium ion: E129 (= E153), E131 (= E155), E186 (= E210), E193 (= E225), H242 (= H274), E330 (= E382)
- binding : Y58 (= Y83), R60 (≠ E85), V187 (= V211), N237 (≠ A269), G299 (≠ H328), Y300 (≠ Q329), R313 (= R342)
Sites not aligning to the query:
A0R079 Glutamine synthetase; GS; Glutamate--ammonia ligase; Glutamine synthetase I beta; GSI beta; EC 6.3.1.2 from Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis) (see paper)
27% identity, 90% coverage: 22:475/506 of query aligns to 2:454/478 of A0R079
- K14 (= K34) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
8oozA Glutamine synthetase (see paper)
26% identity, 85% coverage: 26:453/506 of query aligns to 3:387/430 of 8oozA
- binding adenosine-5'-triphosphate: G117 (≠ M151), E170 (≠ K205), F185 (= F228), K186 (≠ E229), Y187 (≠ T230), N233 (≠ H276), S235 (≠ K278), S315 (≠ K378), R317 (≠ T380)
- binding magnesium ion: E119 (= E153), H231 (= H274), E319 (= E382)
8oooA Glutamine synthetase from methanothermococcus thermolithotrophicus in complex with 2-oxoglutarate and mgatp at 2.15 a resolution (see paper)
26% identity, 83% coverage: 25:443/506 of query aligns to 2:395/447 of 8oooA
- binding 2-oxoglutaric acid: F17 (≠ M40), R19 (≠ N42), A33 (≠ T56), R87 (≠ E106), V93 (≠ T110), P170 (≠ D187), R173 (= R190), R174 (≠ K191), S190 (≠ G207)
- binding adenosine-5'-triphosphate: E136 (= E153), E188 (≠ K205), F203 (= F228), K204 (≠ E229), F205 (≠ T230), H251 (= H276), S253 (≠ K278), R325 (= R347), R335 (≠ T380)
8ooqB Glutamine synthetase from Methanothermococcus thermolithotrophicus (see paper)
26% identity, 83% coverage: 25:443/506 of query aligns to 1:394/446 of 8ooqB
- binding 2-oxoglutaric acid: F16 (≠ M40), R18 (≠ N42), A32 (≠ T56), R86 (≠ E106), V92 (≠ T110), P169 (≠ D187), R172 (= R190), R173 (≠ K191), S189 (≠ G207)
- binding magnesium ion: E137 (= E155), E192 (= E210), E199 (= E225)
P9WN39 Glutamine synthetase; GS; Glutamate--ammonia ligase; Glutamine synthetase I beta; GSI beta; EC 6.3.1.2 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 5 papers)
26% identity, 90% coverage: 22:475/506 of query aligns to 2:454/478 of P9WN39
- E133 (= E153) binding Mg(2+)
- E135 (= E155) binding Mg(2+)
- E219 (= E210) binding Mg(2+)
- E227 (= E225) binding Mg(2+)
- H276 (= H274) binding Mg(2+)
- E366 (= E382) binding Mg(2+)
- Y406 (= Y420) modified: O-AMP-tyrosine; mutation to F: Unable to be adenylylated.
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
1htoA Crystallographic structure of a relaxed glutamine synthetase from mycobacterium tuberculosis (see paper)
26% identity, 90% coverage: 22:475/506 of query aligns to 1:453/477 of 1htoA
- active site: D53 (= D76), E132 (= E153), E134 (= E155), E218 (= E210), E226 (= E225), H275 (= H274), R346 (= R342), E365 (= E382), R367 (= R384)
- binding adenosine monophosphate: Y128 (≠ A150), G130 (= G152), E132 (= E153), F231 (≠ T230), H277 (= H276), S279 (≠ K278), R363 (≠ T380)
- binding manganese (ii) ion: E132 (= E153), H275 (= H274), E365 (= E382)
2whiA Crystal structure of mycobacterium tuberculosis glutamine synthetase in complex with a purine analogue inhibitor and l-methionine-s- sulfoximine phosphate. (see paper)
26% identity, 90% coverage: 23:475/506 of query aligns to 1:452/476 of 2whiA
- active site: D52 (= D76), E131 (= E153), E133 (= E155), E217 (= E210), E225 (= E225), H274 (= H274), R345 (= R342), E364 (= E382), R366 (= R384)
- binding 1-(3,4-dichlorobenzyl)-3,7-dimethyl-8-morpholin-4-yl-3,7-dihydro-1H-purine-2,6-dione: Y127 (≠ A150), G129 (= G152), F230 (≠ T230), H276 (= H276), S278 (≠ K278), W280 (≠ L280), K359 (≠ N367), R362 (≠ T380)
- binding magnesium ion: E131 (= E153), E131 (= E153), E133 (= E155), E217 (= E210), E225 (= E225), E225 (= E225), H274 (= H274), E364 (= E382)
- binding l-methionine-s-sulfoximine phosphate: E131 (= E153), E133 (= E155), E217 (= E210), E225 (= E225), G270 (= G270), H274 (= H274), R327 (= R324), E333 (= E330), R345 (= R342), R366 (= R384)
- binding phosphate ion: E131 (= E153), R350 (= R347), E364 (= E382)
4acfA Crystal structure of mycobacterium tuberculosis glutamine synthetase in complex with imidazopyridine inhibitor ((4-(6-bromo-3- (butylamino)imidazo(1,2-a)pyridin-2-yl)phenoxy) acetic acid) and l- methionine-s-sulfoximine phosphate.
26% identity, 89% coverage: 25:475/506 of query aligns to 2:451/475 of 4acfA
- active site: D51 (= D76), E130 (= E153), E132 (= E155), E216 (= E210), E224 (= E225), H273 (= H274), R344 (= R342), E363 (= E382), R365 (= R384)
- binding {4-[6-bromo-3-(butylamino)imidazo[1,2-a]pyridin-2-yl]phenoxy}acetic acid: Y126 (≠ A150), F229 (≠ T230), H275 (= H276), Q276 (≠ M277), W279 (≠ L280), N356 (= N365), K358 (≠ N367), R361 (≠ T380)
- binding magnesium ion: E130 (= E153), E130 (= E153), E132 (= E155), E216 (= E210), E224 (= E225), E224 (= E225), H273 (= H274), E363 (= E382)
- binding l-methionine-s-sulfoximine phosphate: E130 (= E153), E132 (= E155), E216 (= E210), E224 (= E225), G269 (= G270), H273 (= H274), R326 (= R324), E332 (= E330), R344 (= R342), R365 (= R384)
3zxvA Crystal structure of mycobacterium tuberculosis glutamine synthetase in complex with tri-substituted imidazole inhibitor (4-(2-tert-butyl- 4-(6-methoxynaphthalen-2-yl)-1h-imidazol-5-yl)pyridin-2-amine) and l- methionine-s-sulfoximine phosphate (see paper)
26% identity, 89% coverage: 25:475/506 of query aligns to 2:451/475 of 3zxvA
- active site: D51 (= D76), E130 (= E153), E132 (= E155), E216 (= E210), E224 (= E225), H273 (= H274), R344 (= R342), E363 (= E382), R365 (= R384)
- binding magnesium ion: E130 (= E153), E130 (= E153), E132 (= E155), E216 (= E210), E224 (= E225), E224 (= E225), H273 (= H274), E363 (= E382)
- binding 4-(2-tert-butyl-4-(6-methoxynaphthalen-2-yl)-3h-imidazol-4-yl)pyridin-2-amine: Y126 (≠ A150), G128 (= G152), F229 (≠ T230), H275 (= H276), S277 (≠ K278), K358 (≠ N367), R361 (≠ T380)
- binding l-methionine-s-sulfoximine phosphate: E130 (= E153), E132 (= E155), E216 (= E210), E224 (= E225), G269 (= G270), H273 (= H274), R326 (= R324), E332 (= E330), R344 (= R342), R365 (= R384)
3zxrA Crystal structure of mycobacterium tuberculosis glutamine synthetase in complex with tri-substituted imidazole inhibitor (3-(2-tert-butyl- 5-(pyridin-4-yl)-1h-imidazol-4-yl)quinoline) and l-methionine-s- sulfoximine phosphate. (see paper)
26% identity, 89% coverage: 25:475/506 of query aligns to 2:451/475 of 3zxrA
- active site: D51 (= D76), E130 (= E153), E132 (= E155), E216 (= E210), E224 (= E225), H273 (= H274), R344 (= R342), E363 (= E382), R365 (= R384)
- binding 3-(2-tert-butyl-5-(pyridin-4-yl)-1h-imidazol-4-yl)quinoline: G128 (= G152), F229 (≠ T230), H275 (= H276), S277 (≠ K278), R361 (≠ T380)
- binding magnesium ion: E130 (= E153), E130 (= E153), E132 (= E155), E216 (= E210), E224 (= E225), E224 (= E225), H273 (= H274), E363 (= E382)
- binding l-methionine-s-sulfoximine phosphate: E130 (= E153), E132 (= E155), E216 (= E210), E224 (= E225), H273 (= H274), R326 (= R324), E332 (= E330), R344 (= R342), R365 (= R384)
2bvcA Crystal structure of mycobacterium tuberculosis glutamine synthetase in complex with a transition state mimic (see paper)
26% identity, 89% coverage: 25:475/506 of query aligns to 2:451/475 of 2bvcA
- active site: D51 (= D76), E130 (= E153), E132 (= E155), E216 (= E210), E224 (= E225), H273 (= H274), R344 (= R342), E363 (= E382), R365 (= R384)
- binding adenosine-5'-diphosphate: E130 (= E153), E211 (≠ K205), K212 (≠ Y206), N226 (≠ E227), F229 (≠ T230), H275 (= H276), S277 (≠ K278), R344 (= R342), R349 (= R347), R361 (≠ T380), E363 (= E382)
- binding magnesium ion: E130 (= E153), E130 (= E153), E132 (= E155), E216 (= E210), E224 (= E225), E224 (= E225), H273 (= H274), E363 (= E382)
- binding l-methionine-s-sulfoximine phosphate: E130 (= E153), E132 (= E155), E216 (= E210), E224 (= E225), G269 (= G270), H273 (= H274), R326 (= R324), E332 (= E330), R344 (= R342), R365 (= R384)
8tfbA Glutamine synthetase (see paper)
27% identity, 85% coverage: 25:455/506 of query aligns to 5:402/443 of 8tfbA
8s59O Glutamine synthetase
27% identity, 85% coverage: 25:455/506 of query aligns to 8:405/446 of 8s59O
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)
26% identity, 86% coverage: 22:455/506 of query aligns to 2:400/444 of P12425
- G59 (≠ S82) 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 (≠ E85) 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 (= E153) binding Mg(2+)
- E134 (= E155) binding Mg(2+)
- E189 (= E210) binding Mg(2+)
- V190 (= V211) 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 (= E225) binding Mg(2+)
- G241 (= G270) binding L-glutamate
- H245 (= H274) binding Mg(2+)
- G302 (≠ H328) 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 (= E330) 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 (= P332) 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 (= E382) binding Mg(2+)
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 424 E→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.
8tfkA Glutamine synthetase (see paper)
27% identity, 85% coverage: 25:455/506 of query aligns to 2:399/440 of 8tfkA
- binding adenosine-5'-diphosphate: E128 (= E153), D194 (≠ E227), F195 (= F228), F197 (≠ T230), N243 (≠ H276), R312 (= R342), R317 (= R347), G325 (≠ K378), R327 (≠ T380)
- binding magnesium ion: E128 (= E153), E128 (= E153), E130 (= E155), E185 (= E210), E192 (= E225), E192 (= E225), H241 (= H274), E329 (= E382)
- binding l-methionine-s-sulfoximine phosphate: E128 (= E153), E130 (= E155), E185 (= E210), E192 (= E225), G237 (= G270), H241 (= H274), R294 (= R324), E300 (= E330), R312 (= R342), R331 (= R384)
Query Sequence
>WP_011023309.1 NCBI__GCF_000007345.1:WP_011023309.1
MKTSNVELNPNKLVQYLNKPASEFTKDDIIRFIKENGIKMLNFRYVGGDGRLKALTFVIR
DEEHLDNLLSAGERVDGSSLFSYIEADTSDLYVLPKYRTAFVNPFEEIPTVDILCSYFDK
DGTPLISASETIMKKASQVLTEKTGYELQAMGELEYYIIANSGEVNMGFPAVDQRGYHES
NPFTKYDQLRKEAMMYIAEAGGKIKYGHSEVGNFTDNNYYYEQNEIEFETDTLENSADRL
LIAKWMLRMLADQYGVVISFAPKITVGKAGSGLHVHMKLLKDGKSIMVENGDISDAAKRA
MAGLLDVAAGITAFGNRVPTSYLRLVPHQEAPTNICWGDRNRSALIRVPLGWFSDDCSKM
IAHVNPNYCEDFKSHSYKSTFEFRAADPSADLYLLFAAFAVGIRHGFEMDNALEIAKNLY
IDVNIFKDEHKDRLAQLEHLPASCYESAQALKKYKDIFTQYDVFTEGMIDDTVKYLESLD
DYQLSERLYGKNEEIKKLVDSYIHIA
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