SitesBLAST
Comparing WP_012042168.1 NCBI__GCF_000015165.1:WP_012042168.1 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)
7cqwA Gmas/adp complex-conformation 1 (see paper)
65% identity, 100% coverage: 3:432/432 of query aligns to 2:430/430 of 7cqwA
7cquA Gmas/adp/metsox-p complex (see paper)
65% identity, 100% coverage: 3:432/432 of query aligns to 1:429/429 of 7cquA
- binding adenosine-5'-diphosphate: E121 (= E123), Y173 (= Y175), N187 (= N189), W188 (= W190), D189 (≠ E191), Y190 (≠ F192), H236 (= H238), L237 (≠ V239), S238 (= S240), R316 (= R318), R322 (= R324)
- binding magnesium ion: E121 (= E123), E121 (= E123), E123 (= E125), E178 (= E180), E185 (= E187), E185 (= E187), H234 (= H236), E324 (= E326)
- binding l-methionine-s-sulfoximine phosphate: E121 (= E123), E123 (= E125), E178 (= E180), E185 (= E187), T229 (= T231), G230 (= G232), H234 (= H236), R287 (= R289), W299 (= W301), R311 (= R313), R326 (= R328)
7cqqA Gmas in complex with amppnp and metsox (see paper)
65% identity, 100% coverage: 3:432/432 of query aligns to 1:429/429 of 7cqqA
- binding phosphoaminophosphonic acid-adenylate ester: E121 (= E123), Y173 (= Y175), E185 (= E187), N187 (= N189), D189 (≠ E191), Y190 (≠ F192), H234 (= H236), H236 (= H238), S238 (= S240), R311 (= R313), R316 (= R318), R322 (= R324), E324 (= E326)
- binding magnesium ion: E121 (= E123), E121 (= E123), E123 (= E125), E178 (= E180), E185 (= E187), E185 (= E187), H234 (= H236), E324 (= E326)
- binding (2s)-2-amino-4-(methylsulfonimidoyl)butanoic acid: E123 (= E125), E178 (= E180), T229 (= T231), H234 (= H236), R287 (= R289), W299 (= W301), R311 (= R313), R326 (= R328)
7cqnA Gmas in complex with amppcp (see paper)
65% identity, 100% coverage: 3:432/432 of query aligns to 1:429/429 of 7cqnA
- binding phosphomethylphosphonic acid adenylate ester: G45 (= G47), D61 (= D63), E121 (= E123), Y173 (= Y175), Q174 (= Q176), W188 (= W190), D189 (≠ E191), Y190 (≠ F192), H236 (= H238), S238 (= S240), R311 (= R313), R316 (= R318), R322 (= R324)
7tdpA Structure of paenibacillus polymyxa gs bound to met-sox-p-adp (transition state complex) to 1.98 angstom (see paper)
34% identity, 98% coverage: 8:430/432 of query aligns to 10:436/439 of 7tdpA
- binding adenosine-5'-diphosphate: N123 (≠ K119), G125 (= G121), E127 (= E123), E179 (≠ Y175), D193 (≠ N189), Y196 (≠ F192), N242 (≠ H238), S244 (= S240), R316 (= R318), R326 (= R324)
- binding magnesium ion: E127 (= E123), E127 (= E123), E129 (= E125), E184 (= E180), E191 (= E187), E191 (= E187), H240 (= H236), E328 (= E326)
- binding l-methionine-s-sulfoximine phosphate: E127 (= E123), E129 (= E125), E184 (= E180), E191 (= E187), G236 (= G232), H240 (= H236), R293 (= R289), E299 (≠ T295), R311 (= R313), R330 (= R328)
8oozA Glutamine synthetase (see paper)
31% identity, 98% coverage: 8:430/432 of query aligns to 9:427/430 of 8oozA
- binding adenosine-5'-triphosphate: G117 (= G121), E170 (≠ Y175), F185 (≠ W190), K186 (≠ E191), Y187 (≠ F192), N233 (≠ H238), S235 (= S240), S315 (≠ A322), R317 (= R324)
- binding magnesium ion: E119 (= E123), H231 (= H236), E319 (= E326)
8ooxB Glutamine synthetase (see paper)
31% identity, 99% coverage: 4:430/432 of query aligns to 5:435/438 of 8ooxB
7tfaB Glutamine synthetase (see paper)
34% identity, 98% coverage: 8:430/432 of query aligns to 10:438/441 of 7tfaB
- binding glutamine: E131 (= E125), Y153 (≠ C147), E186 (= E180), G238 (= G232), H242 (= H236), R295 (= R289), E301 (≠ T295)
- binding magnesium ion: E129 (= E123), E131 (= E125), E186 (= E180), E193 (= E187), H242 (= H236), E330 (= E326)
- binding : Y58 (≠ D56), R60 (≠ T58), V187 (≠ D181), N237 (≠ T231), G299 (≠ A293), Y300 (≠ R294), R313 (= R313), M424 (≠ A416)
8tfkA Glutamine synthetase (see paper)
33% identity, 96% coverage: 11:425/432 of query aligns to 12:432/440 of 8tfkA
- binding adenosine-5'-diphosphate: E128 (= E123), D194 (≠ N189), F195 (≠ W190), F197 (= F192), N243 (≠ H238), R312 (= R313), R317 (= R318), G325 (≠ A322), R327 (= R324)
- binding magnesium ion: E128 (= E123), E128 (= E123), E130 (= E125), E185 (= E180), E192 (= E187), E192 (= E187), H241 (= H236), E329 (= E326)
- binding l-methionine-s-sulfoximine phosphate: E128 (= E123), E130 (= E125), E185 (= E180), E192 (= E187), G237 (= G232), H241 (= H236), R294 (= R289), E300 (≠ T295), R312 (= R313), R331 (= R328)
8ufjB Glutamine synthetase (see paper)
32% identity, 96% coverage: 11:425/432 of query aligns to 16:436/444 of 8ufjB
8oooA Glutamine synthetase from methanothermococcus thermolithotrophicus in complex with 2-oxoglutarate and mgatp at 2.15 a resolution (see paper)
32% identity, 97% coverage: 14:430/432 of query aligns to 15:445/447 of 8oooA
- binding 2-oxoglutaric acid: F17 (≠ Y16), R19 (≠ L18), A33 (≠ L32), R87 (≠ K79), V93 (= V82), P170 (≠ Y157), R173 (≠ I160), R174 (≠ A161), S190 (≠ N177)
- binding adenosine-5'-triphosphate: E136 (= E123), E188 (≠ Y175), F203 (≠ W190), K204 (≠ E191), F205 (= F192), H251 (= H238), S253 (= S240), R325 (= R318), R335 (= R324)
8ooqB Glutamine synthetase from Methanothermococcus thermolithotrophicus (see paper)
32% identity, 97% coverage: 14:430/432 of query aligns to 14:444/446 of 8ooqB
- binding 2-oxoglutaric acid: F16 (≠ Y16), R18 (≠ L18), A32 (≠ L32), R86 (≠ K79), V92 (= V82), P169 (≠ Y157), R172 (≠ I160), R173 (≠ A161), S189 (≠ N177)
- binding magnesium ion: E137 (= E125), E192 (= E180), E199 (= E187)
4s0rD Structure of gs-tnra complex (see paper)
31% identity, 99% coverage: 5:430/432 of query aligns to 12:444/447 of 4s0rD
- active site: D56 (≠ A49), E135 (= E123), E137 (= E125), E192 (= E180), E199 (= E187), H248 (= H236), R319 (= R313), E336 (= E326), R338 (= R328)
- binding glutamine: E137 (= E125), E192 (= E180), R301 (= R289), E307 (≠ T295)
- binding magnesium ion: I66 (≠ P59), E135 (= E123), E135 (= E123), E199 (= E187), H248 (= H236), H248 (= H236), E336 (= E326), H419 (≠ C405)
- binding : F63 (≠ D56), V64 (≠ M57), R65 (≠ T58), I66 (≠ P59), D161 (= D149), G241 (≠ D229), V242 (≠ L230), N243 (≠ T231), G305 (≠ A293), Y306 (≠ R294), Y376 (= Y366), I426 (≠ E412), M430 (≠ A416)
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, 99% coverage: 5:430/432 of query aligns to 8:440/443 of 4lnkA
- active site: D52 (≠ A49), E131 (= E123), E133 (= E125), E188 (= E180), E195 (= E187), H244 (= H236), R315 (= R313), E332 (= E326), R334 (= R328)
- binding adenosine-5'-diphosphate: K43 (≠ G40), M50 (≠ G47), F198 (≠ W190), Y200 (≠ F192), N246 (≠ H238), S248 (= S240), S324 (vs. gap), S328 (≠ A322), R330 (= R324)
- binding glutamic acid: E133 (= E125), E188 (= E180), V189 (≠ D181), N239 (≠ T231), G240 (= G232), G242 (= G234), E303 (≠ T295)
- binding magnesium ion: E131 (= E123), E188 (= E180), E195 (= E187), H244 (= H236), E332 (= E326)
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, 99% coverage: 5:430/432 of query aligns to 8:440/443 of 4lniA
- active site: D52 (≠ A49), E131 (= E123), E133 (= E125), E188 (= E180), E195 (= E187), H244 (= H236), R315 (= R313), E332 (= E326), R334 (= R328)
- binding adenosine-5'-diphosphate: E131 (= E123), E183 (≠ Y175), D197 (≠ N189), Y200 (≠ F192), N246 (≠ H238), S248 (= S240), R320 (= R318), R330 (= R324)
- binding magnesium ion: E131 (= E123), E131 (= E123), E133 (= E125), E188 (= E180), E195 (= E187), E195 (= E187), H244 (= H236), E332 (= E326)
- binding l-methionine-s-sulfoximine phosphate: E133 (= E125), E188 (= E180), H244 (= H236), R297 (= R289), E303 (≠ T295), R315 (= R313), R334 (= R328)
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, 99% coverage: 5:430/432 of query aligns to 9:441/444 of P12425
- G59 (≠ L55) 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 (≠ T58) 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 (= E123) binding Mg(2+)
- E134 (= E125) binding Mg(2+)
- E189 (= E180) binding Mg(2+)
- V190 (≠ D181) 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 (= E187) binding Mg(2+)
- G241 (= G232) binding L-glutamate
- H245 (= H236) binding Mg(2+)
- G302 (≠ A293) 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 (≠ T295) 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 (= P303) 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 (= E326) binding Mg(2+)
- E424 (= E413) 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
7tf6A Glutamine synthetase (see paper)
31% identity, 99% coverage: 5:430/432 of query aligns to 7:435/438 of 7tf6A
- binding glutamine: E128 (= E125), E183 (= E180), G235 (= G232), H239 (= H236), R292 (= R289), E298 (≠ T295)
- binding magnesium ion: E126 (= E123), E128 (= E125), E183 (= E180), E190 (= E187), H239 (= H236), E327 (= E326)
- binding : F58 (≠ D56), R60 (≠ T58), G232 (≠ D229), N234 (≠ T231), G296 (≠ A293), Y297 (≠ R294), R310 (= R313), Y367 (= Y366), Y421 (≠ A416), Q433 (≠ T428)
Sites not aligning to the query:
7tdvC Glutamine synthetase (see paper)
31% identity, 97% coverage: 11:430/432 of query aligns to 14:440/443 of 7tdvC
- binding adenosine-5'-diphosphate: G129 (= G121), E131 (= E123), E183 (≠ Y175), D197 (≠ N189), F198 (≠ W190), K199 (≠ E191), Y200 (≠ F192), N246 (≠ H238), V247 (= V239), S248 (= S240), R320 (= R318), S328 (≠ A322), R330 (= R324)
- binding magnesium ion: E131 (= E123), E131 (= E123), E133 (= E125), E188 (= E180), E195 (= E187), E195 (= E187), H244 (= H236), E332 (= E326)
- binding l-methionine-s-sulfoximine phosphate: E131 (= E123), E133 (= E125), E188 (= E180), E195 (= E187), G240 (= G232), H244 (= H236), R297 (= R289), E303 (≠ T295), R315 (= R313)
7tenA Glutamine synthetase (see paper)
31% identity, 98% coverage: 9:432/432 of query aligns to 11:441/442 of 7tenA
- binding adenosine-5'-diphosphate: G128 (= G121), E130 (= E123), E182 (≠ Y175), D196 (≠ N189), F197 (≠ W190), K198 (≠ E191), Y199 (≠ F192), N245 (≠ H238), S247 (= S240), R319 (= R318), S327 (≠ A322), R329 (= R324)
- binding l-methionine-s-sulfoximine phosphate: E130 (= E123), E132 (= E125), E187 (= E180), E194 (= E187), N238 (≠ T231), G239 (= G232), H243 (= H236), R296 (= R289), E302 (≠ T295), R314 (= R313), R333 (= R328)
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, 97% coverage: 11:430/432 of query aligns to 14:444/446 of P9WN37
- K363 (≠ N353) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
Query Sequence
>WP_012042168.1 NCBI__GCF_000015165.1:WP_012042168.1
MSSSLHAVACERGIKYFLISYTDLFGVQRAKLVPAAAIDGMVKTGAGFAGFATWLDMTPA
DPDVFAMPDPASLIQLPWKPEVGWLAADPWMNGKPVAHAPRNLLKRMVADAAAQGYELKS
GVECEFFLITADGSAPSDVADKQSKPCYDQQALMRRYEVIAEICDAMLALGWKPYQNDHE
DANGQFEMNWEFDTALTTADRHAFFKYMVRSIAEKHGLRATFMPKPFVDLTGNGCHAHVS
VWKDGRNLFEDEAGELGVSELGYQFLGGIMHSADALAALFNPTVNSYKRINAARTTSGAT
WAPNSVTYSGNNRTHLIRIPEAGRFEVRLADGAANPYLLQAGLLAAGLDGIANDRDPGPR
LDINMYTDGHAVKTGKKLPLNLLDAIRALQASPVMAEKLGDFIPCYVKLKTEEWNAYARH
LTEWERETTLDC
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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