SitesBLAST
Comparing WP_011970786.1 NCBI__GCF_000017145.1:WP_011970786.1 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)
63% identity, 99% coverage: 4:435/435 of query aligns to 3:430/430 of 7cqwA
7cquA Gmas/adp/metsox-p complex (see paper)
63% identity, 99% coverage: 4:435/435 of query aligns to 2:429/429 of 7cquA
- binding adenosine-5'-diphosphate: E121 (= E123), Y173 (= Y175), N187 (= N189), W188 (= W190), D189 (≠ E191), Y190 (= Y192), H236 (= H238), L237 (≠ I239), S238 (= S240), R316 (= R320), R322 (= R326)
- binding magnesium ion: E121 (= E123), E121 (= E123), E123 (= E125), E178 (= E180), E185 (= E187), E185 (= E187), H234 (= H236), E324 (= E328)
- binding l-methionine-s-sulfoximine phosphate: E121 (= E123), E123 (= E125), E178 (= E180), E185 (= E187), T229 (= T231), G230 (= G232), H234 (= H236), R287 (= R291), W299 (= W303), R311 (= R315), R326 (= R330)
7cqqA Gmas in complex with amppnp and metsox (see paper)
63% identity, 99% coverage: 4:435/435 of query aligns to 2:429/429 of 7cqqA
- binding phosphoaminophosphonic acid-adenylate ester: E121 (= E123), Y173 (= Y175), E185 (= E187), N187 (= N189), D189 (≠ E191), Y190 (= Y192), H234 (= H236), H236 (= H238), S238 (= S240), R311 (= R315), R316 (= R320), R322 (= R326), E324 (= E328)
- binding magnesium ion: E121 (= E123), E121 (= E123), E123 (= E125), E178 (= E180), E185 (= E187), E185 (= E187), H234 (= H236), E324 (= E328)
- binding (2s)-2-amino-4-(methylsulfonimidoyl)butanoic acid: E123 (= E125), E178 (= E180), T229 (= T231), H234 (= H236), R287 (= R291), W299 (= W303), R311 (= R315), R326 (= R330)
7cqnA Gmas in complex with amppcp (see paper)
63% identity, 99% coverage: 4:435/435 of query aligns to 2:429/429 of 7cqnA
- binding phosphomethylphosphonic acid adenylate ester: G45 (= G47), D61 (= D63), E121 (= E123), Y173 (= Y175), Q174 (= Q176), W188 (= W190), D189 (≠ E191), Y190 (= Y192), H236 (= H238), S238 (= S240), R311 (= R315), R316 (= R320), R322 (= R326)
7tdpA Structure of paenibacillus polymyxa gs bound to met-sox-p-adp (transition state complex) to 1.98 angstom (see paper)
34% identity, 99% coverage: 3:433/435 of query aligns to 5:436/439 of 7tdpA
- binding adenosine-5'-diphosphate: N123 (≠ K119), G125 (= G121), E127 (= E123), E179 (≠ Y175), D193 (≠ N189), Y196 (= Y192), N242 (≠ H238), S244 (= S240), R316 (= R320), R326 (= R326)
- binding magnesium ion: E127 (= E123), E127 (= E123), E129 (= E125), E184 (= E180), E191 (= E187), E191 (= E187), H240 (= H236), E328 (= E328)
- binding l-methionine-s-sulfoximine phosphate: E127 (= E123), E129 (= E125), E184 (= E180), E191 (= E187), G236 (= G232), H240 (= H236), R293 (= R291), E299 (≠ T302), R311 (= R315), R330 (= R330)
7tfaB Glutamine synthetase (see paper)
34% identity, 99% coverage: 3:433/435 of query aligns to 5:438/441 of 7tfaB
- binding glutamine: E131 (= E125), Y153 (≠ T142), E186 (= E180), G238 (= G232), H242 (= H236), R295 (= R291), E301 (≠ T302)
- binding magnesium ion: E129 (= E123), E131 (= E125), E186 (= E180), E193 (= E187), H242 (= H236), E330 (= E328)
- binding : Y58 (≠ F51), R60 (≠ T53), V187 (≠ D181), N237 (≠ T231), G299 (= G300), Y300 (≠ A301), R313 (= R315), M424 (≠ T419)
8ooxB Glutamine synthetase (see paper)
34% identity, 98% coverage: 4:428/435 of query aligns to 5:430/438 of 8ooxB
8oozA Glutamine synthetase (see paper)
34% identity, 98% coverage: 4:428/435 of query aligns to 5:422/430 of 8oozA
- binding adenosine-5'-triphosphate: G117 (= G121), E170 (≠ Y175), F185 (≠ W190), K186 (≠ E191), Y187 (= Y192), N233 (≠ H238), S235 (= S240), S315 (vs. gap), R317 (= R326)
- binding magnesium ion: E119 (= E123), H231 (= H236), E319 (= E328)
8oooA Glutamine synthetase from methanothermococcus thermolithotrophicus in complex with 2-oxoglutarate and mgatp at 2.15 a resolution (see paper)
34% identity, 97% coverage: 14:435/435 of query aligns to 15:447/447 of 8oooA
- binding 2-oxoglutaric acid: F17 (≠ Y16), R19 (≠ M18), 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 (≠ Y192), H251 (= H238), S253 (= S240), R325 (= R320), R335 (= R326)
8ooqB Glutamine synthetase from Methanothermococcus thermolithotrophicus (see paper)
34% identity, 97% coverage: 14:435/435 of query aligns to 14:446/446 of 8ooqB
- binding 2-oxoglutaric acid: F16 (≠ Y16), R18 (≠ M18), 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: 3:433/435 of query aligns to 10:444/447 of 4s0rD
- active site: D56 (≠ A49), E135 (= E123), E137 (= E125), E192 (= E180), E199 (= E187), H248 (= H236), R319 (= R315), E336 (= E328), R338 (= R330)
- binding glutamine: E137 (= E125), E192 (= E180), R301 (= R291), E307 (≠ T302)
- binding magnesium ion: I66 (≠ P59), E135 (= E123), E135 (= E123), E199 (= E187), H248 (= H236), H248 (= H236), E336 (= E328), H419 (≠ A408)
- binding : F63 (≠ D56), V64 (≠ L57), R65 (≠ T58), I66 (≠ P59), D161 (≠ Q150), G241 (= G229), V242 (≠ L230), N243 (≠ T231), G305 (= G300), Y306 (≠ A301), Y376 (= Y368), I426 (≠ A415), M430 (≠ T419)
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: 3:433/435 of query aligns to 7:441/444 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 (= G300) 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 (≠ T302) 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 (= P305) 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 (= E328) binding Mg(2+)
- E424 (= E416) 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
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: 3:433/435 of query aligns to 6:440/443 of 4lnkA
- active site: D52 (≠ A49), E131 (= E123), E133 (= E125), E188 (= E180), E195 (= E187), H244 (= H236), R315 (= R315), E332 (= E328), R334 (= R330)
- binding adenosine-5'-diphosphate: K43 (≠ N40), M50 (≠ G47), F198 (≠ W190), Y200 (= Y192), N246 (≠ H238), S248 (= S240), S324 (vs. gap), S328 (≠ P324), R330 (= R326)
- binding glutamic acid: E133 (= E125), E188 (= E180), V189 (≠ D181), N239 (≠ T231), G240 (= G232), G242 (= G234), E303 (≠ T302)
- binding magnesium ion: E131 (= E123), E188 (= E180), E195 (= E187), H244 (= H236), E332 (= E328)
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: 3:433/435 of query aligns to 6:440/443 of 4lniA
- active site: D52 (≠ A49), E131 (= E123), E133 (= E125), E188 (= E180), E195 (= E187), H244 (= H236), R315 (= R315), E332 (= E328), R334 (= R330)
- binding adenosine-5'-diphosphate: E131 (= E123), E183 (≠ Y175), D197 (≠ N189), Y200 (= Y192), N246 (≠ H238), S248 (= S240), R320 (= R320), R330 (= R326)
- binding magnesium ion: E131 (= E123), E131 (= E123), E133 (= E125), E188 (= E180), E195 (= E187), E195 (= E187), H244 (= H236), E332 (= E328)
- binding l-methionine-s-sulfoximine phosphate: E133 (= E125), E188 (= E180), H244 (= H236), R297 (= R291), E303 (≠ T302), R315 (= R315), R334 (= R330)
8tfkA Glutamine synthetase (see paper)
33% identity, 98% coverage: 3:428/435 of query aligns to 4:432/440 of 8tfkA
- binding adenosine-5'-diphosphate: E128 (= E123), D194 (≠ N189), F195 (≠ W190), F197 (≠ Y192), N243 (≠ H238), R312 (= R315), R317 (= R320), G325 (= G325), R327 (= R326)
- binding magnesium ion: E128 (= E123), E128 (= E123), E130 (= E125), E185 (= E180), E192 (= E187), E192 (= E187), H241 (= H236), E329 (= E328)
- binding l-methionine-s-sulfoximine phosphate: E128 (= E123), E130 (= E125), E185 (= E180), E192 (= E187), G237 (= G232), H241 (= H236), R294 (= R291), E300 (≠ T302), R312 (= R315), R331 (= R330)
7tf6A Glutamine synthetase (see paper)
33% identity, 98% coverage: 3:429/435 of query aligns to 5:431/438 of 7tf6A
- binding glutamine: E128 (= E125), E183 (= E180), G235 (= G232), H239 (= H236), R292 (= R291), E298 (≠ T302)
- binding magnesium ion: E126 (= E123), E128 (= E125), E183 (= E180), E190 (= E187), H239 (= H236), E327 (= E328)
- binding : F58 (= F51), R60 (≠ T53), G232 (= G229), N234 (≠ T231), G296 (= G300), Y297 (≠ A301), R310 (= R315), Y367 (≠ I365), Y421 (≠ T419)
Sites not aligning to the query:
7tenA Glutamine synthetase (see paper)
32% identity, 100% coverage: 3:435/435 of query aligns to 5:441/442 of 7tenA
- binding adenosine-5'-diphosphate: G128 (= G121), E130 (= E123), E182 (≠ Y175), D196 (≠ N189), F197 (≠ W190), K198 (≠ E191), Y199 (= Y192), N245 (≠ H238), S247 (= S240), R319 (= R320), S327 (≠ P324), R329 (= R326)
- binding l-methionine-s-sulfoximine phosphate: E130 (= E123), E132 (= E125), E187 (= E180), E194 (= E187), N238 (≠ T231), G239 (= G232), H243 (= H236), R296 (= R291), E302 (≠ T302), R314 (= R315), R333 (= R330)
7tf9S L. Monocytogenes gs(14)-q-glnr peptide (see paper)
32% identity, 100% coverage: 3:435/435 of query aligns to 6:442/443 of 7tf9S
- binding glutamine: E133 (= E125), Y155 (vs. gap), E188 (= E180), G240 (= G232), G242 (= G234), R297 (= R291), E303 (≠ T302)
- binding magnesium ion: E131 (= E123), E133 (= E125), E188 (= E180), E195 (= E187), H244 (= H236), E332 (= E328)
- binding : F59 (≠ D56), V60 (≠ L57), E418 (≠ K411), I422 (≠ A415), M426 (≠ T419)
8ufjB Glutamine synthetase (see paper)
33% identity, 98% coverage: 3:428/435 of query aligns to 8:436/444 of 8ufjB
7tdvC Glutamine synthetase (see paper)
32% identity, 98% coverage: 3:429/435 of query aligns to 6:436/443 of 7tdvC
- binding adenosine-5'-diphosphate: G129 (= G121), E131 (= E123), E183 (≠ Y175), D197 (≠ N189), F198 (≠ W190), K199 (≠ E191), Y200 (= Y192), N246 (≠ H238), V247 (≠ I239), S248 (= S240), R320 (= R320), S328 (≠ P324), R330 (= R326)
- binding magnesium ion: E131 (= E123), E131 (= E123), E133 (= E125), E188 (= E180), E195 (= E187), E195 (= E187), H244 (= H236), E332 (= E328)
- binding l-methionine-s-sulfoximine phosphate: E131 (= E123), E133 (= E125), E188 (= E180), E195 (= E187), G240 (= G232), H244 (= H236), R297 (= R291), E303 (≠ T302), R315 (= R315)
Query Sequence
>WP_011970786.1 NCBI__GCF_000017145.1:WP_011970786.1
MTQDLATIAAERGIKYFMISYTDLFGAQRAKLVPTEAIANMQKDGAGFAGFATWLDLTPA
HPDLFAVPDASSVIQLPWKKDVAWVAADCVMEDKPVGQAPRVVLKKLVAEAAEHGLRVKT
GVEPEFFLISADGEKISDEFDTAEKPCYDQQALMRRYDVIAEICDYMLELGWKPYQNDHE
DANGQFEMNWEYDDALKTADKHSFFKFMVKSVAEKHGLRATFMPKPFKGLTGNGCHAHIS
VWDTDGKINAFADKAMPFGLSAKGKTFLGGIMKHASALAAITNPTVNSYKRINAPRTISG
ATWAPNTVTWTGNNRTHMVRVPGPGRFELRLPDGAVNPYLLQAIIIAAGLSGLKSDADPG
PHYDIDMYRDGHLVNDAPKLPLNLLDALRAYEEDEGLQAALGMEFSAAYLKLKHAEWNTH
CSQFSAWEHQTTLDV
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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