SitesBLAST
Comparing WP_012170027.1 NCBI__GCF_000010525.1:WP_012170027.1 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)
64% identity, 95% coverage: 22:449/450 of query aligns to 4:429/430 of 7cqwA
7cquA Gmas/adp/metsox-p complex (see paper)
64% identity, 95% coverage: 22:449/450 of query aligns to 3:428/429 of 7cquA
- binding adenosine-5'-diphosphate: E121 (= E140), Y173 (= Y192), N187 (= N206), W188 (= W207), D189 (≠ N208), Y190 (= Y209), H236 (= H255), L237 (≠ V256), S238 (= S257), R316 (= R335), R322 (= R341)
- binding magnesium ion: E121 (= E140), E121 (= E140), E123 (= E142), E178 (= E197), E185 (= E204), E185 (= E204), H234 (= H253), E324 (= E343)
- binding l-methionine-s-sulfoximine phosphate: E121 (= E140), E123 (= E142), E178 (= E197), E185 (= E204), T229 (= T248), G230 (= G249), H234 (= H253), R287 (= R306), W299 (= W318), R311 (= R330), R326 (= R345)
7cqqA Gmas in complex with amppnp and metsox (see paper)
64% identity, 95% coverage: 22:449/450 of query aligns to 3:428/429 of 7cqqA
- binding phosphoaminophosphonic acid-adenylate ester: E121 (= E140), Y173 (= Y192), E185 (= E204), N187 (= N206), D189 (≠ N208), Y190 (= Y209), H234 (= H253), H236 (= H255), S238 (= S257), R311 (= R330), R316 (= R335), R322 (= R341), E324 (= E343)
- binding magnesium ion: E121 (= E140), E121 (= E140), E123 (= E142), E178 (= E197), E185 (= E204), E185 (= E204), H234 (= H253), E324 (= E343)
- binding (2s)-2-amino-4-(methylsulfonimidoyl)butanoic acid: E123 (= E142), E178 (= E197), T229 (= T248), H234 (= H253), R287 (= R306), W299 (= W318), R311 (= R330), R326 (= R345)
7cqnA Gmas in complex with amppcp (see paper)
64% identity, 95% coverage: 22:449/450 of query aligns to 3:428/429 of 7cqnA
- binding phosphomethylphosphonic acid adenylate ester: G45 (= G64), D61 (= D80), E121 (= E140), Y173 (= Y192), Q174 (= Q193), W188 (= W207), D189 (≠ N208), Y190 (= Y209), H236 (= H255), S238 (= S257), R311 (= R330), R316 (= R335), R322 (= R341)
7tdpA Structure of paenibacillus polymyxa gs bound to met-sox-p-adp (transition state complex) to 1.98 angstom (see paper)
35% identity, 97% coverage: 16:450/450 of query aligns to 1:438/439 of 7tdpA
- binding adenosine-5'-diphosphate: N123 (≠ K136), G125 (= G138), E127 (= E140), E179 (≠ Y192), D193 (≠ N206), Y196 (= Y209), N242 (≠ H255), S244 (= S257), R316 (= R335), R326 (= R341)
- binding magnesium ion: E127 (= E140), E127 (= E140), E129 (= E142), E184 (= E197), E191 (= E204), E191 (= E204), H240 (= H253), E328 (= E343)
- binding l-methionine-s-sulfoximine phosphate: E127 (= E140), E129 (= E142), E184 (= E197), E191 (= E204), G236 (= G249), H240 (= H253), R293 (= R306), E299 (≠ T317), R311 (= R330), R330 (= R345)
8oozA Glutamine synthetase (see paper)
34% identity, 94% coverage: 25:448/450 of query aligns to 9:427/430 of 8oozA
- binding adenosine-5'-triphosphate: G117 (= G138), E170 (≠ Y192), F185 (≠ W207), K186 (≠ N208), Y187 (= Y209), N233 (≠ H255), S235 (= S257), S315 (≠ A339), R317 (= R341)
- binding magnesium ion: E119 (= E140), H231 (= H253), E319 (= E343)
8ooxB Glutamine synthetase (see paper)
34% identity, 94% coverage: 25:448/450 of query aligns to 9:435/438 of 8ooxB
8tfkA Glutamine synthetase (see paper)
34% identity, 94% coverage: 26:450/450 of query aligns to 10:439/440 of 8tfkA
- binding adenosine-5'-diphosphate: E128 (= E140), D194 (≠ N206), F195 (≠ W207), F197 (≠ Y209), N243 (≠ H255), R312 (= R330), R317 (= R335), G325 (≠ A339), R327 (= R341)
- binding magnesium ion: E128 (= E140), E128 (= E140), E130 (= E142), E185 (= E197), E192 (= E204), E192 (= E204), H241 (= H253), E329 (= E343)
- binding l-methionine-s-sulfoximine phosphate: E128 (= E140), E130 (= E142), E185 (= E197), E192 (= E204), G237 (= G249), H241 (= H253), R294 (= R306), E300 (≠ T317), R312 (= R330), R331 (= R345)
7tfaB Glutamine synthetase (see paper)
35% identity, 97% coverage: 16:450/450 of query aligns to 1:440/441 of 7tfaB
- binding glutamine: E131 (= E142), Y153 (≠ C164), E186 (= E197), G238 (= G249), H242 (= H253), R295 (= R306), E301 (≠ T317)
- binding magnesium ion: E129 (= E140), E131 (= E142), E186 (= E197), E193 (= E204), H242 (= H253), E330 (= E343)
- binding : Y58 (≠ D73), R60 (≠ S75), V187 (≠ D198), N237 (≠ T248), G299 (= G315), Y300 (≠ A316), R313 (= R330), M424 (≠ A434)
8ufjB Glutamine synthetase (see paper)
34% identity, 94% coverage: 26:450/450 of query aligns to 14:443/444 of 8ufjB
7tf6A Glutamine synthetase (see paper)
32% identity, 95% coverage: 22:448/450 of query aligns to 7:435/438 of 7tf6A
- binding glutamine: E128 (= E142), E183 (= E197), G235 (= G249), H239 (= H253), R292 (= R306), E298 (≠ T317)
- binding magnesium ion: E126 (= E140), E128 (= E142), E183 (= E197), E190 (= E204), H239 (= H253), E327 (= E343)
- binding : F58 (= F68), R60 (≠ S75), G232 (≠ N246), N234 (≠ T248), G296 (= G315), Y297 (≠ A316), R310 (= R330), Y367 (= Y383), Y421 (≠ A434), Q433 (≠ H446)
Sites not aligning to the query:
7tf9S L. Monocytogenes gs(14)-q-glnr peptide (see paper)
32% identity, 97% coverage: 15:450/450 of query aligns to 1:442/443 of 7tf9S
- binding glutamine: E133 (= E142), Y155 (≠ C164), E188 (= E197), G240 (= G249), G242 (= G251), R297 (= R306), E303 (≠ T317)
- binding magnesium ion: E131 (= E140), E133 (= E142), E188 (= E197), E195 (= E204), H244 (= H253), E332 (= E343)
- binding : F59 (≠ D73), V60 (≠ M74), E418 (≠ K426), I422 (≠ E430), M426 (≠ A434)
7tenA Glutamine synthetase (see paper)
33% identity, 95% coverage: 25:450/450 of query aligns to 10:441/442 of 7tenA
- binding adenosine-5'-diphosphate: G128 (= G138), E130 (= E140), E182 (≠ Y192), D196 (≠ N206), F197 (≠ W207), K198 (≠ N208), Y199 (= Y209), N245 (≠ H255), S247 (= S257), R319 (= R335), S327 (≠ A339), R329 (= R341)
- binding l-methionine-s-sulfoximine phosphate: E130 (= E140), E132 (= E142), E187 (= E197), E194 (= E204), N238 (≠ T248), G239 (= G249), H243 (= H253), R296 (= R306), E302 (≠ T317), R314 (= R330), R333 (= R345)
7tdvC Glutamine synthetase (see paper)
32% identity, 95% coverage: 22:448/450 of query aligns to 8:440/443 of 7tdvC
- binding adenosine-5'-diphosphate: G129 (= G138), E131 (= E140), E183 (≠ Y192), D197 (≠ N206), F198 (≠ W207), K199 (≠ N208), Y200 (= Y209), N246 (≠ H255), V247 (= V256), S248 (= S257), R320 (= R335), S328 (≠ A339), R330 (= R341)
- binding magnesium ion: E131 (= E140), E131 (= E140), E133 (= E142), E188 (= E197), E195 (= E204), E195 (= E204), H244 (= H253), E332 (= E343)
- binding l-methionine-s-sulfoximine phosphate: E131 (= E140), E133 (= E142), E188 (= E197), E195 (= E204), G240 (= G249), H244 (= H253), R297 (= R306), E303 (≠ T317), R315 (= R330)
4s0rD Structure of gs-tnra complex (see paper)
32% identity, 96% coverage: 15:448/450 of query aligns to 5:444/447 of 4s0rD
- active site: D56 (≠ A66), E135 (= E140), E137 (= E142), E192 (= E197), E199 (= E204), H248 (= H253), R319 (= R330), E336 (= E343), R338 (= R345)
- binding glutamine: E137 (= E142), E192 (= E197), R301 (= R306), E307 (≠ T317)
- binding magnesium ion: I66 (≠ P76), E135 (= E140), E135 (= E140), E199 (= E204), H248 (= H253), H248 (= H253), E336 (= E343), H419 (≠ G423)
- binding : F63 (≠ D73), V64 (≠ M74), R65 (≠ S75), I66 (≠ P76), D161 (= D166), G241 (≠ N246), V242 (≠ L247), N243 (≠ T248), G305 (= G315), Y306 (≠ A316), Y376 (= Y383), I426 (≠ E430), M430 (≠ A434)
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)
32% identity, 96% coverage: 15:448/450 of query aligns to 1:440/443 of 4lnkA
- active site: D52 (≠ A66), E131 (= E140), E133 (= E142), E188 (= E197), E195 (= E204), H244 (= H253), R315 (= R330), E332 (= E343), R334 (= R345)
- binding adenosine-5'-diphosphate: K43 (≠ E57), M50 (≠ G64), F198 (≠ W207), Y200 (= Y209), N246 (≠ H255), S248 (= S257), S324 (vs. gap), S328 (≠ A339), R330 (= R341)
- binding glutamic acid: E133 (= E142), E188 (= E197), V189 (≠ D198), N239 (≠ T248), G240 (= G249), G242 (= G251), E303 (≠ T317)
- binding magnesium ion: E131 (= E140), E188 (= E197), E195 (= E204), H244 (= H253), E332 (= E343)
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)
32% identity, 96% coverage: 15:448/450 of query aligns to 1:440/443 of 4lniA
- active site: D52 (≠ A66), E131 (= E140), E133 (= E142), E188 (= E197), E195 (= E204), H244 (= H253), R315 (= R330), E332 (= E343), R334 (= R345)
- binding adenosine-5'-diphosphate: E131 (= E140), E183 (≠ Y192), D197 (≠ N206), Y200 (= Y209), N246 (≠ H255), S248 (= S257), R320 (= R335), R330 (= R341)
- binding magnesium ion: E131 (= E140), E131 (= E140), E133 (= E142), E188 (= E197), E195 (= E204), E195 (= E204), H244 (= H253), E332 (= E343)
- binding l-methionine-s-sulfoximine phosphate: E133 (= E142), E188 (= E197), H244 (= H253), R297 (= R306), E303 (≠ T317), R315 (= R330), R334 (= R345)
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)
32% identity, 96% coverage: 15:448/450 of query aligns to 2:441/444 of P12425
- G59 (≠ L72) 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 (≠ S75) 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 (= E140) binding Mg(2+)
- E134 (= E142) binding Mg(2+)
- E189 (= E197) binding Mg(2+)
- V190 (≠ D198) 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 (= E204) binding Mg(2+)
- G241 (= G249) binding L-glutamate
- H245 (= H253) binding Mg(2+)
- G302 (= G315) 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 (≠ T317) 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 (= P320) 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 (= E343) binding Mg(2+)
- E424 (= E431) 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
8oooA Glutamine synthetase from methanothermococcus thermolithotrophicus in complex with 2-oxoglutarate and mgatp at 2.15 a resolution (see paper)
33% identity, 94% coverage: 26:450/450 of query aligns to 10:447/447 of 8oooA
- binding 2-oxoglutaric acid: F17 (≠ Y33), R19 (≠ L35), A33 (≠ L49), R87 (≠ N96), V93 (= V99), P170 (≠ Y174), R173 (≠ I177), R174 (≠ K178), S190 (≠ N194)
- binding adenosine-5'-triphosphate: E136 (= E140), E188 (≠ Y192), F203 (≠ W207), K204 (≠ N208), F205 (≠ Y209), H251 (= H255), S253 (= S257), R325 (= R335), R335 (= R341)
8ooqB Glutamine synthetase from Methanothermococcus thermolithotrophicus (see paper)
33% identity, 94% coverage: 26:450/450 of query aligns to 9:446/446 of 8ooqB
- binding 2-oxoglutaric acid: F16 (≠ Y33), R18 (≠ L35), A32 (≠ L49), R86 (≠ N96), V92 (= V99), P169 (≠ Y174), R172 (≠ I177), R173 (≠ K178), S189 (≠ N194)
- binding magnesium ion: E137 (= E142), E192 (= E197), E199 (= E204)
Query Sequence
>WP_012170027.1 NCBI__GCF_000010525.1:WP_012170027.1
MARLPKQVKDAEGRASAASASLATIAQERGIKYFLISYVDLFGGLRAKLVPASAIEEMQK
AGAGFAGFATWLDMSPADPDLFAVPDPSSLIQLPWNPEVGWLASDLVMDGKIVEQAPRSV
LKAQLARAEALGYEMKSGVECEYFLISADGSAIHDGSDTAAKPCYDQSALMRQYGVIKEI
CDSMLQLGWGAYQNDHEDANGQFEMNWNYDNALITADRHVFFKYMVKSIAEKHGLRATFM
PKPFINLTGSGCHVHVSLWKKGGNAFSDPKGELGVSQLGYHFIGGLIHNADALCALTNPT
VNSYKRINAPRTISGATWAPNTVTYTGNNRTHMIRIPDAGRFEFRLADGAANPYLLQAGV
LASGLDGIENERDPGKRLDINMYTEGHKVRGAKRLPLNLLDALRALEKSKVLKDSLGTAL
VDGYLKLKTEEWNAYSRHLTQWEREHTLDI
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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