SitesBLAST
Comparing WP_013075381.1 NCBI__GCF_000092905.1:WP_013075381.1 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)
8oooA Glutamine synthetase from methanothermococcus thermolithotrophicus in complex with 2-oxoglutarate and mgatp at 2.15 a resolution (see paper)
38% identity, 82% coverage: 84:466/467 of query aligns to 74:447/447 of 8oooA
- binding 2-oxoglutaric acid: R87 (≠ A97), V93 (= V100), P170 (≠ L194), R173 (≠ L198), R174 (≠ I199), S190 (≠ A215)
- binding adenosine-5'-triphosphate: E136 (= E142), E188 (= E213), F203 (≠ Y228), K204 (≠ A229), F205 (≠ P230), H251 (= H276), S253 (≠ V278), R325 (= R351), R335 (= R361)
Sites not aligning to the query:
8ooqB Glutamine synthetase from Methanothermococcus thermolithotrophicus (see paper)
38% identity, 82% coverage: 84:466/467 of query aligns to 73:446/446 of 8ooqB
Sites not aligning to the query:
8oozA Glutamine synthetase (see paper)
32% identity, 97% coverage: 9:463/467 of query aligns to 5:426/430 of 8oozA
- binding adenosine-5'-triphosphate: G117 (≠ S140), E170 (= E213), F185 (≠ Y228), K186 (≠ A229), Y187 (≠ P230), N233 (≠ H276), S235 (≠ V278), S315 (≠ A359), R317 (= R361)
- binding magnesium ion: E119 (= E142), H231 (= H274), E319 (= E363)
8ooxB Glutamine synthetase (see paper)
32% identity, 97% coverage: 9:463/467 of query aligns to 5:434/438 of 8ooxB
7tdpA Structure of paenibacillus polymyxa gs bound to met-sox-p-adp (transition state complex) to 1.98 angstom (see paper)
31% identity, 99% coverage: 8:467/467 of query aligns to 5:439/439 of 7tdpA
- binding adenosine-5'-diphosphate: N123 (≠ K138), G125 (≠ S140), E127 (= E142), E179 (= E213), D193 (≠ S227), Y196 (≠ P230), N242 (≠ H276), S244 (≠ V278), R316 (= R351), R326 (= R361)
- binding magnesium ion: E127 (= E142), E127 (= E142), E129 (= E144), E184 (= E218), E191 (= E225), E191 (= E225), H240 (= H274), E328 (= E363)
- binding l-methionine-s-sulfoximine phosphate: E127 (= E142), E129 (= E144), E184 (= E218), E191 (= E225), G236 (= G270), H240 (= H274), R293 (= R328), E299 (≠ F334), R311 (= R346), R330 (= R365)
7tfaB Glutamine synthetase (see paper)
31% identity, 99% coverage: 8:467/467 of query aligns to 5:441/441 of 7tfaB
- binding glutamine: E131 (= E144), Y153 (≠ H173), E186 (= E218), G238 (= G270), H242 (= H274), R295 (= R328), E301 (≠ F334)
- binding magnesium ion: E129 (= E142), E131 (= E144), E186 (= E218), E193 (= E225), H242 (= H274), E330 (= E363)
- binding : Y58 (≠ S64), R60 (= R66), V187 (≠ Y219), N237 (≠ S269), G299 (= G332), Y300 (≠ A333), R313 (= R346), M424 (≠ R450)
8ufjB Glutamine synthetase (see paper)
30% identity, 98% coverage: 8:463/467 of query aligns to 8:440/444 of 8ufjB
8tfkA Glutamine synthetase (see paper)
30% identity, 98% coverage: 8:463/467 of query aligns to 4:436/440 of 8tfkA
- binding adenosine-5'-diphosphate: E128 (= E142), D194 (≠ S227), F195 (≠ Y228), F197 (≠ P230), N243 (≠ H276), R312 (= R346), R317 (= R351), G325 (≠ A359), R327 (= R361)
- binding magnesium ion: E128 (= E142), E128 (= E142), E130 (= E144), E185 (= E218), E192 (= E225), E192 (= E225), H241 (= H274), E329 (= E363)
- binding l-methionine-s-sulfoximine phosphate: E128 (= E142), E130 (= E144), E185 (= E218), E192 (= E225), G237 (= G270), H241 (= H274), R294 (= R328), E300 (≠ F334), R312 (= R346), R331 (= R365)
8wwvA Glutamine synthetase
32% identity, 84% coverage: 77:467/467 of query aligns to 92:490/490 of 8wwvA
- binding adenosine-5'-diphosphate: G155 (≠ S140), E157 (= E142), R224 (≠ E213), F239 (≠ Y228), D240 (≠ A229), V241 (≠ P230), H288 (= H276), S290 (≠ V278), R374 (= R361), E376 (= E363)
- binding magnesium ion: E157 (= E142), E236 (= E225)
- binding manganese (ii) ion: E157 (= E142), E159 (= E144), E229 (= E218), E236 (= E225), H286 (= H274), E376 (= E363)
- binding l-methionine-s-sulfoximine phosphate: E157 (= E142), E159 (= E144), E229 (= E218), E236 (= E225), A282 (≠ G270), H286 (= H274), R340 (= R328), K358 (≠ R346)
4s0rD Structure of gs-tnra complex (see paper)
29% identity, 98% coverage: 8:463/467 of query aligns to 10:443/447 of 4s0rD
- active site: D56 (≠ F54), E135 (vs. gap), E137 (= E144), E192 (= E218), E199 (= E225), H248 (= H274), R319 (= R346), E336 (= E363), R338 (= R365)
- binding glutamine: E137 (= E144), E192 (= E218), R301 (= R328), E307 (≠ F334)
- binding magnesium ion: I66 (≠ S77), E135 (vs. gap), E135 (vs. gap), E199 (= E225), H248 (= H274), H248 (= H274), E336 (= E363), H419 (≠ Q439)
- binding : F63 (= F61), V64 (≠ P75), R65 (= R76), I66 (≠ S77), D161 (≠ P175), G241 (= G267), V242 (≠ F268), N243 (≠ S269), G305 (= G332), Y306 (≠ A333), Y376 (≠ S404), I426 (≠ A446), M430 (≠ R450)
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)
29% identity, 98% coverage: 8:463/467 of query aligns to 7:440/444 of P12425
- G59 (≠ A60) 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 (= R76) 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 (vs. gap) binding Mg(2+)
- E134 (= E144) binding Mg(2+)
- E189 (= E218) binding Mg(2+)
- V190 (≠ Y219) 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 (= G332) 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 (≠ F334) 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 (= P336) 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 (= E363) binding Mg(2+)
- E424 (= E447) 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
8wwuB Glutamine synthetase
32% identity, 84% coverage: 77:467/467 of query aligns to 94:492/492 of 8wwuB
- binding phosphoaminophosphonic acid-adenylate ester: G157 (≠ S140), E159 (= E142), R226 (≠ E213), F241 (≠ Y228), V243 (≠ P230), H290 (= H276), S292 (≠ V278), K360 (≠ R346), R365 (= R351), R376 (= R361)
- binding magnesium ion: E159 (= E142), E238 (= E225)
- binding manganese (ii) ion: E159 (= E142), E161 (= E144), E231 (= E218), E238 (= E225), H288 (= H274), E378 (= E363)
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)
29% identity, 98% coverage: 8:463/467 of query aligns to 6:439/443 of 4lnkA
- active site: D52 (≠ F54), E131 (vs. gap), E133 (= E144), E188 (= E218), E195 (= E225), H244 (= H274), R315 (= R346), E332 (= E363), R334 (= R365)
- binding adenosine-5'-diphosphate: K43 (≠ E45), M50 (≠ L52), F198 (≠ Y228), Y200 (≠ P230), N246 (≠ H276), S248 (≠ V278), S324 (≠ A355), S328 (≠ A359), R330 (= R361)
- binding glutamic acid: E133 (= E144), E188 (= E218), V189 (≠ Y219), N239 (≠ S269), G240 (= G270), G242 (= G272), E303 (≠ F334)
- binding magnesium ion: E131 (vs. gap), E188 (= E218), E195 (= E225), H244 (= H274), E332 (= E363)
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)
29% identity, 98% coverage: 8:463/467 of query aligns to 6:439/443 of 4lniA
- active site: D52 (≠ F54), E131 (vs. gap), E133 (= E144), E188 (= E218), E195 (= E225), H244 (= H274), R315 (= R346), E332 (= E363), R334 (= R365)
- binding adenosine-5'-diphosphate: E131 (vs. gap), E183 (= E213), D197 (≠ S227), Y200 (≠ P230), N246 (≠ H276), S248 (≠ V278), R320 (= R351), R330 (= R361)
- binding magnesium ion: E131 (vs. gap), E131 (vs. gap), E133 (= E144), E188 (= E218), E195 (= E225), E195 (= E225), H244 (= H274), E332 (= E363)
- binding l-methionine-s-sulfoximine phosphate: E133 (= E144), E188 (= E218), H244 (= H274), R297 (= R328), E303 (≠ F334), R315 (= R346), R334 (= R365)
7tdvC Glutamine synthetase (see paper)
30% identity, 98% coverage: 8:463/467 of query aligns to 6:439/443 of 7tdvC
- binding adenosine-5'-diphosphate: G129 (≠ S140), E131 (= E142), E183 (= E213), D197 (≠ S227), F198 (≠ Y228), K199 (≠ A229), Y200 (≠ P230), N246 (≠ H276), V247 (≠ H277), S248 (≠ V278), R320 (= R351), S328 (≠ A359), R330 (= R361)
- binding magnesium ion: E131 (= E142), E131 (= E142), E133 (= E144), E188 (= E218), E195 (= E225), E195 (= E225), H244 (= H274), E332 (= E363)
- binding l-methionine-s-sulfoximine phosphate: E131 (= E142), E133 (= E144), E188 (= E218), E195 (= E225), G240 (= G270), H244 (= H274), R297 (= R328), E303 (≠ F334), R315 (= R346)
7tf6A Glutamine synthetase (see paper)
30% identity, 98% coverage: 8:463/467 of query aligns to 5:434/438 of 7tf6A
- binding glutamine: E128 (= E144), E183 (= E218), G235 (= G270), H239 (= H274), R292 (= R328), E298 (≠ F334)
- binding magnesium ion: E126 (= E142), E128 (= E144), E183 (= E218), E190 (= E225), H239 (= H274), E327 (= E363)
- binding : F58 (≠ S64), R60 (= R66), G232 (= G267), N234 (≠ S269), G296 (= G332), Y297 (≠ A333), R310 (= R346), Y367 (≠ S404), Y421 (≠ R450), Q433 (≠ E462)
Sites not aligning to the query:
7tf9S L. Monocytogenes gs(14)-q-glnr peptide (see paper)
30% identity, 99% coverage: 8:467/467 of query aligns to 6:443/443 of 7tf9S
- binding glutamine: E133 (= E144), Y155 (≠ H173), E188 (= E218), G240 (= G270), G242 (= G272), R297 (= R328), E303 (≠ F334)
- binding magnesium ion: E131 (= E142), E133 (= E144), E188 (= E218), E195 (= E225), H244 (= H274), E332 (= E363)
- binding : F59 (≠ S64), V60 (≠ A65), E418 (≠ R442), I422 (≠ A446), M426 (≠ R450)
7tenA Glutamine synthetase (see paper)
30% identity, 99% coverage: 8:467/467 of query aligns to 5:442/442 of 7tenA
- binding adenosine-5'-diphosphate: G128 (≠ S140), E130 (= E142), E182 (= E213), D196 (≠ S227), F197 (≠ Y228), K198 (≠ A229), Y199 (≠ P230), N245 (≠ H276), S247 (≠ V278), R319 (= R351), S327 (≠ A359), R329 (= R361)
- binding l-methionine-s-sulfoximine phosphate: E130 (= E142), E132 (= E144), E187 (= E218), E194 (= E225), N238 (≠ S269), G239 (= G270), H243 (= H274), R296 (= R328), E302 (≠ F334), R314 (= R346), R333 (= R365)
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)
32% identity, 97% coverage: 10:463/467 of query aligns to 8:443/446 of A0R083
- K363 (≠ R390) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
P78061 Gamma-glutamylputrescine synthetase PuuA; Gamma-Glu-Put synthetase; Glutamate--putrescine ligase; EC 6.3.1.11 from Escherichia coli (strain K12) (see paper)
29% identity, 98% coverage: 6:461/467 of query aligns to 23:468/472 of P78061
- H282 (= H274) mutation to N: Activity is impaired to 9% of wild-type.
- R357 (= R351) mutation to Q: Activity is impaired to 3% of wild-type.
Query Sequence
>WP_013075381.1 NCBI__GCF_000092905.1:WP_013075381.1
MTPPDWHQEVQQMIQAHQIQLVRVCVQDLGHMSRCREVPSGRFLERMATDGLSFPSALFA
FDSSARIVPGAGPGPRSGYPSWHLQPDLSTFSVLPYAPGVARVIADPFEAKGQPVDYAPR
HVLRRVLERARAAGFQVKGSFEFEFYAFARDGDSRGQAPVSPDAISPGPSSPHPPGVPAW
TGLQCFSEIKQAALEPLLIHLVQTLEAMGARPEVANTEYGPGQFEISYAPYWNLEIADMA
FYYRTTIREVLAQHGLKATFMSKPLSGFSGSGAHLHHVLHGSDGANAFADPKARDGLSQL
CRWFIGGQLAHARTVSALMNPTINGYKRLQPGAFAPHWITWGYDHRETMIRVPPARGKAT
RIENRLPGADTDPYLALAAALAAGLDGIERRIDPGDPVADRPVSEMAAPLLPRSLSEALD
AFEEDPWTEEVFGRSFKEQFLRLRRAEVERFFRHVTDWEWMEYEDIF
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