SitesBLAST
Comparing WP_015797716.1 NCBI__GCF_000023265.1:WP_015797716.1 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)
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)
47% identity, 98% coverage: 10:446/447 of query aligns to 6:446/446 of A0R083
- K363 (≠ Q363) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
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)
46% identity, 98% coverage: 10:446/447 of query aligns to 6:446/446 of P9WN37
- K363 (≠ Q363) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
8ooxB Glutamine synthetase (see paper)
45% identity, 97% coverage: 10:444/447 of query aligns to 4:435/438 of 8ooxB
8oozA Glutamine synthetase (see paper)
44% identity, 97% coverage: 10:444/447 of query aligns to 4:427/430 of 8oozA
- binding adenosine-5'-triphosphate: G117 (≠ A129), E170 (≠ K181), F185 (≠ L196), K186 (≠ A197), Y187 (≠ P198), N233 (≠ H244), S235 (≠ A246), S315 (≠ D332), R317 (≠ F334)
- binding magnesium ion: E119 (= E131), H231 (= H242), E319 (= E336)
8oooA Glutamine synthetase from methanothermococcus thermolithotrophicus in complex with 2-oxoglutarate and mgatp at 2.15 a resolution (see paper)
43% identity, 98% coverage: 9:446/447 of query aligns to 3:447/447 of 8oooA
- binding 2-oxoglutaric acid: F17 (= F23), R19 (≠ Q25), A33 (= A37), R87 (≠ L86), V93 (≠ T89), P170 (≠ S163), R173 (= R166), R174 (= R167), S190 (= S183)
- binding adenosine-5'-triphosphate: E136 (= E131), E188 (≠ K181), F203 (≠ L196), K204 (≠ A197), F205 (≠ P198), H251 (= H244), S253 (≠ A246), R325 (= R321), R335 (≠ F334)
8ooqB Glutamine synthetase from Methanothermococcus thermolithotrophicus (see paper)
43% identity, 98% coverage: 9:446/447 of query aligns to 2:446/446 of 8ooqB
- binding 2-oxoglutaric acid: F16 (= F23), R18 (≠ Q25), A32 (= A37), R86 (≠ L86), V92 (≠ T89), P169 (≠ S163), R172 (= R166), R173 (= R167), S189 (= S183)
- binding magnesium ion: E137 (= E133), E192 (= E186), E199 (= E193)
7tdpA Structure of paenibacillus polymyxa gs bound to met-sox-p-adp (transition state complex) to 1.98 angstom (see paper)
45% identity, 98% coverage: 10:446/447 of query aligns to 6:438/439 of 7tdpA
- binding adenosine-5'-diphosphate: N123 (≠ H127), G125 (≠ A129), E127 (= E131), E179 (≠ K181), D193 (= D195), Y196 (≠ P198), N242 (≠ H244), S244 (≠ A246), R316 (= R321), R326 (≠ F334)
- binding magnesium ion: E127 (= E131), E127 (= E131), E129 (= E133), E184 (= E186), E191 (= E193), E191 (= E193), H240 (= H242), E328 (= E336)
- binding l-methionine-s-sulfoximine phosphate: E127 (= E131), E129 (= E133), E184 (= E186), E191 (= E193), G236 (= G238), H240 (= H242), R293 (= R298), E299 (= E304), R311 (= R316), R330 (= R338)
7tfaB Glutamine synthetase (see paper)
45% identity, 98% coverage: 10:446/447 of query aligns to 6:440/441 of 7tfaB
- binding glutamine: E131 (= E133), Y153 (= Y153), E186 (= E186), G238 (= G238), H242 (= H242), R295 (= R298), E301 (= E304)
- binding magnesium ion: E129 (= E131), E131 (= E133), E186 (= E186), E193 (= E193), H242 (= H242), E330 (= E336)
- binding : Y58 (≠ F63), R60 (= R65), V187 (≠ D187), N237 (≠ Q237), G299 (= G302), Y300 (≠ F303), R313 (= R316), M424 (≠ A430)
8ufjB Glutamine synthetase (see paper)
43% identity, 98% coverage: 12:447/447 of query aligns to 10:444/444 of 8ufjB
4s0rD Structure of gs-tnra complex (see paper)
43% identity, 97% coverage: 12:445/447 of query aligns to 12:445/447 of 4s0rD
- active site: D56 (= D56), E135 (= E131), E137 (= E133), E192 (= E186), E199 (= E193), H248 (= H242), R319 (= R316), E336 (= E336), R338 (= R338)
- binding glutamine: E137 (= E133), E192 (= E186), R301 (= R298), E307 (= E304)
- binding magnesium ion: I66 (= I66), E135 (= E131), E135 (= E131), E199 (= E193), H248 (= H242), H248 (= H242), E336 (= E336), H419 (≠ W419)
- binding : F63 (= F63), V64 (≠ S64), R65 (= R65), I66 (= I66), D161 (≠ E155), G241 (= G235), V242 (≠ L236), N243 (≠ Q237), G305 (= G302), Y306 (≠ F303), Y376 (≠ F376), I426 (≠ D426), M430 (≠ A430)
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)
43% identity, 97% coverage: 12:445/447 of query aligns to 9:442/444 of P12425
- G59 (= G62) 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 (= R65) 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 (= E131) binding Mg(2+)
- E134 (= E133) binding Mg(2+)
- E189 (= E186) binding Mg(2+)
- V190 (≠ D187) 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 (= E193) binding Mg(2+)
- G241 (= G238) binding L-glutamate
- H245 (= H242) binding Mg(2+)
- G302 (= G302) 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 (= E304) 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 (= P306) 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 (= E336) binding Mg(2+)
- E424 (= E427) 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)
43% identity, 97% coverage: 12:445/447 of query aligns to 8:441/443 of 4lnkA
- active site: D52 (= D56), E131 (= E131), E133 (= E133), E188 (= E186), E195 (= E193), H244 (= H242), R315 (= R316), E332 (= E336), R334 (= R338)
- binding adenosine-5'-diphosphate: K43 (≠ T47), M50 (≠ T54), F198 (≠ L196), Y200 (≠ P198), N246 (≠ H244), S248 (≠ A246), S324 (≠ A328), S328 (≠ D332), R330 (≠ F334)
- binding glutamic acid: E133 (= E133), E188 (= E186), V189 (≠ D187), N239 (≠ Q237), G240 (= G238), G242 (= G240), E303 (= E304)
- binding magnesium ion: E131 (= E131), E188 (= E186), E195 (= E193), H244 (= H242), E332 (= E336)
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)
43% identity, 97% coverage: 12:445/447 of query aligns to 8:441/443 of 4lniA
- active site: D52 (= D56), E131 (= E131), E133 (= E133), E188 (= E186), E195 (= E193), H244 (= H242), R315 (= R316), E332 (= E336), R334 (= R338)
- binding adenosine-5'-diphosphate: E131 (= E131), E183 (≠ K181), D197 (= D195), Y200 (≠ P198), N246 (≠ H244), S248 (≠ A246), R320 (= R321), R330 (≠ F334)
- binding magnesium ion: E131 (= E131), E131 (= E131), E133 (= E133), E188 (= E186), E195 (= E193), E195 (= E193), H244 (= H242), E332 (= E336)
- binding l-methionine-s-sulfoximine phosphate: E133 (= E133), E188 (= E186), H244 (= H242), R297 (= R298), E303 (= E304), R315 (= R316), R334 (= R338)
8tfkA Glutamine synthetase (see paper)
42% identity, 98% coverage: 12:447/447 of query aligns to 6:440/440 of 8tfkA
- binding adenosine-5'-diphosphate: E128 (= E131), D194 (= D195), F195 (≠ L196), F197 (≠ P198), N243 (≠ H244), R312 (= R316), R317 (= R321), G325 (≠ D332), R327 (≠ F334)
- binding magnesium ion: E128 (= E131), E128 (= E131), E130 (= E133), E185 (= E186), E192 (= E193), E192 (= E193), H241 (= H242), E329 (= E336)
- binding l-methionine-s-sulfoximine phosphate: E128 (= E131), E130 (= E133), E185 (= E186), E192 (= E193), G237 (= G238), H241 (= H242), R294 (= R298), E300 (= E304), R312 (= R316), R331 (= R338)
7tenA Glutamine synthetase (see paper)
43% identity, 97% coverage: 12:446/447 of query aligns to 7:441/442 of 7tenA
- binding adenosine-5'-diphosphate: G128 (≠ A129), E130 (= E131), E182 (≠ K181), D196 (= D195), F197 (≠ L196), K198 (≠ A197), Y199 (≠ P198), N245 (≠ H244), S247 (≠ A246), R319 (= R321), S327 (≠ D332), R329 (≠ F334)
- binding l-methionine-s-sulfoximine phosphate: E130 (= E131), E132 (= E133), E187 (= E186), E194 (= E193), N238 (≠ Q237), G239 (= G238), H243 (= H242), R296 (= R298), E302 (= E304), R314 (= R316), R333 (= R338)
7tf9S L. Monocytogenes gs(14)-q-glnr peptide (see paper)
43% identity, 97% coverage: 12:446/447 of query aligns to 8:442/443 of 7tf9S
- binding glutamine: E133 (= E133), Y155 (= Y153), E188 (= E186), G240 (= G238), G242 (= G240), R297 (= R298), E303 (= E304)
- binding magnesium ion: E131 (= E131), E133 (= E133), E188 (= E186), E195 (= E193), H244 (= H242), E332 (= E336)
- binding : F59 (= F63), V60 (≠ S64), E418 (≠ R422), I422 (≠ D426), M426 (≠ A430)
7tdvC Glutamine synthetase (see paper)
40% identity, 98% coverage: 5:444/447 of query aligns to 1:440/443 of 7tdvC
- binding adenosine-5'-diphosphate: G129 (≠ A129), E131 (= E131), E183 (≠ K181), D197 (= D195), F198 (≠ L196), K199 (≠ A197), Y200 (≠ P198), N246 (≠ H244), V247 (≠ L245), S248 (≠ A246), R320 (= R321), S328 (≠ D332), R330 (≠ F334)
- binding magnesium ion: E131 (= E131), E131 (= E131), E133 (= E133), E188 (= E186), E195 (= E193), E195 (= E193), H244 (= H242), E332 (= E336)
- binding l-methionine-s-sulfoximine phosphate: E131 (= E131), E133 (= E133), E188 (= E186), E195 (= E193), G240 (= G238), H244 (= H242), R297 (= R298), E303 (= E304), R315 (= R316)
7tf6A Glutamine synthetase (see paper)
41% identity, 97% coverage: 12:444/447 of query aligns to 7:435/438 of 7tf6A
- binding glutamine: E128 (= E133), E183 (= E186), G235 (= G238), H239 (= H242), R292 (= R298), E298 (= E304)
- binding magnesium ion: E126 (= E131), E128 (= E133), E183 (= E186), E190 (= E193), H239 (= H242), E327 (= E336)
- binding : F58 (= F63), R60 (= R65), G232 (= G235), N234 (≠ Q237), G296 (= G302), Y297 (≠ F303), R310 (= R316), Y367 (≠ F376), Y421 (≠ A430), Q433 (≠ R442)
Sites not aligning to the query:
5zlpJ Crystal structure of glutamine synthetase from helicobacter pylori (see paper)
32% identity, 87% coverage: 15:404/447 of query aligns to 15:432/478 of 5zlpJ
- binding adenosine-5'-diphosphate: Y132 (≠ H127), E136 (= E131), F215 (≠ K181), F232 (≠ P198), H278 (= H244), S280 (≠ A246), R351 (= R321), R362 (= R329)
- binding magnesium ion: E138 (= E133), E220 (= E186), E227 (= E193)
- binding phosphinothricin: E138 (= E133), E220 (= E186), G272 (= G238), H276 (= H242), E334 (= E304), R346 (= R316), R366 (= R338)
5zlpL Crystal structure of glutamine synthetase from helicobacter pylori (see paper)
32% identity, 87% coverage: 15:404/447 of query aligns to 13:430/476 of 5zlpL
- binding adenosine-5'-diphosphate: G132 (≠ A129), E134 (= E131), F213 (≠ K181), F230 (≠ P198), H276 (= H244), S278 (≠ A246), R349 (= R321), R360 (= R329)
- binding magnesium ion: E136 (= E133), E218 (= E186), E225 (= E193)
- binding (2s)-2-amino-4-[methyl(phosphonooxy)phosphoryl]butanoic acid: E136 (= E133), E218 (= E186), G270 (= G238), H274 (= H242), E332 (= E304), R344 (= R316), R364 (= R338)
Query Sequence
>WP_015797716.1 NCBI__GCF_000023265.1:WP_015797716.1
MPDQRSVGVDYVRHMAEDRRVKFIQLWFTDVLGIPRAFQITQAELATALDEGMTFDGSAI
DGFSRIHEADVLAMPDPATFSVVPGLPSTARMFCDILNLDRTPFEGCPRNVLRRQIDRAR
QQGYLVHAAPELEYFYLRETTPGHWEPLDHGSYFELRLNDLGSELRREAVVVLEELGIPV
KHSQHEDAPSQHEIDLAPDEVLQMADAVISARLVVTETARAKGITASFMPKPFEGLQGSG
MHTHLALYDRHDEEHNAFFDPEAPDGLSRRARSFVAGLLRHAREITAVTNQWVNSYKRLV
PGFEAPMHVAWARNNRSALVRVPSPEAARGEDTFVEYRAPDAGANPYLALALMVAAGLQG
IEQGYELPPEVHDNLFTMPERELASLGIARLPQTLSEALEELEASPLVRSVLGDHVTEWF
LRNKRDEWRASASQVSDAERARYLTLI
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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