SitesBLAST
Comparing WP_010877179.1 NCBI__GCF_000008645.1:WP_010877179.1 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)
8ooqB Glutamine synthetase from Methanothermococcus thermolithotrophicus (see paper)
56% identity, 99% coverage: 5:442/442 of query aligns to 2:446/446 of 8ooqB
- binding 2-oxoglutaric acid: F16 (= F19), R18 (= R21), A32 (= A35), R86 (= R85), V92 (= V91), P169 (≠ T165), R172 (= R168), R173 (= R169), S189 (= S185)
- binding magnesium ion: E137 (= E135), E192 (= E188), E199 (= E195)
8oooA Glutamine synthetase from methanothermococcus thermolithotrophicus in complex with 2-oxoglutarate and mgatp at 2.15 a resolution (see paper)
56% identity, 99% coverage: 5:442/442 of query aligns to 3:447/447 of 8oooA
- binding 2-oxoglutaric acid: F17 (= F19), R19 (= R21), A33 (= A35), R87 (= R85), V93 (= V91), P170 (≠ T165), R173 (= R168), R174 (= R169), S190 (= S185)
- binding adenosine-5'-triphosphate: E136 (= E133), E188 (= E183), F203 (= F198), K204 (= K199), F205 (= F200), H251 (= H246), S253 (= S248), R325 (= R320), R335 (= R330)
8ufjB Glutamine synthetase (see paper)
55% identity, 98% coverage: 8:442/442 of query aligns to 10:443/444 of 8ufjB
8tfkA Glutamine synthetase (see paper)
54% identity, 98% coverage: 8:442/442 of query aligns to 6:439/440 of 8tfkA
- binding adenosine-5'-diphosphate: E128 (= E133), D194 (= D197), F195 (= F198), F197 (= F200), N243 (≠ H246), R312 (= R315), R317 (= R320), G325 (= G328), R327 (= R330)
- binding magnesium ion: E128 (= E133), E128 (= E133), E130 (= E135), E185 (= E188), E192 (= E195), E192 (= E195), H241 (= H244), E329 (= E332)
- binding l-methionine-s-sulfoximine phosphate: E128 (= E133), E130 (= E135), E185 (= E188), E192 (= E195), G237 (= G240), H241 (= H244), R294 (= R297), E300 (= E303), R312 (= R315), R331 (= R334)
8ooxB Glutamine synthetase (see paper)
54% identity, 99% coverage: 3:440/442 of query aligns to 4:435/438 of 8ooxB
8oozA Glutamine synthetase (see paper)
54% identity, 99% coverage: 3:440/442 of query aligns to 4:427/430 of 8oozA
- binding adenosine-5'-triphosphate: G117 (= G131), E170 (= E183), F185 (= F198), K186 (= K199), Y187 (≠ F200), N233 (≠ H246), S235 (= S248), S315 (≠ G328), R317 (= R330)
- binding magnesium ion: E119 (= E133), H231 (= H244), E319 (= E332)
7tdvC Glutamine synthetase (see paper)
52% identity, 97% coverage: 12:440/442 of query aligns to 12:440/443 of 7tdvC
- binding adenosine-5'-diphosphate: G129 (= G131), E131 (= E133), E183 (= E183), D197 (= D197), F198 (= F198), K199 (= K199), Y200 (≠ F200), N246 (≠ H246), V247 (≠ Q247), S248 (= S248), R320 (= R320), S328 (≠ G328), R330 (= R330)
- binding magnesium ion: E131 (= E133), E131 (= E133), E133 (= E135), E188 (= E188), E195 (= E195), E195 (= E195), H244 (= H244), E332 (= E332)
- binding l-methionine-s-sulfoximine phosphate: E131 (= E133), E133 (= E135), E188 (= E188), E195 (= E195), G240 (= G240), H244 (= H244), R297 (= R297), E303 (= E303), R315 (= R315)
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)
52% identity, 97% coverage: 12:440/442 of query aligns to 12:440/443 of 4lnkA
- active site: D52 (= D55), E131 (= E133), E133 (= E135), E188 (= E188), E195 (= E195), H244 (= H244), R315 (= R315), E332 (= E332), R334 (= R334)
- binding adenosine-5'-diphosphate: K43 (≠ D46), M50 (≠ L53), F198 (= F198), Y200 (≠ F200), N246 (≠ H246), S248 (= S248), S324 (= S324), S328 (≠ G328), R330 (= R330)
- binding glutamic acid: E133 (= E135), E188 (= E188), V189 (= V189), N239 (= N239), G240 (= G240), G242 (= G242), E303 (= E303)
- binding magnesium ion: E131 (= E133), E188 (= E188), E195 (= E195), H244 (= H244), E332 (= E332)
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)
52% identity, 97% coverage: 12:440/442 of query aligns to 12:440/443 of 4lniA
- active site: D52 (= D55), E131 (= E133), E133 (= E135), E188 (= E188), E195 (= E195), H244 (= H244), R315 (= R315), E332 (= E332), R334 (= R334)
- binding adenosine-5'-diphosphate: E131 (= E133), E183 (= E183), D197 (= D197), Y200 (≠ F200), N246 (≠ H246), S248 (= S248), R320 (= R320), R330 (= R330)
- binding magnesium ion: E131 (= E133), E131 (= E133), E133 (= E135), E188 (= E188), E195 (= E195), E195 (= E195), H244 (= H244), E332 (= E332)
- binding l-methionine-s-sulfoximine phosphate: E133 (= E135), E188 (= E188), H244 (= H244), R297 (= R297), E303 (= E303), R315 (= R315), R334 (= R334)
4s0rD Structure of gs-tnra complex (see paper)
52% identity, 97% coverage: 12:440/442 of query aligns to 16:444/447 of 4s0rD
- active site: D56 (= D55), E135 (= E133), E137 (= E135), E192 (= E188), E199 (= E195), H248 (= H244), R319 (= R315), E336 (= E332), R338 (= R334)
- binding glutamine: E137 (= E135), E192 (= E188), R301 (= R297), E307 (= E303)
- binding magnesium ion: I66 (= I65), E135 (= E133), E135 (= E133), E199 (= E195), H248 (= H244), H248 (= H244), E336 (= E332), H419 (≠ K415)
- binding : F63 (= F62), V64 (= V63), R65 (≠ D64), I66 (= I65), D161 (= D157), G241 (= G237), V242 (≠ E238), N243 (= N239), G305 (= G301), Y306 (= Y302), Y376 (= Y372), I426 (≠ R422), M430 (≠ D426)
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)
52% identity, 97% coverage: 12:440/442 of query aligns to 13:441/444 of P12425
- G59 (= G61) 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 (≠ D64) 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 (= E133) binding Mg(2+)
- E134 (= E135) binding Mg(2+)
- E189 (= E188) binding Mg(2+)
- V190 (= V189) 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 (= E195) binding Mg(2+)
- G241 (= G240) binding L-glutamate
- H245 (= H244) binding Mg(2+)
- G302 (= G301) 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 (= E303) 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 (= E332) binding Mg(2+)
- E424 (= E423) 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
7tfaB Glutamine synthetase (see paper)
52% identity, 98% coverage: 8:442/442 of query aligns to 7:440/441 of 7tfaB
- binding glutamine: E131 (= E135), Y153 (= Y155), E186 (= E188), G238 (= G240), H242 (= H244), R295 (= R297), E301 (= E303)
- binding magnesium ion: E129 (= E133), E131 (= E135), E186 (= E188), E193 (= E195), H242 (= H244), E330 (= E332)
- binding : Y58 (≠ F62), R60 (≠ D64), V187 (= V189), N237 (= N239), G299 (= G301), Y300 (= Y302), R313 (= R315), M424 (≠ D426)
7tdpA Structure of paenibacillus polymyxa gs bound to met-sox-p-adp (transition state complex) to 1.98 angstom (see paper)
52% identity, 98% coverage: 8:442/442 of query aligns to 7:438/439 of 7tdpA
- binding adenosine-5'-diphosphate: N123 (= N129), G125 (= G131), E127 (= E133), E179 (= E183), D193 (= D197), Y196 (≠ F200), N242 (≠ H246), S244 (= S248), R316 (= R320), R326 (= R330)
- binding magnesium ion: E127 (= E133), E127 (= E133), E129 (= E135), E184 (= E188), E191 (= E195), E191 (= E195), H240 (= H244), E328 (= E332)
- binding l-methionine-s-sulfoximine phosphate: E127 (= E133), E129 (= E135), E184 (= E188), E191 (= E195), G236 (= G240), H240 (= H244), R293 (= R297), E299 (= E303), R311 (= R315), R330 (= R334)
7tf6A Glutamine synthetase (see paper)
52% identity, 97% coverage: 13:440/442 of query aligns to 12:435/438 of 7tf6A
- binding glutamine: E128 (= E135), E183 (= E188), G235 (= G240), H239 (= H244), R292 (= R297), E298 (= E303)
- binding magnesium ion: E126 (= E133), E128 (= E135), E183 (= E188), E190 (= E195), H239 (= H244), E327 (= E332)
- binding : F58 (= F62), R60 (≠ D64), G232 (= G237), N234 (= N239), G296 (= G301), Y297 (= Y302), R310 (= R315), Y367 (= Y372), Y421 (≠ D426), Q433 (≠ R438)
Sites not aligning to the query:
7tf9S L. Monocytogenes gs(14)-q-glnr peptide (see paper)
51% identity, 97% coverage: 13:442/442 of query aligns to 13:442/443 of 7tf9S
- binding glutamine: E133 (= E135), Y155 (= Y155), E188 (= E188), G240 (= G240), G242 (= G242), R297 (= R297), E303 (= E303)
- binding magnesium ion: E131 (= E133), E133 (= E135), E188 (= E188), E195 (= E195), H244 (= H244), E332 (= E332)
- binding : F59 (= F62), V60 (= V63), E418 (= E418), I422 (≠ R422), M426 (≠ D426)
7tenA Glutamine synthetase (see paper)
51% identity, 97% coverage: 13:442/442 of query aligns to 12:441/442 of 7tenA
- binding adenosine-5'-diphosphate: G128 (= G131), E130 (= E133), E182 (= E183), D196 (= D197), F197 (= F198), K198 (= K199), Y199 (≠ F200), N245 (≠ H246), S247 (= S248), R319 (= R320), S327 (≠ G328), R329 (= R330)
- binding l-methionine-s-sulfoximine phosphate: E130 (= E133), E132 (= E135), E187 (= E188), E194 (= E195), N238 (= N239), G239 (= G240), H243 (= H244), R296 (= R297), E302 (= E303), R314 (= R315), R333 (= R334)
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)
44% identity, 98% coverage: 8:442/442 of query aligns to 8:446/446 of P9WN37
- K363 (≠ N359) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
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)
43% identity, 98% coverage: 8:442/442 of query aligns to 8:446/446 of A0R083
- K363 (≠ N359) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
1fpyA Crystal structure of glutamine synthetase from salmonella typhimurium with inhibitor phosphinothricin (see paper)
40% identity, 98% coverage: 8:442/442 of query aligns to 5:468/468 of 1fpyA
- binding adenosine-5'-diphosphate: G127 (= G131), E129 (= E133), E207 (= E183), T223 (≠ F198), F225 (= F200), H271 (= H246), S273 (= S248), R355 (= R330), E357 (= E332)
- binding manganese (ii) ion: E129 (= E133), E131 (= E135), E212 (= E188), E220 (= E195), H269 (= H244), E357 (= E332)
- binding phosphinothricin: E131 (= E135), E212 (= E188), G265 (= G240), H269 (= H244), R321 (= R297), E327 (= E303), R359 (= R334)
1f1hA Crystal structure of glutamine synthetase from salmonella typhimurium with thallium ions (see paper)
40% identity, 98% coverage: 8:442/442 of query aligns to 5:468/468 of 1f1hA
- binding adenosine-5'-diphosphate: E129 (= E133), E207 (= E183), H210 (= H186), E220 (= E195), T223 (≠ F198), F225 (= F200), H271 (= H246), S273 (= S248), R355 (= R330)
- binding manganese (ii) ion: E129 (= E133), E131 (= E135), E212 (= E188), E220 (= E195), H269 (= H244), E357 (= E332)
Query Sequence
>WP_010877179.1 NCBI__GCF_000008645.1:WP_010877179.1
MSDKIGRIIAKMDECGVKFVRLQFVDIHGKPKNMAIPLVRPDQIEDIIKDGLLFDGSSVE
GFVDINESDLVLKPDPDTFSTLPWRPEEKGVCRFICDIYWPDGKPFEGDPRYVLKRALDK
YAHLGYEYNVGPEPEFFILDQDEDGNIIPHDCGAYFDVEPVDQGTDFRRKLVMDLEALNF
DVEVSHHEVAPGQHEIDFKFDKALKTADAVITFKQAIKAIVDKIGYMVTFMPKPFFGENG
SGMHCHQSLFKDGENVFYDPDTETQLSEEALYFIGGLLKHAPALTAVCAPTVNSYKRLVP
GYEAPVYIAYGLKNRSTLIRIPASRGKGTRVELRMPDPSCNPYLAFAAMLEAGMNGIQNK
IDPGEPTEIDVYEKSMSELREMGIETLPSSLWEAYHALEEDDVIKGALGGHVYEKFMEIK
HREWDDYRVRVFKYELERYLDI
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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