SitesBLAST
Comparing WP_005807771.1 NCBI__GCF_000021925.1:WP_005807771.1 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)
7tdvC Glutamine synthetase (see paper)
57% identity, 100% coverage: 3:442/442 of query aligns to 3:443/443 of 7tdvC
- binding adenosine-5'-diphosphate: G129 (= G128), E131 (= E130), E183 (= E182), D197 (= D196), F198 (= F197), K199 (= K198), Y200 (= Y199), N246 (= N245), V247 (≠ M246), S248 (= S247), R320 (= R319), S328 (≠ G327), R330 (= R329)
- binding magnesium ion: E131 (= E130), E131 (= E130), E133 (= E132), E188 (= E187), E195 (= E194), E195 (= E194), H244 (= H243), E332 (= E331)
- binding l-methionine-s-sulfoximine phosphate: E131 (= E130), E133 (= E132), E188 (= E187), E195 (= E194), G240 (= G239), H244 (= H243), R297 (= R296), E303 (= E302), R315 (= R314)
7tf6A Glutamine synthetase (see paper)
56% identity, 100% coverage: 3:442/442 of query aligns to 2:438/438 of 7tf6A
- binding glutamine: E128 (= E132), E183 (= E187), G235 (= G239), H239 (= H243), R292 (= R296), E298 (= E302)
- binding magnesium ion: E126 (= E130), E128 (= E132), E183 (= E187), E190 (= E194), H239 (= H243), E327 (= E331)
- binding : F58 (= F59), R60 (≠ G61), G232 (= G236), N234 (= N238), G296 (= G300), Y297 (= Y301), R310 (= R314), Y367 (= Y371), Y421 (≠ A425), Q433 (≠ S437), Q437 (≠ I441)
7tenA Glutamine synthetase (see paper)
56% identity, 100% coverage: 3:442/442 of query aligns to 2:442/442 of 7tenA
- binding adenosine-5'-diphosphate: G128 (= G128), E130 (= E130), E182 (= E182), D196 (= D196), F197 (= F197), K198 (= K198), Y199 (= Y199), N245 (= N245), S247 (= S247), R319 (= R319), S327 (≠ G327), R329 (= R329)
- binding l-methionine-s-sulfoximine phosphate: E130 (= E130), E132 (= E132), E187 (= E187), E194 (= E194), N238 (= N238), G239 (= G239), H243 (= H243), R296 (= R296), E302 (= E302), R314 (= R314), R333 (= R333)
7tf9S L. Monocytogenes gs(14)-q-glnr peptide (see paper)
56% identity, 100% coverage: 3:442/442 of query aligns to 3:443/443 of 7tf9S
- binding glutamine: E133 (= E132), Y155 (= Y154), E188 (= E187), G240 (= G239), G242 (= G241), R297 (= R296), E303 (= E302)
- binding magnesium ion: E131 (= E130), E133 (= E132), E188 (= E187), E195 (= E194), H244 (= H243), E332 (= E331)
- binding : F59 (= F59), V60 (≠ A60), E418 (≠ A417), I422 (≠ R421), M426 (≠ A425)
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)
54% identity, 100% coverage: 3:442/442 of query aligns to 4:444/444 of P12425
- G59 (= G58) 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 (≠ G61) 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 (= E130) binding Mg(2+)
- E134 (= E132) binding Mg(2+)
- E189 (= E187) binding Mg(2+)
- V190 (≠ S188) 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 (= E194) binding Mg(2+)
- G241 (= G239) binding L-glutamate
- H245 (= H243) 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 (= E302) 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 (= P304) 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 (= E331) binding Mg(2+)
- E424 (= E422) 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
4s0rD Structure of gs-tnra complex (see paper)
54% identity, 100% coverage: 3:442/442 of query aligns to 7:447/447 of 4s0rD
- active site: D56 (= D52), E135 (= E130), E137 (= E132), E192 (= E187), E199 (= E194), H248 (= H243), R319 (= R314), E336 (= E331), R338 (= R333)
- binding glutamine: E137 (= E132), E192 (= E187), R301 (= R296), E307 (= E302)
- binding magnesium ion: I66 (≠ V62), E135 (= E130), E135 (= E130), E199 (= E194), H248 (= H243), H248 (= H243), E336 (= E331), H419 (≠ K414)
- binding : F63 (= F59), V64 (≠ A60), R65 (≠ G61), I66 (≠ V62), D161 (= D156), G241 (= G236), V242 (= V237), N243 (= N238), G305 (= G300), Y306 (= Y301), Y376 (= Y371), I426 (≠ R421), M430 (≠ A425)
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)
54% identity, 100% coverage: 3:442/442 of query aligns to 3:443/443 of 4lnkA
- active site: D52 (= D52), E131 (= E130), E133 (= E132), E188 (= E187), E195 (= E194), H244 (= H243), R315 (= R314), E332 (= E331), R334 (= R333)
- binding adenosine-5'-diphosphate: K43 (≠ Q43), M50 (≠ L50), F198 (= F197), Y200 (= Y199), N246 (= N245), S248 (= S247), S324 (≠ P323), S328 (≠ G327), R330 (= R329)
- binding glutamic acid: E133 (= E132), E188 (= E187), V189 (≠ S188), N239 (= N238), G240 (= G239), G242 (= G241), E303 (= E302)
- binding magnesium ion: E131 (= E130), E188 (= E187), E195 (= E194), H244 (= H243), E332 (= E331)
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)
54% identity, 100% coverage: 3:442/442 of query aligns to 3:443/443 of 4lniA
- active site: D52 (= D52), E131 (= E130), E133 (= E132), E188 (= E187), E195 (= E194), H244 (= H243), R315 (= R314), E332 (= E331), R334 (= R333)
- binding adenosine-5'-diphosphate: E131 (= E130), E183 (= E182), D197 (= D196), Y200 (= Y199), N246 (= N245), S248 (= S247), R320 (= R319), R330 (= R329)
- binding magnesium ion: E131 (= E130), E131 (= E130), E133 (= E132), E188 (= E187), E195 (= E194), E195 (= E194), H244 (= H243), E332 (= E331)
- binding l-methionine-s-sulfoximine phosphate: E133 (= E132), E188 (= E187), H244 (= H243), R297 (= R296), E303 (= E302), R315 (= R314), R334 (= R333)
7tdpA Structure of paenibacillus polymyxa gs bound to met-sox-p-adp (transition state complex) to 1.98 angstom (see paper)
54% identity, 100% coverage: 2:442/442 of query aligns to 1:439/439 of 7tdpA
- binding adenosine-5'-diphosphate: N123 (≠ Q126), G125 (= G128), E127 (= E130), E179 (= E182), D193 (= D196), Y196 (= Y199), N242 (= N245), S244 (= S247), R316 (= R319), R326 (= R329)
- binding magnesium ion: E127 (= E130), E127 (= E130), E129 (= E132), E184 (= E187), E191 (= E194), E191 (= E194), H240 (= H243), E328 (= E331)
- binding l-methionine-s-sulfoximine phosphate: E127 (= E130), E129 (= E132), E184 (= E187), E191 (= E194), G236 (= G239), H240 (= H243), R293 (= R296), E299 (= E302), R311 (= R314), R330 (= R333)
7tfaB Glutamine synthetase (see paper)
54% identity, 100% coverage: 2:442/442 of query aligns to 1:441/441 of 7tfaB
- binding glutamine: E131 (= E132), Y153 (= Y154), E186 (= E187), G238 (= G239), H242 (= H243), R295 (= R296), E301 (= E302)
- binding magnesium ion: E129 (= E130), E131 (= E132), E186 (= E187), E193 (= E194), H242 (= H243), E330 (= E331)
- binding : Y58 (≠ F59), R60 (≠ G61), V187 (≠ S188), N237 (= N238), G299 (= G300), Y300 (= Y301), R313 (= R314), M424 (≠ A425)
8ufjB Glutamine synthetase (see paper)
53% identity, 99% coverage: 4:441/442 of query aligns to 6:443/444 of 8ufjB
8tfkA Glutamine synthetase (see paper)
53% identity, 99% coverage: 4:441/442 of query aligns to 2:439/440 of 8tfkA
- binding adenosine-5'-diphosphate: E128 (= E130), D194 (= D196), F195 (= F197), F197 (≠ Y199), N243 (= N245), R312 (= R314), R317 (= R319), G325 (= G327), R327 (= R329)
- binding magnesium ion: E128 (= E130), E128 (= E130), E130 (= E132), E185 (= E187), E192 (= E194), E192 (= E194), H241 (= H243), E329 (= E331)
- binding l-methionine-s-sulfoximine phosphate: E128 (= E130), E130 (= E132), E185 (= E187), E192 (= E194), G237 (= G239), H241 (= H243), R294 (= R296), E300 (= E302), R312 (= R314), R331 (= R333)
8ooxB Glutamine synthetase (see paper)
53% identity, 99% coverage: 5:442/442 of query aligns to 3:438/438 of 8ooxB
8oozA Glutamine synthetase (see paper)
53% identity, 99% coverage: 5:442/442 of query aligns to 3:430/430 of 8oozA
- binding adenosine-5'-triphosphate: G117 (= G128), E170 (= E182), F185 (= F197), K186 (= K198), Y187 (= Y199), N233 (= N245), S235 (= S247), S315 (≠ G327), R317 (= R329)
- binding magnesium ion: E119 (= E130), H231 (= H243), E319 (= E331)
8oooA Glutamine synthetase from methanothermococcus thermolithotrophicus in complex with 2-oxoglutarate and mgatp at 2.15 a resolution (see paper)
48% identity, 99% coverage: 4:441/442 of query aligns to 2:447/447 of 8oooA
- binding 2-oxoglutaric acid: F17 (= F19), R19 (= R21), A33 (= A35), R87 (= R82), V93 (= V88), P170 (≠ E164), R173 (= R167), R174 (= R168), S190 (= S184)
- binding adenosine-5'-triphosphate: E136 (= E130), E188 (= E182), F203 (= F197), K204 (= K198), F205 (≠ Y199), H251 (≠ N245), S253 (= S247), R325 (= R319), R335 (= R329)
8ooqB Glutamine synthetase from Methanothermococcus thermolithotrophicus (see paper)
48% identity, 99% coverage: 4:441/442 of query aligns to 1:446/446 of 8ooqB
- binding 2-oxoglutaric acid: F16 (= F19), R18 (= R21), A32 (= A35), R86 (= R82), V92 (= V88), P169 (≠ E164), R172 (= R167), R173 (= R168), S189 (= S184)
- binding magnesium ion: E137 (= E132), E192 (= E187), E199 (= E194)
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)
45% identity, 100% coverage: 1:441/442 of query aligns to 1:446/446 of A0R083
- K363 (≠ R358) 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)
45% identity, 100% coverage: 1:441/442 of query aligns to 1:446/446 of P9WN37
- K363 (≠ R358) 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)
38% identity, 99% coverage: 4:441/442 of query aligns to 1:468/468 of 1fpyA
- binding adenosine-5'-diphosphate: G127 (= G128), E129 (= E130), E207 (= E182), T223 (≠ F197), F225 (≠ Y199), H271 (≠ N245), S273 (= S247), R355 (= R329), E357 (= E331)
- binding manganese (ii) ion: E129 (= E130), E131 (= E132), E212 (= E187), E220 (= E194), H269 (= H243), E357 (= E331)
- binding phosphinothricin: E131 (= E132), E212 (= E187), G265 (= G239), H269 (= H243), R321 (= R296), E327 (= E302), R359 (= R333)
1f1hA Crystal structure of glutamine synthetase from salmonella typhimurium with thallium ions (see paper)
38% identity, 99% coverage: 4:441/442 of query aligns to 1:468/468 of 1f1hA
- binding adenosine-5'-diphosphate: E129 (= E130), E207 (= E182), H210 (= H185), E220 (= E194), T223 (≠ F197), F225 (≠ Y199), H271 (≠ N245), S273 (= S247), R355 (= R329)
- binding manganese (ii) ion: E129 (= E130), E131 (= E132), E212 (= E187), E220 (= E194), H269 (= H243), E357 (= E331)
Query Sequence
>WP_005807771.1 NCBI__GCF_000021925.1:WP_005807771.1
MGFTKEECLKYVQENDVRFIRMQFTDIFGQMKNIAITHNQLAQALDEGVLFDGSAIKGFA
GVEASDMLLLPDPSTFTLIPWRPQQGKVARIICDVKNHDGSQFEGDPRYILKRTLQKAHD
LGYVFQVGPECEFFLFHTDEEGQPTTITHDAAGYCDLAPIDQGENTRREICLVLEEMGFE
IETSHHESAAGQHEIDFKYTDALTAADHIMTFKYVVKIVSQRNGLHATFMPKPLHGVNGS
GMHINMSLAKEGRNVFIHPENPGELSETAKQFIAGLLEHIKGITAVANPLVNSYKRLTPG
YEAPVHIAWSPMNRSPLLRVPSPRGAGTRLELRSPDPSCNPYLTLALLLEAGLDGLQREM
KVPEPVNENIYNLTPEQEKALSLERLPSNLLLALEEMEKDPLIQATLGRHIFTKYIAAKA
REWKAYDEMVHQWEIDSYLKIY
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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