SitesBLAST
Comparing WP_015738418.1 NCBI__GCF_000024605.1:WP_015738418.1 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)
4s0rD Structure of gs-tnra complex (see paper)
66% identity, 99% coverage: 7:444/444 of query aligns to 9:447/447 of 4s0rD
- active site: D56 (= D54), E135 (= E132), E137 (= E134), E192 (= E189), E199 (= E196), H248 (= H245), R319 (= R316), E336 (= E333), R338 (= R335)
- binding glutamine: E137 (= E134), E192 (= E189), R301 (= R298), E307 (= E304)
- binding magnesium ion: I66 (= I64), E135 (= E132), E135 (= E132), E199 (= E196), H248 (= H245), H248 (= H245), E336 (= E333), H419 (≠ K416)
- binding : F63 (= F61), V64 (= V62), R65 (= R63), I66 (= I64), D161 (= D158), G241 (= G238), V242 (= V239), N243 (= N240), G305 (= G302), Y306 (= Y303), Y376 (= Y373), I426 (≠ K423), M430 (≠ E427)
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)
66% identity, 99% coverage: 7:444/444 of query aligns to 6:444/444 of P12425
- G59 (= G60) 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 (= R63) 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 (= E132) binding Mg(2+)
- E134 (= E134) binding Mg(2+)
- E189 (= E189) binding Mg(2+)
- V190 (= V190) 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 (= E196) binding Mg(2+)
- G241 (= G241) binding L-glutamate
- H245 (= H245) 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 (= E333) binding Mg(2+)
- E424 (= E424) 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)
66% identity, 99% coverage: 7:444/444 of query aligns to 5:443/443 of 4lnkA
- active site: D52 (= D54), E131 (= E132), E133 (= E134), E188 (= E189), E195 (= E196), H244 (= H245), R315 (= R316), E332 (= E333), R334 (= R335)
- binding adenosine-5'-diphosphate: K43 (= K45), M50 (= M52), F198 (= F199), Y200 (= Y201), N246 (= N247), S248 (= S249), S324 (≠ K325), S328 (= S329), R330 (= R331)
- binding glutamic acid: E133 (= E134), E188 (= E189), V189 (= V190), N239 (= N240), G240 (= G241), G242 (= G243), E303 (= E304)
- binding magnesium ion: E131 (= E132), E188 (= E189), E195 (= E196), H244 (= H245), E332 (= E333)
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)
66% identity, 99% coverage: 7:444/444 of query aligns to 5:443/443 of 4lniA
- active site: D52 (= D54), E131 (= E132), E133 (= E134), E188 (= E189), E195 (= E196), H244 (= H245), R315 (= R316), E332 (= E333), R334 (= R335)
- binding adenosine-5'-diphosphate: E131 (= E132), E183 (= E184), D197 (= D198), Y200 (= Y201), N246 (= N247), S248 (= S249), R320 (= R321), R330 (= R331)
- binding magnesium ion: E131 (= E132), E131 (= E132), E133 (= E134), E188 (= E189), E195 (= E196), E195 (= E196), H244 (= H245), E332 (= E333)
- binding l-methionine-s-sulfoximine phosphate: E133 (= E134), E188 (= E189), H244 (= H245), R297 (= R298), E303 (= E304), R315 (= R316), R334 (= R335)
7tdpA Structure of paenibacillus polymyxa gs bound to met-sox-p-adp (transition state complex) to 1.98 angstom (see paper)
65% identity, 99% coverage: 7:444/444 of query aligns to 4:439/439 of 7tdpA
- binding adenosine-5'-diphosphate: N123 (= N128), G125 (= G130), E127 (= E132), E179 (= E184), D193 (= D198), Y196 (= Y201), N242 (= N247), S244 (= S249), R316 (= R321), R326 (= R331)
- binding magnesium ion: E127 (= E132), E127 (= E132), E129 (= E134), E184 (= E189), E191 (= E196), E191 (= E196), H240 (= H245), E328 (= E333)
- binding l-methionine-s-sulfoximine phosphate: E127 (= E132), E129 (= E134), E184 (= E189), E191 (= E196), G236 (= G241), H240 (= H245), R293 (= R298), E299 (= E304), R311 (= R316), R330 (= R335)
7tf9S L. Monocytogenes gs(14)-q-glnr peptide (see paper)
65% identity, 99% coverage: 7:444/444 of query aligns to 5:443/443 of 7tf9S
- binding glutamine: E133 (= E134), Y155 (= Y156), E188 (= E189), G240 (= G241), G242 (= G243), R297 (= R298), E303 (= E304)
- binding magnesium ion: E131 (= E132), E133 (= E134), E188 (= E189), E195 (= E196), H244 (= H245), E332 (= E333)
- binding : F59 (= F61), V60 (= V62), E418 (= E419), I422 (≠ K423), M426 (≠ E427)
7tenA Glutamine synthetase (see paper)
65% identity, 99% coverage: 7:444/444 of query aligns to 4:442/442 of 7tenA
- binding adenosine-5'-diphosphate: G128 (= G130), E130 (= E132), E182 (= E184), D196 (= D198), F197 (= F199), K198 (= K200), Y199 (= Y201), N245 (= N247), S247 (= S249), R319 (= R321), S327 (= S329), R329 (= R331)
- binding l-methionine-s-sulfoximine phosphate: E130 (= E132), E132 (= E134), E187 (= E189), E194 (= E196), N238 (= N240), G239 (= G241), H243 (= H245), R296 (= R298), E302 (= E304), R314 (= R316), R333 (= R335)
7tfaB Glutamine synthetase (see paper)
65% identity, 99% coverage: 7:444/444 of query aligns to 4:441/441 of 7tfaB
- binding glutamine: E131 (= E134), Y153 (= Y156), E186 (= E189), G238 (= G241), H242 (= H245), R295 (= R298), E301 (= E304)
- binding magnesium ion: E129 (= E132), E131 (= E134), E186 (= E189), E193 (= E196), H242 (= H245), E330 (= E333)
- binding : Y58 (≠ F61), R60 (= R63), V187 (= V190), N237 (= N240), G299 (= G302), Y300 (= Y303), R313 (= R316), M424 (≠ E427)
7tdvC Glutamine synthetase (see paper)
63% identity, 99% coverage: 7:444/444 of query aligns to 5:443/443 of 7tdvC
- binding adenosine-5'-diphosphate: G129 (= G130), E131 (= E132), E183 (= E184), D197 (= D198), F198 (= F199), K199 (= K200), Y200 (= Y201), N246 (= N247), V247 (≠ L248), S248 (= S249), R320 (= R321), S328 (= S329), R330 (= R331)
- binding magnesium ion: E131 (= E132), E131 (= E132), E133 (= E134), E188 (= E189), E195 (= E196), E195 (= E196), H244 (= H245), E332 (= E333)
- binding l-methionine-s-sulfoximine phosphate: E131 (= E132), E133 (= E134), E188 (= E189), E195 (= E196), G240 (= G241), H244 (= H245), R297 (= R298), E303 (= E304), R315 (= R316)
7tf6A Glutamine synthetase (see paper)
63% identity, 99% coverage: 7:444/444 of query aligns to 4:438/438 of 7tf6A
- binding glutamine: E128 (= E134), E183 (= E189), G235 (= G241), H239 (= H245), R292 (= R298), E298 (= E304)
- binding magnesium ion: E126 (= E132), E128 (= E134), E183 (= E189), E190 (= E196), H239 (= H245), E327 (= E333)
- binding : F58 (= F61), R60 (= R63), G232 (= G238), N234 (= N240), G296 (= G302), Y297 (= Y303), R310 (= R316), Y367 (= Y373), Y421 (≠ E427), Q433 (≠ T439), Q437 (≠ R443)
8ooxB Glutamine synthetase (see paper)
63% identity, 99% coverage: 6:444/444 of query aligns to 2:438/438 of 8ooxB
8ufjB Glutamine synthetase (see paper)
61% identity, 99% coverage: 1:441/444 of query aligns to 1:441/444 of 8ufjB
8tfkA Glutamine synthetase (see paper)
61% identity, 98% coverage: 7:441/444 of query aligns to 3:437/440 of 8tfkA
- binding adenosine-5'-diphosphate: E128 (= E132), D194 (= D198), F195 (= F199), F197 (≠ Y201), N243 (= N247), R312 (= R316), R317 (= R321), G325 (≠ S329), R327 (= R331)
- binding magnesium ion: E128 (= E132), E128 (= E132), E130 (= E134), E185 (= E189), E192 (= E196), E192 (= E196), H241 (= H245), E329 (= E333)
- binding l-methionine-s-sulfoximine phosphate: E128 (= E132), E130 (= E134), E185 (= E189), E192 (= E196), G237 (= G241), H241 (= H245), R294 (= R298), E300 (= E304), R312 (= R316), R331 (= R335)
8oozA Glutamine synthetase (see paper)
61% identity, 99% coverage: 6:444/444 of query aligns to 2:430/430 of 8oozA
- binding adenosine-5'-triphosphate: G117 (= G130), E170 (= E184), F185 (= F199), K186 (= K200), Y187 (= Y201), N233 (= N247), S235 (= S249), S315 (= S329), R317 (= R331)
- binding magnesium ion: E119 (= E132), H231 (= H245), E319 (= E333)
8ooqB Glutamine synthetase from Methanothermococcus thermolithotrophicus (see paper)
56% identity, 98% coverage: 8:441/444 of query aligns to 3:444/446 of 8ooqB
- binding 2-oxoglutaric acid: F16 (= F21), R18 (= R23), A32 (= A37), R86 (= R84), V92 (= V90), P169 (≠ E166), R172 (= R169), R173 (= R170), S189 (= S186)
- binding magnesium ion: E137 (= E134), E192 (= E189), E199 (= E196)
8oooA Glutamine synthetase from methanothermococcus thermolithotrophicus in complex with 2-oxoglutarate and mgatp at 2.15 a resolution (see paper)
56% identity, 98% coverage: 8:441/444 of query aligns to 4:445/447 of 8oooA
- binding 2-oxoglutaric acid: F17 (= F21), R19 (= R23), A33 (= A37), R87 (= R84), V93 (= V90), P170 (≠ E166), R173 (= R169), R174 (= R170), S190 (= S186)
- binding adenosine-5'-triphosphate: E136 (= E132), E188 (= E184), F203 (= F199), K204 (= K200), F205 (≠ Y201), H251 (≠ N247), S253 (= S249), R325 (= R321), R335 (= R331)
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: 6:441/444 of query aligns to 4:444/446 of A0R083
- K363 (≠ N360) 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)
47% identity, 98% coverage: 6:441/444 of query aligns to 4:444/446 of P9WN37
- K363 (≠ N360) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
P0A9C5 Glutamine synthetase; GS; Glutamate--ammonia ligase; Glutamine synthetase I beta; GSI beta; EC 6.3.1.2 from Escherichia coli (strain K12) (see 3 papers)
44% identity, 98% coverage: 5:440/444 of query aligns to 1:466/469 of P0A9C5
- M1 (= M5) modified: Initiator methionine, Removed
- Y398 (= Y373) modified: O-AMP-tyrosine
1fpyA Crystal structure of glutamine synthetase from salmonella typhimurium with inhibitor phosphinothricin (see paper)
44% identity, 98% coverage: 8:440/444 of query aligns to 3:465/468 of 1fpyA
- binding adenosine-5'-diphosphate: G127 (= G130), E129 (= E132), E207 (= E184), T223 (≠ F199), F225 (≠ Y201), H271 (≠ N247), S273 (= S249), R355 (= R331), E357 (= E333)
- binding manganese (ii) ion: E129 (= E132), E131 (= E134), E212 (= E189), E220 (= E196), H269 (= H245), E357 (= E333)
- binding phosphinothricin: E131 (= E134), E212 (= E189), G265 (= G241), H269 (= H245), R321 (= R298), E327 (= E304), R359 (= R335)
Query Sequence
>WP_015738418.1 NCBI__GCF_000024605.1:WP_015738418.1
MEELMKREEVLRRAREEGVKFIRLQFTDILGVLKNVAIPIDQLEKALNGELMFDGSSIEG
FVRIEESDMYLRPDPRTFVILPWRPREGAVARLICDVYNPDGTPFLGDPRYALKRVLEEA
AELGYTCNAGPELEFFLFHLDEKGQPTTITHDQASYFDLSPIDLGEEARREIILTLEKMG
FEIEASHHEVAPGQHEIDFKYSDALDVADKIMTFKMVVRVIAQRHGLHATFMPKPLYGVN
GSGMHTNLSLSRNGENAFYDPDRPLQLSEVAYYFIGGIIKHIKAITAVTNPTVNSYKRLV
PGYEAPVYIAWSCRNRSPLIRIPAKRGPSTRIELRSPDPSCNPYLALAAIIKAGLDGIKN
KIEPPPPVDRNIYELSAEERKALGIDCLPGSLIEALQELEKDEVIKEALGPHIYEKFMEA
KLKEWHEYSTRVHPWEIETYLVRY
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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