SitesBLAST
Comparing WP_013075638.1 NCBI__GCF_000092905.1:WP_013075638.1 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)
7tfaB Glutamine synthetase (see paper)
77% identity, 99% coverage: 5:446/446 of query aligns to 2:441/441 of 7tfaB
- binding glutamine: E131 (= E136), Y153 (= Y158), E186 (= E191), G238 (= G243), H242 (= H247), R295 (= R300), E301 (= E306)
- binding magnesium ion: E129 (= E134), E131 (= E136), E186 (= E191), E193 (= E198), H242 (= H247), E330 (= E335)
- binding : Y58 (≠ F61), R60 (= R63), V187 (= V192), N237 (= N242), G299 (= G304), Y300 (= Y305), R313 (= R318), M424 (= M429)
7tdpA Structure of paenibacillus polymyxa gs bound to met-sox-p-adp (transition state complex) to 1.98 angstom (see paper)
77% identity, 99% coverage: 5:446/446 of query aligns to 2:439/439 of 7tdpA
- binding adenosine-5'-diphosphate: N123 (= N130), G125 (= G132), E127 (= E134), E179 (= E186), D193 (= D200), Y196 (= Y203), N242 (≠ H249), S244 (= S251), R316 (= R323), R326 (= R333)
- binding magnesium ion: E127 (= E134), E127 (= E134), E129 (= E136), E184 (= E191), E191 (= E198), E191 (= E198), H240 (= H247), E328 (= E335)
- binding l-methionine-s-sulfoximine phosphate: E127 (= E134), E129 (= E136), E184 (= E191), E191 (= E198), G236 (= G243), H240 (= H247), R293 (= R300), E299 (= E306), R311 (= R318), R330 (= R337)
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)
73% identity, 99% coverage: 4:446/446 of query aligns to 3:444/444 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 (= E134) binding Mg(2+)
- E134 (= E136) binding Mg(2+)
- E189 (= E191) binding Mg(2+)
- V190 (= V192) 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 (= E198) binding Mg(2+)
- G241 (= G243) binding L-glutamate
- H245 (= H247) binding Mg(2+)
- G302 (= G304) 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 (= E306) 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 (= P308) 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 (= E335) binding Mg(2+)
- E424 (= E426) 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)
73% identity, 99% coverage: 4:446/446 of query aligns to 2:443/443 of 4lnkA
- active site: D52 (= D54), E131 (= E134), E133 (= E136), E188 (= E191), E195 (= E198), H244 (= H247), R315 (= R318), E332 (= E335), R334 (= R337)
- binding adenosine-5'-diphosphate: K43 (= K45), M50 (= M52), F198 (= F201), Y200 (= Y203), N246 (≠ H249), S248 (= S251), S324 (= S327), S328 (= S331), R330 (= R333)
- binding glutamic acid: E133 (= E136), E188 (= E191), V189 (= V192), N239 (= N242), G240 (= G243), G242 (= G245), E303 (= E306)
- binding magnesium ion: E131 (= E134), E188 (= E191), E195 (= E198), H244 (= H247), E332 (= E335)
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)
73% identity, 99% coverage: 4:446/446 of query aligns to 2:443/443 of 4lniA
- active site: D52 (= D54), E131 (= E134), E133 (= E136), E188 (= E191), E195 (= E198), H244 (= H247), R315 (= R318), E332 (= E335), R334 (= R337)
- binding adenosine-5'-diphosphate: E131 (= E134), E183 (= E186), D197 (= D200), Y200 (= Y203), N246 (≠ H249), S248 (= S251), R320 (= R323), R330 (= R333)
- binding magnesium ion: E131 (= E134), E131 (= E134), E133 (= E136), E188 (= E191), E195 (= E198), E195 (= E198), H244 (= H247), E332 (= E335)
- binding l-methionine-s-sulfoximine phosphate: E133 (= E136), E188 (= E191), H244 (= H247), R297 (= R300), E303 (= E306), R315 (= R318), R334 (= R337)
4s0rD Structure of gs-tnra complex (see paper)
73% identity, 99% coverage: 4:446/446 of query aligns to 6:447/447 of 4s0rD
- active site: D56 (= D54), E135 (= E134), E137 (= E136), E192 (= E191), E199 (= E198), H248 (= H247), R319 (= R318), E336 (= E335), R338 (= R337)
- binding glutamine: E137 (= E136), E192 (= E191), R301 (= R300), E307 (= E306)
- binding magnesium ion: I66 (= I64), E135 (= E134), E135 (= E134), E199 (= E198), H248 (= H247), H248 (= H247), E336 (= E335), H419 (= H418)
- binding : F63 (= F61), V64 (= V62), R65 (= R63), I66 (= I64), D161 (= D160), G241 (= G240), V242 (≠ I241), N243 (= N242), G305 (= G304), Y306 (= Y305), Y376 (= Y375), I426 (= I425), M430 (= M429)
7tdvC Glutamine synthetase (see paper)
70% identity, 100% coverage: 3:446/446 of query aligns to 1:443/443 of 7tdvC
- binding adenosine-5'-diphosphate: G129 (= G132), E131 (= E134), E183 (= E186), D197 (= D200), F198 (= F201), K199 (= K202), Y200 (= Y203), N246 (≠ H249), V247 (≠ Q250), S248 (= S251), R320 (= R323), S328 (= S331), R330 (= R333)
- binding magnesium ion: E131 (= E134), E131 (= E134), E133 (= E136), E188 (= E191), E195 (= E198), E195 (= E198), H244 (= H247), E332 (= E335)
- binding l-methionine-s-sulfoximine phosphate: E131 (= E134), E133 (= E136), E188 (= E191), E195 (= E198), G240 (= G243), H244 (= H247), R297 (= R300), E303 (= E306), R315 (= R318)
7tf9S L. Monocytogenes gs(14)-q-glnr peptide (see paper)
71% identity, 99% coverage: 4:446/446 of query aligns to 2:443/443 of 7tf9S
- binding glutamine: E133 (= E136), Y155 (= Y158), E188 (= E191), G240 (= G243), G242 (= G245), R297 (= R300), E303 (= E306)
- binding magnesium ion: E131 (= E134), E133 (= E136), E188 (= E191), E195 (= E198), H244 (= H247), E332 (= E335)
- binding : F59 (= F61), V60 (= V62), E418 (= E421), I422 (= I425), M426 (= M429)
7tenA Glutamine synthetase (see paper)
71% identity, 99% coverage: 4:446/446 of query aligns to 1:442/442 of 7tenA
- binding adenosine-5'-diphosphate: G128 (= G132), E130 (= E134), E182 (= E186), D196 (= D200), F197 (= F201), K198 (= K202), Y199 (= Y203), N245 (≠ H249), S247 (= S251), R319 (= R323), S327 (= S331), R329 (= R333)
- binding l-methionine-s-sulfoximine phosphate: E130 (= E134), E132 (= E136), E187 (= E191), E194 (= E198), N238 (= N242), G239 (= G243), H243 (= H247), R296 (= R300), E302 (= E306), R314 (= R318), R333 (= R337)
7tf6A Glutamine synthetase (see paper)
70% identity, 99% coverage: 5:446/446 of query aligns to 2:438/438 of 7tf6A
- binding glutamine: E128 (= E136), E183 (= E191), G235 (= G243), H239 (= H247), R292 (= R300), E298 (= E306)
- binding magnesium ion: E126 (= E134), E128 (= E136), E183 (= E191), E190 (= E198), H239 (= H247), E327 (= E335)
- binding : F58 (= F61), R60 (= R63), G232 (= G240), N234 (= N242), G296 (= G304), Y297 (= Y305), R310 (= R318), Y367 (= Y375), Y421 (≠ M429), Q433 (= Q441), Q437 (≠ L445)
8ufjB Glutamine synthetase (see paper)
59% identity, 100% coverage: 1:445/446 of query aligns to 1:443/444 of 8ufjB
8tfkA Glutamine synthetase (see paper)
59% identity, 99% coverage: 6:445/446 of query aligns to 2:439/440 of 8tfkA
- binding adenosine-5'-diphosphate: E128 (= E134), D194 (= D200), F195 (= F201), F197 (≠ Y203), N243 (≠ H249), R312 (= R318), R317 (= R323), G325 (≠ S331), R327 (= R333)
- binding magnesium ion: E128 (= E134), E128 (= E134), E130 (= E136), E185 (= E191), E192 (= E198), E192 (= E198), H241 (= H247), E329 (= E335)
- binding l-methionine-s-sulfoximine phosphate: E128 (= E134), E130 (= E136), E185 (= E191), E192 (= E198), G237 (= G243), H241 (= H247), R294 (= R300), E300 (= E306), R312 (= R318), R331 (= R337)
8ooxB Glutamine synthetase (see paper)
61% identity, 99% coverage: 6:446/446 of query aligns to 1:438/438 of 8ooxB
8oozA Glutamine synthetase (see paper)
59% identity, 99% coverage: 6:446/446 of query aligns to 1:430/430 of 8oozA
- binding adenosine-5'-triphosphate: G117 (= G132), E170 (= E186), F185 (= F201), K186 (= K202), Y187 (= Y203), N233 (≠ H249), S235 (= S251), S315 (= S331), R317 (= R333)
- binding magnesium ion: E119 (= E134), H231 (= H247), E319 (= E335)
8ooqB Glutamine synthetase from Methanothermococcus thermolithotrophicus (see paper)
56% identity, 99% coverage: 6:445/446 of query aligns to 1:446/446 of 8ooqB
- binding 2-oxoglutaric acid: F16 (≠ Y21), R18 (= R23), A32 (≠ E37), R86 (≠ I84), V92 (= V91), P169 (≠ E168), R172 (= R171), R173 (= R172), S189 (= S188)
- binding magnesium ion: E137 (= E136), E192 (= E191), E199 (= E198)
8oooA Glutamine synthetase from methanothermococcus thermolithotrophicus in complex with 2-oxoglutarate and mgatp at 2.15 a resolution (see paper)
56% identity, 99% coverage: 6:445/446 of query aligns to 2:447/447 of 8oooA
- binding 2-oxoglutaric acid: F17 (≠ Y21), R19 (= R23), A33 (≠ E37), R87 (≠ I84), V93 (= V91), P170 (≠ E168), R173 (= R171), R174 (= R172), S190 (= S188)
- binding adenosine-5'-triphosphate: E136 (= E134), E188 (= E186), F203 (= F201), K204 (= K202), F205 (≠ Y203), H251 (= H249), S253 (= S251), R325 (= R323), R335 (= R333)
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)
48% identity, 100% coverage: 1:445/446 of query aligns to 1:446/446 of A0R083
- K363 (≠ N362) 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, 100% coverage: 1:445/446 of query aligns to 1:446/446 of P9WN37
- K363 (≠ N362) 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)
41% identity, 99% coverage: 6:445/446 of query aligns to 2:469/469 of P0A9C5
- Y398 (= Y375) modified: O-AMP-tyrosine
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
1fpyA Crystal structure of glutamine synthetase from salmonella typhimurium with inhibitor phosphinothricin (see paper)
41% identity, 99% coverage: 6:445/446 of query aligns to 1:468/468 of 1fpyA
- binding adenosine-5'-diphosphate: G127 (= G132), E129 (= E134), E207 (= E186), T223 (≠ F201), F225 (≠ Y203), H271 (= H249), S273 (= S251), R355 (= R333), E357 (= E335)
- binding manganese (ii) ion: E129 (= E134), E131 (= E136), E212 (= E191), E220 (= E198), H269 (= H247), E357 (= E335)
- binding phosphinothricin: E131 (= E136), E212 (= E191), G265 (= G243), H269 (= H247), R321 (= R300), E327 (= E306), R359 (= R337)
Query Sequence
>WP_013075638.1 NCBI__GCF_000092905.1:WP_013075638.1
MPRQYTREDIMRMVKEENVRYIRLQFTDLLGIIKNVEIPVSQLPKALDNKIMFDGSSIEG
FVRIEESDMYLYPDLNTWLIFPWIGGDGGRVARLICDIYLPDGTPFPGDPRGILKRVLRQ
AQDMGFSTMNVGPEPEFFLFKMDESGSPTTEVNDQGGYFDLAPVDLGENCRREIVLALEQ
MGFEIEASHHEVAPGQHEIDFKYADAVSAADNIMTFKLVVKTIARQLGLHATFMPKPVFG
INGSGMHTHQSLFQGSENAFYDERDEFGLSETAKQYLAGILAHARAFTAIANPTVNSYKR
LVPGYEAPVYIAWSFQNRSPLVRVPASRGLSTRIEVRSPDPSANPYLALAAMLAAGLDGI
RNRMPLPEPVNRNIYVMTESERVQAGILTLPASLKEALDELSRDEVIVNALGEHAFTHFV
EAKLIEWDMFRTAVHPWERDQYLNLY
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