SitesBLAST
Comparing 208921 MicrobesOnline__882:208921 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)
8ufjB Glutamine synthetase (see paper)
54% identity, 99% coverage: 7:447/447 of query aligns to 3:444/444 of 8ufjB
8tfkA Glutamine synthetase (see paper)
54% identity, 98% coverage: 12:447/447 of query aligns to 4:440/440 of 8tfkA
- binding adenosine-5'-diphosphate: E128 (= E136), D194 (= D198), F195 (≠ L199), F197 (≠ Y201), N243 (≠ H247), R312 (= R316), R317 (= R321), G325 (≠ A332), R327 (= R334)
- binding magnesium ion: E128 (= E136), E128 (= E136), E130 (= E138), E185 (= E189), E192 (= E196), E192 (= E196), H241 (= H245), E329 (= E336)
- binding l-methionine-s-sulfoximine phosphate: E128 (= E136), E130 (= E138), E185 (= E189), E192 (= E196), G237 (= G241), H241 (= H245), R294 (= R298), E300 (= E304), R312 (= R316), R331 (= R338)
7tfaB Glutamine synthetase (see paper)
50% identity, 97% coverage: 12:446/447 of query aligns to 5:440/441 of 7tfaB
- binding glutamine: E131 (= E138), Y153 (= Y156), E186 (= E189), G238 (= G241), H242 (= H245), R295 (= R298), E301 (= E304)
- binding magnesium ion: E129 (= E136), E131 (= E138), E186 (= E189), E193 (= E196), H242 (= H245), E330 (= E336)
- binding : Y58 (≠ F65), R60 (= R67), V187 (= V190), N237 (= N240), G299 (= G302), Y300 (= Y303), R313 (= R316), M424 (≠ D430)
7tdpA Structure of paenibacillus polymyxa gs bound to met-sox-p-adp (transition state complex) to 1.98 angstom (see paper)
50% identity, 97% coverage: 12:446/447 of query aligns to 5:438/439 of 7tdpA
- binding adenosine-5'-diphosphate: N123 (≠ Y132), G125 (= G134), E127 (= E136), E179 (= E184), D193 (= D198), Y196 (= Y201), N242 (≠ H247), S244 (= S249), R316 (= R321), R326 (= R334)
- binding magnesium ion: E127 (= E136), E127 (= E136), E129 (= E138), E184 (= E189), E191 (= E196), E191 (= E196), H240 (= H245), E328 (= E336)
- binding l-methionine-s-sulfoximine phosphate: E127 (= E136), E129 (= E138), E184 (= E189), E191 (= E196), G236 (= G241), H240 (= H245), R293 (= R298), E299 (= E304), R311 (= R316), R330 (= R338)
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)
51% identity, 97% coverage: 14:446/447 of query aligns to 8:446/446 of A0R083
- K363 (≠ N363) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
8ooxB Glutamine synthetase (see paper)
51% identity, 97% coverage: 12:444/447 of query aligns to 4:435/438 of 8ooxB
8oooA Glutamine synthetase from methanothermococcus thermolithotrophicus in complex with 2-oxoglutarate and mgatp at 2.15 a resolution (see paper)
49% identity, 97% coverage: 12:446/447 of query aligns to 4:447/447 of 8oooA
- binding 2-oxoglutaric acid: F17 (= F25), R19 (≠ Q27), A33 (vs. gap), R87 (= R88), V93 (= V94), P170 (≠ N166), R173 (= R169), R174 (= R170), S190 (= S186)
- binding adenosine-5'-triphosphate: E136 (= E136), E188 (= E184), F203 (≠ L199), K204 (≠ R200), F205 (≠ Y201), H251 (= H247), S253 (= S249), R325 (= R321), R335 (= R334)
8ooqB Glutamine synthetase from Methanothermococcus thermolithotrophicus (see paper)
49% identity, 97% coverage: 12:446/447 of query aligns to 3:446/446 of 8ooqB
- binding 2-oxoglutaric acid: F16 (= F25), R18 (≠ Q27), A32 (vs. gap), R86 (= R88), V92 (= V94), P169 (≠ N166), R172 (= R169), R173 (= R170), S189 (= S186)
- binding magnesium ion: E137 (= E138), E192 (= E189), E199 (= E196)
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)
49% identity, 97% coverage: 12:444/447 of query aligns to 6:440/443 of 4lnkA
- active site: D52 (= D58), E131 (= E136), E133 (= E138), E188 (= E189), E195 (= E196), H244 (= H245), R315 (= R316), E332 (= E336), R334 (= R338)
- binding adenosine-5'-diphosphate: K43 (≠ A49), M50 (≠ G56), F198 (≠ L199), Y200 (= Y201), N246 (≠ H247), S248 (= S249), S324 (≠ G328), S328 (≠ A332), R330 (= R334)
- binding glutamic acid: E133 (= E138), E188 (= E189), V189 (= V190), N239 (= N240), G240 (= G241), G242 (= G243), E303 (= E304)
- binding magnesium ion: E131 (= E136), E188 (= E189), E195 (= E196), H244 (= H245), 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)
49% identity, 97% coverage: 12:444/447 of query aligns to 6:440/443 of 4lniA
- active site: D52 (= D58), E131 (= E136), E133 (= E138), E188 (= E189), E195 (= E196), H244 (= H245), R315 (= R316), E332 (= E336), R334 (= R338)
- binding adenosine-5'-diphosphate: E131 (= E136), E183 (= E184), D197 (= D198), Y200 (= Y201), N246 (≠ H247), S248 (= S249), R320 (= R321), R330 (= R334)
- binding magnesium ion: E131 (= E136), E131 (= E136), E133 (= E138), E188 (= E189), E195 (= E196), E195 (= E196), H244 (= H245), E332 (= E336)
- binding l-methionine-s-sulfoximine phosphate: E133 (= E138), E188 (= E189), H244 (= H245), R297 (= R298), E303 (= E304), R315 (= R316), R334 (= R338)
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)
49% identity, 97% coverage: 12:444/447 of query aligns to 7:441/444 of P12425
- G59 (= G64) 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 (= R67) 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 (= E136) binding
- E134 (= E138) binding
- E189 (= E189) binding
- 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
- G241 (= G241) binding
- H245 (= H245) binding
- 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
- 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
4s0rD Structure of gs-tnra complex (see paper)
49% identity, 97% coverage: 12:444/447 of query aligns to 10:444/447 of 4s0rD
- active site: D56 (= D58), E135 (= E136), E137 (= E138), E192 (= E189), E199 (= E196), H248 (= H245), R319 (= R316), E336 (= E336), R338 (= R338)
- binding glutamine: E137 (= E138), E192 (= E189), R301 (= R298), E307 (= E304)
- binding magnesium ion: I66 (= I68), E135 (= E136), E135 (= E136), E199 (= E196), H248 (= H245), H248 (= H245), E336 (= E336), H419 (≠ N419)
- binding : F63 (= F65), V64 (≠ T66), R65 (= R67), I66 (= I68), D161 (= D158), G241 (= G238), V242 (≠ E239), N243 (= N240), G305 (= G302), Y306 (= Y303), Y376 (≠ F376), I426 (= I426), M430 (≠ D430)
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)
50% identity, 97% coverage: 14:446/447 of query aligns to 8:446/446 of P9WN37
- K363 (≠ N363) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
8oozA Glutamine synthetase (see paper)
50% identity, 97% coverage: 12:444/447 of query aligns to 4:427/430 of 8oozA
- binding adenosine-5'-triphosphate: G117 (= G134), E170 (= E184), F185 (≠ L199), K186 (≠ R200), Y187 (= Y201), N233 (≠ H247), S235 (= S249), S315 (≠ A332), R317 (= R334)
- binding magnesium ion: E119 (= E136), H231 (= H245), E319 (= E336)
7tdvC Glutamine synthetase (see paper)
49% identity, 97% coverage: 12:444/447 of query aligns to 6:440/443 of 7tdvC
- binding adenosine-5'-diphosphate: G129 (= G134), E131 (= E136), E183 (= E184), D197 (= D198), F198 (≠ L199), K199 (≠ R200), Y200 (= Y201), N246 (≠ H247), V247 (≠ Q248), S248 (= S249), R320 (= R321), S328 (≠ A332), R330 (= R334)
- binding magnesium ion: E131 (= E136), E131 (= E136), E133 (= E138), E188 (= E189), E195 (= E196), E195 (= E196), H244 (= H245), E332 (= E336)
- binding l-methionine-s-sulfoximine phosphate: E131 (= E136), E133 (= E138), E188 (= E189), E195 (= E196), G240 (= G241), H244 (= H245), R297 (= R298), E303 (= E304), R315 (= R316)
7tf6A Glutamine synthetase (see paper)
49% identity, 97% coverage: 12:444/447 of query aligns to 5:435/438 of 7tf6A
- binding glutamine: E128 (= E138), E183 (= E189), G235 (= G241), H239 (= H245), R292 (= R298), E298 (= E304)
- binding magnesium ion: E126 (= E136), E128 (= E138), E183 (= E189), E190 (= E196), H239 (= H245), E327 (= E336)
- binding : F58 (= F65), R60 (= R67), G232 (= G238), N234 (= N240), G296 (= G302), Y297 (= Y303), R310 (= R316), Y367 (≠ F376), Y421 (≠ D430), Q433 (≠ R442)
Sites not aligning to the query:
7tenA Glutamine synthetase (see paper)
49% identity, 97% coverage: 12:446/447 of query aligns to 5:441/442 of 7tenA
- binding adenosine-5'-diphosphate: G128 (= G134), E130 (= E136), E182 (= E184), D196 (= D198), F197 (≠ L199), K198 (≠ R200), Y199 (= Y201), N245 (≠ H247), S247 (= S249), R319 (= R321), S327 (≠ A332), R329 (= R334)
- binding l-methionine-s-sulfoximine phosphate: E130 (= E136), E132 (= E138), E187 (= E189), E194 (= E196), N238 (= N240), G239 (= G241), H243 (= H245), R296 (= R298), E302 (= E304), R314 (= R316), R333 (= R338)
7tf9S L. Monocytogenes gs(14)-q-glnr peptide (see paper)
49% identity, 97% coverage: 12:446/447 of query aligns to 6:442/443 of 7tf9S
- binding glutamine: E133 (= E138), Y155 (= Y156), E188 (= E189), G240 (= G241), G242 (= G243), R297 (= R298), E303 (= E304)
- binding magnesium ion: E131 (= E136), E133 (= E138), E188 (= E189), E195 (= E196), H244 (= H245), E332 (= E336)
- binding : F59 (= F65), V60 (≠ T66), E418 (≠ G422), I422 (= I426), M426 (≠ D430)
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, 90% coverage: 10:412/447 of query aligns to 2:429/469 of P0A9C5
- Y398 (≠ F376) modified: O-AMP-tyrosine
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
P0A1P6 Glutamine synthetase; GS; Glutamate--ammonia ligase; Glutamine synthetase I beta; GSI beta; EC 6.3.1.2 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) (see 4 papers)
40% identity, 90% coverage: 10:412/447 of query aligns to 2:429/469 of P0A1P6
Query Sequence
>208921 MicrobesOnline__882:208921
MDIPVFNCKNGDDVIRAVKEYNVSFVQFWFVDILGNLKSFQVTPSELEAAFEEGMGFDGS
SILGFTRIEESDMVAFPDATTFQICSWRPLERPVARMFCDIRTPDGTPYEGDPRYILRKL
IDKAAQKGYTFYVGPELEFFFFSSPQCPTPIDAGGYFDAPPLDLGNDVRRDIIFALQRMG
IPVEYSHHEVAPSQHEIDLRYNEAMKMADVVMTYKVVVKEMARKHGIYATFMPKPIFGEN
GSGMHVHQSLFRNGKNAFFDPNDQHNLSHECRSYIAGLLKHAREFCCVTNQWINSYKRLV
PGYEAPVYIAWAQRNRSALIRVPMYKPGKEAATRIELRSPDPACNPYLAFAVMLGAGLEG
IENNYELPKAVEANIFHMGEEDLGKHGIGSLPGSLYEAAMELRNSNLMKEILGEHTHANI
VGNKLIEWDDYRTHISEFELKRYLPIL
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