SitesBLAST
Comparing Pf1N1B4_5853 FitnessBrowser__pseudo1_N1B4:Pf1N1B4_5853 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)
4hppA Crystal structure of novel glutamine synthase homolog (see paper)
64% identity, 99% coverage: 4:443/443 of query aligns to 3:426/426 of 4hppA
- active site: D55 (≠ A56), E131 (= E133), E133 (= E135), E180 (= E180), E187 (= E187), H236 (= H236), R308 (= R308), E332 (= E332), R334 (= R334)
- binding glutamic acid: E133 (= E135), T232 (≠ C232), G234 (= G234), H236 (= H236), R290 (= R290)
- binding magnesium ion: E133 (= E135), E180 (= E180), E187 (= E187)
7tfaB Glutamine synthetase (see paper)
30% identity, 92% coverage: 16:423/443 of query aligns to 24:421/441 of 7tfaB
- binding glutamine: E131 (= E135), Y153 (≠ E158), E186 (= E180), G238 (≠ C232), H242 (= H236), R295 (= R290), E301 (≠ W296)
- binding magnesium ion: E129 (= E133), E131 (= E135), E186 (= E180), E193 (= E187), H242 (= H236), E330 (= E332)
- binding : Y58 (≠ A63), R60 (vs. gap), V187 (≠ Y181), N237 (≠ V231), G299 (≠ H294), Y300 (≠ H295), R313 (= R308)
Sites not aligning to the query:
7tdpA Structure of paenibacillus polymyxa gs bound to met-sox-p-adp (transition state complex) to 1.98 angstom (see paper)
31% identity, 92% coverage: 16:423/443 of query aligns to 24:419/439 of 7tdpA
- binding adenosine-5'-diphosphate: N123 (= N129), G125 (≠ A131), E127 (= E133), E179 (= E175), D193 (≠ T189), Y196 (≠ P192), N242 (≠ H238), S244 (= S240), R316 (= R313), R326 (≠ K323)
- binding magnesium ion: E127 (= E133), E127 (= E133), E129 (= E135), E184 (= E180), E191 (= E187), E191 (= E187), H240 (= H236), E328 (= E332)
- binding l-methionine-s-sulfoximine phosphate: E127 (= E133), E129 (= E135), E184 (= E180), E191 (= E187), G236 (≠ C232), H240 (= H236), R293 (= R290), E299 (≠ W296), R311 (= R308), R330 (= R334)
8oooA Glutamine synthetase from methanothermococcus thermolithotrophicus in complex with 2-oxoglutarate and mgatp at 2.15 a resolution (see paper)
27% identity, 81% coverage: 66:423/443 of query aligns to 71:428/447 of 8oooA
- binding 2-oxoglutaric acid: R87 (≠ G82), V93 (≠ P88), P170 (≠ A157), R173 (≠ G160), R174 (≠ G161), S190 (≠ F177)
- binding adenosine-5'-triphosphate: E136 (= E133), E188 (= E175), F203 (≠ C190), K204 (≠ R191), F205 (≠ P192), H251 (= H238), S253 (= S240), R325 (= R313), R335 (≠ K323)
Sites not aligning to the query:
8ooqB Glutamine synthetase from Methanothermococcus thermolithotrophicus (see paper)
27% identity, 81% coverage: 66:423/443 of query aligns to 70:427/446 of 8ooqB
Sites not aligning to the query:
7tenA Glutamine synthetase (see paper)
28% identity, 92% coverage: 16:423/443 of query aligns to 24:422/442 of 7tenA
- binding adenosine-5'-diphosphate: G128 (= G139), E130 (≠ A142), E182 (= E175), D196 (≠ T189), F197 (≠ C190), K198 (≠ R191), Y199 (≠ P192), N245 (≠ H238), S247 (= S240), R319 (= R313), S327 (≠ G321), R329 (≠ K323)
- binding l-methionine-s-sulfoximine phosphate: E130 (≠ A142), E132 (= E144), E187 (= E180), E194 (= E187), N238 (≠ V231), G239 (≠ C232), H243 (= H236), R296 (= R290), E302 (≠ W296), R314 (= R308), R333 (= R334)
7tf9S L. Monocytogenes gs(14)-q-glnr peptide (see paper)
28% identity, 92% coverage: 16:423/443 of query aligns to 25:423/443 of 7tf9S
- binding glutamine: E133 (= E144), Y155 (≠ W162), E188 (= E180), G240 (≠ C232), G242 (= G234), R297 (= R290), E303 (≠ W296)
- binding magnesium ion: E131 (≠ A142), E133 (= E144), E188 (= E180), E195 (= E187), H244 (= H236), E332 (= E332)
- binding : F59 (≠ A63), V60 (≠ Y64), E418 (≠ A418), I422 (≠ E422)
Sites not aligning to the query:
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)
28% identity, 85% coverage: 66:443/443 of query aligns to 67:444/444 of P12425
- E132 (≠ A142) binding
- E134 (= E144) binding
- E189 (= E180) binding
- V190 (≠ Y181) 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 (= E187) binding
- G241 (≠ C232) binding
- H245 (= H236) binding
- G302 (≠ H294) 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 (≠ W296) 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 (≠ A298) 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
- 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
- 59 G→R: Unable to form stable complex with TnrA. In the presence of glutamine, this mutant derepresses amtB-lacZ fusion and glnRA-lacZ fusion.
- 62 Important for inhibition by glutamine; R→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.
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)
28% identity, 85% coverage: 66:443/443 of query aligns to 66:443/443 of 4lnkA
- active site: E131 (≠ A142), E133 (= E144), E188 (= E180), E195 (= E187), H244 (= H236), R315 (= R308), E332 (= E332), R334 (= R334)
- binding adenosine-5'-diphosphate: F198 (≠ C190), Y200 (≠ P192), N246 (≠ H238), S248 (= S240), S324 (≠ T317), S328 (≠ G321), R330 (≠ K323)
- binding glutamic acid: E133 (= E144), E188 (= E180), V189 (≠ Y181), N239 (≠ V231), G240 (≠ C232), G242 (= G234), E303 (≠ W296)
- binding magnesium ion: E131 (≠ A142), E188 (= E180), E195 (= E187), H244 (= H236), E332 (= E332)
Sites not aligning to the query:
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)
28% identity, 85% coverage: 66:443/443 of query aligns to 66:443/443 of 4lniA
- active site: E131 (≠ A142), E133 (= E144), E188 (= E180), E195 (= E187), H244 (= H236), R315 (= R308), E332 (= E332), R334 (= R334)
- binding adenosine-5'-diphosphate: E131 (≠ A142), E183 (= E175), D197 (≠ T189), Y200 (≠ P192), N246 (≠ H238), S248 (= S240), R320 (= R313), R330 (≠ K323)
- binding magnesium ion: E131 (≠ A142), E131 (≠ A142), E133 (= E144), E188 (= E180), E195 (= E187), E195 (= E187), H244 (= H236), E332 (= E332)
- binding l-methionine-s-sulfoximine phosphate: E133 (= E144), E188 (= E180), H244 (= H236), R297 (= R290), E303 (≠ W296), R315 (= R308), R334 (= R334)
Sites not aligning to the query:
4s0rD Structure of gs-tnra complex (see paper)
28% identity, 85% coverage: 66:443/443 of query aligns to 70:447/447 of 4s0rD
- active site: E135 (≠ A142), E137 (= E144), E192 (= E180), E199 (= E187), H248 (= H236), R319 (= R308), E336 (= E332), R338 (= R334)
- binding glutamine: E137 (= E144), E192 (= E180), R301 (= R290), E307 (≠ W296)
- binding magnesium ion: E135 (≠ A142), E135 (≠ A142), E199 (= E187), H248 (= H236), H248 (= H236), E336 (= E332), H419 (≠ T415)
- binding : D161 (vs. gap), G241 (≠ Q229), V242 (≠ A230), N243 (≠ V231), G305 (≠ H294), Y306 (≠ H295), Y376 (≠ D372), I426 (≠ E422), M430 (≠ L426)
Sites not aligning to the query:
8oozA Glutamine synthetase (see paper)
28% identity, 71% coverage: 96:408/443 of query aligns to 83:395/430 of 8oozA
- binding adenosine-5'-triphosphate: G117 (≠ A131), E170 (= E175), F185 (≠ C190), K186 (≠ R191), Y187 (≠ P192), N233 (≠ H238), S235 (= S240), S315 (≠ Q328), R317 (≠ N330)
- binding magnesium ion: E119 (= E133), H231 (= H236), E319 (= E332)
8ooxB Glutamine synthetase (see paper)
28% identity, 71% coverage: 96:408/443 of query aligns to 91:403/438 of 8ooxB
7tf6A Glutamine synthetase (see paper)
26% identity, 92% coverage: 16:423/443 of query aligns to 24:418/438 of 7tf6A
- binding glutamine: E128 (= E144), E183 (= E180), G235 (≠ C232), H239 (= H236), R292 (= R290), E298 (≠ W296)
- binding magnesium ion: E126 (≠ A142), E128 (= E144), E183 (= E180), E190 (= E187), H239 (= H236), E327 (= E332)
- binding : F58 (≠ Q52), R60 (≠ I54), G232 (≠ Q229), N234 (≠ V231), G296 (≠ H294), Y297 (≠ H295), R310 (= R308), Y367 (≠ D372)
Sites not aligning to the query:
8ufjB Glutamine synthetase (see paper)
27% identity, 92% coverage: 16:423/443 of query aligns to 27:424/444 of 8ufjB
7tdvC Glutamine synthetase (see paper)
26% identity, 92% coverage: 16:423/443 of query aligns to 25:423/443 of 7tdvC
- binding adenosine-5'-diphosphate: G129 (= G139), E131 (≠ A142), E183 (= E175), D197 (≠ T189), F198 (≠ C190), K199 (≠ R191), Y200 (≠ P192), N246 (≠ H238), V247 (≠ L239), S248 (= S240), R320 (= R313), S328 (≠ G321), R330 (≠ K323)
- binding magnesium ion: E131 (≠ A142), E131 (≠ A142), E133 (= E144), E188 (= E180), E195 (= E187), E195 (= E187), H244 (= H236), E332 (= E332)
- binding l-methionine-s-sulfoximine phosphate: E131 (≠ A142), E133 (= E144), E188 (= E180), E195 (= E187), G240 (≠ C232), H244 (= H236), R297 (= R290), E303 (≠ W296), R315 (= R308)
8tfkA Glutamine synthetase (see paper)
27% identity, 92% coverage: 16:423/443 of query aligns to 23:420/440 of 8tfkA
- binding adenosine-5'-diphosphate: E128 (= E133), D194 (≠ T189), F195 (≠ C190), F197 (≠ P192), N243 (≠ H238), R312 (= R308), R317 (= R313), G325 (= G321), R327 (≠ K323)
- binding magnesium ion: E128 (= E133), E128 (= E133), E130 (= E135), E185 (= E180), E192 (= E187), E192 (= E187), H241 (= H236), E329 (= E332)
- binding l-methionine-s-sulfoximine phosphate: E128 (= E133), E130 (= E135), E185 (= E180), E192 (= E187), G237 (≠ C232), H241 (= H236), R294 (= R290), E300 (≠ W296), R312 (= R308), R331 (= R334)
A0R079 Glutamine synthetase; GS; Glutamate--ammonia ligase; Glutamine synthetase I beta; GSI beta; EC 6.3.1.2 from Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis) (see paper)
34% identity, 56% coverage: 185:432/443 of query aligns to 225:467/478 of A0R079
Sites not aligning to the query:
- 14 modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
4acfA Crystal structure of mycobacterium tuberculosis glutamine synthetase in complex with imidazopyridine inhibitor ((4-(6-bromo-3- (butylamino)imidazo(1,2-a)pyridin-2-yl)phenoxy) acetic acid) and l- methionine-s-sulfoximine phosphate.
33% identity, 59% coverage: 177:438/443 of query aligns to 208:465/475 of 4acfA
- active site: E216 (vs. gap), E224 (= E187), H273 (= H236), R344 (= R308), E363 (= E332), R365 (= R334)
- binding {4-[6-bromo-3-(butylamino)imidazo[1,2-a]pyridin-2-yl]phenoxy}acetic acid: F229 (≠ P192), H275 (= H238), Q276 (≠ L239), W279 (≠ Q242), N356 (≠ G321), K358 (= K323), R361 (≠ N330)
- binding magnesium ion: E216 (vs. gap), E224 (= E187), E224 (= E187), H273 (= H236), E363 (= E332)
- binding l-methionine-s-sulfoximine phosphate: E216 (vs. gap), E224 (= E187), G269 (≠ C232), H273 (= H236), R326 (= R290), E332 (≠ W296), R344 (= R308), R365 (= R334)
Sites not aligning to the query:
3zxvA Crystal structure of mycobacterium tuberculosis glutamine synthetase in complex with tri-substituted imidazole inhibitor (4-(2-tert-butyl- 4-(6-methoxynaphthalen-2-yl)-1h-imidazol-5-yl)pyridin-2-amine) and l- methionine-s-sulfoximine phosphate (see paper)
33% identity, 59% coverage: 177:438/443 of query aligns to 208:465/475 of 3zxvA
- active site: E216 (vs. gap), E224 (= E187), H273 (= H236), R344 (= R308), E363 (= E332), R365 (= R334)
- binding magnesium ion: E216 (vs. gap), E224 (= E187), E224 (= E187), H273 (= H236), E363 (= E332)
- binding 4-(2-tert-butyl-4-(6-methoxynaphthalen-2-yl)-3h-imidazol-4-yl)pyridin-2-amine: F229 (≠ P192), H275 (= H238), S277 (= S240), K358 (= K323), R361 (≠ N330)
- binding l-methionine-s-sulfoximine phosphate: E216 (vs. gap), E224 (= E187), G269 (≠ C232), H273 (= H236), R326 (= R290), E332 (≠ W296), R344 (= R308), R365 (= R334)
Sites not aligning to the query:
Query Sequence
>Pf1N1B4_5853 FitnessBrowser__pseudo1_N1B4:Pf1N1B4_5853
MSERLSPLPMTTIVTTDLIGVTRGRSFPTDELEAYRVAGCGWVPANSALTPQDIIASSNP
WGAYGDLRLIPDLSSRVTVNNGPDANAPALDFIHGDIRETDGRPWGACPRTLLRNEVERY
RSELGLQINAAFEHEFNLGSGAAEHLAFSLEAQRQGAEFGGWLLSALRAGGVEPEMFLPE
YGKHQYEITCRPALGVAAADRAVNLREITREIARQMGLDLSFAPKTSEQAVCNGVHLHLS
LQDLTGHPVMYDAGTSNGLSTLGQHWAAGVLHYLPALCAFTAPTPVSYERLQPHHWSASY
ACLGQRNREAALRICPTVSLGGKAVAAQYNLEFRAMDATASPHLAMAALLIAGRLGIEQR
LALNAITDEVPDSLNEEQRQARGIVALPASLSQALKCLRNSEALIEALPSALLDTWFALK
TEELRLTEQLSPAELCEHYARLY
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