SitesBLAST
Comparing GFF1137 FitnessBrowser__Phaeo:GFF1137 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)
P78061 Gamma-glutamylputrescine synthetase PuuA; Gamma-Glu-Put synthetase; Glutamate--putrescine ligase; EC 6.3.1.11 from Escherichia coli (strain K12) (see paper)
34% identity, 95% coverage: 24:451/452 of query aligns to 40:471/472 of P78061
- H282 (= H262) mutation to N: Activity is impaired to 9% of wild-type.
- R357 (= R338) mutation to Q: Activity is impaired to 3% of wild-type.
8ooxB Glutamine synthetase (see paper)
29% identity, 96% coverage: 16:449/452 of query aligns to 10:435/438 of 8ooxB
8ooqB Glutamine synthetase from Methanothermococcus thermolithotrophicus (see paper)
32% identity, 83% coverage: 74:449/452 of query aligns to 65:444/446 of 8ooqB
Sites not aligning to the query:
8oooA Glutamine synthetase from methanothermococcus thermolithotrophicus in complex with 2-oxoglutarate and mgatp at 2.15 a resolution (see paper)
32% identity, 83% coverage: 74:449/452 of query aligns to 66:445/447 of 8oooA
- binding 2-oxoglutaric acid: R87 (vs. gap), V93 (≠ T99), P170 (≠ G183), R173 (≠ I186), R174 (≠ D187), S190 (≠ I203)
- binding adenosine-5'-triphosphate: E136 (= E141), E188 (≠ D201), F203 (≠ L216), K204 (≠ R217), F205 (≠ H218), H251 (= H264), S253 (= S266), R325 (= R338), R335 (= R348)
Sites not aligning to the query:
8oozA Glutamine synthetase (see paper)
29% identity, 96% coverage: 16:449/452 of query aligns to 10:427/430 of 8oozA
- binding adenosine-5'-triphosphate: G117 (≠ A139), E170 (≠ D201), F185 (≠ L216), K186 (≠ R217), Y187 (≠ H218), N233 (≠ H264), S235 (= S266), S315 (≠ A346), R317 (= R348)
- binding magnesium ion: E119 (= E141), H231 (= H262), E319 (= E350)
8tfkA Glutamine synthetase (see paper)
30% identity, 95% coverage: 19:449/452 of query aligns to 13:437/440 of 8tfkA
- binding adenosine-5'-diphosphate: E128 (= E141), D194 (≠ N215), F195 (≠ L216), F197 (≠ H218), N243 (≠ H264), R312 (= R333), R317 (= R338), G325 (≠ A346), R327 (= R348)
- binding magnesium ion: E128 (= E141), E128 (= E141), E130 (= E143), E185 (= E206), E192 (= E213), E192 (= E213), H241 (= H262), E329 (= E350)
- binding l-methionine-s-sulfoximine phosphate: E128 (= E141), E130 (= E143), E185 (= E206), E192 (= E213), G237 (= G258), H241 (= H262), R294 (= R315), E300 (≠ A321), R312 (= R333), R331 (= R352)
7tf9S L. Monocytogenes gs(14)-q-glnr peptide (see paper)
30% identity, 93% coverage: 28:449/452 of query aligns to 24:440/443 of 7tf9S
- binding glutamine: E133 (= E143), Y155 (≠ A173), E188 (= E206), G240 (= G258), G242 (≠ A260), R297 (= R315), E303 (≠ A321)
- binding magnesium ion: E131 (= E141), E133 (= E143), E188 (= E206), E195 (= E213), H244 (= H262), E332 (= E350)
- binding : F59 (≠ W75), V60 (≠ I76), E418 (≠ I427), I422 (≠ A431), M426 (≠ E435)
7tenA Glutamine synthetase (see paper)
30% identity, 93% coverage: 28:449/452 of query aligns to 23:439/442 of 7tenA
- binding adenosine-5'-diphosphate: G128 (≠ A139), E130 (= E141), E182 (≠ D201), D196 (≠ N215), F197 (≠ L216), K198 (≠ R217), Y199 (≠ H218), N245 (≠ H264), S247 (= S266), R319 (= R338), S327 (≠ A346), R329 (= R348)
- binding l-methionine-s-sulfoximine phosphate: E130 (= E141), E132 (= E143), E187 (= E206), E194 (= E213), N238 (≠ P257), G239 (= G258), H243 (= H262), R296 (= R315), E302 (≠ A321), R314 (= R333), R333 (= R352)
8ufjB Glutamine synthetase (see paper)
30% identity, 95% coverage: 19:449/452 of query aligns to 17:441/444 of 8ufjB
4s0rD Structure of gs-tnra complex (see paper)
29% identity, 93% coverage: 28:449/452 of query aligns to 28:444/447 of 4s0rD
- active site: D56 (≠ E68), E135 (= E141), E137 (= E143), E192 (= E206), E199 (= E213), H248 (= H262), R319 (= R333), E336 (= E350), R338 (= R352)
- binding glutamine: E137 (= E143), E192 (= E206), R301 (= R315), E307 (≠ A321)
- binding magnesium ion: I66 (vs. gap), E135 (= E141), E135 (= E141), E199 (= E213), H248 (= H262), H248 (= H262), E336 (= E350), H419 (≠ V424)
- binding : F63 (≠ W75), V64 (≠ I76), R65 (vs. gap), I66 (vs. gap), D161 (≠ S175), G241 (≠ D255), V242 (≠ E256), N243 (≠ P257), G305 (≠ E319), Y306 (≠ Q320), Y376 (= Y390), I426 (≠ A431), M430 (≠ E435)
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)
29% identity, 93% coverage: 28:449/452 of query aligns to 24:440/443 of 4lnkA
- active site: D52 (≠ E68), E131 (= E141), E133 (= E143), E188 (= E206), E195 (= E213), H244 (= H262), R315 (= R333), E332 (= E350), R334 (= R352)
- binding adenosine-5'-diphosphate: K43 (= K47), M50 (≠ F58), F198 (≠ L216), Y200 (≠ H218), N246 (≠ H264), S248 (= S266), S324 (= S342), S328 (≠ A346), R330 (= R348)
- binding glutamic acid: E133 (= E143), E188 (= E206), V189 (≠ G207), N239 (≠ P257), G240 (= G258), G242 (≠ A260), E303 (≠ A321)
- binding magnesium ion: E131 (= E141), E188 (= E206), E195 (= E213), H244 (= H262), E332 (= E350)
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)
29% identity, 93% coverage: 28:449/452 of query aligns to 24:440/443 of 4lniA
- active site: D52 (≠ E68), E131 (= E141), E133 (= E143), E188 (= E206), E195 (= E213), H244 (= H262), R315 (= R333), E332 (= E350), R334 (= R352)
- binding adenosine-5'-diphosphate: E131 (= E141), E183 (≠ D201), D197 (≠ N215), Y200 (≠ H218), N246 (≠ H264), S248 (= S266), R320 (= R338), R330 (= R348)
- binding magnesium ion: E131 (= E141), E131 (= E141), E133 (= E143), E188 (= E206), E195 (= E213), E195 (= E213), H244 (= H262), E332 (= E350)
- binding l-methionine-s-sulfoximine phosphate: E133 (= E143), E188 (= E206), H244 (= H262), R297 (= R315), E303 (≠ A321), R315 (= R333), R334 (= R352)
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)
29% identity, 93% coverage: 28:449/452 of query aligns to 25:441/444 of P12425
- G59 (= G74) 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 (vs. gap) 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 (= E141) binding
- E134 (= E143) binding
- E189 (= E206) binding
- V190 (≠ G207) 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 (= E213) binding
- G241 (= G258) binding
- H245 (= H262) binding
- G302 (≠ E319) 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 (≠ A321) 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 (= P323) 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 (= E350) binding
- E424 (= E432) 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
5dm3C Crystal structure of glutamine synthetase from chromohalobacter salexigens dsm 3043(csal_0679, target efi-550015) with bound adp
29% identity, 96% coverage: 13:444/452 of query aligns to 6:390/396 of 5dm3C
- active site: E115 (= E141), E117 (= E143), E162 (= E206), E169 (= E213), H218 (= H262), R286 (= R333), E303 (= E350), R305 (= R352)
- binding adenosine-5'-diphosphate: R173 (= R217), C174 (≠ H218), H220 (= H264), S222 (= S266), R301 (= R348)
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)
31% identity, 83% coverage: 76:449/452 of query aligns to 63:444/446 of A0R083
- K363 (≠ N377) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
7tfaB Glutamine synthetase (see paper)
28% identity, 93% coverage: 28:449/452 of query aligns to 23:438/441 of 7tfaB
- binding glutamine: E131 (= E143), Y153 (≠ A173), E186 (= E206), G238 (= G258), H242 (= H262), R295 (= R315), E301 (≠ A321)
- binding magnesium ion: E129 (= E141), E131 (= E143), E186 (= E206), E193 (= E213), H242 (= H262), E330 (= E350)
- binding : Y58 (≠ W75), R60 (vs. gap), V187 (≠ G207), N237 (≠ P257), G299 (≠ E319), Y300 (≠ Q320), R313 (= R333), M424 (≠ E435)
7tdpA Structure of paenibacillus polymyxa gs bound to met-sox-p-adp (transition state complex) to 1.98 angstom (see paper)
28% identity, 93% coverage: 28:449/452 of query aligns to 23:436/439 of 7tdpA
- binding adenosine-5'-diphosphate: N123 (vs. gap), G125 (≠ A139), E127 (= E141), E179 (≠ D201), D193 (≠ N215), Y196 (≠ H218), N242 (≠ H264), S244 (= S266), R316 (= R338), R326 (= R348)
- binding magnesium ion: E127 (= E141), E127 (= E141), E129 (= E143), E184 (= E206), E191 (= E213), E191 (= E213), H240 (= H262), E328 (= E350)
- binding l-methionine-s-sulfoximine phosphate: E127 (= E141), E129 (= E143), E184 (= E206), E191 (= E213), G236 (= G258), H240 (= H262), R293 (= R315), E299 (≠ A321), R311 (= R333), R330 (= R352)
7tdvC Glutamine synthetase (see paper)
28% identity, 97% coverage: 10:449/452 of query aligns to 6:440/443 of 7tdvC
- binding adenosine-5'-diphosphate: G129 (≠ A139), E131 (= E141), E183 (≠ D201), D197 (≠ N215), F198 (≠ L216), K199 (≠ R217), Y200 (≠ H218), N246 (≠ H264), V247 (≠ H265), S248 (= S266), R320 (= R338), S328 (≠ A346), R330 (= R348)
- binding magnesium ion: E131 (= E141), E131 (= E141), E133 (= E143), E188 (= E206), E195 (= E213), E195 (= E213), H244 (= H262), E332 (= E350)
- binding l-methionine-s-sulfoximine phosphate: E131 (= E141), E133 (= E143), E188 (= E206), E195 (= E213), G240 (= G258), H244 (= H262), R297 (= R315), E303 (≠ A321), R315 (= R333)
7tf6A Glutamine synthetase (see paper)
27% identity, 97% coverage: 10:449/452 of query aligns to 5:435/438 of 7tf6A
- binding glutamine: E128 (= E143), E183 (= E206), G235 (= G258), H239 (= H262), R292 (= R315), E298 (≠ A321)
- binding magnesium ion: E126 (= E141), E128 (= E143), E183 (= E206), E190 (= E213), H239 (= H262), E327 (= E350)
- binding : F58 (≠ W75), R60 (vs. gap), G232 (≠ D255), N234 (≠ P257), G296 (≠ E319), Y297 (≠ Q320), R310 (= R333), Y367 (= Y390), Y421 (≠ E435), Q433 (≠ H447)
Sites not aligning to the query:
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)
30% identity, 83% coverage: 77:450/452 of query aligns to 64:446/446 of P9WN37
- K363 (≠ N377) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
Query Sequence
>GFF1137 FitnessBrowser__Phaeo:GFF1137
MSAWLDTLPEAAKTYLEGRRLDEVECIISDLPGIARGKAVPASKFAKQDYFHLPDSIFYQ
TITGDWAEAADDDGWIEKDMILKPDMSTATAAPWTGDWTLQVIHDAYDRDHKPIPFSPRN
VLKRVVQLYHDKGWQPVVAPEMEFFLVARNIDPAREIEPMMGRSGRPAAARQAYSMTAVD
EFGPVIDDIYDFAEAQGFEIDGITQEGGAGQLEINLRHGDPVKLADEVFYFKRLIREAAL
RHDCFATFMAKPIADEPGSAMHIHHSIIDMESGDNIFSGPQGGETDAFYHFIGGLQNHLP
AGLAVMAPYVNSYRRYVKEQAAPINLEWARDNRTTGIRVPLSGPEARRVENRIAGMDCNP
YLGIALSLACGYLGLVNEERPRKQFKGDAYAGDGDIPQVMGQALDLFEEASALHEVLGPE
FARVYSIVKRAEYDEFLQVISPWEREHLLLNV
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