SitesBLAST
Comparing WP_029001753.1 NCBI__GCF_000430725.1:WP_029001753.1 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)
P78061 Gamma-glutamylputrescine synthetase PuuA; Gamma-Glu-Put synthetase; Glutamate--putrescine ligase; EC 6.3.1.11 from Escherichia coli (strain K12) (see paper)
35% identity, 99% coverage: 3:452/455 of query aligns to 17:469/472 of P78061
- H282 (= H265) mutation to N: Activity is impaired to 9% of wild-type.
- R357 (= R341) mutation to Q: Activity is impaired to 3% of wild-type.
8oozA Glutamine synthetase (see paper)
33% identity, 84% coverage: 70:452/455 of query aligns to 46:427/430 of 8oozA
- binding adenosine-5'-triphosphate: G117 (≠ A142), E170 (≠ D204), F185 (= F219), K186 (≠ F220), Y187 (≠ H221), N233 (≠ H267), S235 (= S269), S315 (≠ A349), R317 (= R351)
- binding magnesium ion: E119 (= E144), H231 (= H265), E319 (= E353)
8ooxB Glutamine synthetase (see paper)
33% identity, 82% coverage: 80:452/455 of query aligns to 62:435/438 of 8ooxB
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)
30% identity, 98% coverage: 7:452/455 of query aligns to 4:441/444 of P12425
- G59 (≠ D74) 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 (≠ T77) 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 (= E144) binding Mg(2+)
- E134 (= E146) binding Mg(2+)
- E189 (= E209) binding Mg(2+)
- V190 (≠ I210) 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 (= E216) binding Mg(2+)
- G241 (= G261) binding L-glutamate
- H245 (= H265) binding Mg(2+)
- G302 (≠ F322) 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 (≠ A324) 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 (= P326) 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 (= E353) binding Mg(2+)
- E424 (= E435) 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)
30% identity, 98% coverage: 7:452/455 of query aligns to 3:440/443 of 4lnkA
- active site: D52 (≠ M60), E131 (= E144), E133 (= E146), E188 (= E209), E195 (= E216), H244 (= H265), R315 (= R336), E332 (= E353), R334 (= R355)
- binding adenosine-5'-diphosphate: K43 (≠ M51), M50 (≠ V58), F198 (= F219), Y200 (≠ H221), N246 (≠ H267), S248 (= S269), S324 (≠ A345), S328 (≠ A349), R330 (= R351)
- binding glutamic acid: E133 (= E146), E188 (= E209), V189 (≠ I210), N239 (≠ P260), G240 (= G261), G242 (≠ A263), E303 (≠ A324)
- binding magnesium ion: E131 (= E144), E188 (= E209), E195 (= E216), H244 (= H265), E332 (= E353)
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)
30% identity, 98% coverage: 7:452/455 of query aligns to 3:440/443 of 4lniA
- active site: D52 (≠ M60), E131 (= E144), E133 (= E146), E188 (= E209), E195 (= E216), H244 (= H265), R315 (= R336), E332 (= E353), R334 (= R355)
- binding adenosine-5'-diphosphate: E131 (= E144), E183 (≠ D204), D197 (≠ N218), Y200 (≠ H221), N246 (≠ H267), S248 (= S269), R320 (= R341), R330 (= R351)
- binding magnesium ion: E131 (= E144), E131 (= E144), E133 (= E146), E188 (= E209), E195 (= E216), E195 (= E216), H244 (= H265), E332 (= E353)
- binding l-methionine-s-sulfoximine phosphate: E133 (= E146), E188 (= E209), H244 (= H265), R297 (= R318), E303 (≠ A324), R315 (= R336), R334 (= R355)
4s0rD Structure of gs-tnra complex (see paper)
30% identity, 98% coverage: 7:452/455 of query aligns to 7:444/447 of 4s0rD
- active site: D56 (≠ M60), E135 (= E144), E137 (= E146), E192 (= E209), E199 (= E216), H248 (= H265), R319 (= R336), E336 (= E353), R338 (= R355)
- binding glutamine: E137 (= E146), E192 (= E209), R301 (= R318), E307 (≠ A324)
- binding magnesium ion: I66 (≠ P78), E135 (= E144), E135 (= E144), E199 (= E216), H248 (= H265), H248 (= H265), E336 (= E353), H419 (≠ V427)
- binding : F63 (≠ V75), V64 (≠ I76), R65 (≠ T77), I66 (≠ P78), D161 (≠ G168), G241 (= G258), V242 (≠ E259), N243 (≠ P260), G305 (≠ F322), Y306 (≠ T323), Y376 (= Y393), I426 (≠ T434), M430 (≠ E438)
8s59O Glutamine synthetase
33% identity, 82% coverage: 80:452/455 of query aligns to 68:443/446 of 8s59O
Sites not aligning to the query:
8tfbA Glutamine synthetase (see paper)
33% identity, 82% coverage: 80:452/455 of query aligns to 65:440/443 of 8tfbA
8tfkA Glutamine synthetase (see paper)
33% identity, 82% coverage: 80:452/455 of query aligns to 62:437/440 of 8tfkA
- binding adenosine-5'-diphosphate: E128 (= E144), D194 (≠ N218), F195 (= F219), F197 (≠ H221), N243 (≠ H267), R312 (= R336), R317 (= R341), G325 (≠ A349), R327 (= R351)
- binding magnesium ion: E128 (= E144), E128 (= E144), E130 (= E146), E185 (= E209), E192 (= E216), E192 (= E216), H241 (= H265), E329 (= E353)
- binding l-methionine-s-sulfoximine phosphate: E128 (= E144), E130 (= E146), E185 (= E209), E192 (= E216), G237 (= G261), H241 (= H265), R294 (= R318), E300 (≠ A324), R312 (= R336), R331 (= R355)
8oooA Glutamine synthetase from methanothermococcus thermolithotrophicus in complex with 2-oxoglutarate and mgatp at 2.15 a resolution (see paper)
31% identity, 84% coverage: 68:447/455 of query aligns to 51:440/447 of 8oooA
- binding 2-oxoglutaric acid: R87 (vs. gap), V93 (≠ T102), P170 (≠ D186), R173 (≠ F189), R174 (≠ E190), S190 (≠ L206)
- binding adenosine-5'-triphosphate: E136 (= E144), E188 (≠ D204), F203 (= F219), K204 (≠ F220), F205 (≠ H221), H251 (= H267), S253 (= S269), R325 (= R341), R335 (= R351)
Sites not aligning to the query:
8ooqB Glutamine synthetase from Methanothermococcus thermolithotrophicus (see paper)
31% identity, 84% coverage: 68:447/455 of query aligns to 50:439/446 of 8ooqB
Sites not aligning to the query:
5dm3C Crystal structure of glutamine synthetase from chromohalobacter salexigens dsm 3043(csal_0679, target efi-550015) with bound adp
34% identity, 80% coverage: 85:447/455 of query aligns to 56:390/396 of 5dm3C
- active site: E115 (= E144), E117 (= E146), E162 (= E209), E169 (= E216), H218 (= H265), R286 (= R336), E303 (= E353), R305 (= R355)
- binding adenosine-5'-diphosphate: R173 (≠ F220), C174 (≠ H221), H220 (= H267), S222 (= S269), R301 (= R351)
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)
32% identity, 82% coverage: 79:453/455 of query aligns to 63:446/446 of P9WN37
- K363 (≠ N380) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
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, 82% coverage: 80:452/455 of query aligns to 64:444/446 of A0R083
- K363 (≠ N380) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
7tenA Glutamine synthetase (see paper)
28% identity, 98% coverage: 7:452/455 of query aligns to 2:439/442 of 7tenA
- binding adenosine-5'-diphosphate: G128 (≠ A142), E130 (= E144), E182 (≠ D204), D196 (≠ N218), F197 (= F219), K198 (≠ F220), Y199 (≠ H221), N245 (≠ H267), S247 (= S269), R319 (= R341), S327 (≠ A349), R329 (= R351)
- binding l-methionine-s-sulfoximine phosphate: E130 (= E144), E132 (= E146), E187 (= E209), E194 (= E216), N238 (≠ P260), G239 (= G261), H243 (= H265), R296 (= R318), E302 (≠ A324), R314 (= R336), R333 (= R355)
7tf9S L. Monocytogenes gs(14)-q-glnr peptide (see paper)
28% identity, 98% coverage: 7:452/455 of query aligns to 3:440/443 of 7tf9S
- binding glutamine: E133 (= E146), Y155 (≠ R166), E188 (= E209), G240 (= G261), G242 (≠ A263), R297 (= R318), E303 (≠ A324)
- binding magnesium ion: E131 (= E144), E133 (= E146), E188 (= E209), E195 (= E216), H244 (= H265), E332 (= E353)
- binding : F59 (≠ V75), V60 (≠ I76), E418 (= E430), I422 (≠ T434), M426 (≠ E438)
7tfaB Glutamine synthetase (see paper)
31% identity, 82% coverage: 80:452/455 of query aligns to 63:438/441 of 7tfaB
- binding glutamine: E131 (= E146), Y153 (≠ A176), E186 (= E209), G238 (= G261), H242 (= H265), R295 (= R318), E301 (≠ A324)
- binding magnesium ion: E129 (= E144), E131 (= E146), E186 (= E209), E193 (= E216), H242 (= H265), E330 (= E353)
- binding : V187 (≠ I210), N237 (≠ P260), G299 (≠ F322), Y300 (≠ T323), R313 (= R336), M424 (≠ E438)
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, 82% coverage: 80:452/455 of query aligns to 63:436/439 of 7tdpA
- binding adenosine-5'-diphosphate: N123 (vs. gap), G125 (≠ A142), E127 (= E144), E179 (≠ D204), D193 (≠ N218), Y196 (≠ H221), N242 (≠ H267), S244 (= S269), R316 (= R341), R326 (= R351)
- binding magnesium ion: E127 (= E144), E127 (= E144), E129 (= E146), E184 (= E209), E191 (= E216), E191 (= E216), H240 (= H265), E328 (= E353)
- binding l-methionine-s-sulfoximine phosphate: E127 (= E144), E129 (= E146), E184 (= E209), E191 (= E216), G236 (= G261), H240 (= H265), R293 (= R318), E299 (≠ A324), R311 (= R336), R330 (= R355)
7tf6A Glutamine synthetase (see paper)
30% identity, 82% coverage: 80:452/455 of query aligns to 63:435/438 of 7tf6A
- binding glutamine: E128 (= E146), E183 (= E209), G235 (= G261), H239 (= H265), R292 (= R318), E298 (≠ A324)
- binding magnesium ion: E126 (= E144), E128 (= E146), E183 (= E209), E190 (= E216), H239 (= H265), E327 (= E353)
- binding : G232 (= G258), N234 (≠ P260), G296 (≠ F322), Y297 (≠ T323), R310 (= R336), Y367 (= Y393), Y421 (≠ E438), Q433 (≠ H450)
Sites not aligning to the query:
Query Sequence
>WP_029001753.1 NCBI__GCF_000430725.1:WP_029001753.1
MAERKDFTYSDLEHWLDQHRVTEIECLVPDLTGVARGKILPRQKFTEDRGMRLPEIVVAM
GVTGEFPEEGPYYDVITPTDRDMHLRPDPATVRIVPWATDPTAQVIHDCFDRDGRLVPFA
PRSVLRRVCDLYAAAGLEPVVAPELEFYLVARNTDPDMPLKPPIGRSGRAETSRQAYSID
AVNEFDPLFEDVYDYCEKMELNVDTLIHEIGAGQMEINFFHAHPLGLADEVFFFKRTVRE
AAMRHDMFATFMAKPIAGEPGSAMHIHQSVLRKDTGLNIFSNADGSPSREFYWYIGGLQK
YVPAAMALFAPYVNSYRRLARFTAAPINIQWGTDNRTVGIRSPVAPPAARRVENRVVGAD
ANPYVALAATLACGWLGIKNRIEPTPECKGDAYLGDYALPRSLGEALEKLRAEEALAEVL
GEEFVTVYTEVKETEFAEFMKVISPWEREHLLLHV
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