SitesBLAST
Comparing WP_011778857.1 NCBI__GCF_000015305.1:WP_011778857.1 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)
5dm3C Crystal structure of glutamine synthetase from chromohalobacter salexigens dsm 3043(csal_0679, target efi-550015) with bound adp
35% identity, 95% coverage: 21:466/468 of query aligns to 1:396/396 of 5dm3C
- active site: E115 (= E158), E117 (= E160), E162 (= E221), E169 (= E228), H218 (= H277), R286 (= R348), E303 (= E365), R305 (= R367)
- binding adenosine-5'-diphosphate: R173 (≠ E232), C174 (≠ H233), H220 (= H279), S222 (= S281), R301 (= R363)
5dm3A Crystal structure of glutamine synthetase from chromohalobacter salexigens dsm 3043(csal_0679, target efi-550015) with bound adp
33% identity, 95% coverage: 21:466/468 of query aligns to 3:374/374 of 5dm3A
- active site: E107 (= E158), E109 (= E160), E146 (≠ A224), E150 (= E228), H199 (= H277), R265 (= R348), E282 (= E365), R284 (= R367)
- binding adenosine-5'-diphosphate: I103 (≠ T154), E141 (≠ L216), R154 (≠ E232), C155 (≠ H233), H201 (= H279), S203 (= S281), R280 (= R363)
8ufjB Glutamine synthetase (see paper)
32% identity, 95% coverage: 23:468/468 of query aligns to 9:444/444 of 8ufjB
8wwuB Glutamine synthetase
31% identity, 97% coverage: 14:466/468 of query aligns to 12:490/492 of 8wwuB
- binding phosphoaminophosphonic acid-adenylate ester: G157 (= G156), E159 (= E158), R226 (≠ L216), F241 (≠ I231), V243 (≠ H233), H290 (= H279), S292 (= S281), K360 (≠ R348), R365 (= R353), R376 (= R363)
- binding magnesium ion: E159 (= E158), E238 (= E228)
- binding manganese (ii) ion: E159 (= E158), E161 (= E160), E231 (= E221), E238 (= E228), H288 (= H277), E378 (= E365)
8tfkA Glutamine synthetase (see paper)
32% identity, 95% coverage: 23:468/468 of query aligns to 5:440/440 of 8tfkA
- binding adenosine-5'-diphosphate: E128 (= E158), D194 (≠ N230), F195 (≠ I231), F197 (≠ H233), N243 (≠ H279), R312 (= R348), R317 (= R353), G325 (≠ T361), R327 (= R363)
- binding magnesium ion: E128 (= E158), E128 (= E158), E130 (= E160), E185 (= E221), E192 (= E228), E192 (= E228), H241 (= H277), E329 (= E365)
- binding l-methionine-s-sulfoximine phosphate: E128 (= E158), E130 (= E160), E185 (= E221), E192 (= E228), G237 (= G273), H241 (= H277), R294 (= R330), E300 (≠ W336), R312 (= R348), R331 (= R367)
8wwvA Glutamine synthetase
31% identity, 97% coverage: 14:466/468 of query aligns to 10:488/490 of 8wwvA
- binding adenosine-5'-diphosphate: G155 (= G156), E157 (= E158), R224 (≠ L216), F239 (≠ I231), D240 (≠ E232), V241 (≠ H233), H288 (= H279), S290 (= S281), R374 (= R363), E376 (= E365)
- binding magnesium ion: E157 (= E158), E236 (= E228)
- binding manganese (ii) ion: E157 (= E158), E159 (= E160), E229 (= E221), E236 (= E228), H286 (= H277), E376 (= E365)
- binding l-methionine-s-sulfoximine phosphate: E157 (= E158), E159 (= E160), E229 (= E221), E236 (= E228), A282 (≠ S274), H286 (= H277), R340 (= R330), K358 (≠ R348)
P78061 Gamma-glutamylputrescine synthetase PuuA; Gamma-Glu-Put synthetase; Glutamate--putrescine ligase; EC 6.3.1.11 from Escherichia coli (strain K12) (see paper)
33% identity, 93% coverage: 25:460/468 of query aligns to 27:464/472 of P78061
- H282 (= H277) mutation to N: Activity is impaired to 9% of wild-type.
- R357 (= R353) mutation to Q: Activity is impaired to 3% of wild-type.
8oozA Glutamine synthetase (see paper)
32% identity, 96% coverage: 20:466/468 of query aligns to 1:428/430 of 8oozA
- binding adenosine-5'-triphosphate: G117 (= G156), E170 (≠ L216), F185 (≠ I231), K186 (≠ E232), Y187 (≠ H233), N233 (≠ H279), S235 (= S281), S315 (≠ T361), R317 (= R363)
- binding magnesium ion: E119 (= E158), H231 (= H277), E319 (= E365)
8ooxB Glutamine synthetase (see paper)
31% identity, 96% coverage: 20:466/468 of query aligns to 1:436/438 of 8ooxB
8ooqB Glutamine synthetase from Methanothermococcus thermolithotrophicus (see paper)
34% identity, 79% coverage: 96:466/468 of query aligns to 69:445/446 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)
34% identity, 79% coverage: 96:466/468 of query aligns to 70:446/447 of 8oooA
- binding 2-oxoglutaric acid: R87 (≠ E113), V93 (vs. gap), P170 (≠ E198), R173 (≠ I201), R174 (≠ G202), S190 (= S218)
- binding adenosine-5'-triphosphate: E136 (= E158), E188 (≠ L216), F203 (≠ I231), K204 (≠ E232), F205 (≠ H233), H251 (= H279), S253 (= S281), R325 (= R353), R335 (= R363)
Sites not aligning to the query:
4s0rD Structure of gs-tnra complex (see paper)
30% identity, 95% coverage: 25:467/468 of query aligns to 12:446/447 of 4s0rD
- active site: D56 (= D84), E135 (= E158), E137 (= E160), E192 (= E221), E199 (= E228), H248 (= H277), R319 (= R348), E336 (= E365), R338 (= R367)
- binding glutamine: E137 (= E160), E192 (= E221), R301 (= R330), E307 (≠ W336)
- binding magnesium ion: I66 (≠ T93), E135 (= E158), E135 (= E158), E199 (= E228), H248 (= H277), H248 (= H277), E336 (= E365), H419 (= H440)
- binding : F63 (≠ W91), V64 (vs. gap), R65 (≠ H92), I66 (≠ T93), D161 (≠ N178), G241 (≠ D270), V242 (≠ S271), N243 (≠ A272), G305 (= G334), Y306 (≠ S335), Y376 (= Y405), I426 (≠ W447), M430 (≠ R451)
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, 95% coverage: 25:467/468 of query aligns to 9:443/444 of P12425
- G59 (= G90) 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 (≠ H92) 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 (= E158) binding Mg(2+)
- E134 (= E160) binding Mg(2+)
- E189 (= E221) binding Mg(2+)
- V190 (≠ Y222) 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 (= E228) binding Mg(2+)
- G241 (= G273) binding L-glutamate
- H245 (= H277) binding Mg(2+)
- G302 (= G334) 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 (≠ W336) 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 (= P338) 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 (= E365) binding Mg(2+)
- E424 (= E448) 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, 95% coverage: 25:467/468 of query aligns to 8:442/443 of 4lnkA
- active site: D52 (= D84), E131 (= E158), E133 (= E160), E188 (= E221), E195 (= E228), H244 (= H277), R315 (= R348), E332 (= E365), R334 (= R367)
- binding adenosine-5'-diphosphate: K43 (≠ S67), M50 (≠ L82), F198 (≠ I231), Y200 (≠ H233), N246 (≠ H279), S248 (= S281), S324 (≠ H357), S328 (≠ T361), R330 (= R363)
- binding glutamic acid: E133 (= E160), E188 (= E221), V189 (≠ Y222), N239 (≠ A272), G240 (= G273), G242 (≠ S275), E303 (≠ W336)
- binding magnesium ion: E131 (= E158), E188 (= E221), E195 (= E228), H244 (= H277), E332 (= E365)
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, 95% coverage: 25:467/468 of query aligns to 8:442/443 of 4lniA
- active site: D52 (= D84), E131 (= E158), E133 (= E160), E188 (= E221), E195 (= E228), H244 (= H277), R315 (= R348), E332 (= E365), R334 (= R367)
- binding adenosine-5'-diphosphate: E131 (= E158), E183 (≠ L216), D197 (≠ N230), Y200 (≠ H233), N246 (≠ H279), S248 (= S281), R320 (= R353), R330 (= R363)
- binding magnesium ion: E131 (= E158), E131 (= E158), E133 (= E160), E188 (= E221), E195 (= E228), E195 (= E228), H244 (= H277), E332 (= E365)
- binding l-methionine-s-sulfoximine phosphate: E133 (= E160), E188 (= E221), H244 (= H277), R297 (= R330), E303 (≠ W336), R315 (= R348), R334 (= R367)
7tdvC Glutamine synthetase (see paper)
31% identity, 95% coverage: 25:467/468 of query aligns to 8:442/443 of 7tdvC
- binding adenosine-5'-diphosphate: G129 (= G156), E131 (= E158), E183 (≠ L216), D197 (≠ N230), F198 (≠ I231), K199 (≠ E232), Y200 (≠ H233), N246 (≠ H279), V247 (≠ Q280), S248 (= S281), R320 (= R353), S328 (≠ T361), R330 (= R363)
- binding magnesium ion: E131 (= E158), E131 (= E158), E133 (= E160), E188 (= E221), E195 (= E228), E195 (= E228), H244 (= H277), E332 (= E365)
- binding l-methionine-s-sulfoximine phosphate: E131 (= E158), E133 (= E160), E188 (= E221), E195 (= E228), G240 (= G273), H244 (= H277), R297 (= R330), E303 (≠ W336), R315 (= R348)
7tdpA Structure of paenibacillus polymyxa gs bound to met-sox-p-adp (transition state complex) to 1.98 angstom (see paper)
30% identity, 93% coverage: 30:466/468 of query aligns to 12:437/439 of 7tdpA
- binding adenosine-5'-diphosphate: N123 (≠ T154), G125 (= G156), E127 (= E158), E179 (≠ L216), D193 (≠ N230), Y196 (≠ H233), N242 (≠ H279), S244 (= S281), R316 (= R353), R326 (= R363)
- binding magnesium ion: E127 (= E158), E127 (= E158), E129 (= E160), E184 (= E221), E191 (= E228), E191 (= E228), H240 (= H277), E328 (= E365)
- binding l-methionine-s-sulfoximine phosphate: E127 (= E158), E129 (= E160), E184 (= E221), E191 (= E228), G236 (= G273), H240 (= H277), R293 (= R330), E299 (≠ W336), R311 (= R348), R330 (= R367)
7tf6A Glutamine synthetase (see paper)
31% identity, 95% coverage: 25:467/468 of query aligns to 7:437/438 of 7tf6A
- binding glutamine: E128 (= E160), E183 (= E221), G235 (= G273), H239 (= H277), R292 (= R330), E298 (≠ W336)
- binding magnesium ion: E126 (= E158), E128 (= E160), E183 (= E221), E190 (= E228), H239 (= H277), E327 (= E365)
- binding : F58 (≠ I72), R60 (≠ D77), G232 (≠ D270), N234 (≠ A272), G296 (= G334), Y297 (≠ S335), R310 (= R348), Y367 (= Y405), Y421 (≠ R451), Q433 (≠ R463), Q437 (≠ R467)
7tfaB Glutamine synthetase (see paper)
30% identity, 93% coverage: 30:466/468 of query aligns to 12:439/441 of 7tfaB
- binding glutamine: E131 (= E160), Y153 (= Y176), E186 (= E221), G238 (= G273), H242 (= H277), R295 (= R330), E301 (≠ W336)
- binding magnesium ion: E129 (= E158), E131 (= E160), E186 (= E221), E193 (= E228), H242 (= H277), E330 (= E365)
- binding : Y58 (≠ W91), R60 (≠ H92), V187 (≠ Y222), N237 (≠ A272), G299 (= G334), Y300 (≠ S335), R313 (= R348), M424 (≠ R451)
7tf9S L. Monocytogenes gs(14)-q-glnr peptide (see paper)
29% identity, 93% coverage: 30:466/468 of query aligns to 13:441/443 of 7tf9S
- binding glutamine: E133 (= E160), Y155 (= Y176), E188 (= E221), G240 (= G273), G242 (≠ S275), R297 (= R330), E303 (≠ W336)
- binding magnesium ion: E131 (= E158), E133 (= E160), E188 (= E221), E195 (= E228), H244 (= H277), E332 (= E365)
- binding : F59 (≠ W91), V60 (vs. gap), E418 (≠ A443), I422 (≠ W447), M426 (≠ R451)
Query Sequence
>WP_011778857.1 NCBI__GCF_000015305.1:WP_011778857.1
MTNASIRPGRIDATNGQVESAPDAVRAMFERHGIRTVQFGMADIDGQVRGKFVPAEFFLD
SVARRGSSIPNIVFGWDIEDTLMDCFTVSGWHTGYSDVVLAPDLSTLRPVPWEPGHAFVL
CDVVNTDGSPVPVAPRTVLAGQVERAAALGYRLTAGYELEFYLYRETPETAAAKGYRNLT
PASPGTATFSLNRHSALEDVIGAIREGMRACDIPVLASNTEYGAGQIEINIEHADALTTA
DRVAIYKNGVRRIAEQHGYLATFMAKVATDSAGSSAHIHQSMQQLDAPARNAMWDGDRPS
ALMRQAVAGQLASMRDFTVLYCPTVNSYKRRVPGSWSPVSAAWGVDNRTAALRVIAHDEA
TCRMENRVPGADANPYLALAACLAGVLHGIENQLEPPAAVTGNAYQGADSPLPRSLAEAV
DAFGASSLARTAFGDAFVDHYLASRGWERDRHREAVSDWETGRYFSRV
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