SitesBLAST
Comparing WP_090446702.1 NCBI__GCF_900100495.1:WP_090446702.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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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, 95% coverage: 20:449/452 of query aligns to 40:469/472 of P78061
- H282 (= H261) mutation to N: Activity is impaired to 9% of wild-type.
- R357 (= R337) mutation to Q: Activity is impaired to 3% of wild-type.
8oooA Glutamine synthetase from methanothermococcus thermolithotrophicus in complex with 2-oxoglutarate and mgatp at 2.15 a resolution (see paper)
27% identity, 98% coverage: 3:444/452 of query aligns to 1:440/447 of 8oooA
- binding 2-oxoglutaric acid: F17 (≠ E19), R19 (≠ E21), A33 (≠ I35), R87 (vs. gap), V93 (≠ T98), P170 (≠ D182), R173 (≠ F185), R174 (≠ E186), S190 (≠ L202)
- binding adenosine-5'-triphosphate: E136 (= E140), E188 (≠ D200), F203 (= F215), K204 (≠ R216), F205 (≠ H217), H251 (= H263), S253 (= S265), R325 (= R337), R335 (= R347)
8ooqB Glutamine synthetase from Methanothermococcus thermolithotrophicus (see paper)
27% identity, 97% coverage: 5:444/452 of query aligns to 2:439/446 of 8ooqB
- binding 2-oxoglutaric acid: F16 (≠ E19), R18 (≠ E21), A32 (≠ I35), R86 (vs. gap), V92 (≠ T98), P169 (≠ D182), R172 (≠ F185), R173 (≠ E186), S189 (≠ L202)
- binding magnesium ion: E137 (= E142), E192 (= E205), E199 (= E212)
8tfkA Glutamine synthetase (see paper)
29% identity, 98% coverage: 2:444/452 of query aligns to 1:432/440 of 8tfkA
- binding adenosine-5'-diphosphate: E128 (= E140), D194 (≠ N214), F195 (= F215), F197 (≠ H217), N243 (≠ H263), R312 (= R332), R317 (= R337), G325 (≠ N345), R327 (= R347)
- binding magnesium ion: E128 (= E140), E128 (= E140), E130 (= E142), E185 (= E205), E192 (= E212), E192 (= E212), H241 (= H261), E329 (= E349)
- binding l-methionine-s-sulfoximine phosphate: E128 (= E140), E130 (= E142), E185 (= E205), E192 (= E212), G237 (= G257), H241 (= H261), R294 (= R314), E300 (≠ S320), R312 (= R332), R331 (= R351)
8ufjB Glutamine synthetase (see paper)
28% identity, 98% coverage: 2:444/452 of query aligns to 5:436/444 of 8ufjB
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, 98% coverage: 6:446/452 of query aligns to 6:437/443 of 4lnkA
- active site: D52 (≠ Q56), E131 (= E140), E133 (= E142), E188 (= E205), E195 (= E212), H244 (= H261), R315 (= R332), E332 (= E349), R334 (= R351)
- binding adenosine-5'-diphosphate: K43 (≠ M47), M50 (≠ L54), F198 (= F215), Y200 (≠ H217), N246 (≠ H263), S248 (= S265), S324 (≠ A341), S328 (≠ N345), R330 (= R347)
- binding glutamic acid: E133 (= E142), E188 (= E205), V189 (≠ D206), N239 (≠ P256), G240 (= G257), G242 (≠ A259), E303 (≠ S320)
- binding magnesium ion: E131 (= E140), E188 (= E205), E195 (= E212), H244 (= H261), E332 (= E349)
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, 98% coverage: 6:446/452 of query aligns to 6:437/443 of 4lniA
- active site: D52 (≠ Q56), E131 (= E140), E133 (= E142), E188 (= E205), E195 (= E212), H244 (= H261), R315 (= R332), E332 (= E349), R334 (= R351)
- binding adenosine-5'-diphosphate: E131 (= E140), E183 (≠ D200), D197 (≠ N214), Y200 (≠ H217), N246 (≠ H263), S248 (= S265), R320 (= R337), R330 (= R347)
- binding magnesium ion: E131 (= E140), E131 (= E140), E133 (= E142), E188 (= E205), E195 (= E212), E195 (= E212), H244 (= H261), E332 (= E349)
- binding l-methionine-s-sulfoximine phosphate: E133 (= E142), E188 (= E205), H244 (= H261), R297 (= R314), E303 (≠ S320), R315 (= R332), R334 (= R351)
4s0rD Structure of gs-tnra complex (see paper)
28% identity, 98% coverage: 6:446/452 of query aligns to 10:441/447 of 4s0rD
- active site: D56 (≠ Q56), E135 (= E140), E137 (= E142), E192 (= E205), E199 (= E212), H248 (= H261), R319 (= R332), E336 (= E349), R338 (= R351)
- binding glutamine: E137 (= E142), E192 (= E205), R301 (= R314), E307 (≠ S320)
- binding magnesium ion: I66 (≠ Y69), E135 (= E140), E135 (= E140), E199 (= E212), H248 (= H261), H248 (= H261), E336 (= E349), H419 (≠ G424)
- binding : F63 (≠ D66), V64 (≠ I67), R65 (≠ Y68), I66 (≠ Y69), D161 (≠ S174), G241 (≠ D254), V242 (≠ Q255), N243 (≠ P256), G305 (≠ D318), Y306 (≠ T319), Y376 (= Y389), I426 (≠ A431), M430 (≠ N435)
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, 98% coverage: 6:446/452 of query aligns to 7:438/444 of P12425
- G59 (≠ D65) 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 (≠ Y68) 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 (= E140) binding Mg(2+)
- E134 (= E142) binding Mg(2+)
- E189 (= E205) binding Mg(2+)
- V190 (≠ D206) 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 (= E212) binding Mg(2+)
- G241 (= G257) binding L-glutamate
- H245 (= H261) binding Mg(2+)
- G302 (≠ D318) 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 (≠ S320) 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 (= P322) 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 (= E349) binding Mg(2+)
- 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
8ooxB Glutamine synthetase (see paper)
29% identity, 98% coverage: 3:444/452 of query aligns to 1:430/438 of 8ooxB
8oozA Glutamine synthetase (see paper)
32% identity, 81% coverage: 78:444/452 of query aligns to 58:422/430 of 8oozA
- binding adenosine-5'-triphosphate: G117 (≠ A138), E170 (≠ D200), F185 (= F215), K186 (≠ R216), Y187 (≠ H217), N233 (≠ H263), S235 (= S265), S315 (≠ N345), R317 (= R347)
- binding magnesium ion: E119 (= E140), H231 (= H261), E319 (= E349)
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)
29% identity, 83% coverage: 75:450/452 of query aligns to 63:446/446 of P9WN37
- K363 (≠ E376) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
7tdpA Structure of paenibacillus polymyxa gs bound to met-sox-p-adp (transition state complex) to 1.98 angstom (see paper)
30% identity, 82% coverage: 78:449/452 of query aligns to 65:436/439 of 7tdpA
- binding adenosine-5'-diphosphate: N123 (vs. gap), G125 (≠ A138), E127 (= E140), E179 (≠ D200), D193 (≠ N214), Y196 (≠ H217), N242 (≠ H263), S244 (= S265), R316 (= R337), R326 (= R347)
- binding magnesium ion: E127 (= E140), E127 (= E140), E129 (= E142), E184 (= E205), E191 (= E212), E191 (= E212), H240 (= H261), E328 (= E349)
- binding l-methionine-s-sulfoximine phosphate: E127 (= E140), E129 (= E142), E184 (= E205), E191 (= E212), G236 (= G257), H240 (= H261), R293 (= R314), E299 (≠ S320), R311 (= R332), R330 (= R351)
7tf6A Glutamine synthetase (see paper)
30% identity, 82% coverage: 78:446/452 of query aligns to 65:432/438 of 7tf6A
- binding glutamine: E128 (= E142), E183 (= E205), G235 (= G257), H239 (= H261), R292 (= R314), E298 (≠ S320)
- binding magnesium ion: E126 (= E140), E128 (= E142), E183 (= E205), E190 (= E212), H239 (= H261), E327 (= E349)
- binding : G232 (≠ D254), N234 (≠ P256), G296 (≠ D318), Y297 (≠ T319), R310 (= R332), Y367 (= Y389), Y421 (≠ N435)
Sites not aligning to the query:
7tfaB Glutamine synthetase (see paper)
30% identity, 82% coverage: 78:449/452 of query aligns to 65:438/441 of 7tfaB
- binding glutamine: E131 (= E142), Y153 (vs. gap), E186 (= E205), G238 (= G257), H242 (= H261), R295 (= R314), E301 (≠ S320)
- binding magnesium ion: E129 (= E140), E131 (= E142), E186 (= E205), E193 (= E212), H242 (= H261), E330 (= E349)
- binding : V187 (≠ D206), N237 (≠ P256), G299 (≠ D318), Y300 (≠ T319), R313 (= R332), M424 (≠ N435)
Sites not aligning to the query:
7tdvC Glutamine synthetase (see paper)
30% identity, 82% coverage: 78:446/452 of query aligns to 66:437/443 of 7tdvC
- binding adenosine-5'-diphosphate: G129 (≠ A138), E131 (= E140), E183 (≠ D200), D197 (≠ N214), F198 (= F215), K199 (≠ R216), Y200 (≠ H217), N246 (≠ H263), V247 (≠ Q264), S248 (= S265), R320 (= R337), S328 (≠ N345), R330 (= R347)
- binding magnesium ion: E131 (= E140), E131 (= E140), E133 (= E142), E188 (= E205), E195 (= E212), E195 (= E212), H244 (= H261), E332 (= E349)
- binding l-methionine-s-sulfoximine phosphate: E131 (= E140), E133 (= E142), E188 (= E205), E195 (= E212), G240 (= G257), H244 (= H261), R297 (= R314), E303 (≠ S320), R315 (= R332)
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)
30% identity, 81% coverage: 78:444/452 of query aligns to 66:439/446 of A0R083
- K363 (≠ E376) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
5dm3C Crystal structure of glutamine synthetase from chromohalobacter salexigens dsm 3043(csal_0679, target efi-550015) with bound adp
30% identity, 80% coverage: 82:444/452 of query aligns to 57:390/396 of 5dm3C
- active site: E115 (= E140), E117 (= E142), E162 (= E205), E169 (= E212), H218 (= H261), R286 (= R332), E303 (= E349), R305 (= R351)
- binding adenosine-5'-diphosphate: R173 (= R216), C174 (≠ H217), H220 (= H263), S222 (= S265), R301 (= R347)
7tenA Glutamine synthetase (see paper)
29% identity, 82% coverage: 78:446/452 of query aligns to 65:436/442 of 7tenA
- binding adenosine-5'-diphosphate: G128 (≠ A138), E130 (= E140), E182 (≠ D200), D196 (≠ N214), F197 (= F215), K198 (≠ R216), Y199 (≠ H217), N245 (≠ H263), S247 (= S265), R319 (= R337), S327 (≠ N345), R329 (= R347)
- binding l-methionine-s-sulfoximine phosphate: E130 (= E140), E132 (= E142), E187 (= E205), E194 (= E212), N238 (≠ P256), G239 (= G257), H243 (= H261), R296 (= R314), E302 (≠ S320), R314 (= R332), R333 (= R351)
7tf9S L. Monocytogenes gs(14)-q-glnr peptide (see paper)
29% identity, 82% coverage: 78:446/452 of query aligns to 66:437/443 of 7tf9S
- binding glutamine: E133 (= E142), Y155 (≠ E180), E188 (= E205), G240 (= G257), G242 (≠ A259), R297 (= R314), E303 (≠ S320)
- binding magnesium ion: E131 (= E140), E133 (= E142), E188 (= E205), E195 (= E212), H244 (= H261), E332 (= E349)
- binding : E418 (≠ A427), I422 (≠ A431), M426 (≠ N435)
Sites not aligning to the query:
Query Sequence
>WP_090446702.1 NCBI__GCF_900100495.1:WP_090446702.1
MSTKLDQLASWLKERKITEVECLVSDLTGIARGKISPTNKFLDERGMRLPESVLLQTVTG
DYVEDDIYYELLDEADIDMFCRPDENAVFVVPWAIEPTAMVIHDTFDKQGNPIELSPRNI
LKKVLKMYADKGWQPIVAPEMEFYLTKRCGDPDFPLVAPMGRSGRPEVGRQSFSIDAANE
FDPLFEDVYDWCELQNLDLDTLIHEDGPAQMEINFRHGEPLSLADQITVFKRTMREAALK
HDVAATFMAKPITDQPGSAMHIHQSVVDVATGKNIFSNDDGSMSELFLYHIGGLQKYIPE
LLPLFAPSVNSFRRFLPDTSAPVNVEWGEENRTVGLRVPEAGPQNRRVENRLAGADANPY
LVLAATLLCGYIGMVEGIHASAPVKGRGYERRNLRLPLTLEAALERMEACKDAEKYLGEK
FVRGYVAVKRAEHENFKRVISSWEREFLLLSV
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