SitesBLAST
Comparing WP_012706904.1 NCBI__GCF_000018545.1:WP_012706904.1 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)
34% identity, 90% coverage: 48:477/478 of query aligns to 40:471/472 of P78061
- H282 (= H288) mutation to N: Activity is impaired to 9% of wild-type.
- R357 (= R364) mutation to Q: Activity is impaired to 3% of wild-type.
8tfkA Glutamine synthetase (see paper)
32% identity, 77% coverage: 103:470/478 of query aligns to 62:432/440 of 8tfkA
- binding adenosine-5'-diphosphate: E128 (= E167), D194 (≠ N241), F195 (≠ L242), F197 (≠ H244), N243 (≠ H290), R312 (= R359), R317 (= R364), G325 (≠ A372), R327 (= R374)
- binding magnesium ion: E128 (= E167), E128 (= E167), E130 (= E169), E185 (= E232), E192 (= E239), E192 (= E239), H241 (= H288), E329 (= E376)
- binding l-methionine-s-sulfoximine phosphate: E128 (= E167), E130 (= E169), E185 (= E232), E192 (= E239), G237 (= G284), H241 (= H288), R294 (= R341), E300 (≠ S347), R312 (= R359), R331 (= R378)
8oooA Glutamine synthetase from methanothermococcus thermolithotrophicus in complex with 2-oxoglutarate and mgatp at 2.15 a resolution (see paper)
32% identity, 77% coverage: 102:470/478 of query aligns to 68:440/447 of 8oooA
- binding 2-oxoglutaric acid: R87 (≠ E121), V93 (≠ T125), P170 (≠ D209), R173 (≠ I212), R174 (≠ D213), S190 (≠ L229)
- binding adenosine-5'-triphosphate: E136 (= E167), E188 (≠ D227), F203 (≠ L242), K204 (≠ R243), F205 (≠ H244), H251 (= H290), S253 (= S292), R325 (= R364), R335 (= R374)
Sites not aligning to the query:
8ooqB Glutamine synthetase from Methanothermococcus thermolithotrophicus (see paper)
32% identity, 77% coverage: 102:470/478 of query aligns to 67:439/446 of 8ooqB
Sites not aligning to the query:
8ufjB Glutamine synthetase (see paper)
32% identity, 77% coverage: 103:470/478 of query aligns to 66:436/444 of 8ufjB
7tdpA Structure of paenibacillus polymyxa gs bound to met-sox-p-adp (transition state complex) to 1.98 angstom (see paper)
33% identity, 78% coverage: 103:475/478 of query aligns to 63:436/439 of 7tdpA
- binding adenosine-5'-diphosphate: N123 (vs. gap), G125 (≠ A165), E127 (= E167), E179 (≠ D227), D193 (≠ N241), Y196 (≠ H244), N242 (≠ H290), S244 (= S292), R316 (= R364), R326 (= R374)
- binding magnesium ion: E127 (= E167), E127 (= E167), E129 (= E169), E184 (= E232), E191 (= E239), E191 (= E239), H240 (= H288), E328 (= E376)
- binding l-methionine-s-sulfoximine phosphate: E127 (= E167), E129 (= E169), E184 (= E232), E191 (= E239), G236 (= G284), H240 (= H288), R293 (= R341), E299 (≠ S347), R311 (= R359), R330 (= R378)
7tfaB Glutamine synthetase (see paper)
32% identity, 78% coverage: 103:475/478 of query aligns to 63:438/441 of 7tfaB
- binding glutamine: E131 (= E169), Y153 (≠ R189), E186 (= E232), G238 (= G284), H242 (= H288), R295 (= R341), E301 (≠ S347)
- binding magnesium ion: E129 (= E167), E131 (= E169), E186 (= E232), E193 (= E239), H242 (= H288), E330 (= E376)
- binding : V187 (≠ E233), N237 (≠ P283), G299 (≠ D345), Y300 (≠ M346), R313 (= R359), M424 (≠ T461)
Sites not aligning to the query:
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)
32% identity, 77% coverage: 103:472/478 of query aligns to 64:437/443 of 4lnkA
- active site: E131 (= E167), E133 (= E169), E188 (= E232), E195 (= E239), H244 (= H288), R315 (= R359), E332 (= E376), R334 (= R378)
- binding adenosine-5'-diphosphate: F198 (≠ L242), Y200 (≠ H244), N246 (≠ H290), S248 (= S292), S324 (= S368), S328 (≠ A372), R330 (= R374)
- binding glutamic acid: E133 (= E169), E188 (= E232), V189 (≠ E233), N239 (≠ P283), G240 (= G284), G242 (≠ A286), E303 (≠ S347)
- binding magnesium ion: E131 (= E167), E188 (= E232), E195 (= E239), H244 (= H288), E332 (= E376)
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)
32% identity, 77% coverage: 103:472/478 of query aligns to 64:437/443 of 4lniA
- active site: E131 (= E167), E133 (= E169), E188 (= E232), E195 (= E239), H244 (= H288), R315 (= R359), E332 (= E376), R334 (= R378)
- binding adenosine-5'-diphosphate: E131 (= E167), E183 (≠ D227), D197 (≠ N241), Y200 (≠ H244), N246 (≠ H290), S248 (= S292), R320 (= R364), R330 (= R374)
- binding magnesium ion: E131 (= E167), E131 (= E167), E133 (= E169), E188 (= E232), E195 (= E239), E195 (= E239), H244 (= H288), E332 (= E376)
- binding l-methionine-s-sulfoximine phosphate: E133 (= E169), E188 (= E232), H244 (= H288), R297 (= R341), E303 (≠ S347), R315 (= R359), R334 (= R378)
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)
32% identity, 77% coverage: 103:472/478 of query aligns to 65:438/444 of P12425
- E132 (= E167) binding Mg(2+)
- E134 (= E169) binding Mg(2+)
- E189 (= E232) binding Mg(2+)
- V190 (≠ E233) 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 (= E239) binding Mg(2+)
- G241 (= G284) binding L-glutamate
- H245 (= H288) binding Mg(2+)
- G302 (≠ D345) 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 (≠ S347) 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 (= P349) 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 (= E376) binding Mg(2+)
- E424 (= E458) 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.
4s0rD Structure of gs-tnra complex (see paper)
32% identity, 77% coverage: 103:472/478 of query aligns to 68:441/447 of 4s0rD
- active site: E135 (= E167), E137 (= E169), E192 (= E232), E199 (= E239), H248 (= H288), R319 (= R359), E336 (= E376), R338 (= R378)
- binding glutamine: E137 (= E169), E192 (= E232), R301 (= R341), E307 (≠ S347)
- binding magnesium ion: E135 (= E167), E135 (= E167), E199 (= E239), H248 (= H288), H248 (= H288), E336 (= E376), H419 (≠ I450)
- binding : D161 (≠ S201), G241 (= G281), V242 (≠ Q282), N243 (≠ P283), G305 (≠ D345), Y306 (≠ M346), Y376 (vs. gap), I426 (≠ G457), M430 (≠ T461)
Sites not aligning to the query:
7tf9S L. Monocytogenes gs(14)-q-glnr peptide (see paper)
32% identity, 77% coverage: 103:472/478 of query aligns to 64:437/443 of 7tf9S
- binding glutamine: E133 (= E169), Y155 (≠ G199), E188 (= E232), G240 (= G284), G242 (≠ A286), R297 (= R341), E303 (≠ S347)
- binding magnesium ion: E131 (= E167), E133 (= E169), E188 (= E232), E195 (= E239), H244 (= H288), E332 (= E376)
- binding : E418 (≠ G453), I422 (≠ G457), M426 (≠ T461)
Sites not aligning to the query:
7tenA Glutamine synthetase (see paper)
32% identity, 77% coverage: 103:472/478 of query aligns to 63:436/442 of 7tenA
- binding adenosine-5'-diphosphate: G128 (≠ A165), E130 (= E167), E182 (≠ D227), D196 (≠ N241), F197 (≠ L242), K198 (≠ R243), Y199 (≠ H244), N245 (≠ H290), S247 (= S292), R319 (= R364), S327 (≠ A372), R329 (= R374)
- binding l-methionine-s-sulfoximine phosphate: E130 (= E167), E132 (= E169), E187 (= E232), E194 (= E239), N238 (≠ P283), G239 (= G284), H243 (= H288), R296 (= R341), E302 (≠ S347), R314 (= R359), R333 (= R378)
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)
32% identity, 77% coverage: 103:470/478 of query aligns to 64:439/446 of A0R083
- K363 (≠ E403) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
8ooxB Glutamine synthetase (see paper)
29% identity, 87% coverage: 54:470/478 of query aligns to 24:430/438 of 8ooxB
8oozA Glutamine synthetase (see paper)
31% identity, 77% coverage: 104:470/478 of query aligns to 57:422/430 of 8oozA
- binding adenosine-5'-triphosphate: G117 (≠ A165), E170 (≠ D227), F185 (≠ L242), K186 (≠ R243), Y187 (≠ H244), N233 (≠ H290), S235 (= S292), S315 (≠ A372), R317 (= R374)
- binding magnesium ion: E119 (= E167), H231 (= H288), E319 (= E376)
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)
31% identity, 78% coverage: 103:476/478 of query aligns to 64:446/446 of P9WN37
- K363 (≠ E403) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
7tf6A Glutamine synthetase (see paper)
30% identity, 77% coverage: 103:472/478 of query aligns to 63:432/438 of 7tf6A
- binding glutamine: E128 (= E169), E183 (= E232), G235 (= G284), H239 (= H288), R292 (= R341), E298 (≠ S347)
- binding magnesium ion: E126 (= E167), E128 (= E169), E183 (= E232), E190 (= E239), H239 (= H288), E327 (= E376)
- binding : G232 (= G281), N234 (≠ P283), G296 (≠ D345), Y297 (≠ M346), R310 (= R359), Y367 (≠ N416), Y421 (≠ T461)
Sites not aligning to the query:
7tdvC Glutamine synthetase (see paper)
30% identity, 77% coverage: 103:472/478 of query aligns to 64:437/443 of 7tdvC
- binding adenosine-5'-diphosphate: G129 (≠ A165), E131 (= E167), E183 (≠ D227), D197 (≠ N241), F198 (≠ L242), K199 (≠ R243), Y200 (≠ H244), N246 (≠ H290), V247 (≠ Q291), S248 (= S292), R320 (= R364), S328 (≠ A372), R330 (= R374)
- binding magnesium ion: E131 (= E167), E131 (= E167), E133 (= E169), E188 (= E232), E195 (= E239), E195 (= E239), H244 (= H288), E332 (= E376)
- binding l-methionine-s-sulfoximine phosphate: E131 (= E167), E133 (= E169), E188 (= E232), E195 (= E239), G240 (= G284), H244 (= H288), R297 (= R341), E303 (≠ S347), R315 (= R359)
5dm3C Crystal structure of glutamine synthetase from chromohalobacter salexigens dsm 3043(csal_0679, target efi-550015) with bound adp
29% identity, 76% coverage: 110:470/478 of query aligns to 58:390/396 of 5dm3C
- active site: E115 (= E167), E117 (= E169), E162 (= E232), E169 (= E239), H218 (= H288), R286 (= R359), E303 (= E376), R305 (= R378)
- binding adenosine-5'-diphosphate: R173 (= R243), C174 (≠ H244), H220 (= H290), S222 (= S292), R301 (= R374)
Query Sequence
>WP_012706904.1 NCBI__GCF_000018545.1:WP_012706904.1
MSSKRSVGQQTAKVSKSSGVPLALHAPRGVKTWKEAVDWLKIRGIEDIECITPDLAGVPR
GKMMPTSKFTSNTSLALPSAIYRHTISGEYPEETGQFRYDSRDSDIKLVPDLSTISIVPW
ESDPTAQVICDIVGSQGEQISYTPRNVLKRVLDLYRQKGWKPVVAPEIEFYLVAQNDDPD
YPLRPPKGRSGRSILGGQGYSIAGINEFDELIDDIYHFSEKQGLEIDTLIHEEGPAQLEI
NLRHGDPIELADQVFMFKRTIREAALKHGIYATFMAKPMQGQPGSAMHIHQSVIDIETGR
NIFSSPDGSPSKEFFAFIGGMQHYVPKTLSMMAPYVNSYRRLTPDMSAPVNTAWGYDNRT
TAFRIPVSDPVARRIENRLPSSDANPYLALAASLGCGYLGIMEDLQPTPPSEDTANEGEI
DLPRGLLEAISLLESEPSLAEVFSAEFIAIYAGVKRGEFETFMQVISPWEREFLLLNV
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