SitesBLAST
Comparing WP_012043321.1 NCBI__GCF_000015165.1:WP_012043321.1 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)
8wwvA Glutamine synthetase
48% identity, 98% coverage: 11:498/500 of query aligns to 2:488/490 of 8wwvA
- binding adenosine-5'-diphosphate: G155 (= G165), E157 (= E167), R224 (= R234), F239 (= F249), D240 (= D250), V241 (= V251), H288 (= H298), S290 (= S300), R374 (≠ H385), E376 (= E387)
- binding magnesium ion: E157 (= E167), E236 (= E246)
- binding manganese (ii) ion: E157 (= E167), E159 (= E169), E229 (= E239), E236 (= E246), H286 (= H296), E376 (= E387)
- binding l-methionine-s-sulfoximine phosphate: E157 (= E167), E159 (= E169), E229 (= E239), E236 (= E246), A282 (= A292), H286 (= H296), R340 (= R351), K358 (≠ R369)
8wwuB Glutamine synthetase
48% identity, 98% coverage: 11:498/500 of query aligns to 4:490/492 of 8wwuB
- binding phosphoaminophosphonic acid-adenylate ester: G157 (= G165), E159 (= E167), R226 (= R234), F241 (= F249), V243 (= V251), H290 (= H298), S292 (= S300), K360 (≠ R369), R365 (= R374), R376 (≠ H385)
- binding magnesium ion: E159 (= E167), E238 (= E246)
- binding manganese (ii) ion: E159 (= E167), E161 (= E169), E231 (= E239), E238 (= E246), H288 (= H296), E378 (= E387)
8tfkA Glutamine synthetase (see paper)
30% identity, 91% coverage: 28:484/500 of query aligns to 5:434/440 of 8tfkA
- binding adenosine-5'-diphosphate: E128 (= E167), D194 (≠ T248), F195 (= F249), F197 (≠ V251), N243 (≠ H298), R312 (= R369), R317 (= R374), G325 (≠ S383), R327 (≠ H385)
- binding magnesium ion: E128 (= E167), E128 (= E167), E130 (= E169), E185 (= E239), E192 (= E246), E192 (= E246), H241 (= H296), E329 (= E387)
- binding l-methionine-s-sulfoximine phosphate: E128 (= E167), E130 (= E169), E185 (= E239), E192 (= E246), G237 (≠ A292), H241 (= H296), R294 (= R351), E300 (≠ L357), R312 (= R369), R331 (= R389)
8oozA Glutamine synthetase (see paper)
31% identity, 95% coverage: 28:500/500 of query aligns to 5:430/430 of 8oozA
- binding adenosine-5'-triphosphate: G117 (= G165), E170 (≠ R234), F185 (= F249), K186 (≠ D250), Y187 (≠ V251), N233 (≠ H298), S235 (= S300), S315 (= S383), R317 (≠ H385)
- binding magnesium ion: E119 (= E167), H231 (= H296), E319 (= E387)
8ufjB Glutamine synthetase (see paper)
30% identity, 91% coverage: 28:484/500 of query aligns to 9:438/444 of 8ufjB
8ooxB Glutamine synthetase (see paper)
32% identity, 95% coverage: 28:500/500 of query aligns to 5:438/438 of 8ooxB
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: 34:500/500 of query aligns to 12:439/439 of 7tdpA
- binding adenosine-5'-diphosphate: N123 (vs. gap), G125 (= G165), E127 (= E167), E179 (≠ R234), D193 (≠ T248), Y196 (≠ V251), N242 (≠ H298), S244 (= S300), R316 (= R374), R326 (≠ H385)
- binding magnesium ion: E127 (= E167), E127 (= E167), E129 (= E169), E184 (= E239), E191 (= E246), E191 (= E246), H240 (= H296), E328 (= E387)
- binding l-methionine-s-sulfoximine phosphate: E127 (= E167), E129 (= E169), E184 (= E239), E191 (= E246), G236 (≠ A292), H240 (= H296), R293 (= R351), E299 (≠ L357), R311 (= R369), R330 (= R389)
8ooqB Glutamine synthetase from Methanothermococcus thermolithotrophicus (see paper)
33% identity, 79% coverage: 92:484/500 of query aligns to 51:441/446 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)
33% identity, 79% coverage: 92:484/500 of query aligns to 52:442/447 of 8oooA
- binding 2-oxoglutaric acid: R87 (≠ S122), V93 (≠ T125), P170 (≠ A200), R173 (≠ M215), R174 (≠ D216), S190 (≠ M236)
- binding adenosine-5'-triphosphate: E136 (= E167), E188 (≠ R234), F203 (= F249), K204 (≠ D250), F205 (≠ V251), H251 (= H298), S253 (= S300), R325 (= R374), R335 (≠ H385)
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)
29% identity, 94% coverage: 33:500/500 of query aligns to 13:444/444 of P12425
- G59 (= G95) 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 (≠ M98) 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 (= E167) binding Mg(2+)
- E134 (= E169) binding Mg(2+)
- E189 (= E239) binding Mg(2+)
- V190 (≠ M240) 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 (= E246) binding Mg(2+)
- G241 (≠ A292) binding L-glutamate
- H245 (= H296) binding Mg(2+)
- G302 (≠ N355) 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 (≠ L357) 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 (= P359) 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 (= E387) binding Mg(2+)
- E424 (= E470) 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)
29% identity, 94% coverage: 33:500/500 of query aligns to 12:443/443 of 4lnkA
- active site: D52 (≠ T73), E131 (= E167), E133 (= E169), E188 (= E239), E195 (= E246), H244 (= H296), R315 (= R369), E332 (= E387), R334 (= R389)
- binding adenosine-5'-diphosphate: K43 (≠ A64), M50 (≠ E71), F198 (= F249), Y200 (≠ V251), N246 (≠ H298), S248 (= S300), S324 (≠ M378), S328 (= S383), R330 (≠ H385)
- binding glutamic acid: E133 (= E169), E188 (= E239), V189 (≠ M240), N239 (≠ V291), G240 (≠ A292), G242 (= G294), E303 (≠ L357)
- binding magnesium ion: E131 (= E167), E188 (= E239), E195 (= E246), H244 (= H296), E332 (= E387)
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, 94% coverage: 33:500/500 of query aligns to 12:443/443 of 4lniA
- active site: D52 (≠ T73), E131 (= E167), E133 (= E169), E188 (= E239), E195 (= E246), H244 (= H296), R315 (= R369), E332 (= E387), R334 (= R389)
- binding adenosine-5'-diphosphate: E131 (= E167), E183 (≠ R234), D197 (≠ T248), Y200 (≠ V251), N246 (≠ H298), S248 (= S300), R320 (= R374), R330 (≠ H385)
- binding magnesium ion: E131 (= E167), E131 (= E167), E133 (= E169), E188 (= E239), E195 (= E246), E195 (= E246), H244 (= H296), E332 (= E387)
- binding l-methionine-s-sulfoximine phosphate: E133 (= E169), E188 (= E239), H244 (= H296), R297 (= R351), E303 (≠ L357), R315 (= R369), R334 (= R389)
4s0rD Structure of gs-tnra complex (see paper)
29% identity, 94% coverage: 33:500/500 of query aligns to 16:447/447 of 4s0rD
- active site: D56 (≠ T73), E135 (= E167), E137 (= E169), E192 (= E239), E199 (= E246), H248 (= H296), R319 (= R369), E336 (= E387), R338 (= R389)
- binding glutamine: E137 (= E169), E192 (= E239), R301 (= R351), E307 (≠ L357)
- binding magnesium ion: I66 (≠ A99), E135 (= E167), E135 (= E167), E199 (= E246), H248 (= H296), H248 (= H296), E336 (= E387), H419 (≠ W462)
- binding : F63 (= F96), V64 (≠ G97), R65 (≠ M98), I66 (≠ A99), D161 (≠ G189), G241 (≠ N289), V242 (≠ Y290), N243 (≠ V291), G305 (≠ N355), Y306 (≠ S356), Y376 (= Y426), I426 (≠ S469), M430 (≠ A483)
7tfaB Glutamine synthetase (see paper)
30% identity, 93% coverage: 34:500/500 of query aligns to 12:441/441 of 7tfaB
- binding glutamine: E131 (= E169), Y153 (≠ T187), E186 (= E239), G238 (≠ A292), H242 (= H296), R295 (= R351), E301 (≠ L357)
- binding magnesium ion: E129 (= E167), E131 (= E169), E186 (= E239), E193 (= E246), H242 (= H296), E330 (= E387)
- binding : Y58 (≠ A99), R60 (≠ M101), V187 (≠ M240), N237 (≠ V291), G299 (≠ N355), Y300 (≠ S356), R313 (= R369), M424 (≠ A483)
7cqwA Gmas/adp complex-conformation 1 (see paper)
34% identity, 71% coverage: 91:447/500 of query aligns to 42:389/430 of 7cqwA
7cquA Gmas/adp/metsox-p complex (see paper)
34% identity, 71% coverage: 91:447/500 of query aligns to 41:388/429 of 7cquA
- binding adenosine-5'-diphosphate: E121 (= E167), Y173 (≠ R234), N187 (≠ T248), W188 (≠ F249), D189 (= D250), Y190 (≠ V251), H236 (= H298), L237 (≠ Q299), S238 (= S300), R316 (= R374), R322 (≠ H385)
- binding magnesium ion: E121 (= E167), E121 (= E167), E123 (= E169), E178 (= E239), E185 (= E246), E185 (= E246), H234 (= H296), E324 (= E387)
- binding l-methionine-s-sulfoximine phosphate: E121 (= E167), E123 (= E169), E178 (= E239), E185 (= E246), T229 (≠ V291), G230 (≠ A292), H234 (= H296), R287 (= R351), W299 (≠ L357), R311 (= R369), R326 (= R389)
7cqqA Gmas in complex with amppnp and metsox (see paper)
34% identity, 71% coverage: 91:447/500 of query aligns to 41:388/429 of 7cqqA
- binding phosphoaminophosphonic acid-adenylate ester: E121 (= E167), Y173 (≠ R234), E185 (= E246), N187 (≠ T248), D189 (= D250), Y190 (≠ V251), H234 (= H296), H236 (= H298), S238 (= S300), R311 (= R369), R316 (= R374), R322 (≠ H385), E324 (= E387)
- binding magnesium ion: E121 (= E167), E121 (= E167), E123 (= E169), E178 (= E239), E185 (= E246), E185 (= E246), H234 (= H296), E324 (= E387)
- binding (2s)-2-amino-4-(methylsulfonimidoyl)butanoic acid: E123 (= E169), E178 (= E239), T229 (≠ V291), H234 (= H296), R287 (= R351), W299 (≠ L357), R311 (= R369), R326 (= R389)
7cqnA Gmas in complex with amppcp (see paper)
34% identity, 71% coverage: 91:447/500 of query aligns to 41:388/429 of 7cqnA
- binding phosphomethylphosphonic acid adenylate ester: G45 (= G95), D61 (≠ N106), E121 (= E167), Y173 (≠ R234), Q174 (≠ T235), W188 (≠ F249), D189 (= D250), Y190 (≠ V251), H236 (= H298), S238 (= S300), R311 (= R369), R316 (= R374), R322 (≠ H385)
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, 94% coverage: 30:498/500 of query aligns to 9:445/446 of A0R083
- K363 (≠ R414) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
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, 94% coverage: 30:498/500 of query aligns to 9:445/446 of P9WN37
- K363 (≠ R414) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
Query Sequence
>WP_012043321.1 NCBI__GCF_000015165.1:WP_012043321.1
MRGGANVSSGFIEAHGLWSDEQKAAAGEALAAVKETGLRCIRVSVADPQGKLRSKTLMPG
PFHAALKNGIEFTNAQYGFDSAEGIAYNPFVDGGGFGMAEMAGFANVILVPDPTTFRVLP
WSPGTGWVLGDLYFRDGRPVPFDARHKLKAALAELAREKYTFITGLEIEFYVTKVIDPKL
APEDMGTLGLPPTPPVVEAAARGFSYQVEDNLDRMDDFICTLADHCVALNLPLRTMENEM
GPGQLEFTFDVQTGLKTADTMSLFRSMVKQVATRMGLHATFMTRPGLPNYVASGWHLHQS
LATADGRNAFVSEPGSGELLSEVGRRFVGGLLEHAAAASVFTTPTVNGYRRRKPNSLAPD
RATWGYDNRAAMIRVQGMPGEPSAHIENRIGEPGANPYLYIASQALAGLDGLRRKLDPGP
LETSPYTATHRPLLPTNLMEALEALKGSSYFRAQLGDVFVDWLLGMKQSEVNRFLAAEPD
WQATPDDVTAWEHREYFTRY
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