SitesBLAST
Comparing WP_011446251.1 NCBI__GCF_000013325.1:WP_011446251.1 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)
8tfkA Glutamine synthetase (see paper)
29% identity, 85% coverage: 49:421/441 of query aligns to 28:420/440 of 8tfkA
- binding adenosine-5'-diphosphate: E128 (= E134), D194 (≠ T200), F195 (≠ L201), F197 (≠ Y203), N243 (= N249), R312 (= R319), R317 (= R324), G325 (≠ A332), R327 (= R334)
- binding magnesium ion: E128 (= E134), E128 (= E134), E130 (= E136), E185 (= E191), E192 (= E198), E192 (= E198), H241 (= H247), E329 (= E336)
- binding l-methionine-s-sulfoximine phosphate: E128 (= E134), E130 (= E136), E185 (= E191), E192 (= E198), G237 (= G243), H241 (= H247), R294 (= R301), E300 (≠ L307), R312 (= R319), R331 (= R338)
8ufjB Glutamine synthetase (see paper)
29% identity, 85% coverage: 49:421/441 of query aligns to 32:424/444 of 8ufjB
P78061 Gamma-glutamylputrescine synthetase PuuA; Gamma-Glu-Put synthetase; Glutamate--putrescine ligase; EC 6.3.1.11 from Escherichia coli (strain K12) (see paper)
31% identity, 91% coverage: 22:422/441 of query aligns to 42:453/472 of P78061
- H282 (= H247) mutation to N: Activity is impaired to 9% of wild-type.
- R357 (= R324) mutation to Q: Activity is impaired to 3% of wild-type.
8ooqB Glutamine synthetase from Methanothermococcus thermolithotrophicus (see paper)
30% identity, 79% coverage: 74:421/441 of query aligns to 75:427/446 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)
30% identity, 79% coverage: 74:421/441 of query aligns to 76:428/447 of 8oooA
- binding 2-oxoglutaric acid: R87 (= R86), V93 (≠ G92), P170 (≠ A168), R173 (≠ I171), R174 (≠ D172), S190 (≠ M188)
- binding adenosine-5'-triphosphate: E136 (= E134), E188 (= E186), F203 (≠ L201), K204 (≠ R202), F205 (≠ Y203), H251 (≠ N249), S253 (= S251), R325 (= R324), R335 (= R334)
Sites not aligning to the query:
8oozA Glutamine synthetase (see paper)
30% identity, 71% coverage: 104:417/441 of query aligns to 89:406/430 of 8oozA
- binding adenosine-5'-triphosphate: G117 (= G132), E170 (= E186), F185 (≠ L201), K186 (≠ R202), Y187 (= Y203), N233 (= N249), S235 (= S251), S315 (≠ A332), R317 (= R334)
- binding magnesium ion: E119 (= E134), H231 (= H247), E319 (= E336)
8ooxB Glutamine synthetase (see paper)
30% identity, 71% coverage: 104:417/441 of query aligns to 97:414/438 of 8ooxB
7tdpA Structure of paenibacillus polymyxa gs bound to met-sox-p-adp (transition state complex) to 1.98 angstom (see paper)
31% identity, 72% coverage: 104:421/441 of query aligns to 96:419/439 of 7tdpA
- binding adenosine-5'-diphosphate: N123 (vs. gap), G125 (= G132), E127 (= E134), E179 (= E186), D193 (≠ T200), Y196 (= Y203), N242 (= N249), S244 (= S251), R316 (= R324), R326 (= R334)
- binding magnesium ion: E127 (= E134), E127 (= E134), E129 (= E136), E184 (= E191), E191 (= E198), E191 (= E198), H240 (= H247), E328 (= E336)
- binding l-methionine-s-sulfoximine phosphate: E127 (= E134), E129 (= E136), E184 (= E191), E191 (= E198), G236 (= G243), H240 (= H247), R293 (= R301), E299 (≠ L307), R311 (= R319), R330 (= R338)
7tfaB Glutamine synthetase (see paper)
31% identity, 72% coverage: 104:421/441 of query aligns to 98:421/441 of 7tfaB
- binding glutamine: E131 (= E136), Y153 (≠ V158), E186 (= E191), G238 (= G243), H242 (= H247), R295 (= R301), E301 (≠ L307)
- binding magnesium ion: E129 (= E134), E131 (= E136), E186 (= E191), E193 (= E198), H242 (= H247), E330 (= E336)
- binding : V187 (≠ F192), N237 (≠ S242), G299 (≠ A305), Y300 (≠ S306), R313 (= R319)
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, 72% coverage: 104:421/441 of query aligns to 101:424/444 of P12425
- E132 (= E134) binding Mg(2+)
- E134 (= E136) binding Mg(2+)
- E189 (= E191) binding Mg(2+)
- V190 (≠ F192) 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 (= E198) binding Mg(2+)
- G241 (= G243) binding L-glutamate
- H245 (= H247) binding Mg(2+)
- G302 (≠ A305) 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 (≠ L307) 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 (≠ G309) 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 (= E336) binding Mg(2+)
- E424 (= E421) 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.
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, 72% coverage: 104:421/441 of query aligns to 100:423/443 of 4lnkA
- active site: E131 (= E134), E133 (= E136), E188 (= E191), E195 (= E198), H244 (= H247), R315 (= R319), E332 (= E336), R334 (= R338)
- binding adenosine-5'-diphosphate: F198 (≠ L201), Y200 (= Y203), N246 (= N249), S248 (= S251), S324 (≠ E328), S328 (≠ A332), R330 (= R334)
- binding glutamic acid: E133 (= E136), E188 (= E191), V189 (≠ F192), N239 (≠ S242), G240 (= G243), G242 (= G245), E303 (≠ L307)
- binding magnesium ion: E131 (= E134), E188 (= E191), E195 (= E198), H244 (= H247), E332 (= E336)
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)
29% identity, 72% coverage: 104:421/441 of query aligns to 100:423/443 of 4lniA
- active site: E131 (= E134), E133 (= E136), E188 (= E191), E195 (= E198), H244 (= H247), R315 (= R319), E332 (= E336), R334 (= R338)
- binding adenosine-5'-diphosphate: E131 (= E134), E183 (= E186), D197 (≠ T200), Y200 (= Y203), N246 (= N249), S248 (= S251), R320 (= R324), R330 (= R334)
- binding magnesium ion: E131 (= E134), E131 (= E134), E133 (= E136), E188 (= E191), E195 (= E198), E195 (= E198), H244 (= H247), E332 (= E336)
- binding l-methionine-s-sulfoximine phosphate: E133 (= E136), E188 (= E191), H244 (= H247), R297 (= R301), E303 (≠ L307), R315 (= R319), R334 (= R338)
Sites not aligning to the query:
4s0rD Structure of gs-tnra complex (see paper)
29% identity, 72% coverage: 104:421/441 of query aligns to 104:427/447 of 4s0rD
- active site: E135 (= E134), E137 (= E136), E192 (= E191), E199 (= E198), H248 (= H247), R319 (= R319), E336 (= E336), R338 (= R338)
- binding glutamine: E137 (= E136), E192 (= E191), R301 (= R301), E307 (≠ L307)
- binding magnesium ion: E135 (= E134), E135 (= E134), E199 (= E198), H248 (= H247), H248 (= H247), E336 (= E336), H419 (≠ N413)
- binding : D161 (≠ G160), G241 (≠ Q240), V242 (≠ K241), N243 (≠ S242), G305 (≠ A305), Y306 (≠ S306), Y376 (≠ L376), I426 (≠ D420)
Sites not aligning to the query:
7cquA Gmas/adp/metsox-p complex (see paper)
31% identity, 89% coverage: 9:399/441 of query aligns to 4:389/429 of 7cquA
- binding adenosine-5'-diphosphate: E121 (= E134), Y173 (≠ S187), N187 (≠ T200), W188 (≠ L201), D189 (≠ R202), Y190 (= Y203), H236 (≠ N249), L237 (= L250), S238 (= S251), R316 (= R324), R322 (= R334)
- binding magnesium ion: E121 (= E134), E121 (= E134), E123 (= E136), E178 (≠ F192), E185 (= E198), E185 (= E198), H234 (= H247), E324 (= E336)
- binding l-methionine-s-sulfoximine phosphate: E121 (= E134), E123 (= E136), E178 (≠ F192), E185 (= E198), T229 (≠ S242), G230 (= G243), H234 (= H247), R287 (= R301), W299 (= W311), R311 (= R319), R326 (= R338)
7cqqA Gmas in complex with amppnp and metsox (see paper)
31% identity, 89% coverage: 9:399/441 of query aligns to 4:389/429 of 7cqqA
- binding phosphoaminophosphonic acid-adenylate ester: E121 (= E134), Y173 (≠ S187), E185 (= E198), N187 (≠ T200), D189 (≠ R202), Y190 (= Y203), H234 (= H247), H236 (≠ N249), S238 (= S251), R311 (= R319), R316 (= R324), R322 (= R334), E324 (= E336)
- binding magnesium ion: E121 (= E134), E121 (= E134), E123 (= E136), E178 (≠ F192), E185 (= E198), E185 (= E198), H234 (= H247), E324 (= E336)
- binding (2s)-2-amino-4-(methylsulfonimidoyl)butanoic acid: E123 (= E136), E178 (≠ F192), T229 (≠ S242), H234 (= H247), R287 (= R301), W299 (= W311), R311 (= R319), R326 (= R338)
7cqnA Gmas in complex with amppcp (see paper)
31% identity, 89% coverage: 9:399/441 of query aligns to 4:389/429 of 7cqnA
- binding phosphomethylphosphonic acid adenylate ester: G45 (≠ F53), D61 (≠ M69), E121 (= E134), Y173 (≠ S187), Q174 (≠ M188), W188 (≠ L201), D189 (≠ R202), Y190 (= Y203), H236 (≠ N249), S238 (= S251), R311 (= R319), R316 (= R324), R322 (= R334)
7cqwA Gmas/adp complex-conformation 1 (see paper)
31% identity, 89% coverage: 9:399/441 of query aligns to 5:390/430 of 7cqwA
7tf6A Glutamine synthetase (see paper)
28% identity, 80% coverage: 89:440/441 of query aligns to 80:438/438 of 7tf6A
- binding glutamine: E128 (= E136), E183 (= E191), G235 (= G243), H239 (= H247), R292 (= R301), E298 (≠ L307)
- binding magnesium ion: E126 (= E134), E128 (= E136), E183 (= E191), E190 (= E198), H239 (= H247), E327 (= E336)
- binding : G232 (≠ Q240), N234 (≠ S242), G296 (≠ A305), Y297 (≠ S306), R310 (= R319), Y367 (≠ L376), Y421 (≠ E421), Q433 (≠ A435), Q437 (≠ H439)
Sites not aligning to the query:
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, 72% coverage: 104:421/441 of query aligns to 102:427/446 of A0R083
- K363 (≠ N363) 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)
31% identity, 72% coverage: 104:421/441 of query aligns to 102:427/446 of P9WN37
- K363 (≠ N363) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
Query Sequence
>WP_011446251.1 NCBI__GCF_000013325.1:WP_011446251.1
MNTMPKIDAQFAQGLAAERCRVLFADQLNLARGKYVPMADAARGHTRMCVGTFAVTYDKA
LVAAPGGGMLDGLPDMEVTFDPQALRPSWDPGTKIALGSLRFKGEPFALCGRSALQRAID
AWRARGLEPMVGIEMEAYVFQRGADGGWVPYDTPGAFVYGTGPFSDPAGLIDEIWRTAEA
CGIPVESMNAEFDAPQFELTLRYADAMKAADDAFLFRQMAREVLYKRGYLLSFLPKPFAQ
KSGSGLHFNLSFTKDDGGNVFANDVATGTLSPEMKGCIAGLIRHHEALAAIMAPITNSYA
RLQPASLSGYWANWGIDHRSVTVRVSAETGPAARIEHRMADCAASPYFAMAAMLQAALLG
LENGYDLPEPETNDGLETINTDRHTPHCLSDALDALEADTALAYAVGADLVANFVAIKRD
EVRIVGDLSEAEQLAYYLHYV
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