SitesBLAST
Comparing WP_110205265.1 NCBI__GCF_003194585.1:WP_110205265.1 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)
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)
63% identity, 99% coverage: 1:442/445 of query aligns to 1:444/446 of A0R083
- K363 (≠ E361) 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)
64% identity, 98% coverage: 1:437/445 of query aligns to 1:439/446 of P9WN37
- K363 (≠ E361) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
8ooxB Glutamine synthetase (see paper)
50% identity, 99% coverage: 4:442/445 of query aligns to 2:435/438 of 8ooxB
8oozA Glutamine synthetase (see paper)
49% identity, 99% coverage: 4:442/445 of query aligns to 2:427/430 of 8oozA
- binding adenosine-5'-triphosphate: G117 (≠ H128), E170 (= E182), F185 (≠ L197), K186 (≠ R198), Y187 (= Y199), N233 (≠ H245), S235 (= S247), S315 (= S330), R317 (= R332)
- binding magnesium ion: E119 (= E130), H231 (= H243), E319 (= E334)
8ufjB Glutamine synthetase (see paper)
47% identity, 99% coverage: 4:445/445 of query aligns to 7:444/444 of 8ufjB
8tfkA Glutamine synthetase (see paper)
46% identity, 99% coverage: 4:445/445 of query aligns to 3:440/440 of 8tfkA
- binding adenosine-5'-diphosphate: E128 (= E130), D194 (= D196), F195 (≠ L197), F197 (≠ Y199), N243 (≠ H245), R312 (= R314), R317 (= R319), G325 (≠ S330), R327 (= R332)
- binding magnesium ion: E128 (= E130), E128 (= E130), E130 (= E132), E185 (= E187), E192 (= E194), E192 (= E194), H241 (= H243), E329 (= E334)
- binding l-methionine-s-sulfoximine phosphate: E128 (= E130), E130 (= E132), E185 (= E187), E192 (= E194), G237 (= G239), H241 (= H243), R294 (= R296), E300 (= E302), R312 (= R314), R331 (= R336)
7tdvC Glutamine synthetase (see paper)
46% identity, 98% coverage: 8:442/445 of query aligns to 8:440/443 of 7tdvC
- binding adenosine-5'-diphosphate: G129 (≠ H128), E131 (= E130), E183 (= E182), D197 (= D196), F198 (≠ L197), K199 (≠ R198), Y200 (= Y199), N246 (≠ H245), V247 (= V246), S248 (= S247), R320 (= R319), S328 (= S330), R330 (= R332)
- binding magnesium ion: E131 (= E130), E131 (= E130), E133 (= E132), E188 (= E187), E195 (= E194), E195 (= E194), H244 (= H243), E332 (= E334)
- binding l-methionine-s-sulfoximine phosphate: E131 (= E130), E133 (= E132), E188 (= E187), E195 (= E194), G240 (= G239), H244 (= H243), R297 (= R296), E303 (= E302), R315 (= R314)
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)
44% identity, 97% coverage: 10:442/445 of query aligns to 10:440/443 of 4lnkA
- active site: D52 (= D52), E131 (= E130), E133 (= E132), E188 (= E187), E195 (= E194), H244 (= H243), R315 (= R314), E332 (= E334), R334 (= R336)
- binding adenosine-5'-diphosphate: K43 (≠ G43), M50 (≠ G50), F198 (≠ L197), Y200 (= Y199), N246 (≠ H245), S248 (= S247), S324 (≠ N326), S328 (= S330), R330 (= R332)
- binding glutamic acid: E133 (= E132), E188 (= E187), V189 (≠ G188), N239 (≠ P238), G240 (= G239), G242 (= G241), E303 (= E302)
- binding magnesium ion: E131 (= E130), E188 (= E187), E195 (= E194), H244 (= H243), E332 (= E334)
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)
44% identity, 97% coverage: 10:442/445 of query aligns to 10:440/443 of 4lniA
- active site: D52 (= D52), E131 (= E130), E133 (= E132), E188 (= E187), E195 (= E194), H244 (= H243), R315 (= R314), E332 (= E334), R334 (= R336)
- binding adenosine-5'-diphosphate: E131 (= E130), E183 (= E182), D197 (= D196), Y200 (= Y199), N246 (≠ H245), S248 (= S247), R320 (= R319), R330 (= R332)
- binding magnesium ion: E131 (= E130), E131 (= E130), E133 (= E132), E188 (= E187), E195 (= E194), E195 (= E194), H244 (= H243), E332 (= E334)
- binding l-methionine-s-sulfoximine phosphate: E133 (= E132), E188 (= E187), H244 (= H243), R297 (= R296), E303 (= E302), R315 (= R314), R334 (= R336)
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)
44% identity, 97% coverage: 10:442/445 of query aligns to 11:441/444 of P12425
- G59 (= G58) 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 (= R61) 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 (= E130) binding Mg(2+)
- E134 (= E132) binding Mg(2+)
- E189 (= E187) binding Mg(2+)
- V190 (≠ G188) 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 (= E194) binding Mg(2+)
- G241 (= G239) binding L-glutamate
- H245 (= H243) binding Mg(2+)
- G302 (= G300) 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 (= E302) 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 (= P304) 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 (= E334) binding Mg(2+)
- E424 (= E425) 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
7tf6A Glutamine synthetase (see paper)
46% identity, 97% coverage: 13:442/445 of query aligns to 12:435/438 of 7tf6A