SitesBLAST
Comparing WP_068170530.1 NCBI__GCF_001592305.1:WP_068170530.1 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)
34% identity, 94% coverage: 25:453/456 of query aligns to 40:469/472 of P78061
- H282 (= H266) mutation to N: Activity is impaired to 9% of wild-type.
- R357 (= R342) 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)
33% identity, 83% coverage: 69:448/456 of query aligns to 51:440/447 of 8oooA
- binding 2-oxoglutaric acid: R87 (vs. gap), V93 (≠ T103), P170 (≠ D187), R173 (≠ F190), R174 (≠ E191), S190 (≠ L207)
- binding adenosine-5'-triphosphate: E136 (= E145), E188 (≠ D205), F203 (= F220), K204 (≠ F221), F205 (≠ H222), H251 (= H268), S253 (= S270), R325 (= R342), R335 (= R352)
Sites not aligning to the query:
8ooqB Glutamine synthetase from Methanothermococcus thermolithotrophicus (see paper)
33% identity, 83% coverage: 69:448/456 of query aligns to 50:439/446 of 8ooqB
Sites not aligning to the query:
8tfkA Glutamine synthetase (see paper)
33% identity, 90% coverage: 43:453/456 of query aligns to 19:437/440 of 8tfkA
- binding adenosine-5'-diphosphate: E128 (= E145), D194 (≠ N219), F195 (= F220), F197 (≠ H222), N243 (≠ H268), R312 (= R337), R317 (= R342), G325 (≠ A350), R327 (= R352)
- binding magnesium ion: E128 (= E145), E128 (= E145), E130 (= E147), E185 (= E210), E192 (= E217), E192 (= E217), H241 (= H266), E329 (= E354)
- binding l-methionine-s-sulfoximine phosphate: E128 (= E145), E130 (= E147), E185 (= E210), E192 (= E217), G237 (= G262), H241 (= H266), R294 (= R319), E300 (≠ A325), R312 (= R337), R331 (= R356)
8ufjB Glutamine synthetase (see paper)
33% identity, 90% coverage: 43:453/456 of query aligns to 23:441/444 of 8ufjB
8oozA Glutamine synthetase (see paper)
32% identity, 84% coverage: 71:453/456 of query aligns to 46:427/430 of 8oozA
- binding adenosine-5'-triphosphate: G117 (≠ A143), E170 (≠ D205), F185 (= F220), K186 (≠ F221), Y187 (≠ H222), N233 (≠ H268), S235 (= S270), S315 (≠ A350), R317 (= R352)
- binding magnesium ion: E119 (= E145), H231 (= H266), E319 (= E354)
8ooxB Glutamine synthetase (see paper)
32% identity, 82% coverage: 81:453/456 of query aligns to 62:435/438 of 8ooxB
7tfaB Glutamine synthetase (see paper)
32% identity, 82% coverage: 81:453/456 of query aligns to 63:438/441 of 7tfaB
- binding glutamine: E131 (= E147), Y153 (≠ R167), E186 (= E210), G238 (= G262), H242 (= H266), R295 (= R319), E301 (≠ A325)
- binding magnesium ion: E129 (= E145), E131 (= E147), E186 (= E210), E193 (= E217), H242 (= H266), E330 (= E354)
- binding : V187 (= V211), N237 (≠ P261), G299 (≠ H323), Y300 (≠ T324), R313 (= R337), M424 (≠ E439)
Sites not aligning to the query:
5dm3C Crystal structure of glutamine synthetase from chromohalobacter salexigens dsm 3043(csal_0679, target efi-550015) with bound adp
32% identity, 80% coverage: 86:448/456 of query aligns to 56:390/396 of 5dm3C
- active site: E115 (= E145), E117 (= E147), E162 (= E210), E169 (= E217), H218 (= H266), R286 (= R337), E303 (= E354), R305 (= R356)
- binding adenosine-5'-diphosphate: R173 (≠ F221), C174 (≠ H222), H220 (= H268), S222 (= S270), R301 (= R352)
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, 97% coverage: 12:453/456 of query aligns to 8:441/444 of P12425
- G59 (≠ D75) 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 (≠ D78) 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 (= E145) binding Mg(2+)
- E134 (= E147) binding Mg(2+)
- E189 (= E210) binding Mg(2+)
- V190 (= V211) 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 (= E217) binding Mg(2+)
- G241 (= G262) binding L-glutamate
- H245 (= H266) binding Mg(2+)
- G302 (≠ H323) 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 (≠ A325) 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 (= P327) 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 (= E354) binding Mg(2+)
- E424 (= E436) 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
4s0rD Structure of gs-tnra complex (see paper)
29% identity, 97% coverage: 12:453/456 of query aligns to 11:444/447 of 4s0rD
- active site: D56 (≠ M61), E135 (= E145), E137 (= E147), E192 (= E210), E199 (= E217), H248 (= H266), R319 (= R337), E336 (= E354), R338 (= R356)
- binding glutamine: E137 (= E147), E192 (= E210), R301 (= R319), E307 (≠ A325)
- binding magnesium ion: <