SitesBLAST
Comparing Pf1N1B4_2254 FitnessBrowser__pseudo1_N1B4:Pf1N1B4_2254 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)
44% identity, 99% coverage: 1:423/426 of query aligns to 47:469/472 of P78061
- H282 (= H236) mutation to N: Activity is impaired to 9% of wild-type.
- R357 (= R311) mutation to Q: Activity is impaired to 3% of wild-type.
7tdpA Structure of paenibacillus polymyxa gs bound to met-sox-p-adp (transition state complex) to 1.98 angstom (see paper)
31% identity, 98% coverage: 5:423/426 of query aligns to 16:436/439 of 7tdpA
- binding adenosine-5'-diphosphate: N123 (≠ C110), G125 (≠ A112), E127 (= E114), E179 (≠ D174), D193 (≠ N188), Y196 (≠ H191), N242 (≠ H238), S244 (= S240), R316 (= R311), R326 (= R321)
- binding magnesium ion: E127 (= E114), E127 (= E114), E129 (= E116), E184 (= E179), E191 (= E186), E191 (= E186), H240 (= H236), E328 (= E323)
- binding l-methionine-s-sulfoximine phosphate: E127 (= E114), E129 (= E116), E184 (= E179), E191 (= E186), G236 (= G232), H240 (= H236), R293 (= R288), E299 (≠ Y294), R311 (= R306), R330 (= R325)
8wwuB Glutamine synthetase
31% identity, 96% coverage: 3:410/426 of query aligns to 43:465/492 of 8wwuB
- binding phosphoaminophosphonic acid-adenylate ester: G157 (≠ A112), E159 (= E114), R226 (≠ D174), F241 (≠ L189), V243 (= V192), H290 (= H238), S292 (= S240), K360 (≠ R306), R365 (= R311), R376 (= R321)
- binding magnesium ion: E159 (= E114), E238 (= E186)
- binding manganese (ii) ion: E159 (= E114), E161 (= E116), E231 (= E179), E238 (= E186), H288 (= H236), E378 (= E323)
8wwvA Glutamine synthetase
31% identity, 96% coverage: 3:410/426 of query aligns to 41:463/490 of 8wwvA
- binding adenosine-5'-diphosphate: G155 (≠ A112), E157 (= E114), R224 (≠ D174), F239 (≠ L189), D240 (≠ H190), V241 (= V192), H288 (= H238), S290 (= S240), R374 (= R321), E376 (= E323)
- binding magnesium ion: E157 (= E114), E236 (= E186)
- binding manganese (ii) ion: E157 (= E114), E159 (= E116), E229 (= E179), E236 (= E186), H286 (= H236), E376 (= E323)
- binding l-methionine-s-sulfoximine phosphate: E157 (= E114), E159 (= E116), E229 (= E179), E236 (= E186), A282 (≠ G232), H286 (= H236), R340 (= R288), K358 (≠ R306)
8oooA Glutamine synthetase from methanothermococcus thermolithotrophicus in complex with 2-oxoglutarate and mgatp at 2.15 a resolution (see paper)
30% identity, 96% coverage: 17:423/426 of query aligns to 37:445/447 of 8oooA
- binding 2-oxoglutaric acid: R87 (≠ Q68), V93 (≠ T72), P170 (≠ V156), R173 (≠ L159), R174 (≠ Q160), S190 (≠ I176)
- binding adenosine-5'-triphosphate: E136 (= E114), E188 (≠ D174), F203 (≠ L189), K204 (≠ H190), F205 (≠ V192), H251 (= H238), S253 (= S240), R325 (= R311), R335 (= R321)
Sites not aligning to the query:
8ooqB Glutamine synthetase from Methanothermococcus thermolithotrophicus (see paper)
30% identity, 96% coverage: 17:423/426 of query aligns to 36:444/446 of 8ooqB
Sites not aligning to the query:
7tfaB Glutamine synthetase (see paper)
30% identity, 98% coverage: 5:423/426 of query aligns to 16:438/441 of 7tfaB
- binding glutamine: E131 (= E116), Y153 (≠ V146), E186 (= E179), G238 (= G232), H242 (= H236), R295 (= R288), E301 (≠ Y294)
- binding magnesium ion: E129 (= E114), E131 (= E116), E186 (= E179), E193 (= E186), H242 (= H236), E330 (= E323)
- binding : Y58 (≠ T42), R60 (≠ D47), V187 (≠ S180), N237 (≠ A231), G299 (≠ Q292), Y300 (≠ F293), R313 (= R306), M424 (≠ E409)
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, 95% coverage: 21:423/426 of query aligns to 32:440/443 of 4lnkA
- active site: D52 (≠ N35), E131 (= E114), E133 (= E116), E188 (= E179), E195 (= E186), H244 (= H236), R315 (= R306), E332 (= E323), R334 (= R325)
- binding adenosine-5'-diphosphate: K43 (vs. gap), M50 (vs. gap), F198 (≠ L189), Y200 (≠ H191), N246 (≠ H238), S248 (= S240), S324 (≠ G315), S328 (≠ A319), R330 (= R321)
- binding glutamic acid: E133 (= E116), E188 (= E179), V189 (≠ S180), N239 (≠ A231), G240 (= G232), G242 (= G234), E303 (≠ Y294)
- binding magnesium ion: E131 (= E114), E188 (= E179), E195 (= E186), H244 (= H236), E332 (= E323)
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, 95% coverage: 21:423/426 of query aligns to 32:440/443 of 4lniA
- active site: D52 (≠ N35), E131 (= E114), E133 (= E116), E188 (= E179), E195 (= E186), H244 (= H236), R315 (= R306), E332 (= E323), R334 (= R325)
- binding adenosine-5'-diphosphate: E131 (= E114), E183 (≠ D174), D197 (≠ N188), Y200 (≠ H191), N246 (≠ H238), S248 (= S240), R320 (= R311), R330 (= R321)
- binding magnesium ion: E131 (= E114), E131 (= E114), E133 (= E116), E188 (= E179), E195 (= E186), E195 (= E186), H244 (= H236), E332 (= E323)
- binding l-methionine-s-sulfoximine phosphate: E133 (= E116), E188 (= E179), H244 (= H236), R297 (= R288), E303 (≠ Y294), R315 (= R306), R334 (= R325)
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, 95% coverage: 21:423/426 of query aligns to 33:441/444 of P12425
- G59 (≠ S41) 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 (≠ D47) 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 (= E114) binding
- E134 (= E116) binding
- E189 (= E179) binding
- V190 (≠ S180) 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 (= E186) binding
- G241 (= G232) binding
- H245 (= H236) binding
- G302 (≠ Q292) 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 (≠ Y294) 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 (= P296) 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 (= E323) binding
- E424 (= E406) 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, 95% coverage: 21:423/426 of query aligns to 36:444/447 of 4s0rD
- active site: D56 (≠ N35), E135 (= E114), E137 (= E116), E192 (= E179), E199 (= E186), H248 (= H236), R319 (= R306), E336 (= E323), R338 (= R325)
- binding glutamine: E137 (= E116), E192 (= E179), R301 (= R288), E307 (≠ Y294)
- binding magnesium ion: I66 (= I48), E135 (= E114), E135 (= E114), E199 (= E186), H248 (= H236), H248 (= H236), E336 (= E323), H419 (≠ I398)
- binding : F63 (≠ T42), V64 (≠ L46), R65 (≠ D47), I66 (= I48), D161 (≠ P141), G241 (= G229), V242 (≠ Q230), N243 (≠ A231), G305 (≠ Q292), Y306 (≠ F293), Y376 (= Y363), I426 (≠ S405), M430 (≠ E409)
8tfkA Glutamine synthetase (see paper)
29% identity, 99% coverage: 3:423/426 of query aligns to 27:437/440 of 8tfkA
- binding adenosine-5'-diphosphate: E128 (= E114), D194 (≠ N188), F195 (≠ L189), F197 (≠ V192), N243 (≠ H238), R312 (= R306), R317 (= R311), G325 (≠ A319), R327 (= R321)
- binding magnesium ion: E128 (= E114), E128 (= E114), E130 (= E116), E185 (= E179), E192 (= E186), E192 (= E186), H241 (= H236), E329 (= E323)
- binding l-methionine-s-sulfoximine phosphate: E128 (= E114), E130 (= E116), E185 (= E179), E192 (= E186), G237 (= G232), H241 (= H236), R294 (= R288), E300 (≠ Y294), R312 (= R306), R331 (= R325)
7tf9S L. Monocytogenes gs(14)-q-glnr peptide (see paper)
29% identity, 98% coverage: 5:423/426 of query aligns to 17:440/443 of 7tf9S
- binding glutamine: E133 (= E116), Y155 (≠ K139), E188 (= E179), G240 (= G232), G242 (= G234), R297 (= R288), E303 (≠ Y294)
- binding magnesium ion: E131 (= E114), E133 (= E116), E188 (= E179), E195 (= E186), H244 (= H236), E332 (= E323)
- binding : F59 (≠ T42), V60 (≠ L46), E418 (≠ A401), I422 (≠ S405), M426 (≠ E409)
7tenA Glutamine synthetase (see paper)
29% identity, 98% coverage: 5:423/426 of query aligns to 16:439/442 of 7tenA
- binding adenosine-5'-diphosphate: G128 (≠ A112), E130 (= E114), E182 (≠ D174), D196 (≠ N188), F197 (≠ L189), K198 (≠ H190), Y199 (≠ H191), N245 (≠ H238), S247 (= S240), R319 (= R311), S327 (≠ A319), R329 (= R321)
- binding l-methionine-s-sulfoximine phosphate: E130 (= E114), E132 (= E116), E187 (= E179), E194 (= E186), N238 (≠ A231), G239 (= G232), H243 (= H236), R296 (= R288), E302 (≠ Y294), R314 (= R306), R333 (= R325)
8ufjB Glutamine synthetase (see paper)
29% identity, 99% coverage: 3:423/426 of query aligns to 31:441/444 of 8ufjB
7tf6A Glutamine synthetase (see paper)
30% identity, 92% coverage: 34:423/426 of query aligns to 50:435/438 of 7tf6A
- binding glutamine: E128 (= E116), E183 (= E179), G235 (= G232), H239 (= H236), R292 (= R288), E298 (≠ Y294)
- binding magnesium ion: E126 (= E114), E128 (= E116), E183 (= E179), E190 (= E186), H239 (= H236), E327 (= E323)
- binding : F58 (≠ T42), R60 (≠ D47), G232 (= G229), N234 (≠ A231), G296 (≠ Q292), Y297 (≠ F293), R310 (= R306), Y367 (= Y363), Y421 (≠ E409), Q433 (≠ W421)
Sites not aligning to the query:
8ooxB Glutamine synthetase (see paper)
29% identity, 93% coverage: 31:425/426 of query aligns to 46:437/438 of 8ooxB
7tdvC Glutamine synthetase (see paper)
30% identity, 92% coverage: 34:423/426 of query aligns to 51:440/443 of 7tdvC
- binding adenosine-5'-diphosphate: G129 (≠ A112), E131 (= E114), E183 (≠ D174), D197 (≠ N188), F198 (≠ L189), K199 (≠ H190), Y200 (≠ H191), N246 (≠ H238), V247 (≠ I239), S248 (= S240), R320 (= R311), S328 (≠ A319), R330 (= R321)
- binding magnesium ion: E131 (= E114), E131 (= E114), E133 (= E116), E188 (= E179), E195 (= E186), E195 (= E186), H244 (= H236), E332 (= E323)
- binding l-methionine-s-sulfoximine phosphate: E131 (= E114), E133 (= E116), E188 (= E179), E195 (= E186), G240 (= G232), H244 (= H236), R297 (= R288), E303 (≠ Y294), R315 (= R306)
8oozA Glutamine synthetase (see paper)
30% identity, 89% coverage: 45:425/426 of query aligns to 51:429/430 of 8oozA
- binding adenosine-5'-triphosphate: G117 (≠ A112), E170 (≠ D174), F185 (≠ L189), K186 (≠ H190), Y187 (≠ H191), N233 (≠ H238), S235 (= S240), S315 (≠ A319), R317 (= R321)
- binding magnesium ion: E119 (= E114), H231 (= H236), E319 (= E323)
7cqwA Gmas/adp complex-conformation 1 (see paper)
32% identity, 85% coverage: 25:386/426 of query aligns to 32:392/430 of 7cqwA
Query Sequence
>Pf1N1B4_2254 FitnessBrowser__pseudo1_N1B4:Pf1N1B4_2254
MNGVVRGKRIERTSLHKVYEKGINLPASLFALDINGSTVESTGLGLDIGDADRICYPIPD
TLCNEPWQKRPTAQLLMTMHELEGDPFFADPREVLRQVVAKFDEMGLTICAAFELEFYLI
DQENVNGRPQPPRSPISGKRPHSTQVYLIDDLDEYVDCLQDILEGAKEQGIPADAIVKES
APAQFEVNLHHVADPIKACDYAVLLKRLIKNIAYDHEMDTTFMAKPYPGQAGNGLHVHIS
ILDKDGKNIFASEDPEQNAALRHAIGGVLETLPAQMAFLCPNVNSYRRFGAQFYVPNSPC
WGLDNRTVAIRVPTGSSDAVRIEHRVAGADANPYLLMASVLAGVHHGLTNKIEPGAPVEG
NSYEQNEQSLPNNLRDALRELDDSEVMAKYIDPKYIDIFVACKESELEEFEHSISDLEYN
WYLHTV
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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