SitesBLAST
Comparing PP_5184 FitnessBrowser__Putida:PP_5184 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)
P78061 Gamma-glutamylputrescine synthetase PuuA; Gamma-Glu-Put synthetase; Glutamate--putrescine ligase; EC 6.3.1.11 from Escherichia coli (strain K12) (see paper)
45% identity, 97% coverage: 12:455/458 of query aligns to 26:469/472 of P78061
- H282 (= H268) mutation to N: Activity is impaired to 9% of wild-type.
- R357 (= R343) mutation to Q: Activity is impaired to 3% of wild-type.
8wwuB Glutamine synthetase (see paper)
31% identity, 91% coverage: 26:442/458 of query aligns to 34:465/492 of 8wwuB
- binding phosphoaminophosphonic acid-adenylate ester: G157 (≠ A144), E159 (= E146), R226 (≠ D206), F241 (≠ L221), V243 (= V224), H290 (= H270), S292 (= S272), K360 (≠ R338), R365 (= R343), R376 (= R353)
- binding magnesium ion: E159 (= E146), E238 (= E218)
- binding manganese (ii) ion: E159 (= E146), E161 (= E148), E231 (= E211), E238 (= E218), H288 (= H268), E378 (= E355)
8wwvA Glutamine synthetase (see paper)
31% identity, 91% coverage: 26:442/458 of query aligns to 32:463/490 of 8wwvA
- binding adenosine-5'-diphosphate: G155 (≠ A144), E157 (= E146), R224 (≠ D206), F239 (≠ L221), D240 (≠ H222), V241 (= V224), H288 (= H270), S290 (= S272), R374 (= R353), E376 (= E355)
- binding magnesium ion: E157 (= E146), E236 (= E218)
- binding manganese (ii) ion: E157 (= E146), E159 (= E148), E229 (= E211), E236 (= E218), H286 (= H268), E376 (= E355)
- binding l-methionine-s-sulfoximine phosphate: E157 (= E146), E159 (= E148), E229 (= E211), E236 (= E218), A282 (≠ G264), H286 (= H268), R340 (= R320), K358 (≠ R338)
7tdpA Structure of paenibacillus polymyxa gs bound to met-sox-p-adp (transition state complex) to 1.98 angstom (see paper)
29% identity, 96% coverage: 17:455/458 of query aligns to 10:436/439 of 7tdpA
- binding adenosine-5'-diphosphate: N123 (≠ C142), G125 (≠ A144), E127 (= E146), E179 (≠ D206), D193 (≠ N220), Y196 (≠ H223), N242 (≠ H270), S244 (= S272), R316 (= R343), R326 (= R353)
- binding magnesium ion: E127 (= E146), E127 (= E146), E129 (= E148), E184 (= E211), E191 (= E218), E191 (= E218), H240 (= H268), E328 (= E355)
- binding l-methionine-s-sulfoximine phosphate: E127 (= E146), E129 (= E148), E184 (= E211), E191 (= E218), G236 (= G264), H240 (= H268), R293 (= R320), E299 (≠ Y326), R311 (= R338), R330 (= R357)
8ooqB Glutamine synthetase from Methanothermococcus thermolithotrophicus (see paper)
29% identity, 89% coverage: 49:455/458 of query aligns to 36:444/446 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)
29% identity, 89% coverage: 49:455/458 of query aligns to 37:445/447 of 8oooA
- binding 2-oxoglutaric acid: R87 (≠ Q100), V93 (≠ T104), P170 (≠ A188), R173 (≠ L191), R174 (≠ Q192), S190 (≠ I208)
- binding adenosine-5'-triphosphate: E136 (= E146), E188 (≠ D206), F203 (≠ L221), K204 (≠ H222), F205 (≠ V224), H251 (= H270), S253 (= S272), R325 (= R343), R335 (= R353)
Sites not aligning to the query:
7tfaB Glutamine synthetase (see paper)
29% identity, 96% coverage: 17:455/458 of query aligns to 10:438/441 of 7tfaB
- binding glutamine: E131 (= E148), Y153 (≠ V178), E186 (= E211), G238 (= G264), H242 (= H268), R295 (= R320), E301 (≠ Y326)
- binding magnesium ion: E129 (= E146), E131 (= E148), E186 (= E211), E193 (= E218), H242 (= H268), E330 (= E355)
- binding : Y58 (≠ T74), R60 (≠ D79), V187 (≠ S212), N237 (≠ A263), G299 (≠ Q324), Y300 (≠ F325), R313 (= R338), M424 (≠ E441)
4s0rD Structure of gs-tnra complex (see paper)
28% identity, 95% coverage: 23:455/458 of query aligns to 21:444/447 of 4s0rD
- active site: D56 (≠ N67), E135 (= E146), E137 (= E148), E192 (= E211), E199 (= E218), H248 (= H268), R319 (= R338), E336 (= E355), R338 (= R357)
- binding glutamine: E137 (= E148), E192 (= E211), R301 (= R320), E307 (≠ Y326)
- binding magnesium ion: I66 (= I80), E135 (= E146), E135 (= E146), E199 (= E218), H248 (= H268), H248 (= H268), E336 (= E355), H419 (≠ I430)
- binding : F63 (≠ T74), V64 (≠ L78), R65 (≠ D79), I66 (= I80), D161 (≠ L180), G241 (= G261), V242 (≠ Q262), N243 (≠ A263), G305 (≠ Q324), Y306 (≠ F325), Y376 (= Y395), I426 (≠ S437), M430 (≠ E441)
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)
28% identity, 95% coverage: 23:455/458 of query aligns to 17:440/443 of 4lnkA
- active site: D52 (≠ N67), E131 (= E146), E133 (= E148), E188 (= E211), E195 (= E218), H244 (= H268), R315 (= R338), E332 (= E355), R334 (= R357)
- binding adenosine-5'-diphosphate: K43 (= K49), M50 (≠ N56), F198 (≠ L221), Y200 (≠ H223), N246 (≠ H270), S248 (= S272), S324 (≠ G347), S328 (≠ A351), R330 (= R353)
- binding glutamic acid: E133 (= E148), E188 (= E211), V189 (≠ S212), N239 (≠ A263), G240 (= G264), G242 (= G266), E303 (≠ Y326)
- binding magnesium ion: E131 (= E146), E188 (= E211), E195 (= E218), H244 (= H268), E332 (= E355)
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)
28% identity, 95% coverage: 23:455/458 of query aligns to 17:440/443 of 4lniA
- active site: D52 (≠ N67), E131 (= E146), E133 (= E148), E188 (= E211), E195 (= E218), H244 (= H268), R315 (= R338), E332 (= E355), R334 (= R357)
- binding adenosine-5'-diphosphate: E131 (= E146), E183 (≠ D206), D197 (≠ N220), Y200 (≠ H223), N246 (≠ H270), S248 (= S272), R320 (= R343), R330 (= R353)
- binding magnesium ion: E131 (= E146), E131 (= E146), E133 (= E148), E188 (= E211), E195 (= E218), E195 (= E218), H244 (= H268), E332 (= E355)
- binding l-methionine-s-sulfoximine phosphate: E133 (= E148), E188 (= E211), H244 (= H268), R297 (= R320), E303 (≠ Y326), R315 (= R338), R334 (= R357)
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)
28% identity, 95% coverage: 23:455/458 of query aligns to 18:441/444 of P12425
- G59 (≠ S73) 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 (≠ D79) 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 (= E146) binding Mg(2+)
- E134 (= E148) binding Mg(2+)
- E189 (= E211) binding Mg(2+)
- V190 (≠ S212) 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 (= E218) binding Mg(2+)
- G241 (= G264) binding L-glutamate
- H245 (= H268) binding Mg(2+)
- G302 (≠ Q324) 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 (≠ Y326) 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 (= P328) 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 (= E355) binding Mg(2+)
- E424 (= E438) 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
8ooxB Glutamine synthetase (see paper)
29% identity, 96% coverage: 19:457/458 of query aligns to 11:437/438 of 8ooxB
7tenA Glutamine synthetase (see paper)
28% identity, 95% coverage: 23:455/458 of query aligns to 16:439/442 of 7tenA
- binding adenosine-5'-diphosphate: G128 (≠ A144), E130 (= E146), E182 (≠ D206), D196 (≠ N220), F197 (≠ L221), K198 (≠ H222), Y199 (≠ H223), N245 (≠ H270), S247 (= S272), R319 (= R343), S327 (≠ A351), R329 (= R353)
- binding l-methionine-s-sulfoximine phosphate: E130 (= E146), E132 (= E148), E187 (= E211), E194 (= E218), N238 (≠ A263), G239 (= G264), H243 (= H268), R296 (= R320), E302 (≠ Y326), R314 (= R338), R333 (= R357)
7tf9S L. Monocytogenes gs(14)-q-glnr peptide (see paper)
28% identity, 95% coverage: 23:455/458 of query aligns to 17:440/443 of 7tf9S
- binding glutamine: E133 (= E148), Y155 (≠ V178), E188 (= E211), G240 (= G264), G242 (= G266), R297 (= R320), E303 (≠ Y326)
- binding magnesium ion: E131 (= E146), E133 (= E148), E188 (= E211), E195 (= E218), H244 (= H268), E332 (= E355)
- binding : F59 (≠ T74), V60 (≠ L78), E418 (≠ A433), I422 (≠ S437), M426 (≠ E441)
8oozA Glutamine synthetase (see paper)
29% identity, 96% coverage: 19:457/458 of query aligns to 11:429/430 of 8oozA
- binding adenosine-5'-triphosphate: G117 (≠ A144), E170 (≠ D206), F185 (≠ L221), K186 (≠ H222), Y187 (≠ H223), N233 (≠ H270), S235 (= S272), S315 (≠ A351), R317 (= R353)
- binding magnesium ion: E119 (= E146), H231 (= H268), E319 (= E355)
7tf6A Glutamine synthetase (see paper)
28% identity, 95% coverage: 19:455/458 of query aligns to 12:435/438 of 7tf6A
- binding glutamine: E128 (= E148), E183 (= E211), G235 (= G264), H239 (= H268), R292 (= R320), E298 (≠ Y326)
- binding magnesium ion: E126 (= E146), E128 (= E148), E183 (= E211), E190 (= E218), H239 (= H268), E327 (= E355)
- binding : F58 (≠ T74), R60 (≠ D79), G232 (= G261), N234 (≠ A263), G296 (≠ Q324), Y297 (≠ F325), R310 (= R338), Y367 (= Y395), Y421 (≠ E441), Q433 (≠ W453)
Sites not aligning to the query:
8s59O Glutamine synthetase
28% identity, 95% coverage: 22:455/458 of query aligns to 20:443/446 of 8s59O
8tfbA Glutamine synthetase (see paper)
28% identity, 95% coverage: 22:455/458 of query aligns to 17:440/443 of 8tfbA
8tfkA Glutamine synthetase (see paper)
28% identity, 95% coverage: 22:455/458 of query aligns to 14:437/440 of 8tfkA
- binding adenosine-5'-diphosphate: E128 (= E146), D194 (≠ N220), F195 (≠ L221), F197 (≠ V224), N243 (≠ H270), R312 (= R338), R317 (= R343), G325 (≠ A351), R327 (= R353)
- binding magnesium ion: E128 (= E146), E128 (= E146), E130 (= E148), E185 (= E211), E192 (= E218), E192 (= E218), H241 (= H268), E329 (= E355)
- binding l-methionine-s-sulfoximine phosphate: E128 (= E146), E130 (= E148), E185 (= E211), E192 (= E218), G237 (= G264), H241 (= H268), R294 (= R320), E300 (≠ Y326), R312 (= R338), R331 (= R357)
7tdvC Glutamine synthetase (see paper)
27% identity, 95% coverage: 19:455/458 of query aligns to 13:440/443 of 7tdvC
- binding adenosine-5'-diphosphate: G129 (≠ A144), E131 (= E146), E183 (≠ D206), D197 (≠ N220), F198 (≠ L221), K199 (≠ H222), Y200 (≠ H223), N246 (≠ H270), V247 (≠ I271), S248 (= S272), R320 (= R343), S328 (≠ A351), R330 (= R353)
- binding magnesium ion: E131 (= E146), E131 (= E146), E133 (= E148), E188 (= E211), E195 (= E218), E195 (= E218), H244 (= H268), E332 (= E355)
- binding l-methionine-s-sulfoximine phosphate: E131 (= E146), E133 (= E148), E188 (= E211), E195 (= E218), G240 (= G264), H244 (= H268), R297 (= R320), E303 (≠ Y326), R315 (= R338)
Query Sequence
>PP_5184 FitnessBrowser__Putida:PP_5184
MSVPPRAVQLNEANAFLKEHPEVLYVDLLIADMNGVVRGKRIERTSLHKVYEKGINLPAS
LFALDINGSTVESTGLGLDIGDADRICYPIPDTLCNEPWQKRPTAQLLMTMHELEGEPFF
ADPREVLRQVVTKFDELGLTICAAFELEFYLIDQENVNGRPQPPRSPISGKRPQSTQVYL
IDDLDEYADCLQDILEGAKEQGIPADAIVKESAPAQFEVNLHHVADPLKACDYAVLLKRL
IKNIAYDHEMDTTFMAKPYPGQAGNGLHVHISVLDKDGNNIFTSEDPEQNAALRHAVGGV
LETLPASMAFLCPNVNSYRRFGAQFYVPNAPSWGLDNRTVALRVPTGSADAVRIEHRVAG
ADANPYLMMAAVLAGVHHGLTNKIEPGAPIEGNSYEQLEQSLPNNLRDALRELDDSEILN
KYIDPKYIDIFVACKESELEEFEHSISDLEYNWYLHTV
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