SitesBLAST
Comparing PP_4547 FitnessBrowser__Putida:PP_4547 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)
37% identity, 99% coverage: 4:454/454 of query aligns to 22:472/472 of P78061
- H282 (= H264) mutation to N: Activity is impaired to 9% of wild-type.
- R357 (= R339) 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)
28% identity, 98% coverage: 6:451/454 of query aligns to 3:445/447 of 8oooA
- binding 2-oxoglutaric acid: F17 (≠ L21), R19 (≠ E23), A33 (≠ L37), R87 (= R96), V93 (≠ T100), P170 (≠ E185), R173 (≠ L188), R174 (≠ A189), S190 (≠ A205)
- binding adenosine-5'-triphosphate: E136 (= E143), E188 (≠ R203), F203 (≠ L218), K204 (≠ E219), F205 (≠ H220), H251 (= H266), S253 (= S268), R325 (= R339), R335 (≠ H349)
8ooqB Glutamine synthetase from Methanothermococcus thermolithotrophicus (see paper)
28% identity, 98% coverage: 6:451/454 of query aligns to 2:444/446 of 8ooqB
- binding 2-oxoglutaric acid: F16 (≠ L21), R18 (≠ E23), A32 (≠ L37), R86 (= R96), V92 (≠ T100), P169 (≠ E185), R172 (≠ L188), R173 (≠ A189), S189 (≠ A205)
- binding magnesium ion: E137 (= E145), E192 (= E208), E199 (= E215)
8tfkA Glutamine synthetase (see paper)
29% identity, 96% coverage: 18:451/454 of query aligns to 14:437/440 of 8tfkA
- binding adenosine-5'-diphosphate: E128 (= E143), D194 (≠ T217), F195 (≠ L218), F197 (≠ H220), N243 (≠ H266), R312 (= R334), R317 (= R339), G325 (≠ S347), R327 (≠ H349)
- binding magnesium ion: E128 (= E143), E128 (= E143), E130 (= E145), E185 (= E208), E192 (= E215), E192 (= E215), H241 (= H264), E329 (= E351)
- binding l-methionine-s-sulfoximine phosphate: E128 (= E143), E130 (= E145), E185 (= E208), E192 (= E215), G237 (= G260), H241 (= H264), R294 (= R316), E300 (≠ Y322), R312 (= R334), R331 (= R353)
8ufjB Glutamine synthetase (see paper)
29% identity, 96% coverage: 18:451/454 of query aligns to 18:441/444 of 8ufjB
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)
29% identity, 96% coverage: 18:451/454 of query aligns to 16:444/446 of A0R083
- K363 (≠ E378) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
7tdpA Structure of paenibacillus polymyxa gs bound to met-sox-p-adp (transition state complex) to 1.98 angstom (see paper)
30% identity, 83% coverage: 76:451/454 of query aligns to 61:436/439 of 7tdpA
- binding adenosine-5'-diphosphate: N123 (vs. gap), G125 (≠ A141), E127 (= E143), E179 (≠ R203), D193 (≠ T217), Y196 (≠ H220), N242 (≠ H266), S244 (= S268), R316 (= R339), R326 (≠ H349)
- binding magnesium ion: E127 (= E143), E127 (= E143), E129 (= E145), E184 (= E208), E191 (= E215), E191 (= E215), H240 (= H264), E328 (= E351)
- binding l-methionine-s-sulfoximine phosphate: E127 (= E143), E129 (= E145), E184 (= E208), E191 (= E215), G236 (= G260), H240 (= H264), R293 (= R316), E299 (≠ Y322), R311 (= R334), R330 (= R353)
7tf6A Glutamine synthetase (see paper)
29% identity, 87% coverage: 60:453/454 of query aligns to 48:437/438 of 7tf6A
- binding glutamine: E128 (= E145), E183 (= E208), G235 (= G260), H239 (= H264), R292 (= R316), E298 (≠ Y322)
- binding magnesium ion: E126 (= E143), E128 (= E145), E183 (= E208), E190 (= E215), H239 (= H264), E327 (= E351)
- binding : F58 (≠ L72), R60 (≠ D75), G232 (≠ Q257), N234 (≠ A259), G296 (≠ N320), Y297 (≠ S321), R310 (= R334), Y367 (= Y391), Y421 (≠ Q437), Q433 (≠ W449), Q437 (= Q453)
7tfaB Glutamine synthetase (see paper)
30% identity, 83% coverage: 76:451/454 of query aligns to 61:438/441 of 7tfaB
- binding glutamine: E131 (= E145), Y153 (≠ V175), E186 (= E208), G238 (= G260), H242 (= H264), R295 (= R316), E301 (≠ Y322)
- binding magnesium ion: E129 (= E143), E131 (= E145), E186 (= E208), E193 (= E215), H242 (= H264), E330 (= E351)
- binding : V187 (≠ Y209), N237 (≠ A259), G299 (≠ N320), Y300 (≠ S321), R313 (= R334), M424 (≠ Q437)
Sites not aligning to the query:
7tf9S L. Monocytogenes gs(14)-q-glnr peptide (see paper)
29% identity, 98% coverage: 7:451/454 of query aligns to 6:440/443 of 7tf9S
- binding glutamine: E133 (= E145), Y155 (≠ V175), E188 (= E208), G240 (= G260), G242 (= G262), R297 (= R316), E303 (≠ Y322)
- binding magnesium ion: E131 (= E143), E133 (= E145), E188 (= E208), E195 (= E215), H244 (= H264), E332 (= E351)
- binding : F59 (≠ L72), V60 (= V73), E418 (≠ K429), I422 (≠ A433), M426 (≠ Q437)
7tenA Glutamine synthetase (see paper)
29% identity, 98% coverage: 7:451/454 of query aligns to 5:439/442 of 7tenA
- binding adenosine-5'-diphosphate: G128 (≠ A141), E130 (= E143), E182 (≠ R203), D196 (≠ T217), F197 (≠ L218), K198 (≠ E219), Y199 (≠ H220), N245 (≠ H266), S247 (= S268), R319 (= R339), S327 (= S347), R329 (≠ H349)
- binding l-methionine-s-sulfoximine phosphate: E130 (= E143), E132 (= E145), E187 (= E208), E194 (= E215), N238 (≠ A259), G239 (= G260), H243 (= H264), R296 (= R316), E302 (≠ Y322), R314 (= R334), R333 (= R353)
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)
27% identity, 90% coverage: 44:453/454 of query aligns to 37:443/444 of P12425
- G59 (= G71) 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 (≠ D75) 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 (= E143) binding
- E134 (= E145) binding
- E189 (= E208) binding
- V190 (≠ Y209) 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 (= E215) binding
- G241 (= G260) binding
- H245 (= H264) binding
- G302 (≠ N320) 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 (≠ Y322) 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 (= P324) 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 (= E351) binding
- E424 (= E434) 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
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)
27% identity, 90% coverage: 44:453/454 of query aligns to 36:442/443 of 4lnkA
- active site: D52 (≠ N63), E131 (= E143), E133 (= E145), E188 (= E208), E195 (= E215), H244 (= H264), R315 (= R334), E332 (= E351), R334 (= R353)
- binding adenosine-5'-diphosphate: K43 (≠ R51), M50 (≠ L58), F198 (≠ L218), Y200 (≠ H220), N246 (≠ H266), S248 (= S268), S324 (≠ G343), S328 (= S347), R330 (≠ H349)
- binding glutamic acid: E133 (= E145), E188 (= E208), V189 (≠ Y209), N239 (≠ A259), G240 (= G260), G242 (= G262), E303 (≠ Y322)
- binding magnesium ion: E131 (= E143), E188 (= E208), E195 (= E215), H244 (= H264), E332 (= E351)
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)
27% identity, 90% coverage: 44:453/454 of query aligns to 36:442/443 of 4lniA
- active site: D52 (≠ N63), E131 (= E143), E133 (= E145), E188 (= E208), E195 (= E215), H244 (= H264), R315 (= R334), E332 (= E351), R334 (= R353)
- binding adenosine-5'-diphosphate: E131 (= E143), E183 (≠ R203), D197 (≠ T217), Y200 (≠ H220), N246 (≠ H266), S248 (= S268), R320 (= R339), R330 (≠ H349)
- binding magnesium ion: E131 (= E143), E131 (= E143), E133 (= E145), E188 (= E208), E195 (= E215), E195 (= E215), H244 (= H264), E332 (= E351)
- binding l-methionine-s-sulfoximine phosphate: E133 (= E145), E188 (= E208), H244 (= H264), R297 (= R316), E303 (≠ Y322), R315 (= R334), R334 (= R353)
4s0rD Structure of gs-tnra complex (see paper)
27% identity, 90% coverage: 44:453/454 of query aligns to 40:446/447 of 4s0rD
- active site: D56 (≠ N63), E135 (= E143), E137 (= E145), E192 (= E208), E199 (= E215), H248 (= H264), R319 (= R334), E336 (= E351), R338 (= R353)
- binding glutamine: E137 (= E145), E192 (= E208), R301 (= R316), E307 (≠ Y322)
- binding magnesium ion: I66 (≠ V76), E135 (= E143), E135 (= E143), E199 (= E215), H248 (= H264), H248 (= H264), E336 (= E351), H419 (≠ V426)
- binding : F63 (≠ L72), V64 (= V73), R65 (≠ D75), I66 (≠ V76), D161 (≠ G177), G241 (≠ Q257), V242 (≠ L258), N243 (≠ A259), G305 (≠ N320), Y306 (≠ S321), Y376 (= Y391), I426 (≠ A433), M430 (≠ Q437)
7tdvC Glutamine synthetase (see paper)
29% identity, 87% coverage: 60:453/454 of query aligns to 49:442/443 of 7tdvC
- binding adenosine-5'-diphosphate: G129 (≠ A141), E131 (= E143), E183 (≠ R203), D197 (≠ T217), F198 (≠ L218), K199 (≠ E219), Y200 (≠ H220), N246 (≠ H266), V247 (≠ L267), S248 (= S268), R320 (= R339), S328 (= S347), R330 (≠ H349)
- binding magnesium ion: E131 (= E143), E131 (= E143), E133 (= E145), E188 (= E208), E195 (= E215), E195 (= E215), H244 (= H264), E332 (= E351)
- binding l-methionine-s-sulfoximine phosphate: E131 (= E143), E133 (= E145), E188 (= E208), E195 (= E215), G240 (= G260), H244 (= H264), R297 (= R316), E303 (≠ Y322), R315 (= R334)
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)
29% identity, 96% coverage: 18:451/454 of query aligns to 16:444/446 of P9WN37
- K363 (≠ E378) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
8wwvA Glutamine synthetase
29% identity, 94% coverage: 15:439/454 of query aligns to 25:464/490 of 8wwvA
- binding adenosine-5'-diphosphate: G155 (≠ A141), E157 (= E143), R224 (= R203), F239 (≠ L218), D240 (≠ E219), V241 (≠ H220), H288 (= H266), S290 (= S268), R374 (≠ H349), E376 (= E351)
- binding magnesium ion: E157 (= E143), E236 (= E215)
- binding manganese (ii) ion: E157 (= E143), E159 (= E145), E229 (= E208), E236 (= E215), H286 (= H264), E376 (= E351)
- binding l-methionine-s-sulfoximine phosphate: E157 (= E143), E159 (= E145), E229 (= E208), E236 (= E215), A282 (≠ G260), H286 (= H264), R340 (= R316), K358 (≠ R334)
8wwuB Glutamine synthetase
29% identity, 94% coverage: 15:439/454 of query aligns to 27:466/492 of 8wwuB
- binding phosphoaminophosphonic acid-adenylate ester: G157 (≠ A141), E159 (= E143), R226 (= R203), F241 (≠ L218), V243 (≠ H220), H290 (= H266), S292 (= S268), K360 (≠ R334), R365 (= R339), R376 (≠ H349)
- binding magnesium ion: E159 (= E143), E238 (= E215)
- binding manganese (ii) ion: E159 (= E143), E161 (= E145), E231 (= E208), E238 (= E215), H288 (= H264), E378 (= E351)
7cqwA Gmas/adp complex-conformation 1 (see paper)
30% identity, 97% coverage: 13:451/454 of query aligns to 7:428/430 of 7cqwA
Query Sequence
>PP_4547 FitnessBrowser__Putida:PP_4547
MHFAPVEQATRFLADNPDIELFELFILDANGVPRGKLLHREELLAVYQTGRPLPSTILGL
TLNGDDVENSGLVWDVGDIDCRAYPLDGSLVRLPWRRVPTAAVQVSMHPSEGLPASIADP
RHVLLRTIEALKADGYHPVMACELEFYLLDQQRDAQGRPQPALDNDGGRPRSTQVYGLRE
LEQIEPFLADLYAACKAQGIPARTAISEYAPGQVEITLEHGDALQAMDQAVRYKRLVKGV
AHAHGMQACFMAKPFAQLAGTGMHMHLSLADSAGNNLFASEDKAGTPLLRQAVAGMLRHL
RDSLLLFCPNANSFRRFQANSYAPLAPTWGVDNRTVSLRVPGGPANSRHVEHRICGADAN
PYLAAAAILAASHWGIREQLDPGAPVEGNGYAQATEHLPTDWLTALDALQHSDWAREALG
EDFLGVYLKVKRAEYRQFMAEVSEQDWRWYLHQA
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