SitesBLAST
Comparing PP_4399 FitnessBrowser__Putida:PP_4399 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)
8tfkA Glutamine synthetase (see paper)
32% identity, 90% coverage: 36:405/413 of query aligns to 61:432/440 of 8tfkA
- binding adenosine-5'-diphosphate: E128 (= E101), D194 (≠ N175), F195 (≠ L176), F197 (≠ H178), N243 (≠ H224), R312 (= R293), R317 (= R298), G325 (≠ A306), R327 (= R308)
- binding magnesium ion: E128 (= E101), E128 (= E101), E130 (= E103), E185 (= E166), E192 (= E173), E192 (= E173), H241 (= H222), E329 (= E310)
- binding l-methionine-s-sulfoximine phosphate: E128 (= E101), E130 (= E103), E185 (= E166), E192 (= E173), G237 (= G218), H241 (= H222), R294 (= R275), E300 (≠ A281), R312 (= R293), R331 (= R312)
8ufjB Glutamine synthetase (see paper)
32% identity, 90% coverage: 36:405/413 of query aligns to 65:436/444 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)
31% identity, 89% coverage: 37:405/413 of query aligns to 64:439/446 of A0R083
- K363 (≠ Q337) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
4s0rD Structure of gs-tnra complex (see paper)
30% identity, 97% coverage: 13:412/413 of query aligns to 44:446/447 of 4s0rD
- active site: D56 (≠ G25), E135 (= E101), E137 (= E103), E192 (= E166), E199 (= E173), H248 (= H222), R319 (= R293), E336 (= E310), R338 (= R312)
- binding glutamine: E137 (= E103), E192 (= E166), R301 (= R275), E307 (≠ A281)
- binding magnesium ion: I66 (≠ S35), E135 (= E101), E135 (= E101), E199 (= E173), H248 (= H222), H248 (= H222), E336 (= E310), H419 (≠ G385)
- binding : F63 (= F32), V64 (≠ Y33), R65 (≠ G34), I66 (≠ S35), D161 (≠ E128), G241 (≠ R215), V242 (≠ T216), N243 (≠ P217), G305 (≠ P279), Y306 (= Y280), Y376 (≠ F349), I426 (≠ L392), M430 (≠ D396)
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)
30% identity, 97% coverage: 13:412/413 of query aligns to 40:442/443 of 4lnkA
- active site: D52 (≠ G25), E131 (= E101), E133 (= E103), E188 (= E166), E195 (= E173), H244 (= H222), R315 (= R293), E332 (= E310), R334 (= R312)
- binding adenosine-5'-diphosphate: K43 (≠ R16), M50 (≠ I23), F198 (≠ L176), Y200 (≠ H178), N246 (≠ H224), S248 (= S226), S324 (= S302), S328 (≠ A306), R330 (= R308)
- binding glutamic acid: E133 (= E103), E188 (= E166), V189 (≠ M167), N239 (≠ P217), G240 (= G218), G242 (≠ S220), E303 (≠ A281)
- binding magnesium ion: E131 (= E101), E188 (= E166), E195 (= E173), H244 (= H222), E332 (= E310)
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)
30% identity, 97% coverage: 13:412/413 of query aligns to 40:442/443 of 4lniA
- active site: D52 (≠ G25), E131 (= E101), E133 (= E103), E188 (= E166), E195 (= E173), H244 (= H222), R315 (= R293), E332 (= E310), R334 (= R312)
- binding adenosine-5'-diphosphate: E131 (= E101), E183 (≠ D161), D197 (≠ N175), Y200 (≠ H178), N246 (≠ H224), S248 (= S226), R320 (= R298), R330 (= R308)
- binding magnesium ion: E131 (= E101), E131 (= E101), E133 (= E103), E188 (= E166), E195 (= E173), E195 (= E173), H244 (= H222), E332 (= E310)
- binding l-methionine-s-sulfoximine phosphate: E133 (= E103), E188 (= E166), H244 (= H222), R297 (= R275), E303 (≠ A281), R315 (= R293), R334 (= R312)
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)
30% identity, 97% coverage: 13:412/413 of query aligns to 41:443/444 of P12425
- G59 (≠ K31) 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 (≠ G34) 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 (= E101) binding
- E134 (= E103) binding
- E189 (= E166) binding
- V190 (≠ M167) 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 (= E173) binding
- G241 (= G218) binding
- H245 (= H222) binding
- G302 (≠ P279) 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 (≠ A281) 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 (= P283) 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 (= E310) binding
- E424 (= E393) 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
5dm3C Crystal structure of glutamine synthetase from chromohalobacter salexigens dsm 3043(csal_0679, target efi-550015) with bound adp
34% identity, 86% coverage: 52:405/413 of query aligns to 66:390/396 of 5dm3C
- active site: E115 (= E101), E117 (= E103), E162 (= E166), E169 (= E173), H218 (= H222), R286 (= R293), E303 (= E310), R305 (= R312)
- binding adenosine-5'-diphosphate: R173 (≠ L177), C174 (≠ H178), H220 (= H224), S222 (= S226), R301 (= R308)
P78061 Gamma-glutamylputrescine synthetase PuuA; Gamma-Glu-Put synthetase; Glutamate--putrescine ligase; EC 6.3.1.11 from Escherichia coli (strain K12) (see paper)
35% identity, 81% coverage: 70:405/413 of query aligns to 128:464/472 of P78061
- H282 (= H222) mutation to N: Activity is impaired to 9% of wild-type.
- R357 (= R298) mutation to Q: Activity is impaired to 3% of wild-type.
8ooqB Glutamine synthetase from Methanothermococcus thermolithotrophicus (see paper)
30% identity, 91% coverage: 32:405/413 of query aligns to 63:439/446 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)
30% identity, 91% coverage: 32:405/413 of query aligns to 64:440/447 of 8oooA
- binding 2-oxoglutaric acid: R87 (vs. gap), V93 (≠ R59), P170 (≠ R143), R173 (≠ F146), R174 (≠ K147), S190 (≠ F163)
- binding adenosine-5'-triphosphate: E136 (= E101), E188 (≠ D161), F203 (≠ L176), K204 (≠ L177), F205 (≠ H178), H251 (= H224), S253 (= S226), R325 (= R298), R335 (= R308)
Sites not aligning to the query:
7tdpA Structure of paenibacillus polymyxa gs bound to met-sox-p-adp (transition state complex) to 1.98 angstom (see paper)
32% identity, 95% coverage: 13:406/413 of query aligns to 39:432/439 of 7tdpA
- binding adenosine-5'-diphosphate: N123 (vs. gap), G125 (≠ A99), E127 (= E101), E179 (≠ D161), D193 (≠ N175), Y196 (≠ H178), N242 (≠ H224), S244 (= S226), R316 (= R298), R326 (= R308)
- binding magnesium ion: E127 (= E101), E127 (= E101), E129 (= E103), E184 (= E166), E191 (= E173), E191 (= E173), H240 (= H222), E328 (= E310)
- binding l-methionine-s-sulfoximine phosphate: E127 (= E101), E129 (= E103), E184 (= E166), E191 (= E173), G236 (= G218), H240 (= H222), R293 (= R275), E299 (≠ A281), R311 (= R293), R330 (= R312)
7tfaB Glutamine synthetase (see paper)
31% identity, 95% coverage: 13:406/413 of query aligns to 39:434/441 of 7tfaB
- binding glutamine: E131 (= E103), Y153 (vs. gap), E186 (= E166), G238 (= G218), H242 (= H222), R295 (= R275), E301 (≠ A281)
- binding magnesium ion: E129 (= E101), E131 (= E103), E186 (= E166), E193 (= E173), H242 (= H222), E330 (= E310)
- binding : Y58 (≠ F32), R60 (≠ G34), V187 (≠ M167), N237 (≠ P217), G299 (≠ P279), Y300 (= Y280), R313 (= R293), M424 (≠ D396)
8ooxB Glutamine synthetase (see paper)
30% identity, 91% coverage: 32:405/413 of query aligns to 57:430/438 of 8ooxB
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)
31% identity, 90% coverage: 37:408/413 of query aligns to 64:442/446 of P9WN37
- K363 (≠ Q337) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
8oozA Glutamine synthetase (see paper)
30% identity, 92% coverage: 28:405/413 of query aligns to 45:422/430 of 8oozA
- binding adenosine-5'-triphosphate: G117 (≠ A99), E170 (≠ D161), F185 (≠ L176), K186 (≠ L177), Y187 (≠ H178), N233 (≠ H224), S235 (= S226), S315 (≠ A306), R317 (= R308)
- binding magnesium ion: E119 (= E101), H231 (= H222), E319 (= E310)
7tf6A Glutamine synthetase (see paper)
29% identity, 97% coverage: 13:412/413 of query aligns to 39:437/438 of 7tf6A
- binding glutamine: E128 (= E103), E183 (= E166), G235 (= G218), H239 (= H222), R292 (= R275), E298 (≠ A281)
- binding magnesium ion: E126 (= E101), E128 (= E103), E183 (= E166), E190 (= E173), H239 (= H222), E327 (= E310)
- binding : F58 (= F32), R60 (≠ G34), G232 (≠ R215), N234 (≠ P217), G296 (≠ P279), Y297 (= Y280), R310 (= R293), Y367 (≠ F349), Y421 (≠ D396), Q433 (≠ V408), Q437 (= Q412)
7tdvC Glutamine synthetase (see paper)
29% identity, 97% coverage: 13:412/413 of query aligns to 40:442/443 of 7tdvC
- binding adenosine-5'-diphosphate: G129 (≠ A99), E131 (= E101), E183 (≠ D161), D197 (≠ N175), F198 (≠ L176), K199 (≠ L177), Y200 (≠ H178), N246 (≠ H224), V247 (≠ Q225), S248 (= S226), R320 (= R298), S328 (≠ A306), R330 (= R308)
- binding magnesium ion: E131 (= E101), E131 (= E101), E133 (= E103), E188 (= E166), E195 (= E173), E195 (= E173), H244 (= H222), E332 (= E310)
- binding l-methionine-s-sulfoximine phosphate: E131 (= E101), E133 (= E103), E188 (= E166), E195 (= E173), G240 (= G218), H244 (= H222), R297 (= R275), E303 (≠ A281), R315 (= R293)
7tf9S L. Monocytogenes gs(14)-q-glnr peptide (see paper)
29% identity, 95% coverage: 13:406/413 of query aligns to 40:436/443 of 7tf9S
- binding glutamine: E133 (= E103), Y155 (≠ R126), E188 (= E166), G240 (= G218), G242 (≠ S220), R297 (= R275), E303 (≠ A281)
- binding magnesium ion: E131 (= E101), E133 (= E103), E188 (= E166), E195 (= E173), H244 (= H222), E332 (= E310)
- binding : F59 (= F32), V60 (≠ Y33), E418 (≠ A388), I422 (≠ L392), M426 (≠ D396)
7tenA Glutamine synthetase (see paper)
29% identity, 95% coverage: 13:406/413 of query aligns to 39:435/442 of 7tenA
- binding adenosine-5'-diphosphate: G128 (≠ A99), E130 (= E101), E182 (≠ D161), D196 (≠ N175), F197 (≠ L176), K198 (≠ L177), Y199 (≠ H178), N245 (≠ H224), S247 (= S226), R319 (= R298), S327 (≠ A306), R329 (= R308)
- binding l-methionine-s-sulfoximine phosphate: E130 (= E101), E132 (= E103), E187 (= E166), E194 (= E173), N238 (≠ P217), G239 (= G218), H243 (= H222), R296 (= R275), E302 (≠ A281), R314 (= R293), R333 (= R312)
Query Sequence
>PP_4399 FitnessBrowser__Putida:PP_4399
MTAEGFLEGRRLQMARGVLLQCIMGGYPPAKFYGSDDGDLALVAEPSQVHRLPWSDDGRA
LAICDANELDGRPSALSTRGQLKAVIARYAALGLAPVVATELEFFVFAPNTDPQQPFLPP
VGSDGRRELGHSAFSVSSNNGLRPFFKEVYHCMAALGLPRDTFMHEMGVSQFEINLLHGD
PLLLADQTFLFKHLLKEVALKHGLTVVCMAKPLARTPGSSMHIHQSLVEAGSGRNVFSDE
QGLPTETFHHFIGGLQACMADFTALFAPNVNSYQRLCHPYASPNNACWSEDNRAAGLRIP
ASAPVARRVENRLPGADANPYLAIAASLAAGLHGIEQRLQPSPAIQGEFEVPEHLSLPCT
LHAALERLKRSTLARELFGSEFIEGYIASKTLELSDFFDEITPWERRVLAAQA
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