SitesBLAST
Comparing WP_013528949.1 NCBI__GCF_000185905.1:WP_013528949.1 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)
33% identity, 96% coverage: 15:456/459 of query aligns to 26:469/472 of P78061
- H282 (= H270) mutation to N: Activity is impaired to 9% of wild-type.
- R357 (= R345) mutation to Q: Activity is impaired to 3% of wild-type.
8tfkA Glutamine synthetase (see paper)
31% identity, 92% coverage: 34:456/459 of query aligns to 24:437/440 of 8tfkA
- binding adenosine-5'-diphosphate: E128 (= E149), D194 (≠ N223), F195 (= F224), F197 (≠ H226), N243 (≠ H272), R312 (= R340), R317 (= R345), G325 (≠ A353), R327 (= R355)
- binding magnesium ion: E128 (= E149), E128 (= E149), E130 (= E151), E185 (= E214), E192 (= E221), E192 (= E221), H241 (= H270), E329 (= E357)
- binding l-methionine-s-sulfoximine phosphate: E128 (= E149), E130 (= E151), E185 (= E214), E192 (= E221), G237 (= G266), H241 (= H270), R294 (= R322), E300 (≠ S328), R312 (= R340), R331 (= R359)
8ufjB Glutamine synthetase (see paper)
31% identity, 92% coverage: 34:456/459 of query aligns to 28:441/444 of 8ufjB
8ooqB Glutamine synthetase from Methanothermococcus thermolithotrophicus (see paper)
31% identity, 91% coverage: 34:451/459 of query aligns to 23:439/446 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)
31% identity, 91% coverage: 34:451/459 of query aligns to 24:440/447 of 8oooA
- binding 2-oxoglutaric acid: A33 (= A43), R87 (≠ A103), V93 (vs. gap), P170 (= P192), R173 (= R195), R174 (= R196), S190 (≠ L211)
- binding adenosine-5'-triphosphate: E136 (= E149), E188 (≠ D209), F203 (= F224), K204 (≠ L225), F205 (≠ H226), H251 (= H272), S253 (= S274), R325 (= R345), R335 (= R355)
Sites not aligning to the query:
7tf9S L. Monocytogenes gs(14)-q-glnr peptide (see paper)
30% identity, 92% coverage: 34:456/459 of query aligns to 26:440/443 of 7tf9S
- binding glutamine: E133 (= E151), Y155 (≠ A175), E188 (= E214), G240 (= G266), G242 (≠ S268), R297 (= R322), E303 (≠ S328)
- binding magnesium ion: E131 (= E149), E133 (= E151), E188 (= E214), E195 (= E221), H244 (= H270), E332 (= E357)
- binding : F59 (= F81), V60 (≠ A82), E418 (≠ R434), I422 (≠ V438), M426 (≠ L442)
7tenA Glutamine synthetase (see paper)
30% identity, 92% coverage: 34:456/459 of query aligns to 25:439/442 of 7tenA
- binding adenosine-5'-diphosphate: G128 (≠ A147), E130 (= E149), E182 (≠ D209), D196 (≠ N223), F197 (= F224), K198 (≠ L225), Y199 (≠ H226), N245 (≠ H272), S247 (= S274), R319 (= R345), S327 (≠ A353), R329 (= R355)
- binding l-methionine-s-sulfoximine phosphate: E130 (= E149), E132 (= E151), E187 (= E214), E194 (= E221), N238 (≠ A265), G239 (= G266), H243 (= H270), R296 (= R322), E302 (≠ S328), R314 (= R340), R333 (= R359)
8ooxB Glutamine synthetase (see paper)
31% identity, 92% coverage: 34:456/459 of query aligns to 24:435/438 of 8ooxB
7tfaB Glutamine synthetase (see paper)
28% identity, 92% coverage: 34:456/459 of query aligns to 25:438/441 of 7tfaB
- binding glutamine: E131 (= E151), Y153 (≠ A171), E186 (= E214), G238 (= G266), H242 (= H270), R295 (= R322), E301 (≠ S328)
- binding magnesium ion: E129 (= E149), E131 (= E151), E186 (= E214), E193 (= E221), H242 (= H270), E330 (= E357)
- binding : Y58 (≠ F81), R60 (vs. gap), V187 (≠ S215), N237 (≠ A265), G299 (≠ N326), Y300 (≠ H327), R313 (= R340), M424 (≠ L442)
7tdpA Structure of paenibacillus polymyxa gs bound to met-sox-p-adp (transition state complex) to 1.98 angstom (see paper)
28% identity, 92% coverage: 34:456/459 of query aligns to 25:436/439 of 7tdpA
- binding adenosine-5'-diphosphate: N123 (vs. gap), G125 (≠ A147), E127 (= E149), E179 (≠ D209), D193 (≠ N223), Y196 (≠ H226), N242 (≠ H272), S244 (= S274), R316 (= R345), R326 (= R355)
- binding magnesium ion: E127 (= E149), E127 (= E149), E129 (= E151), E184 (= E214), E191 (= E221), E191 (= E221), H240 (= H270), E328 (= E357)
- binding l-methionine-s-sulfoximine phosphate: E127 (= E149), E129 (= E151), E184 (= E214), E191 (= E221), G236 (= G266), H240 (= H270), R293 (= R322), E299 (≠ S328), R311 (= R340), R330 (= R359)
8oozA Glutamine synthetase (see paper)
31% identity, 92% coverage: 34:456/459 of query aligns to 24:427/430 of 8oozA
- binding adenosine-5'-triphosphate: G117 (≠ A147), E170 (≠ D209), F185 (= F224), K186 (≠ L225), Y187 (≠ H226), N233 (≠ H272), S235 (= S274), S315 (≠ A353), R317 (= R355)
- binding magnesium ion: E119 (= E149), H231 (= H270), E319 (= E357)
5dm3C Crystal structure of glutamine synthetase from chromohalobacter salexigens dsm 3043(csal_0679, target efi-550015) with bound adp
35% identity, 79% coverage: 90:451/459 of query aligns to 56:390/396 of 5dm3C
- active site: E115 (= E149), E117 (= E151), E162 (= E214), E169 (= E221), H218 (= H270), R286 (= R340), E303 (= E357), R305 (= R359)
- binding adenosine-5'-diphosphate: R173 (≠ L225), C174 (≠ H226), H220 (= H272), S222 (= S274), R301 (= R355)
4s0rD Structure of gs-tnra complex (see paper)
28% identity, 96% coverage: 15:456/459 of query aligns to 11:444/447 of 4s0rD
- active site: D56 (≠ S74), E135 (= E149), E137 (= E151), E192 (= E214), E199 (= E221), H248 (= H270), R319 (= R340), E336 (= E357), R338 (= R359)
- binding glutamine: E137 (= E151), E192 (= E214), R301 (= R322), E307 (≠ S328)
- binding magnesium ion: I66 (≠ Y83), E135 (= E149), E135 (= E149), E199 (= E221), H248 (= H270), H248 (= H270), E336 (= E357), H419 (≠ T431)
- binding : F63 (= F81), V64 (≠ A82), R65 (vs. gap), I66 (≠ Y83), D161 (= D183), G241 (≠ A263), V242 (≠ Q264), N243 (≠ A265), G305 (≠ N326), Y306 (≠ H327), Y376 (= Y397), I426 (≠ V438), M430 (≠ L442)
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, 96% coverage: 15:456/459 of query aligns to 8:441/444 of P12425
- G59 (= G80) 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 (vs. gap) 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 (= E149) binding Mg(2+)
- E134 (= E151) binding Mg(2+)
- E189 (= E214) binding Mg(2+)
- V190 (≠ S215) 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 (= E221) binding Mg(2+)
- G241 (= G266) binding L-glutamate
- H245 (= H270) binding Mg(2+)
- G302 (≠ N326) 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 (≠ S328) 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 (= P330) 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 (= E357) binding Mg(2+)
- E424 (= E439) 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)
28% identity, 96% coverage: 15:456/459 of query aligns to 7:440/443 of 4lnkA
- active site: D52 (≠ S74), E131 (= E149), E133 (= E151), E188 (= E214), E195 (= E221), H244 (= H270), R315 (= R340), E332 (= E357), R334 (= R359)
- binding adenosine-5'-diphosphate: K43 (≠ Q51), M50 (≠ L58), F198 (= F224), Y200 (≠ H226), N246 (≠ H272), S248 (= S274), S324 (≠ G349), S328 (≠ A353), R330 (= R355)
- binding glutamic acid: E133 (= E151), E188 (= E214), V189 (≠ S215), N239 (≠ A265), G240 (= G266), G242 (≠ S268), E303 (≠ S328)
- binding magnesium ion: E131 (= E149), E188 (= E214), E195 (= E221), H244 (= H270), E332 (= E357)
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, 96% coverage: 15:456/459 of query aligns to 7:440/443 of 4lniA
- active site: D52 (≠ S74), E131 (= E149), E133 (= E151), E188 (= E214), E195 (= E221), H244 (= H270), R315 (= R340), E332 (= E357), R334 (= R359)
- binding adenosine-5'-diphosphate: E131 (= E149), E183 (≠ D209), D197 (≠ N223), Y200 (≠ H226), N246 (≠ H272), S248 (= S274), R320 (= R345), R330 (= R355)
- binding magnesium ion: E131 (= E149), E131 (= E149), E133 (= E151), E188 (= E214), E195 (= E221), E195 (= E221), H244 (= H270), E332 (= E357)
- binding l-methionine-s-sulfoximine phosphate: E133 (= E151), E188 (= E214), H244 (= H270), R297 (= R322), E303 (≠ S328), R315 (= R340), R334 (= R359)
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, 95% coverage: 20:457/459 of query aligns to 12:446/446 of P9WN37
- K363 (≠ Q384) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
5dm3A Crystal structure of glutamine synthetase from chromohalobacter salexigens dsm 3043(csal_0679, target efi-550015) with bound adp
32% identity, 84% coverage: 66:451/459 of query aligns to 23:368/374 of 5dm3A
- active site: E107 (= E149), E109 (= E151), E146 (≠ T217), E150 (= E221), H199 (= H270), R265 (= R340), E282 (= E357), R284 (= R359)
- binding adenosine-5'-diphosphate: I103 (≠ V145), E141 (≠ D209), R154 (≠ L225), C155 (≠ H226), H201 (= H272), S203 (= S274), R280 (= R355)
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)
33% identity, 84% coverage: 73:456/459 of query aligns to 51:444/446 of A0R083
- K363 (≠ Q384) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
7tdvC Glutamine synthetase (see paper)
26% identity, 96% coverage: 15:456/459 of query aligns to 7:440/443 of 7tdvC
- binding adenosine-5'-diphosphate: G129 (≠ A147), E131 (= E149), E183 (≠ D209), D197 (≠ N223), F198 (= F224), K199 (≠ L225), Y200 (≠ H226), N246 (≠ H272), V247 (≠ M273), S248 (= S274), R320 (= R345), S328 (≠ A353), R330 (= R355)
- binding magnesium ion: E131 (= E149), E131 (= E149), E133 (= E151), E188 (= E214), E195 (= E221), E195 (= E221), H244 (= H270), E332 (= E357)
- binding l-methionine-s-sulfoximine phosphate: E131 (= E149), E133 (= E151), E188 (= E214), E195 (= E221), G240 (= G266), H244 (= H270), R297 (= R322), E303 (≠ S328), R315 (= R340)
Query Sequence
>WP_013528949.1 NCBI__GCF_000185905.1:WP_013528949.1
MPDNNTNISLSSGTDAKAWLTRHGINEVECLVPDMNGVLRGKALPTAKFLQALEDRALYL
PSSAFLVSIDGRYSGSIDEGFAYSDPDMRMVPDVSTLCLAPGAAPGKAYVFADAFHMDDR
PWMASPRHVLRAVLDLYAKRGWRAVVAPEVEFYLTAPNPDPDRPLTAPVGANGRAETVQH
PYDMAGLEEFEPVIRRIYDYAAAAGLPLDTLIHESGTAQLEINFLHGDALPLADKVLLFK
RLTRQAAQQSGMHATFMAKPIAAQAGSSMHLHMSVIDEAGRTLFAGSDDADTAMFGHFIG
GLQKYVPEIMPLFAPNVNSFRRIRPNHSAPANIEWSHDNRSCGLRVPAGGRAARRVENRL
PGADSNPYLAIAGSLLAGYLGVEQKLARSPEASGNAYKIKSTLPKTMEEALDRFEACGPV
RELLGEDFFQTYLRVKSVELDLFQGVVTSWERDHLLLKV
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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