SitesBLAST
Comparing WP_011802240.1 NCBI__GCF_000015505.1:WP_011802240.1 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)
34% identity, 98% coverage: 9:456/459 of query aligns to 19:469/472 of P78061
- H282 (= H269) mutation to N: Activity is impaired to 9% of wild-type.
- R357 (= R345) mutation to Q: Activity is impaired to 3% of wild-type.
8ufjB Glutamine synthetase (see paper)
32% identity, 99% coverage: 7:459/459 of query aligns to 1:444/444 of 8ufjB
8tfkA Glutamine synthetase (see paper)
34% identity, 90% coverage: 46:459/459 of query aligns to 19:440/440 of 8tfkA
- binding adenosine-5'-diphosphate: E128 (= E148), D194 (≠ N222), F195 (= F223), F197 (≠ H225), N243 (≠ H271), R312 (= R340), R317 (= R345), G325 (≠ A353), R327 (= R355)
- binding magnesium ion: E128 (= E148), E128 (= E148), E130 (= E150), E185 (= E213), E192 (= E220), E192 (= E220), H241 (= H269), E329 (= E357)
- binding l-methionine-s-sulfoximine phosphate: E128 (= E148), E130 (= E150), E185 (= E213), E192 (= E220), G237 (= G265), H241 (= H269), R294 (= R322), E300 (≠ A328), R312 (= R340), R331 (= R359)
8ooqB Glutamine synthetase from Methanothermococcus thermolithotrophicus (see paper)
33% identity, 83% coverage: 72:451/459 of query aligns to 50:439/446 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)
33% identity, 83% coverage: 72:451/459 of query aligns to 51:440/447 of 8oooA
- binding 2-oxoglutaric acid: R87 (vs. gap), V93 (≠ T106), P170 (≠ D190), R173 (≠ F193), R174 (≠ E194), S190 (≠ L210)
- binding adenosine-5'-triphosphate: E136 (= E148), E188 (≠ D208), F203 (= F223), K204 (≠ F224), F205 (≠ H225), H251 (= H271), S253 (= S273), R325 (= R345), R335 (= R355)
Sites not aligning to the query:
8oozA Glutamine synthetase (see paper)
31% identity, 95% coverage: 20:456/459 of query aligns to 10:427/430 of 8oozA
- binding adenosine-5'-triphosphate: G117 (≠ A146), E170 (≠ D208), F185 (= F223), K186 (≠ F224), Y187 (≠ H225), N233 (≠ H271), S235 (= S273), S315 (≠ A353), R317 (= R355)
- binding magnesium ion: E119 (= E148), H231 (= H269), E319 (= E357)
8ooxB Glutamine synthetase (see paper)
31% identity, 95% coverage: 20:456/459 of query aligns to 10:435/438 of 8ooxB
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: 12:456/459 of query aligns to 4:440/443 of 4lnkA
- active site: D52 (≠ M64), E131 (= E148), E133 (= E150), E188 (= E213), E195 (= E220), H244 (= H269), R315 (= R340), E332 (= E357), R334 (= R359)
- binding adenosine-5'-diphosphate: K43 (≠ M55), M50 (≠ V62), F198 (= F223), Y200 (≠ H225), N246 (≠ H271), S248 (= S273), S324 (≠ A349), S328 (≠ A353), R330 (= R355)
- binding glutamic acid: E133 (= E150), E188 (= E213), V189 (= V214), N239 (≠ P264), G240 (= G265), G242 (≠ A267), E303 (≠ A328)
- binding magnesium ion: E131 (= E148), E188 (= E213), E195 (= E220), H244 (= H269), 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)
30% identity, 97% coverage: 12:456/459 of query aligns to 4:440/443 of 4lniA
- active site: D52 (≠ M64), E131 (= E148), E133 (= E150), E188 (= E213), E195 (= E220), H244 (= H269), R315 (= R340), E332 (= E357), R334 (= R359)
- binding adenosine-5'-diphosphate: E131 (= E148), E183 (≠ D208), D197 (≠ N222), Y200 (≠ H225), N246 (≠ H271), S248 (= S273), R320 (= R345), R330 (= R355)
- binding magnesium ion: E131 (= E148), E131 (= E148), E133 (= E150), E188 (= E213), E195 (= E220), E195 (= E220), H244 (= H269), E332 (= E357)
- binding l-methionine-s-sulfoximine phosphate: E133 (= E150), E188 (= E213), H244 (= H269), R297 (= R322), E303 (≠ A328), R315 (= R340), R334 (= R359)
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: 12:456/459 of query aligns to 5:441/444 of P12425
- G59 (≠ D78) 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 (≠ S81) 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 (= E148) binding Mg(2+)
- E134 (= E150) binding Mg(2+)
- E189 (= E213) binding Mg(2+)
- V190 (= V214) 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 (= E220) binding Mg(2+)
- G241 (= G265) binding L-glutamate
- H245 (= H269) binding Mg(2+)
- G302 (≠ D326) 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 (≠ A328) 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
4s0rD Structure of gs-tnra complex (see paper)
30% identity, 97% coverage: 12:456/459 of query aligns to 8:444/447 of 4s0rD
- active site: D56 (≠ M64), E135 (= E148), E137 (= E150), E192 (= E213), E199 (= E220), H248 (= H269), R319 (= R340), E336 (= E357), R338 (= R359)
- binding glutamine: E137 (= E150), E192 (= E213), R301 (= R322), E307 (≠ A328)
- binding magnesium ion: I66 (≠ P82), E135 (= E148), E135 (= E148), E199 (= E220), H248 (= H269), H248 (= H269), E336 (= E357), H419 (≠ V431)
- binding : F63 (≠ V79), V64 (≠ I80), R65 (≠ S81), I66 (≠ P82), D161 (≠ G172), G241 (= G262), V242 (≠ E263), N243 (≠ P264), G305 (≠ D326), Y306 (≠ T327), Y376 (= Y397), I426 (≠ M438), M430 (≠ E442)
7tfaB Glutamine synthetase (see paper)
33% identity, 82% coverage: 84:458/459 of query aligns to 63:440/441 of 7tfaB
- binding glutamine: E131 (= E150), Y153 (≠ A180), E186 (= E213), G238 (= G265), H242 (= H269), R295 (= R322), E301 (≠ A328)
- binding magnesium ion: E129 (= E148), E131 (= E150), E186 (= E213), E193 (= E220), H242 (= H269), E330 (= E357)
- binding : V187 (= V214), N237 (≠ P264), G299 (≠ D326), Y300 (≠ T327), R313 (= R340), M424 (≠ E442)
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)
33% identity, 82% coverage: 84:458/459 of query aligns to 63:438/439 of 7tdpA
- binding adenosine-5'-diphosphate: N123 (vs. gap), G125 (≠ A146), E127 (= E148), E179 (≠ D208), D193 (≠ N222), Y196 (≠ H225), N242 (≠ H271), S244 (= S273), R316 (= R345), R326 (= R355)
- binding magnesium ion: E127 (= E148), E127 (= E148), E129 (= E150), E184 (= E213), E191 (= E220), E191 (= E220), H240 (= H269), E328 (= E357)
- binding l-methionine-s-sulfoximine phosphate: E127 (= E148), E129 (= E150), E184 (= E213), E191 (= E220), G236 (= G265), H240 (= H269), R293 (= R322), E299 (≠ A328), R311 (= R340), R330 (= R359)
5dm3C Crystal structure of glutamine synthetase from chromohalobacter salexigens dsm 3043(csal_0679, target efi-550015) with bound adp
32% identity, 79% coverage: 89:451/459 of query aligns to 56:390/396 of 5dm3C
- active site: E115 (= E148), E117 (= E150), E162 (= E213), E169 (= E220), H218 (= H269), R286 (= R340), E303 (= E357), R305 (= R359)
- binding adenosine-5'-diphosphate: R173 (≠ F224), C174 (≠ H225), H220 (= H271), S222 (= S273), R301 (= R355)
7tenA Glutamine synthetase (see paper)
31% identity, 81% coverage: 84:456/459 of query aligns to 63:439/442 of 7tenA
- binding adenosine-5'-diphosphate: G128 (≠ A146), E130 (= E148), E182 (≠ D208), D196 (≠ N222), F197 (= F223), K198 (≠ F224), Y199 (≠ H225), N245 (≠ H271), S247 (= S273), R319 (= R345), S327 (≠ A353), R329 (= R355)
- binding l-methionine-s-sulfoximine phosphate: E130 (= E148), E132 (= E150), E187 (= E213), E194 (= E220), N238 (≠ P264), G239 (= G265), H243 (= H269), R296 (= R322), E302 (≠ A328), R314 (= R340), R333 (= R359)
7tf9S L. Monocytogenes gs(14)-q-glnr peptide (see paper)
31% identity, 81% coverage: 84:456/459 of query aligns to 64:440/443 of 7tf9S
- binding glutamine: E133 (= E150), Y155 (≠ A180), E188 (= E213), G240 (= G265), G242 (≠ A267), R297 (= R322), E303 (≠ A328)
- binding magnesium ion: E131 (= E148), E133 (= E150), E188 (= E213), E195 (= E220), H244 (= H269), E332 (= E357)
- binding : E418 (= E434), I422 (≠ M438), M426 (≠ E442)
Sites not aligning to the query:
8wwuB Glutamine synthetase
31% identity, 93% coverage: 19:444/459 of query aligns to 11:466/492 of 8wwuB
- binding phosphoaminophosphonic acid-adenylate ester: G157 (≠ A146), E159 (= E148), R226 (≠ D208), F241 (= F223), V243 (≠ H225), H290 (= H271), S292 (= S273), K360 (≠ R340), R365 (= R345), R376 (= R355)
- binding magnesium ion: E159 (= E148), E238 (= E220)
- binding manganese (ii) ion: E159 (= E148), E161 (= E150), E231 (= E213), E238 (= E220), H288 (= H269), E378 (= E357)
8wwvA Glutamine synthetase
31% identity, 93% coverage: 19:444/459 of query aligns to 9:464/490 of 8wwvA
- binding adenosine-5'-diphosphate: G155 (≠ A146), E157 (= E148), R224 (≠ D208), F239 (= F223), D240 (≠ F224), V241 (≠ H225), H288 (= H271), S290 (= S273), R374 (= R355), E376 (= E357)
- binding magnesium ion: E157 (= E148), E236 (= E220)
- binding manganese (ii) ion: E157 (= E148), E159 (= E150), E229 (= E213), E236 (= E220), H286 (= H269), E376 (= E357)
- binding l-methionine-s-sulfoximine phosphate: E157 (= E148), E159 (= E150), E229 (= E213), E236 (= E220), A282 (≠ G265), H286 (= H269), R340 (= R322), K358 (≠ R340)
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, 82% coverage: 84:458/459 of query aligns to 64:446/446 of A0R083
- K363 (≠ N384) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
7tf6A Glutamine synthetase (see paper)
31% identity, 81% coverage: 84:456/459 of query aligns to 63:435/438 of 7tf6A
- binding glutamine: E128 (= E150), E183 (= E213), G235 (= G265), H239 (= H269), R292 (= R322), E298 (≠ A328)
- binding magnesium ion: E126 (= E148), E128 (= E150), E183 (= E213), E190 (= E220), H239 (= H269), E327 (= E357)
- binding : G232 (= G262), N234 (≠ P264), G296 (≠ D326), Y297 (≠ T327), R310 (= R340), Y367 (vs. gap), Y421 (≠ E442), Q433 (≠ H454)
Sites not aligning to the query:
Query Sequence
>WP_011802240.1 NCBI__GCF_000015505.1:WP_011802240.1
MSFNMSMSKASTFTDLENWLNERRVTEVECLVPDLTGVARGKILPRGKFTEDRGMRLPEA
VVAMGVTGEFPESGPYYDVISPTDKDMHLRPDPSTVRIVPWASNPTAQVIHDCFDPAGKL
IPFAPRSVLRRVCELYEAEGLVPVVAPELEFYLVARNTDPNTLLRPPIGRSGRAETSRQA
YSIDAVNEFDPLFEDIYDYCEKMELNVDTLIHEVGAGQMEINFFHAHPLGLADEVFFFKR
TVREAALRHNMYATFMAKPIAGEPGSAMHVHQSILSKETGLNIFSNPDGSESEAFFHYIG
GLQRYIPAAMALVAPYVNSYRRLSRDTAAPINIAWGHDNRTVGIRSPIATPQARRVENRV
IGADANPYVALAMTLACGYLGIKNKIKPKPEMKGDAYLSPYSLPRSLGEALDWLRRESDL
HEVLGREFVTVYSEIKEMEFAEFMKVISPWEREHLLLLV
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