SitesBLAST
Comparing WP_011781186.1 NCBI__GCF_000015305.1:WP_011781186.1 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)
3o6xA Crystal structure of the type iii glutamine synthetase from bacteroides fragilis (see paper)
39% identity, 99% coverage: 6:723/725 of query aligns to 2:637/638 of 3o6xA
- binding adenosine-5'-diphosphate: E180 (= E223), E244 (= E301), F249 (= F306), N295 (= N352), S297 (= S354), R388 (= R475), E390 (= E477)
- binding magnesium ion: E180 (= E223), E182 (= E225), E237 (= E294), E244 (= E301), H293 (= H350), E390 (= E477)
- binding l-methionine-s-sulfoximine phosphate: E180 (= E223), E182 (= E225), E237 (= E294), G289 (= G346), G291 (= G348), H293 (= H350), R349 (= R406), E354 (= E411), R378 (= R465)
7tf9S L. Monocytogenes gs(14)-q-glnr peptide (see paper)
44% identity, 11% coverage: 276:357/725 of query aligns to 170:251/443 of 7tf9S
Sites not aligning to the query:
7tenA Glutamine synthetase (see paper)
44% identity, 11% coverage: 276:357/725 of query aligns to 169:250/442 of 7tenA
- binding adenosine-5'-diphosphate: E182 (≠ K289), D196 (≠ A303), F197 (≠ P304), K198 (≠ M305), Y199 (≠ F306), N245 (= N352), S247 (= S354)
- binding l-methionine-s-sulfoximine phosphate: E187 (= E294), E194 (= E301), N238 (= N345), G239 (= G346), H243 (= H350)
Sites not aligning to the query:
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)
32% identity, 17% coverage: 276:400/725 of query aligns to 170:294/443 of 4lnkA
- active site: E188 (= E294), E195 (= E301), H244 (= H350)
- binding adenosine-5'-diphosphate: F198 (≠ P304), Y200 (≠ F306), N246 (= N352), S248 (= S354)
- binding glutamic acid: E188 (= E294), V189 (= V295), N239 (= N345), G240 (= G346), G242 (= G348)
- binding magnesium ion: E188 (= E294), E195 (= E301), H244 (= H350)
Sites not aligning to the query:
- active site: 52, 131, 133, 315, 332, 334
- binding adenosine-5'-diphosphate: 43, 50, 324, 328, 330
- binding glutamic acid: 133, 303
- binding magnesium ion: 131, 332
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)
32% identity, 17% coverage: 276:400/725 of query aligns to 170:294/443 of 4lniA
- active site: E188 (= E294), E195 (= E301), H244 (= H350)
- binding adenosine-5'-diphosphate: E183 (≠ K289), D197 (≠ A303), Y200 (≠ F306), N246 (= N352), S248 (= S354)
- binding magnesium ion: E188 (= E294), E195 (= E301), E195 (= E301), H244 (= H350)
- binding l-methionine-s-sulfoximine phosphate: E188 (= E294), H244 (= H350)
Sites not aligning to the query:
- active site: 52, 131, 133, 315, 332, 334
- binding adenosine-5'-diphosphate: 131, 320, 330
- binding magnesium ion: 131, 131, 133, 332
- binding l-methionine-s-sulfoximine phosphate: 133, 297, 303, 315, 334
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)
32% identity, 17% coverage: 276:400/725 of query aligns to 171:295/444 of P12425
- E189 (= E294) binding Mg(2+)
- V190 (= V295) 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 (= E301) binding Mg(2+)
- G241 (= G346) binding L-glutamate
- H245 (= H350) binding Mg(2+)
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 59 G→R: Unable to form stable complex with TnrA. In the presence of glutamine, this mutant derepresses amtB-lacZ fusion and glnRA-lacZ fusion.
- 62 Important for inhibition by glutamine; R→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.
- 132 binding Mg(2+)
- 134 binding Mg(2+)
- 302 G→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.
- 304 E→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.
- 306 P→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.
- 333 binding Mg(2+)
- 424 E→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.
4s0rD Structure of gs-tnra complex (see paper)
41% identity, 11% coverage: 276:355/725 of query aligns to 174:253/447 of 4s0rD
Sites not aligning to the query:
- active site: 56, 135, 137, 319, 336, 338
- binding glutamine: 137, 301, 307
- binding magnesium ion: 66, 135, 135, 336, 419
- binding : 63, 64, 65, 66, 161, 305, 306, 376, 426, 430
7tf6A Glutamine synthetase (see paper)
31% identity, 17% coverage: 280:400/725 of query aligns to 169:289/438 of 7tf6A
Sites not aligning to the query:
- binding glutamine: 128, 292, 298
- binding magnesium ion: 126, 128, 327
- binding : 58, 60, 296, 297, 310, 367, 421, 433, 437
7tdvC Glutamine synthetase (see paper)
31% identity, 17% coverage: 280:400/725 of query aligns to 174:294/443 of 7tdvC
- binding adenosine-5'-diphosphate: E183 (≠ K289), D197 (≠ A303), F198 (≠ P304), K199 (≠ M305), Y200 (≠ F306), N246 (= N352), V247 (≠ F353), S248 (= S354)
- binding magnesium ion: E188 (= E294), E195 (= E301), E195 (= E301), H244 (= H350)
- binding l-methionine-s-sulfoximine phosphate: E188 (= E294), E195 (= E301), G240 (= G346), H244 (= H350)
Sites not aligning to the query:
- binding adenosine-5'-diphosphate: 129, 131, 320, 328, 330
- binding magnesium ion: 131, 131, 133, 332
- binding l-methionine-s-sulfoximine phosphate: 131, 133, 297, 303, 315
7tfaB Glutamine synthetase (see paper)
41% identity, 10% coverage: 280:355/725 of query aligns to 172:247/441 of 7tfaB
Sites not aligning to the query:
- binding glutamine: 131, 153, 295, 301
- binding magnesium ion: 129, 131, 330
- binding : 58, 60, 299, 300, 313, 424
7tdpA Structure of paenibacillus polymyxa gs bound to met-sox-p-adp (transition state complex) to 1.98 angstom (see paper)
41% identity, 10% coverage: 280:355/725 of query aligns to 170:245/439 of 7tdpA
- binding adenosine-5'-diphosphate: E179 (≠ K289), D193 (≠ A303), Y196 (≠ F306), N242 (= N352), S244 (= S354)
- binding magnesium ion: E184 (= E294), E191 (= E301), E191 (= E301), H240 (= H350)
- binding l-methionine-s-sulfoximine phosphate: E184 (= E294), E191 (= E301), G236 (= G346), H240 (= H350)
Sites not aligning to the query:
- binding adenosine-5'-diphosphate: 123, 125, 127, 316, 326
- binding magnesium ion: 127, 127, 129, 328
- binding l-methionine-s-sulfoximine phosphate: 127, 129, 293, 299, 311, 330
8oooA Glutamine synthetase from methanothermococcus thermolithotrophicus in complex with 2-oxoglutarate and mgatp at 2.15 a resolution (see paper)
31% identity, 19% coverage: 219:355/725 of query aligns to 132:254/447 of 8oooA
Sites not aligning to the query:
8ooqB Glutamine synthetase from Methanothermococcus thermolithotrophicus (see paper)
31% identity, 19% coverage: 219:355/725 of query aligns to 131:253/446 of 8ooqB
Sites not aligning to the query:
5zlpJ Crystal structure of glutamine synthetase from helicobacter pylori (see paper)
28% identity, 31% coverage: 217:440/725 of query aligns to 130:360/478 of 5zlpJ
- binding adenosine-5'-diphosphate: Y132 (≠ F219), E136 (= E223), F215 (≠ K289), F232 (= F306), H278 (≠ N352), S280 (= S354), R351 (≠ Q431)
- binding magnesium ion: E138 (= E225), E220 (= E294), E227 (= E301)
- binding phosphinothricin: E138 (= E225), E220 (= E294), G272 (= G346), H276 (= H350), E334 (≠ A412), R346 (≠ Q424)
Sites not aligning to the query:
5zlpL Crystal structure of glutamine synthetase from helicobacter pylori (see paper)
28% identity, 31% coverage: 217:440/725 of query aligns to 128:358/476 of 5zlpL
- binding adenosine-5'-diphosphate: G132 (= G221), E134 (= E223), F213 (≠ K289), F230 (= F306), H276 (≠ N352), S278 (= S354), R349 (≠ Q431)
- binding magnesium ion: E136 (= E225), E218 (= E294), E225 (= E301)
- binding (2s)-2-amino-4-[methyl(phosphonooxy)phosphoryl]butanoic acid: E136 (= E225), E218 (= E294), G270 (= G346), H274 (= H350), E332 (≠ A412), R344 (≠ Q424)
Sites not aligning to the query:
5zlpA Crystal structure of glutamine synthetase from helicobacter pylori (see paper)
28% identity, 31% coverage: 217:440/725 of query aligns to 128:358/476 of 5zlpA
Sites not aligning to the query:
8tfkA Glutamine synthetase (see paper)
31% identity, 18% coverage: 262:395/725 of query aligns to 152:276/440 of 8tfkA
Sites not aligning to the query:
- binding adenosine-5'-diphosphate: 128, 312, 317, 325, 327
- binding magnesium ion: 128, 128, 130, 329
- binding l-methionine-s-sulfoximine phosphate: 128, 130, 294, 300, 312, 331
8oozA Glutamine synthetase (see paper)
29% identity, 19% coverage: 221:355/725 of query aligns to 117:236/430 of 8oozA
Sites not aligning to the query:
8ooxB Glutamine synthetase (see paper)
29% identity, 19% coverage: 221:355/725 of query aligns to 125:244/438 of 8ooxB
7cqwA Gmas/adp complex-conformation 1 (see paper)
30% identity, 19% coverage: 229:368/725 of query aligns to 121:252/430 of 7cqwA
Sites not aligning to the query:
Query Sequence
>WP_011781186.1 NCBI__GCF_000015305.1:WP_011781186.1
MSGNAVRLQAINNVEAYVPPAISFDPTEAPGQIFGSNVFTKAEMQLRLPKSVYKSVVATI
EKGAKLDPAIADAVASAMKDWALSKGATHYAHVFYPMTGLTAEKHDSFLEPISDGETLAE
FAGKTLIQGEPDASSFPSGGLRSTFEARGYTGWDVTSPAYILENPNGNTLCIPTVFVSMT
GEALDYKTPLLRSQQAMGVHAERILALFGHDNLQKVVSFCGPEQEYFLVDRHFFLARPDL
VNAGRTLFGAKPPKGQEFDDHYFGAVPERVLGFMMDTERELFKLGIPAKTRHNEVAPAQF
EVAPMFERANIASDHQQLLMTVFKTVAKKHGMECLFHEKPFAGVNGSGKHVNFSVGNADL
GSLLVPGDTPHENAQFLVFCAAIIRAVHKFGGLLRVSVASATNDHRLGANEAPPAIISIF
LGEQLADVFDQIAKGAATSSKGKGVMHIGVDTLPTLPTDPGDRNRTSPFAFTGNRFEFRA
PGSGQTVAVPMIILNTIMADSFDYMATALEKAVAGGVDFDSAVQTLLTEIITEHGAVVFN
GDGYSENWQIEAAERGLPNLKTTLDAIPELIKPAAVEVFERYGVFSERELHSRYEVRLEQ
YALTIAVEAKLALELGTTVILPAAIRYQTELAQNVATLKAAGMDADTTLLQAVSAPIAEL
TTALGALKAALSGHSGETALDEATHAQQALLPAMEAVRTAADTLETVVADDLWPLPTYQE
MLYIL
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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