SitesBLAST
Comparing Synpcc7942_0169 FitnessBrowser__SynE:Synpcc7942_0169 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)
3o6xA Crystal structure of the type iii glutamine synthetase from bacteroides fragilis (see paper)
39% identity, 99% coverage: 7:721/723 of query aligns to 3:637/638 of 3o6xA
- binding adenosine-5'-diphosphate: E180 (= E221), E244 (= E299), F249 (= F304), N295 (= N350), S297 (= S352), R388 (= R473), E390 (= E475)
- binding magnesium ion: E180 (= E221), E182 (= E223), E237 (= E292), E244 (= E299), H293 (= H348), E390 (= E475)
- binding l-methionine-s-sulfoximine phosphate: E180 (= E221), E182 (= E223), E237 (= E292), G289 (= G344), G291 (= G346), H293 (= H348), R349 (= R404), E354 (= E409), R378 (= R463)
7tf9S L. Monocytogenes gs(14)-q-glnr peptide (see paper)
33% identity, 23% coverage: 197:363/723 of query aligns to 112:259/443 of 7tf9S
Sites not aligning to the query:
7tenA Glutamine synthetase (see paper)
33% identity, 23% coverage: 197:363/723 of query aligns to 111:258/442 of 7tenA
- binding adenosine-5'-diphosphate: G128 (= G219), E130 (= E221), E182 (≠ K287), D196 (≠ A301), F197 (≠ P302), K198 (≠ F303), Y199 (≠ F304), N245 (= N350), S247 (= S352)
- binding l-methionine-s-sulfoximine phosphate: E130 (= E221), E132 (= E223), E187 (= E292), E194 (= E299), N238 (= N343), G239 (= G344), H243 (= H348)
Sites not aligning to the query:
7tf6A Glutamine synthetase (see paper)
30% identity, 19% coverage: 226:365/723 of query aligns to 118:256/438 of 7tf6A
Sites not aligning to the query:
7tdvC Glutamine synthetase (see paper)
30% identity, 19% coverage: 226:365/723 of query aligns to 123:261/443 of 7tdvC
- binding adenosine-5'-diphosphate: G129 (≠ A232), E131 (≠ Q234), E183 (≠ K287), D197 (≠ A301), F198 (≠ P302), K199 (≠ F303), Y200 (≠ F304), N246 (= N350), V247 (≠ W351), S248 (= S352)
- binding magnesium ion: E131 (≠ Q234), E131 (≠ Q234), E133 (≠ D237), E188 (= E292), E195 (= E299), E195 (= E299), H244 (= H348)
- binding l-methionine-s-sulfoximine phosphate: E131 (≠ Q234), E133 (≠ D237), E188 (= E292), E195 (= E299), G240 (= G344), H244 (= H348)
Sites not aligning to the query:
8tfkA Glutamine synthetase (see paper)
28% identity, 26% coverage: 200:388/723 of query aligns to 106:281/440 of 8tfkA
- binding adenosine-5'-diphosphate: E128 (= E221), D194 (≠ A301), F195 (≠ P302), F197 (= F304), N243 (= N350)
- binding magnesium ion: E128 (= E221), E128 (= E221), E130 (= E223), E185 (= E292), E192 (= E299), E192 (= E299), H241 (= H348)
- binding l-methionine-s-sulfoximine phosphate: E128 (= E221), E130 (= E223), E185 (= E292), E192 (= E299), G237 (= G344), H241 (= H348)
Sites not aligning to the query:
7tfaB Glutamine synthetase (see paper)
36% identity, 12% coverage: 279:366/723 of query aligns to 173:260/441 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)
36% identity, 12% coverage: 279:366/723 of query aligns to 171:258/439 of 7tdpA
- binding adenosine-5'-diphosphate: E179 (≠ K287), D193 (≠ A301), Y196 (≠ F304), N242 (= N350), S244 (= S352)
- binding magnesium ion: E184 (= E292), E191 (= E299), E191 (= E299), H240 (= H348)
- binding l-methionine-s-sulfoximine phosphate: E184 (= E292), E191 (= E299), G236 (= G344), H240 (= H348)
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
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)
38% identity, 11% coverage: 273:353/723 of query aligns to 169:249/443 of 4lnkA
- active site: E188 (= E292), E195 (= E299), H244 (= H348)
- binding adenosine-5'-diphosphate: F198 (≠ P302), Y200 (≠ F304), N246 (= N350), S248 (= S352)
- binding glutamic acid: E188 (= E292), V189 (= V293), N239 (= N343), G240 (= G344), G242 (= G346)
- binding magnesium ion: E188 (= E292), E195 (= E299), H244 (= H348)
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)
38% identity, 11% coverage: 273:353/723 of query aligns to 169:249/443 of 4lniA
- active site: E188 (= E292), E195 (= E299), H244 (= H348)
- binding adenosine-5'-diphosphate: E183 (≠ K287), D197 (≠ A301), Y200 (≠ F304), N246 (= N350), S248 (= S352)
- binding magnesium ion: E188 (= E292), E195 (= E299), E195 (= E299), H244 (= H348)
- binding l-methionine-s-sulfoximine phosphate: E188 (= E292), H244 (= H348)
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)
38% identity, 11% coverage: 273:353/723 of query aligns to 170:250/444 of P12425
- E189 (= E292) binding Mg(2+)
- V190 (= V293) 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 (= E299) binding Mg(2+)
- G241 (= G344) binding L-glutamate
- H245 (= H348) 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)
38% identity, 11% coverage: 273:353/723 of query aligns to 173:253/447 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
8ooqB Glutamine synthetase from Methanothermococcus thermolithotrophicus (see paper)
24% identity, 40% coverage: 219:509/723 of query aligns to 133:367/446 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)
24% identity, 40% coverage: 219:509/723 of query aligns to 134:368/447 of 8oooA
- binding 2-oxoglutaric acid: P170 (= P265), R173 (≠ M272), R174 (≠ Q273), S190 (≠ R289)
- binding adenosine-5'-triphosphate: E136 (= E221), E188 (≠ K287), F203 (≠ P302), K204 (≠ F303), F205 (= F304), H251 (≠ N350), S253 (= S352), R325 (= R463), R335 (= R473)
Sites not aligning to the query:
8ufjB Glutamine synthetase (see paper)
28% identity, 26% coverage: 200:388/723 of query aligns to 110:285/444 of 8ufjB
Sites not aligning to the query:
8ooxB Glutamine synthetase (see paper)
27% identity, 24% coverage: 217:386/723 of query aligns to 123:277/438 of 8ooxB
8oozA Glutamine synthetase (see paper)
27% identity, 24% coverage: 217:386/723 of query aligns to 115:269/430 of 8oozA
Sites not aligning to the query:
5zlpJ Crystal structure of glutamine synthetase from helicobacter pylori (see paper)
25% identity, 46% coverage: 199:531/723 of query aligns to 115:414/478 of 5zlpJ
- binding adenosine-5'-diphosphate: Y132 (≠ S217), E136 (= E221), F215 (≠ K287), F232 (= F304), H278 (≠ N350), S280 (= S352), R351 (vs. gap), R362 (= R473)
- binding magnesium ion: E138 (= E223), E220 (= E292), E227 (= E299)
- binding phosphinothricin: E138 (= E223), E220 (= E292), G272 (= G344), H276 (= H348), E334 (= E409), R346 (= R461), R366 (= R477)
5zlpL Crystal structure of glutamine synthetase from helicobacter pylori (see paper)
25% identity, 46% coverage: 199:531/723 of query aligns to 113:412/476 of 5zlpL
- binding adenosine-5'-diphosphate: G132 (= G219), E134 (= E221), F213 (≠ K287), F230 (= F304), H276 (≠ N350), S278 (= S352), R349 (vs. gap), R360 (= R473)
- binding magnesium ion: E136 (= E223), E218 (= E292), E225 (= E299)
- binding (2s)-2-amino-4-[methyl(phosphonooxy)phosphoryl]butanoic acid: E136 (= E223), E218 (= E292), G270 (= G344), H274 (= H348), E332 (= E409), R344 (= R461), R364 (= R477)
5zlpA Crystal structure of glutamine synthetase from helicobacter pylori (see paper)
25% identity, 46% coverage: 199:531/723 of query aligns to 113:412/476 of 5zlpA
Query Sequence
>Synpcc7942_0169 FitnessBrowser__SynE:Synpcc7942_0169
MSGNAARVNAVHQITNREPLPSKPPMSLEAIWAENVFDLSKMQARLPKAVFKSIKNTIVT
GQKLDPSVADAVATAMKDWAMSKGALYYAHVFYPMTNVTAEKHDGFISVQGDGKVISEFS
GKVLVQGEPDGSSFPNGGIRDTFEARGYTGWDVTSPAYIMETDNGSTLCIPTVFVSWTGE
ALDKKVPLLRSIAAMDKAARKVLTLLGNTEVSQVNSSCGAEQEYFLVDANFAAQRPDLLL
AGRTLFGRPSAKGQEFDDHYFGAIPERVQVFMQDVEETLYKLGIPAKTRHNEVAPGQFEI
APFFEAANVASDHQQLIMTVLKQTAKKHGFMCLLHEKPFAGINGSGKHVNWSVGNATQGN
LLDPGDSPHDNAQFLVFCGAVIRGVHKYGPLMRAAIATASNDHRLGANEAPPAIMSVYLG
TQLEEVFEQIKTGTVTESKQKGIMDLGVDVLPYLTKDAGDRNRTSPFAFTGNRFEFRAVG
ASQSVSGPLIVLNTILADSLDWIGNRLESELAKGLDLNTAILTVLKEVMEEHGNVIFGGN
GYSEEWHREAVEKRGLANLPTTADALPVLKEEYIEDLFKKTGVLTPVELESRFEVYAEQY
ILSIEVEAKLAVSIAKTIIYPAAVEYLAKLSGTIASLSGLGIDFEKESARKIAELTSSLV
GAATQLSEALEHESSDTVEHLQYCAKTLRPLMDNVRTYADALEAEVADSFWPLPTYQEML
FIK
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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