SitesBLAST
Comparing Synpcc7942_2296 FitnessBrowser__SynE:Synpcc7942_2296 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)
7cqwA Gmas/adp complex-conformation 1 (see paper)
61% identity, 100% coverage: 1:434/434 of query aligns to 1:430/430 of 7cqwA
7cquA Gmas/adp/metsox-p complex (see paper)
61% identity, 99% coverage: 4:434/434 of query aligns to 3:429/429 of 7cquA
- binding adenosine-5'-diphosphate: E121 (= E122), Y173 (= Y174), N187 (= N188), W188 (= W189), D189 (≠ T190), Y190 (= Y191), H236 (= H237), L237 (= L238), S238 (= S239), R316 (= R319), R322 (= R325)
- binding magnesium ion: E121 (= E122), E121 (= E122), E123 (= E124), E178 (= E179), E185 (= E186), E185 (= E186), H234 (= H235), E324 (= E327)
- binding l-methionine-s-sulfoximine phosphate: E121 (= E122), E123 (= E124), E178 (= E179), E185 (= E186), T229 (= T230), G230 (= G231), H234 (= H235), R287 (= R290), W299 (= W302), R311 (= R314), R326 (= R329)
7cqqA Gmas in complex with amppnp and metsox (see paper)
61% identity, 99% coverage: 4:434/434 of query aligns to 3:429/429 of 7cqqA
- binding phosphoaminophosphonic acid-adenylate ester: E121 (= E122), Y173 (= Y174), E185 (= E186), N187 (= N188), D189 (≠ T190), Y190 (= Y191), H234 (= H235), H236 (= H237), S238 (= S239), R311 (= R314), R316 (= R319), R322 (= R325), E324 (= E327)
- binding magnesium ion: E121 (= E122), E121 (= E122), E123 (= E124), E178 (= E179), E185 (= E186), E185 (= E186), H234 (= H235), E324 (= E327)
- binding (2s)-2-amino-4-(methylsulfonimidoyl)butanoic acid: E123 (= E124), E178 (= E179), T229 (= T230), H234 (= H235), R287 (= R290), W299 (= W302), R311 (= R314), R326 (= R329)
7cqnA Gmas in complex with amppcp (see paper)
61% identity, 99% coverage: 4:434/434 of query aligns to 3:429/429 of 7cqnA
- binding phosphomethylphosphonic acid adenylate ester: G45 (= G46), D61 (= D62), E121 (= E122), Y173 (= Y174), Q174 (= Q175), W188 (= W189), D189 (≠ T190), Y190 (= Y191), H236 (= H237), S238 (= S239), R311 (= R314), R316 (= R319), R322 (= R325)
8tfkA Glutamine synthetase (see paper)
35% identity, 99% coverage: 2:432/434 of query aligns to 5:437/440 of 8tfkA
- binding adenosine-5'-diphosphate: E128 (= E122), D194 (≠ N188), F195 (≠ W189), F197 (≠ Y191), N243 (≠ H237), R312 (= R314), R317 (= R319), G325 (≠ A323), R327 (= R325)
- binding magnesium ion: E128 (= E122), E128 (= E122), E130 (= E124), E185 (= E179), E192 (= E186), E192 (= E186), H241 (= H235), E329 (= E327)
- binding l-methionine-s-sulfoximine phosphate: E128 (= E122), E130 (= E124), E185 (= E179), E192 (= E186), G237 (= G231), H241 (= H235), R294 (= R290), E300 (≠ T297), R312 (= R314), R331 (= R329)
7tdpA Structure of paenibacillus polymyxa gs bound to met-sox-p-adp (transition state complex) to 1.98 angstom (see paper)
34% identity, 99% coverage: 2:432/434 of query aligns to 5:436/439 of 7tdpA
- binding adenosine-5'-diphosphate: N123 (≠ K118), G125 (= G120), E127 (= E122), E179 (≠ Y174), D193 (≠ N188), Y196 (= Y191), N242 (≠ H237), S244 (= S239), R316 (= R319), R326 (= R325)
- binding magnesium ion: E127 (= E122), E127 (= E122), E129 (= E124), E184 (= E179), E191 (= E186), E191 (= E186), H240 (= H235), E328 (= E327)
- binding l-methionine-s-sulfoximine phosphate: E127 (= E122), E129 (= E124), E184 (= E179), E191 (= E186), G236 (= G231), H240 (= H235), R293 (= R290), E299 (≠ T297), R311 (= R314), R330 (= R329)
7tf6A Glutamine synthetase (see paper)
34% identity, 98% coverage: 2:428/434 of query aligns to 5:431/438 of 7tf6A
- binding glutamine: E128 (= E124), E183 (= E179), G235 (= G231), H239 (= H235), R292 (= R290), E298 (≠ T297)
- binding magnesium ion: E126 (= E122), E128 (= E124), E183 (= E179), E190 (= E186), H239 (= H235), E327 (= E327)
- binding : F58 (≠ D55), R60 (≠ S57), G232 (≠ D228), N234 (≠ T230), G296 (≠ A295), Y297 (≠ T296), R310 (= R314), Y367 (vs. gap), Y421 (≠ S418)
Sites not aligning to the query:
7tdvC Glutamine synthetase (see paper)
34% identity, 98% coverage: 2:428/434 of query aligns to 6:436/443 of 7tdvC
- binding adenosine-5'-diphosphate: G129 (= G120), E131 (= E122), E183 (≠ Y174), D197 (≠ N188), F198 (≠ W189), K199 (≠ T190), Y200 (= Y191), N246 (≠ H237), V247 (≠ L238), S248 (= S239), R320 (= R319), S328 (≠ A323), R330 (= R325)
- binding magnesium ion: E131 (= E122), E131 (= E122), E133 (= E124), E188 (= E179), E195 (= E186), E195 (= E186), H244 (= H235), E332 (= E327)
- binding l-methionine-s-sulfoximine phosphate: E131 (= E122), E133 (= E124), E188 (= E179), E195 (= E186), G240 (= G231), H244 (= H235), R297 (= R290), E303 (≠ T297), R315 (= R314)
8ufjB Glutamine synthetase (see paper)
34% identity, 99% coverage: 2:432/434 of query aligns to 9:441/444 of 8ufjB
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)
34% identity, 98% coverage: 2:428/434 of query aligns to 6:436/443 of 4lnkA
- active site: D52 (≠ A48), E131 (= E122), E133 (= E124), E188 (= E179), E195 (= E186), H244 (= H235), R315 (= R314), E332 (= E327), R334 (= R329)
- binding adenosine-5'-diphosphate: K43 (≠ L39), M50 (≠ G46), F198 (≠ W189), Y200 (= Y191), N246 (≠ H237), S248 (= S239), S324 (vs. gap), S328 (≠ A323), R330 (= R325)
- binding glutamic acid: E133 (= E124), E188 (= E179), V189 (≠ D180), N239 (≠ T230), G240 (= G231), G242 (= G233), E303 (≠ T297)
- binding magnesium ion: E131 (= E122), E188 (= E179), E195 (= E186), H244 (= H235), E332 (= E327)
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)
34% identity, 98% coverage: 2:428/434 of query aligns to 6:436/443 of 4lniA
- active site: D52 (≠ A48), E131 (= E122), E133 (= E124), E188 (= E179), E195 (= E186), H244 (= H235), R315 (= R314), E332 (= E327), R334 (= R329)
- binding adenosine-5'-diphosphate: E131 (= E122), E183 (≠ Y174), D197 (≠ N188), Y200 (= Y191), N246 (≠ H237), S248 (= S239), R320 (= R319), R330 (= R325)
- binding magnesium ion: E131 (= E122), E131 (= E122), E133 (= E124), E188 (= E179), E195 (= E186), E195 (= E186), H244 (= H235), E332 (= E327)
- binding l-methionine-s-sulfoximine phosphate: E133 (= E124), E188 (= E179), H244 (= H235), R297 (= R290), E303 (≠ T297), R315 (= R314), R334 (= R329)
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)
34% identity, 98% coverage: 2:428/434 of query aligns to 7:437/444 of P12425
- G59 (≠ L54) 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 (≠ S57) 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 (= E122) binding
- E134 (= E124) binding
- E189 (= E179) binding
- V190 (≠ D180) 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 (= E186) binding
- G241 (= G231) binding
- H245 (= H235) binding
- G302 (≠ A295) 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 (≠ T297) 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 (= P304) 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 (= E327) binding
- E424 (= E415) 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)
34% identity, 98% coverage: 2:428/434 of query aligns to 10:440/447 of 4s0rD
- active site: D56 (≠ A48), E135 (= E122), E137 (= E124), E192 (= E179), E199 (= E186), H248 (= H235), R319 (= R314), E336 (= E327), R338 (= R329)
- binding glutamine: E137 (= E124), E192 (= E179), R301 (= R290), E307 (≠ T297)
- binding magnesium ion: I66 (≠ P58), E135 (= E122), E135 (= E122), E199 (= E186), H248 (= H235), H248 (= H235), E336 (= E327), H419 (≠ A407)
- binding : F63 (≠ D55), V64 (≠ L56), R65 (≠ S57), I66 (≠ P58), D161 (≠ C146), G241 (≠ D228), V242 (≠ L229), N243 (≠ T230), G305 (≠ A295), Y306 (≠ T296), Y376 (= Y367), I426 (≠ Q414), M430 (≠ S418)
8oozA Glutamine synthetase (see paper)
33% identity, 98% coverage: 2:427/434 of query aligns to 4:422/430 of 8oozA
- binding adenosine-5'-triphosphate: G117 (= G120), E170 (≠ Y174), F185 (≠ W189), K186 (≠ T190), Y187 (= Y191), N233 (≠ H237), S235 (= S239), S315 (≠ A323), R317 (= R325)
- binding magnesium ion: E119 (= E122), H231 (= H235), E319 (= E327)
7tfaB Glutamine synthetase (see paper)
34% identity, 99% coverage: 2:432/434 of query aligns to 5:438/441 of 7tfaB
- binding glutamine: E131 (= E124), Y153 (≠ C146), E186 (= E179), G238 (= G231), H242 (= H235), R295 (= R290), E301 (≠ T297)
- binding magnesium ion: E129 (= E122), E131 (= E124), E186 (= E179), E193 (= E186), H242 (= H235), E330 (= E327)
- binding : Y58 (≠ D55), R60 (≠ S57), V187 (≠ D180), N237 (≠ T230), G299 (≠ A295), Y300 (≠ T296), R313 (= R314), M424 (≠ S418)
8ooxB Glutamine synthetase (see paper)
32% identity, 98% coverage: 2:427/434 of query aligns to 4:430/438 of 8ooxB
7tenA Glutamine synthetase (see paper)
33% identity, 100% coverage: 2:434/434 of query aligns to 5:441/442 of 7tenA
- binding adenosine-5'-diphosphate: G128 (= G120), E130 (= E122), E182 (≠ Y174), D196 (≠ N188), F197 (≠ W189), K198 (≠ T190), Y199 (= Y191), N245 (≠ H237), S247 (= S239), R319 (= R319), S327 (≠ A323), R329 (= R325)
- binding l-methionine-s-sulfoximine phosphate: E130 (= E122), E132 (= E124), E187 (= E179), E194 (= E186), N238 (≠ T230), G239 (= G231), H243 (= H235), R296 (= R290), E302 (≠ T297), R314 (= R314), R333 (= R329)
7tf9S L. Monocytogenes gs(14)-q-glnr peptide (see paper)
33% identity, 100% coverage: 2:434/434 of query aligns to 6:442/443 of 7tf9S
- binding glutamine: E133 (= E124), Y155 (≠ R155), E188 (= E179), G240 (= G231), G242 (= G233), R297 (= R290), E303 (≠ T297)
- binding magnesium ion: E131 (= E122), E133 (= E124), E188 (= E179), E195 (= E186), H244 (= H235), E332 (= E327)
- binding : F59 (≠ D55), V60 (≠ L56), E418 (≠ K410), I422 (≠ Q414), M426 (≠ S418)
8ooqB Glutamine synthetase from Methanothermococcus thermolithotrophicus (see paper)
32% identity, 100% coverage: 1:432/434 of query aligns to 2:444/446 of 8ooqB
- binding 2-oxoglutaric acid: F16 (≠ Y15), R18 (≠ L17), A32 (≠ L31), R86 (≠ Q78), V92 (= V81), P169 (≠ Y156), R172 (≠ I159), R173 (≠ T160), S189 (= S176)
- binding magnesium ion: E137 (= E124), E192 (= E179), E199 (= E186)
8oooA Glutamine synthetase from methanothermococcus thermolithotrophicus in complex with 2-oxoglutarate and mgatp at 2.15 a resolution (see paper)
32% identity, 100% coverage: 1:432/434 of query aligns to 3:445/447 of 8oooA
- binding 2-oxoglutaric acid: F17 (≠ Y15), R19 (≠ L17), A33 (≠ L31), R87 (≠ Q78), V93 (= V81), P170 (≠ Y156), R173 (≠ I159), R174 (≠ T160), S190 (= S176)
- binding adenosine-5'-triphosphate: E136 (= E122), E188 (≠ Y174), F203 (≠ W189), K204 (≠ T190), F205 (≠ Y191), H251 (= H237), S253 (= S239), R325 (= R319), R335 (= R325)
Query Sequence
>Synpcc7942_2296 FitnessBrowser__SynE:Synpcc7942_2296
MDSLAALARDRGIRYFLIAFTDLFGVQRAKLVPASSIDLMATSGAGFAGFAAWLDLSPAD
ADVLAIPDRDSLFQLPWQPEVAWMPADLYLNDQPLEQAPRWVLKRVLSVAESLGYRPKTG
VECEFFLLDETGDAIADPRDRQAKPCYDQQSLMRRYDLITQISEAMEELGWGPYQSDHED
ANGQFEMNWTYADALVTADRQAFFKYMVKTLAERQGLRATFMPKPFADLTGNGCHMHLSL
WNREGTTNTFVDPVATAPLSTLGYQFIGGLLHSAASLCALTNPTINSYKRINAPATTSGA
TWSPNGISYSGNNRTHLIRIPDAGRFELRLADGAANPYLLPAAAIAAGLDGIQNKRDPGP
RYDNDNYAQPLPPGTVPTLPEHLLDALRSLQESTVLTEGLGAAFTSAYLKLKHQEWRSFC
AEITPWERATTLDC
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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