SitesBLAST
Comparing 206697 FitnessBrowser__DvH:206697 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)
37% identity, 99% coverage: 5:724/726 of query aligns to 1:637/638 of 3o6xA
- binding adenosine-5'-diphosphate: E180 (= E224), E244 (= E302), F249 (≠ Y307), N295 (= N353), S297 (= S355), R388 (= R476), E390 (= E478)
- binding magnesium ion: E180 (= E224), E182 (= E226), E237 (= E295), E244 (= E302), H293 (= H351), E390 (= E478)
- binding l-methionine-s-sulfoximine phosphate: E180 (= E224), E182 (= E226), E237 (= E295), G289 (= G347), G291 (= G349), H293 (= H351), R349 (= R407), E354 (= E412), R378 (= R466)
7tf9S L. Monocytogenes gs(14)-q-glnr peptide (see paper)
31% identity, 20% coverage: 222:366/726 of query aligns to 129:259/443 of 7tf9S
Sites not aligning to the query:
7tenA Glutamine synthetase (see paper)
31% identity, 20% coverage: 222:366/726 of query aligns to 128:258/442 of 7tenA
- binding adenosine-5'-diphosphate: G128 (= G222), E130 (= E224), E182 (≠ K290), D196 (≠ A304), F197 (≠ P305), K198 (≠ I306), Y199 (= Y307), N245 (= N353), S247 (= S355)
- binding l-methionine-s-sulfoximine phosphate: E130 (= E224), E132 (= E226), E187 (= E295), E194 (= E302), N238 (= N346), G239 (= G347), H243 (= H351)
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)
25% identity, 32% coverage: 281:511/726 of query aligns to 174:362/443 of 4lnkA
- active site: E188 (= E295), E195 (= E302), H244 (= H351), R315 (≠ L454), E332 (= E478), R334 (= R480)
- binding adenosine-5'-diphosphate: F198 (≠ P305), Y200 (= Y307), N246 (= N353), S248 (= S355), S324 (≠ D463), S328 (≠ T467), R330 (= R476)
- binding glutamic acid: E188 (= E295), V189 (= V296), N239 (= N346), G240 (= G347), G242 (= G349), E303 (≠ K442)
- binding magnesium ion: E188 (= E295), E195 (= E302), H244 (= H351), E332 (= E478)
Sites not aligning to the query:
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)
25% identity, 32% coverage: 281:511/726 of query aligns to 174:362/443 of 4lniA
- active site: E188 (= E295), E195 (= E302), H244 (= H351), R315 (≠ L454), E332 (= E478), R334 (= R480)
- binding adenosine-5'-diphosphate: E183 (≠ K290), D197 (≠ A304), Y200 (= Y307), N246 (= N353), S248 (= S355), R320 (= R459), R330 (= R476)
- binding magnesium ion: E188 (= E295), E195 (= E302), E195 (= E302), H244 (= H351), E332 (= E478)
- binding l-methionine-s-sulfoximine phosphate: E188 (= E295), H244 (= H351), R297 (= R407), E303 (≠ K442), R315 (≠ L454), R334 (= R480)
Sites not aligning to the query:
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)
25% identity, 32% coverage: 281:511/726 of query aligns to 175:363/444 of P12425
- E189 (= E295) binding Mg(2+)
- V190 (= V296) 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 (= E302) binding Mg(2+)
- G241 (= G347) binding L-glutamate
- H245 (= H351) binding Mg(2+)
- G302 (= G440) 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 (≠ K442) 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 (≠ K444) 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 (= E478) 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+)
- 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)
25% identity, 32% coverage: 281:511/726 of query aligns to 178:366/447 of 4s0rD
- active site: E192 (= E295), E199 (= E302), H248 (= H351), R319 (≠ L454), E336 (= E478), R338 (= R480)
- binding glutamine: E192 (= E295), R301 (= R407), E307 (≠ K442)
- binding magnesium ion: E199 (= E302), H248 (= H351), H248 (= H351), E336 (= E478)
- binding : G241 (= G344), V242 (≠ I345), N243 (= N346), G305 (= G440), Y306 (≠ C441)
Sites not aligning to the query:
- active site: 56, 135, 137
- binding glutamine: 137
- binding magnesium ion: 66, 135, 135, 419
- binding : 63, 64, 65, 66, 161, 376, 426, 430
7tf6A Glutamine synthetase (see paper)
33% identity, 12% coverage: 281:367/726 of query aligns to 169:255/438 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)
33% identity, 12% coverage: 281:367/726 of query aligns to 174:260/443 of 7tdvC
- binding adenosine-5'-diphosphate: E183 (≠ K290), D197 (≠ A304), F198 (≠ P305), K199 (≠ I306), Y200 (= Y307), N246 (= N353), V247 (≠ Y354), S248 (= S355)
- binding magnesium ion: E188 (= E295), E195 (= E302), E195 (= E302), H244 (= H351)
- binding l-methionine-s-sulfoximine phosphate: E188 (= E295), E195 (= E302), G240 (= G347), H244 (= H351)
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
8oooA Glutamine synthetase from methanothermococcus thermolithotrophicus in complex with 2-oxoglutarate and mgatp at 2.15 a resolution (see paper)
30% identity, 19% coverage: 220:356/726 of query aligns to 132:254/447 of 8oooA
Sites not aligning to the query:
8ooqB Glutamine synthetase from Methanothermococcus thermolithotrophicus (see paper)
30% identity, 19% coverage: 220:356/726 of query aligns to 131:253/446 of 8ooqB
Sites not aligning to the query:
7tfaB Glutamine synthetase (see paper)
31% identity, 13% coverage: 277:369/726 of query aligns to 168:260/441 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)
31% identity, 13% coverage: 277:369/726 of query aligns to 166:258/439 of 7tdpA
- binding adenosine-5'-diphosphate: E179 (≠ K290), D193 (≠ A304), Y196 (= Y307), N242 (= N353), S244 (= S355)
- binding magnesium ion: E184 (= E295), E191 (= E302), E191 (= E302), H240 (= H351)
- binding l-methionine-s-sulfoximine phosphate: E184 (= E295), E191 (= E302), G236 (= G347), H240 (= H351)
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
8ooxB Glutamine synthetase (see paper)
29% identity, 24% coverage: 214:385/726 of query aligns to 117:272/438 of 8ooxB
8oozA Glutamine synthetase (see paper)
29% identity, 24% coverage: 214:385/726 of query aligns to 109:264/430 of 8oozA
Sites not aligning to the query:
8tfkA Glutamine synthetase (see paper)
27% identity, 20% coverage: 258:401/726 of query aligns to 145:291/440 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
8ufjB Glutamine synthetase (see paper)
27% identity, 20% coverage: 258:401/726 of query aligns to 149:295/444 of 8ufjB
Sites not aligning to the query:
3ng0A Crystal structure of glutamine synthetase from synechocystis sp. Pcc 6803
27% identity, 23% coverage: 193:356/726 of query aligns to 103:275/465 of 3ng0A
- active site: E130 (= E224), E132 (= E226), E213 (= E295), E221 (= E302), H270 (= H351)
- binding phosphoaminophosphonic acid-adenylate ester: Y126 (≠ F220), E130 (= E224), K209 (≠ T291), I224 (≠ P305), F226 (≠ Y307), H272 (≠ N353), S274 (= S355)
- binding manganese (ii) ion: E130 (= E224), E132 (= E226), E213 (= E295), E221 (= E302), H270 (= H351)
Sites not aligning to the query:
P0A9C5 Glutamine synthetase; GS; Glutamate--ammonia ligase; Glutamine synthetase I beta; GSI beta; EC 6.3.1.2 from Escherichia coli (strain K12) (see 3 papers)
28% identity, 23% coverage: 193:356/726 of query aligns to 103:275/469 of P0A9C5
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 398 modified: O-AMP-tyrosine
1fpyA Crystal structure of glutamine synthetase from salmonella typhimurium with inhibitor phosphinothricin (see paper)
28% identity, 23% coverage: 193:356/726 of query aligns to 102:274/468 of 1fpyA
- binding adenosine-5'-diphosphate: G127 (= G222), E129 (= E224), E207 (≠ K290), T223 (≠ P305), F225 (≠ Y307), H271 (≠ N353), S273 (= S355)
- binding manganese (ii) ion: E129 (= E224), E131 (= E226), E212 (= E295), E220 (= E302), H269 (= H351)
- binding phosphinothricin: E131 (= E226), E212 (= E295), G265 (= G347), H269 (= H351)
Sites not aligning to the query:
Query Sequence
>206697 FitnessBrowser__DvH:206697
MSGIQARLNAISAVTNYKPSTAPMNFSETKLTEFFGCNVFNEKVMRERLPKDVFKSLQKT
IELGEKLDPSIADIVANTMKDWAIEKGATHFTHVFYPLTGLTAEKHDSFLTPDGKGGALA
EFSGKMLIQGEPDASSFPSGGLRSTFEARGYTAWDVTSPAYILENPNGTFLCIPTAFLSW
TGEALDKKTPLLRSMQALNTQAKRVLKLFGIETKLPVIAFAGPEQEYFLIDRNFAFSRPD
LLIAGRSLFGARPPKGQEFEDQYFGVIPRRVLAFMMEVERELYKLGVPVKTRHNEVAPSQ
YEIAPIYETGNLATDHNQIIMTTLRSVAKRYGMLCLLHEKPFAGINGSGKHLNYSIGNAE
LGSLFDPGDTPHENAKFLVFCAAAIRALHKFGPMLRATVASASNDHRLGANEAPPAIMSM
YLGEQLTDVFEQFKQGKVNGCKQKCVMNVGVDTLPPLPRDPGDRNRTSPFAFTGNRFEFR
AVGSSMSIAGSQVALNTMMADSLDYIASELEKAIGGDASKLNEAVQSLLQKIMVEHEAII
FNGDGYSEAWHKEAERRGLPNLRTTPDALPMLTKPEVIELFTKYGVFSEAELRSREEIYL
EQYCKTVKTEANLVIRMARTIIFPAAMRYQGELATTCANLKAAGHDYQMVTLEDVTAKLR
SMQKAANELEKLLDHEAASVLEEARHMCDAILPAMNDVRKWADSLETIVADDLWSLPSYQ
EMLFIK
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