SitesBLAST
Comparing 8500852 FitnessBrowser__Miya:8500852 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)
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 (= F307), 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)
7tenA Glutamine synthetase (see paper)
28% identity, 25% coverage: 222:401/726 of query aligns to 128:293/442 of 7tenA
- binding adenosine-5'-diphosphate: G128 (= G222), E130 (= E224), E182 (≠ K290), D196 (≠ A304), F197 (≠ P305), K198 (≠ I306), Y199 (≠ F307), 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:
7tf9S L. Monocytogenes gs(14)-q-glnr peptide (see paper)
28% identity, 25% coverage: 222:401/726 of query aligns to 129:294/443 of 7tf9S
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 (≠ F307), 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 (≠ F307), N246 (= N353), S248 (= S355), R320 (≠ M459), 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
- 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
- G241 (= G347) binding
- H245 (= H351) binding
- 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 (≠ A444) 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
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
- 134 binding
- 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
7tdvC Glutamine synthetase (see paper)
28% identity, 17% coverage: 281:401/726 of query aligns to 174:294/443 of 7tdvC
- binding adenosine-5'-diphosphate: E183 (≠ K290), D197 (≠ A304), F198 (≠ P305), K199 (≠ I306), Y200 (≠ F307), 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
7tf6A Glutamine synthetase (see paper)
28% identity, 17% coverage: 281:401/726 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
8ooqB Glutamine synthetase from Methanothermococcus thermolithotrophicus (see paper)
24% identity, 40% coverage: 220:511/726 of query aligns to 131:366/446 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: 220:511/726 of query aligns to 132:367/447 of 8oooA
- binding 2-oxoglutaric acid: P170 (vs. gap), R173 (= R269), R174 (= R270), S190 (≠ R292)
- binding adenosine-5'-triphosphate: E136 (= E224), E188 (≠ K290), F203 (≠ P305), K204 (≠ I306), F205 (= F307), H251 (≠ N353), S253 (= S355), R325 (≠ M447), R335 (= R476)
Sites not aligning to the query:
8ooxB Glutamine synthetase (see paper)
25% identity, 26% coverage: 214:401/726 of query aligns to 117:289/438 of 8ooxB
8oozA Glutamine synthetase (see paper)
25% identity, 26% coverage: 214:401/726 of query aligns to 109:281/430 of 8oozA
Sites not aligning to the query:
7tfaB Glutamine synthetase (see paper)
25% identity, 25% coverage: 222:401/726 of query aligns to 127:292/441 of 7tfaB
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)
25% identity, 25% coverage: 222:401/726 of query aligns to 125:290/439 of 7tdpA
- binding adenosine-5'-diphosphate: G125 (= G222), E127 (= E224), E179 (≠ K290), D193 (≠ A304), Y196 (≠ F307), N242 (= N353), S244 (= S355)
- binding magnesium ion: E127 (= E224), E127 (= E224), E129 (= E226), E184 (= E295), E191 (= E302), E191 (= E302), H240 (= H351)
- binding l-methionine-s-sulfoximine phosphate: E127 (= E224), E129 (= E226), E184 (= E295), E191 (= E302), G236 (= G347), H240 (= H351)
Sites not aligning to the query:
8tfkA Glutamine synthetase (see paper)
25% identity, 25% coverage: 222:401/726 of query aligns to 126:291/440 of 8tfkA
- binding adenosine-5'-diphosphate: E128 (= E224), D194 (≠ A304), F195 (≠ P305), F197 (= F307), N243 (= N353)
- binding magnesium ion: E128 (= E224), E128 (= E224), E130 (= E226), E185 (= E295), E192 (= E302), E192 (= E302), H241 (= H351)
- binding l-methionine-s-sulfoximine phosphate: E128 (= E224), E130 (= E226), E185 (= E295), E192 (= E302), G237 (= G347), H241 (= H351)
Sites not aligning to the query:
8ufjB Glutamine synthetase (see paper)
26% identity, 25% coverage: 222:401/726 of query aligns to 130:295/444 of 8ufjB
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)
26% identity, 29% coverage: 193:401/726 of query aligns to 103:319/469 of P0A9C5
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 398 modified: O-AMP-tyrosine
P0A1P6 Glutamine synthetase; GS; Glutamate--ammonia ligase; Glutamine synthetase I beta; GSI beta; EC 6.3.1.2 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) (see 4 papers)
27% identity, 29% coverage: 193:401/726 of query aligns to 103:319/469 of P0A1P6
Sites not aligning to the query:
- 322 binding
- 358 binding
- 360 binding
1fpyA Crystal structure of glutamine synthetase from salmonella typhimurium with inhibitor phosphinothricin (see paper)
27% identity, 29% coverage: 193:401/726 of query aligns to 102:318/468 of 1fpyA
- binding adenosine-5'-diphosphate: G127 (= G222), E129 (= E224), E207 (≠ K290), T223 (≠ P305), F225 (= F307), 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
>8500852 FitnessBrowser__Miya:8500852
MSGIQARLNAISAITNYKPSAAPMNFAETKPTELFGCNVFNDKVMKDRLPKTVYKSLKKT
IELGEKLDPSIADVVANAMKDWAIEKGATHFTHVFYPLTGLTAEKHDAFLVPDGKGGALS
EFSGKLLIQGEPDASSFPSGGLRATFEARGYTAWDVTSPAYLLENPNGTFLCIPTAFVSW
TGEALDKKTPLLRANQALNKQAQRVLKLFGTETKLPLVSYAGPEQEYFLIDRNFAFARPD
LHICGRSLFGAKPAKGQEFEDQYFGVIPRRVLSFMMEVERELFKLGVPVKTRHNEVAPSQ
YEIAPIFETSNLATDHNQLIMTVLRSVAKRYGMVCLLHEKPFAGINGSGKHLNYSIGNAD
LGSLFDPGESPHENAQFLVFCAAAIRAVHKYGALLRATVASASNDHRLGANEAPPAIMSV
YLGEQLTDVFEQIKTGKVNGCKKACVMNIGVDVLPPLPMDPGDRNRTSPFAFTGNRFEFR
AVGSSMSIAGPQVALNTMMAESLDYIATELEKATKGDPAKLNEAVQKLLQKIMKEHDKVI
FNGDGYSEEWHKEAERRGLPNLKTTPDALPVLSSPEVVKLFTSYGVFSEAEVKSREEIYL
EQYCKTVKTEANLVIRMARTIIFPAAMRYQGELAATCANLKAAGHDYKVVTLEDVTTKLR
AMQAAVGELEKKLDHEAASTHAEAKHMCDVILPAMLKVREYADALEAVVADDLWALPSYQ
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