SitesBLAST
Comparing GFF1139 FitnessBrowser__Phaeo:GFF1139 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)
P78061 Gamma-glutamylputrescine synthetase PuuA; Gamma-Glu-Put synthetase; Glutamate--putrescine ligase; EC 6.3.1.11 from Escherichia coli (strain K12) (see paper)
38% identity, 96% coverage: 16:445/448 of query aligns to 38:468/472 of P78061
- H282 (= H257) mutation to N: Activity is impaired to 9% of wild-type.
- R357 (= R332) mutation to Q: Activity is impaired to 3% of wild-type.
7tfaB Glutamine synthetase (see paper)
33% identity, 93% coverage: 14:428/448 of query aligns to 15:421/441 of 7tfaB
- binding glutamine: E131 (= E140), Y153 (≠ V168), E186 (= E201), G238 (= G253), H242 (= H257), R295 (= R309), E301 (≠ H315)
- binding magnesium ion: E129 (= E138), E131 (= E140), E186 (= E201), E193 (= E208), H242 (= H257), E330 (= E344)
- binding : Y58 (≠ W59), R60 (= R61), V187 (≠ A202), N237 (≠ A252), G299 (= G313), Y300 (≠ A314), R313 (= R327)
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)
33% identity, 93% coverage: 14:428/448 of query aligns to 15:419/439 of 7tdpA
- binding adenosine-5'-diphosphate: N123 (vs. gap), G125 (≠ A136), E127 (= E138), E179 (≠ Q196), D193 (≠ N210), Y196 (≠ H213), N242 (≠ H259), S244 (= S261), R316 (= R332), R326 (= R342)
- binding magnesium ion: E127 (= E138), E127 (= E138), E129 (= E140), E184 (= E201), E191 (= E208), E191 (= E208), H240 (= H257), E328 (= E344)
- binding l-methionine-s-sulfoximine phosphate: E127 (= E138), E129 (= E140), E184 (= E201), E191 (= E208), G236 (= G253), H240 (= H257), R293 (= R309), E299 (≠ H315), R311 (= R327), R330 (= R346)
8ooxB Glutamine synthetase (see paper)
30% identity, 92% coverage: 13:422/448 of query aligns to 13:412/438 of 8ooxB
8oozA Glutamine synthetase (see paper)
30% identity, 92% coverage: 13:422/448 of query aligns to 13:404/430 of 8oozA
- binding adenosine-5'-triphosphate: G117 (≠ A136), E170 (≠ Q196), F185 (≠ L211), K186 (≠ N212), Y187 (≠ H213), N233 (≠ H259), S235 (= S261), S315 (≠ A340), R317 (= R342)
- binding magnesium ion: E119 (= E138), H231 (= H257), E319 (= E344)
8oooA Glutamine synthetase from methanothermococcus thermolithotrophicus in complex with 2-oxoglutarate and mgatp at 2.15 a resolution (see paper)
30% identity, 85% coverage: 61:441/448 of query aligns to 47:439/447 of 8oooA
- binding 2-oxoglutaric acid: R87 (vs. gap), V93 (vs. gap), P170 (≠ A172), R173 (≠ D175), R174 (≠ T182), S190 (≠ A198)
- binding adenosine-5'-triphosphate: E136 (= E138), E188 (≠ Q196), F203 (≠ L211), K204 (≠ N212), F205 (≠ H213), H251 (= H259), S253 (= S261), R325 (= R332), R335 (= R342)
Sites not aligning to the query:
7tenA Glutamine synthetase (see paper)
29% identity, 94% coverage: 11:432/448 of query aligns to 12:426/442 of 7tenA
- binding adenosine-5'-diphosphate: G128 (≠ A136), E130 (= E138), E182 (≠ Q196), D196 (≠ N210), F197 (≠ L211), K198 (≠ N212), Y199 (≠ H213), N245 (≠ H259), S247 (= S261), R319 (= R332), S327 (≠ A340), R329 (= R342)
- binding l-methionine-s-sulfoximine phosphate: E130 (= E138), E132 (= E140), E187 (= E201), E194 (= E208), N238 (≠ A252), G239 (= G253), H243 (= H257), R296 (= R309), E302 (≠ H315), R314 (= R327), R333 (= R346)
7tf9S L. Monocytogenes gs(14)-q-glnr peptide (see paper)
29% identity, 94% coverage: 11:432/448 of query aligns to 13:427/443 of 7tf9S
- binding glutamine: E133 (= E140), Y155 (≠ V168), E188 (= E201), G240 (= G253), G242 (= G255), R297 (= R309), E303 (≠ H315)
- binding magnesium ion: E131 (= E138), E133 (= E140), E188 (= E201), E195 (= E208), H244 (= H257), E332 (= E344)
- binding : F59 (≠ V69), V60 (≠ F70), E418 (≠ M423), I422 (≠ Q427), M426 (≠ G431)
8ooqB Glutamine synthetase from Methanothermococcus thermolithotrophicus (see paper)
30% identity, 85% coverage: 61:441/448 of query aligns to 46:438/446 of 8ooqB
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)
29% identity, 96% coverage: 1:428/448 of query aligns to 1:424/444 of P12425
- M1 (= M1) modified: Initiator methionine, Removed
- G59 (≠ D65) 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 (≠ E71) 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 (= E138) binding
- E134 (= E140) binding
- E189 (= E201) binding
- V190 (≠ A202) 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 (= E208) binding
- G241 (= G253) binding
- H245 (= H257) binding
- G302 (= G313) 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 (≠ H315) 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 (= P317) 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 (= E344) binding
- E424 (= E428) 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.
4s0rD Structure of gs-tnra complex (see paper)
29% identity, 96% coverage: 1:428/448 of query aligns to 4:427/447 of 4s0rD
- active site: D56 (≠ W59), E135 (= E138), E137 (= E140), E192 (= E201), E199 (= E208), H248 (= H257), R319 (= R327), E336 (= E344), R338 (= R346)
- binding glutamine: E137 (= E140), E192 (= E201), R301 (= R309), E307 (≠ H315)
- binding magnesium ion: I66 (≠ T72), E135 (= E138), E135 (= E138), E199 (= E208), H248 (= H257), H248 (= H257), E336 (= E344), H419 (≠ N420)
- binding : F63 (≠ V69), V64 (≠ F70), R65 (≠ E71), I66 (≠ T72), D161 (≠ S170), G241 (≠ E250), V242 (≠ E251), N243 (≠ A252), G305 (= G313), Y306 (≠ A314), Y376 (= Y384), I426 (≠ Q427)
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)
29% identity, 93% coverage: 14:428/448 of query aligns to 16:423/443 of 4lnkA
- active site: D52 (≠ W59), E131 (= E138), E133 (= E140), E188 (= E201), E195 (= E208), H244 (= H257), R315 (= R327), E332 (= E344), R334 (= R346)
- binding adenosine-5'-diphosphate: K43 (= K41), M50 (≠ D57), F198 (≠ L211), Y200 (≠ H213), N246 (≠ H259), S248 (= S261), S324 (≠ G336), S328 (≠ A340), R330 (= R342)
- binding glutamic acid: E133 (= E140), E188 (= E201), V189 (≠ A202), N239 (≠ A252), G240 (= G253), G242 (= G255), E303 (≠ H315)
- binding magnesium ion: E131 (= E138), E188 (= E201), E195 (= E208), H244 (= H257), E332 (= E344)
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)
29% identity, 93% coverage: 14:428/448 of query aligns to 16:423/443 of 4lniA
- active site: D52 (≠ W59), E131 (= E138), E133 (= E140), E188 (= E201), E195 (= E208), H244 (= H257), R315 (= R327), E332 (= E344), R334 (= R346)
- binding adenosine-5'-diphosphate: E131 (= E138), E183 (≠ Q196), D197 (≠ N210), Y200 (≠ H213), N246 (≠ H259), S248 (= S261), R320 (= R332), R330 (= R342)
- binding magnesium ion: E131 (= E138), E131 (= E138), E133 (= E140), E188 (= E201), E195 (= E208), E195 (= E208), H244 (= H257), E332 (= E344)
- binding l-methionine-s-sulfoximine phosphate: E133 (= E140), E188 (= E201), H244 (= H257), R297 (= R309), E303 (≠ H315), R315 (= R327), R334 (= R346)
8tfkA Glutamine synthetase (see paper)
32% identity, 76% coverage: 89:428/448 of query aligns to 77:420/440 of 8tfkA
- binding adenosine-5'-diphosphate: E128 (= E138), D194 (≠ N210), F195 (≠ L211), F197 (≠ H213), N243 (≠ H259), R312 (= R327), R317 (= R332), G325 (≠ A340), R327 (= R342)
- binding magnesium ion: E128 (= E138), E128 (= E138), E130 (= E140), E185 (= E201), E192 (= E208), E192 (= E208), H241 (= H257), E329 (= E344)
- binding l-methionine-s-sulfoximine phosphate: E128 (= E138), E130 (= E140), E185 (= E201), E192 (= E208), G237 (= G253), H241 (= H257), R294 (= R309), E300 (≠ H315), R312 (= R327), R331 (= R346)
8ufjB Glutamine synthetase (see paper)
32% identity, 76% coverage: 89:428/448 of query aligns to 81:424/444 of 8ufjB
7tdvC Glutamine synthetase (see paper)
28% identity, 96% coverage: 14:441/448 of query aligns to 16:434/443 of 7tdvC
- binding adenosine-5'-diphosphate: G129 (≠ A136), E131 (= E138), E183 (≠ Q196), D197 (≠ N210), F198 (≠ L211), K199 (≠ N212), Y200 (≠ H213), N246 (≠ H259), V247 (≠ F260), S248 (= S261), R320 (= R332), S328 (≠ A340), R330 (= R342)
- binding magnesium ion: E131 (= E138), E131 (= E138), E133 (= E140), E188 (= E201), E195 (= E208), E195 (= E208), H244 (= H257), E332 (= E344)
- binding l-methionine-s-sulfoximine phosphate: E131 (= E138), E133 (= E140), E188 (= E201), E195 (= E208), G240 (= G253), H244 (= H257), R297 (= R309), E303 (≠ H315), R315 (= R327)
7tf6A Glutamine synthetase (see paper)
29% identity, 96% coverage: 14:441/448 of query aligns to 15:429/438 of 7tf6A
- binding glutamine: E128 (= E140), E183 (= E201), G235 (= G253), H239 (= H257), R292 (= R309), E298 (≠ H315)
- binding magnesium ion: E126 (= E138), E128 (= E140), E183 (= E201), E190 (= E208), H239 (= H257), E327 (= E344)
- binding : F58 (≠ V69), R60 (≠ E71), G232 (≠ E250), N234 (≠ A252), G296 (= G313), Y297 (≠ A314), R310 (= R327), Y367 (= Y384), Y421 (≠ G431)
Sites not aligning to the query:
A0R083 Glutamine synthetase; GS; Glutamate--ammonia ligase; Glutamine synthetase I alpha; GSI alpha; EC 6.3.1.2 from Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis) (see paper)
30% identity, 93% coverage: 15:432/448 of query aligns to 17:431/446 of A0R083
- K363 (≠ D371) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
P9WN37 Glutamine synthetase; GS; Glutamate--ammonia ligase; Glutamine synthetase I alpha; GSI alpha; EC 6.3.1.2 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see paper)
28% identity, 81% coverage: 72:432/448 of query aligns to 62:431/446 of P9WN37
- K363 (≠ D371) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
7cqwA Gmas/adp complex-conformation 1 (see paper)
33% identity, 79% coverage: 20:375/448 of query aligns to 18:356/430 of 7cqwA
Query Sequence
>GFF1139 FitnessBrowser__Phaeo:GFF1139
MGQSTKEPPMDLSHLRTIRIAACDLNGQMRGKRMPVGLADKLADGAARMPISTLNVDLWG
RDVEDNPLVFETGDADGVMLPTERGAVPMPWLANPSALVPMAMYWEDGRPFMGDPRHVLA
DVLARYQQRGWRVVAATEMEFSLLDDSGAQPAPPIDPLTGRELDQQSVLSVAELDAFDAF
FTDLYEGSDAMGIPAQSAISEAGLGQFEINLNHQEAMRAADDAWLFKALVKGLARKHGFA
ATFMAKPYAEEAGNGMHVHFSVEDEDGNNVFNDGTERGSGLLMNAVAGCLTAMPASTLIL
APHGNSYDRLVPGAHAPVSAAWAYENRTAAIRIPGGSPKARRIEHRVAGGDINPYLMLAV
VLGAALAGIEDGATPPAPSEGNIYEIDGLPQLAPDWKAAIDLFDSDPLIARILPDRVIRN
LVMMKRQEQAGFAERPAESHWLSWLEAV
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