SitesBLAST
Comparing WP_011389007.1 NCBI__GCF_000013085.1:WP_011389007.1 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)
34% identity, 96% coverage: 17:447/450 of query aligns to 40:469/472 of P78061
- H282 (= H259) mutation to N: Activity is impaired to 9% of wild-type.
- R357 (= R335) mutation to Q: Activity is impaired to 3% of wild-type.
8ufjB Glutamine synthetase (see paper)
30% identity, 98% coverage: 9:447/450 of query aligns to 14:441/444 of 8ufjB
8tfkA Glutamine synthetase (see paper)
30% identity, 98% coverage: 9:447/450 of query aligns to 10:437/440 of 8tfkA
- binding adenosine-5'-diphosphate: E128 (= E138), D194 (≠ N212), F195 (= F213), F197 (≠ H215), N243 (≠ H261), R312 (= R330), R317 (= R335), G325 (≠ N343), R327 (= R345)
- binding magnesium ion: E128 (= E138), E128 (= E138), E130 (= E140), E185 (= E203), E192 (= E210), E192 (= E210), H241 (= H259), E329 (= E347)
- binding l-methionine-s-sulfoximine phosphate: E128 (= E138), E130 (= E140), E185 (= E203), E192 (= E210), G237 (= G255), H241 (= H259), R294 (= R312), E300 (≠ S318), R312 (= R330), R331 (= R349)
7tenA Glutamine synthetase (see paper)
32% identity, 98% coverage: 8:447/450 of query aligns to 10:439/442 of 7tenA
- binding adenosine-5'-diphosphate: G128 (≠ A136), E130 (= E138), E182 (≠ D198), D196 (≠ N212), F197 (= F213), K198 (≠ L214), Y199 (≠ H215), N245 (≠ H261), S247 (= S263), R319 (= R335), S327 (≠ N343), R329 (= R345)
- binding l-methionine-s-sulfoximine phosphate: E130 (= E138), E132 (= E140), E187 (= E203), E194 (= E210), N238 (≠ P254), G239 (= G255), H243 (= H259), R296 (= R312), E302 (≠ S318), R314 (= R330), R333 (= R349)
7tf9S L. Monocytogenes gs(14)-q-glnr peptide (see paper)
32% identity, 98% coverage: 8:447/450 of query aligns to 11:440/443 of 7tf9S
- binding glutamine: E133 (= E140), Y155 (≠ R160), E188 (= E203), G240 (= G255), G242 (≠ A257), R297 (= R312), E303 (≠ S318)
- binding magnesium ion: E131 (= E138), E133 (= E140), E188 (= E203), E195 (= E210), H244 (= H259), E332 (= E347)
- binding : F59 (≠ N69), V60 (≠ T70), E418 (≠ M425), I422 (≠ V429), M426 (≠ A433)
8oooA Glutamine synthetase from methanothermococcus thermolithotrophicus in complex with 2-oxoglutarate and mgatp at 2.15 a resolution (see paper)
32% identity, 83% coverage: 74:447/450 of query aligns to 69:445/447 of 8oooA
- binding 2-oxoglutaric acid: R87 (vs. gap), V93 (≠ T96), P170 (≠ E180), R173 (≠ I183), R174 (≠ E184), S190 (≠ L200)
- binding adenosine-5'-triphosphate: E136 (= E138), E188 (≠ D198), F203 (= F213), K204 (≠ L214), F205 (≠ H215), H251 (= H261), S253 (= S263), R325 (= R335), R335 (= R345)
Sites not aligning to the query:
8ooqB Glutamine synthetase from Methanothermococcus thermolithotrophicus (see paper)
32% identity, 83% coverage: 74:447/450 of query aligns to 68:444/446 of 8ooqB
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)
29% identity, 97% coverage: 11:447/450 of query aligns to 13:436/439 of 7tdpA
- binding adenosine-5'-diphosphate: N123 (vs. gap), G125 (≠ A136), E127 (= E138), E179 (≠ D198), D193 (≠ N212), Y196 (≠ H215), N242 (≠ H261), S244 (= S263), R316 (= R335), R326 (= R345)
- binding magnesium ion: E127 (= E138), E127 (= E138), E129 (= E140), E184 (= E203), E191 (= E210), E191 (= E210), H240 (= H259), E328 (= E347)
- binding l-methionine-s-sulfoximine phosphate: E127 (= E138), E129 (= E140), E184 (= E203), E191 (= E210), G236 (= G255), H240 (= H259), R293 (= R312), E299 (≠ S318), R311 (= R330), R330 (= R349)
7tfaB Glutamine synthetase (see paper)
29% identity, 97% coverage: 11:447/450 of query aligns to 13:438/441 of 7tfaB
- binding glutamine: E131 (= E140), Y153 (≠ R163), E186 (= E203), G238 (= G255), H242 (= H259), R295 (= R312), E301 (≠ S318)
- binding magnesium ion: E129 (= E138), E131 (= E140), E186 (= E203), E193 (= E210), H242 (= H259), E330 (= E347)
- binding : Y58 (≠ N69), R60 (≠ V71), V187 (≠ A204), N237 (≠ P254), G299 (≠ H316), Y300 (≠ H317), R313 (= R330), M424 (≠ A433)
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)
28% identity, 99% coverage: 4:447/450 of query aligns to 7:440/443 of 4lnkA
- active site: D52 (≠ I49), E131 (= E138), E133 (= E140), E188 (= E203), E195 (= E210), H244 (= H259), R315 (= R330), E332 (= E347), R334 (= R349)
- binding adenosine-5'-diphosphate: K43 (≠ R40), M50 (≠ L47), F198 (= F213), Y200 (≠ H215), N246 (≠ H261), S248 (= S263), S324 (= S339), S328 (≠ N343), R330 (= R345)
- binding glutamic acid: E133 (= E140), E188 (= E203), V189 (≠ A204), N239 (≠ P254), G240 (= G255), G242 (≠ A257), E303 (≠ S318)
- binding magnesium ion: E131 (= E138), E188 (= E203), E195 (= E210), H244 (= H259), E332 (= E347)
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)
28% identity, 99% coverage: 4:447/450 of query aligns to 7:440/443 of 4lniA
- active site: D52 (≠ I49), E131 (= E138), E133 (= E140), E188 (= E203), E195 (= E210), H244 (= H259), R315 (= R330), E332 (= E347), R334 (= R349)
- binding adenosine-5'-diphosphate: E131 (= E138), E183 (≠ D198), D197 (≠ N212), Y200 (≠ H215), N246 (≠ H261), S248 (= S263), R320 (= R335), R330 (= R345)
- binding magnesium ion: E131 (= E138), E131 (= E138), E133 (= E140), E188 (= E203), E195 (= E210), E195 (= E210), H244 (= H259), E332 (= E347)
- binding l-methionine-s-sulfoximine phosphate: E133 (= E140), E188 (= E203), H244 (= H259), R297 (= R312), E303 (≠ S318), R315 (= R330), R334 (= R349)
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)
28% identity, 99% coverage: 4:447/450 of query aligns to 8:441/444 of P12425
- G59 (≠ N68) 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 (≠ V71) 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 Mg(2+)
- E134 (= E140) binding Mg(2+)
- E189 (= E203) binding Mg(2+)
- V190 (≠ A204) 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 (= E210) binding Mg(2+)
- G241 (= G255) binding L-glutamate
- H245 (= H259) binding Mg(2+)
- G302 (≠ H316) 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 (≠ S318) 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 (= P320) 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 (= E347) binding Mg(2+)
- E424 (= E430) 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)
28% identity, 99% coverage: 4:447/450 of query aligns to 11:444/447 of 4s0rD
- active site: D56 (≠ I49), E135 (= E138), E137 (= E140), E192 (= E203), E199 (= E210), H248 (= H259), R319 (= R330), E336 (= E347), R338 (= R349)
- binding glutamine: E137 (= E140), E192 (= E203), R301 (= R312), E307 (≠ S318)
- binding magnesium ion: I66 (≠ V72), E135 (= E138), E135 (= E138), E199 (= E210), H248 (= H259), H248 (= H259), E336 (= E347), H419 (≠ A422)
- binding : F63 (≠ N69), V64 (≠ T70), R65 (≠ V71), I66 (≠ V72), D161 (≠ E165), G241 (≠ D252), V242 (≠ Q253), N243 (≠ P254), G305 (≠ H316), Y306 (≠ H317), Y376 (= Y388), I426 (≠ V429), M430 (≠ A433)
8oozA Glutamine synthetase (see paper)
31% identity, 83% coverage: 76:447/450 of query aligns to 58:427/430 of 8oozA
- binding adenosine-5'-triphosphate: G117 (≠ A136), E170 (≠ D198), F185 (= F213), K186 (≠ L214), Y187 (≠ H215), N233 (≠ H261), S235 (= S263), S315 (≠ N343), R317 (= R345)
- binding magnesium ion: E119 (= E138), H231 (= H259), E319 (= E347)
8ooxB Glutamine synthetase (see paper)
31% identity, 83% coverage: 74:447/450 of query aligns to 62:435/438 of 8ooxB
8wwvA Glutamine synthetase
29% identity, 95% coverage: 9:437/450 of query aligns to 24:466/490 of 8wwvA
- binding adenosine-5'-diphosphate: G155 (≠ A136), E157 (= E138), R224 (vs. gap), F239 (= F213), D240 (≠ L214), V241 (≠ H215), H288 (= H261), S290 (= S263), R374 (= R345), E376 (= E347)
- binding magnesium ion: E157 (= E138), E236 (= E210)
- binding manganese (ii) ion: E157 (= E138), E159 (= E140), E229 (= E203), E236 (= E210), H286 (= H259), E376 (= E347)
- binding l-methionine-s-sulfoximine phosphate: E157 (= E138), E159 (= E140), E229 (= E203), E236 (= E210), A282 (≠ G255), H286 (= H259), R340 (= R312), K358 (≠ R330)
8wwuB Glutamine synthetase
29% identity, 95% coverage: 9:437/450 of query aligns to 26:468/492 of 8wwuB
- binding phosphoaminophosphonic acid-adenylate ester: G157 (≠ A136), E159 (= E138), R226 (vs. gap), F241 (= F213), V243 (≠ H215), H290 (= H261), S292 (= S263), K360 (≠ R330), R365 (= R335), R376 (= R345)
- binding magnesium ion: E159 (= E138), E238 (= E210)
- binding manganese (ii) ion: E159 (= E138), E161 (= E140), E231 (= E203), E238 (= E210), H288 (= H259), E378 (= E347)
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)
32% identity, 84% coverage: 72:448/450 of query aligns to 62:446/446 of A0R083
- K363 (≠ E374) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
7tdvC Glutamine synthetase (see paper)
28% identity, 98% coverage: 8:447/450 of query aligns to 11:440/443 of 7tdvC
- binding adenosine-5'-diphosphate: G129 (≠ A136), E131 (= E138), E183 (≠ D198), D197 (≠ N212), F198 (= F213), K199 (≠ L214), Y200 (≠ H215), N246 (≠ H261), V247 (≠ Q262), S248 (= S263), R320 (= R335), S328 (≠ N343), R330 (= R345)
- binding magnesium ion: E131 (= E138), E131 (= E138), E133 (= E140), E188 (= E203), E195 (= E210), E195 (= E210), H244 (= H259), E332 (= E347)
- binding l-methionine-s-sulfoximine phosphate: E131 (= E138), E133 (= E140), E188 (= E203), E195 (= E210), G240 (= G255), H244 (= H259), R297 (= R312), E303 (≠ S318), R315 (= R330)
7tf6A Glutamine synthetase (see paper)
28% identity, 97% coverage: 11:447/450 of query aligns to 13:435/438 of 7tf6A
- binding glutamine: E128 (= E140), E183 (= E203), G235 (= G255), H239 (= H259), R292 (= R312), E298 (≠ S318)
- binding magnesium ion: E126 (= E138), E128 (= E140), E183 (= E203), E190 (= E210), H239 (= H259), E327 (= E347)
- binding : F58 (≠ N69), R60 (≠ V71), G232 (≠ D252), N234 (≠ P254), G296 (≠ H316), Y297 (≠ H317), R310 (= R330), Y367 (= Y388), Y421 (≠ A433), Q433 (≠ H445)
Sites not aligning to the query:
Query Sequence
>WP_011389007.1 NCBI__GCF_000013085.1:WP_011389007.1
MINEFEAWINEHGIAEVECLLSDMNGIVRGKVLPARKFLRSLEDNSLRIPSSVFLVTVTG
EYPFADDNNTVVIDPDADLRPDFRTLCVAPGYRTPTAFVVVDAYKSNGIPLDLSPRQVLK
RVLALYSEQGWKPVVAPEIEFYLTQVNADPDLPLSPPAGRSGRPETSPQPYGLEAITEFE
DLIENIYEHAEIAGLQIDTLIHEAGAAQLEINFLHGDPITLSDQVVVFKRLVRQVALKHG
VYATFMAKPMADQPGSAMHIHQSLVEIGTGKNLFVRDDGSDSPMFRHYIGGLQALLAQVT
PLFAPNINSFRRMRPHHSAPINLECGYDNRSCGLRVPLSDPANRRLENRLPGADANPYLA
MAASLACGYIGIMERIEPSIMVEGGNAYRRSRTLPRTLDEALDRLEKCTVIKNVLGEHFF
EAFTMIKRVELDAFQDVISSWERNHLLLKV
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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