SitesBLAST
Comparing WP_013840878.1 NCBI__GCF_000215085.1:WP_013840878.1 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)
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)
64% identity, 100% coverage: 1:444/444 of query aligns to 1:444/444 of P12425
- M1 (= M1) modified: Initiator methionine, Removed
- G59 (= G59) 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 (= R62) 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 (= E131) binding Mg(2+)
- E134 (= E133) binding Mg(2+)
- E189 (= E188) binding Mg(2+)
- V190 (= V189) 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 (= E195) binding Mg(2+)
- G241 (= G240) binding L-glutamate
- H245 (= H244) binding Mg(2+)
- G302 (= G302) 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 (= E304) 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 (= P306) 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 (= E333) binding Mg(2+)
- E424 (= E424) 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)
64% identity, 100% coverage: 1:444/444 of query aligns to 4:447/447 of 4s0rD
- active site: D56 (= D53), E135 (= E131), E137 (= E133), E192 (= E188), E199 (= E195), H248 (= H244), R319 (= R316), E336 (= E333), R338 (= R335)
- binding glutamine: E137 (= E133), E192 (= E188), R301 (= R298), E307 (= E304)
- binding magnesium ion: I66 (= I63), E135 (= E131), E135 (= E131), E199 (= E195), H248 (= H244), H248 (= H244), E336 (= E333), H419 (≠ R416)
- binding : F63 (= F60), V64 (= V61), R65 (= R62), I66 (= I63), D161 (= D157), G241 (= G237), V242 (≠ I238), N243 (= N239), G305 (= G302), Y306 (= Y303), Y376 (= Y373), I426 (= I423), M430 (≠ R427)
7tdpA Structure of paenibacillus polymyxa gs bound to met-sox-p-adp (transition state complex) to 1.98 angstom (see paper)
66% identity, 98% coverage: 5:441/444 of query aligns to 3:436/439 of 7tdpA
- binding adenosine-5'-diphosphate: N123 (= N127), G125 (= G129), E127 (= E131), E179 (= E183), D193 (= D197), Y196 (= Y200), N242 (= N246), S244 (= S248), R316 (= R321), R326 (= R331)
- binding magnesium ion: E127 (= E131), E127 (= E131), E129 (= E133), E184 (= E188), E191 (= E195), E191 (= E195), H240 (= H244), E328 (= E333)
- binding l-methionine-s-sulfoximine phosphate: E127 (= E131), E129 (= E133), E184 (= E188), E191 (= E195), G236 (= G240), H240 (= H244), R293 (= R298), E299 (= E304), R311 (= R316), R330 (= R335)
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)
64% identity, 100% coverage: 3:444/444 of query aligns to 2:443/443 of 4lnkA
- active site: D52 (= D53), E131 (= E131), E133 (= E133), E188 (= E188), E195 (= E195), H244 (= H244), R315 (= R316), E332 (= E333), R334 (= R335)
- binding adenosine-5'-diphosphate: K43 (= K44), M50 (= M51), F198 (= F198), Y200 (= Y200), N246 (= N246), S248 (= S248), S324 (≠ K325), S328 (= S329), R330 (= R331)
- binding glutamic acid: E133 (= E133), E188 (= E188), V189 (= V189), N239 (= N239), G240 (= G240), G242 (= G242), E303 (= E304)
- binding magnesium ion: E131 (= E131), E188 (= E188), E195 (= E195), H244 (= H244), E332 (= E333)
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)
64% identity, 100% coverage: 3:444/444 of query aligns to 2:443/443 of 4lniA
- active site: D52 (= D53), E131 (= E131), E133 (= E133), E188 (= E188), E195 (= E195), H244 (= H244), R315 (= R316), E332 (= E333), R334 (= R335)
- binding adenosine-5'-diphosphate: E131 (= E131), E183 (= E183), D197 (= D197), Y200 (= Y200), N246 (= N246), S248 (= S248), R320 (= R321), R330 (= R331)
- binding magnesium ion: E131 (= E131), E131 (= E131), E133 (= E133), E188 (= E188), E195 (= E195), E195 (= E195), H244 (= H244), E332 (= E333)
- binding l-methionine-s-sulfoximine phosphate: E133 (= E133), E188 (= E188), H244 (= H244), R297 (= R298), E303 (= E304), R315 (= R316), R334 (= R335)
7tfaB Glutamine synthetase (see paper)
66% identity, 98% coverage: 5:441/444 of query aligns to 3:438/441 of 7tfaB
- binding glutamine: E131 (= E133), Y153 (= Y155), E186 (= E188), G238 (= G240), H242 (= H244), R295 (= R298), E301 (= E304)
- binding magnesium ion: E129 (= E131), E131 (= E133), E186 (= E188), E193 (= E195), H242 (= H244), E330 (= E333)
- binding : Y58 (≠ F60), R60 (= R62), V187 (= V189), N237 (= N239), G299 (= G302), Y300 (= Y303), R313 (= R316), M424 (≠ R427)
7tdvC Glutamine synthetase (see paper)
62% identity, 99% coverage: 4:444/444 of query aligns to 3:443/443 of 7tdvC
- binding adenosine-5'-diphosphate: G129 (= G129), E131 (= E131), E183 (= E183), D197 (= D197), F198 (= F198), K199 (= K199), Y200 (= Y200), N246 (= N246), V247 (≠ Q247), S248 (= S248), R320 (= R321), S328 (= S329), R330 (= R331)
- binding magnesium ion: E131 (= E131), E131 (= E131), E133 (= E133), E188 (= E188), E195 (= E195), E195 (= E195), H244 (= H244), E332 (= E333)
- binding l-methionine-s-sulfoximine phosphate: E131 (= E131), E133 (= E133), E188 (= E188), E195 (= E195), G240 (= G240), H244 (= H244), R297 (= R298), E303 (= E304), R315 (= R316)
7tf9S L. Monocytogenes gs(14)-q-glnr peptide (see paper)
63% identity, 100% coverage: 3:444/444 of query aligns to 2:443/443 of 7tf9S
- binding glutamine: E133 (= E133), Y155 (= Y155), E188 (= E188), G240 (= G240), G242 (= G242), R297 (= R298), E303 (= E304)
- binding magnesium ion: E131 (= E131), E133 (= E133), E188 (= E188), E195 (= E195), H244 (= H244), E332 (= E333)
- binding : F59 (= F60), V60 (= V61), E418 (= E419), I422 (= I423), M426 (≠ R427)
7tenA Glutamine synthetase (see paper)
63% identity, 100% coverage: 3:444/444 of query aligns to 1:442/442 of 7tenA
- binding adenosine-5'-diphosphate: G128 (= G129), E130 (= E131), E182 (= E183), D196 (= D197), F197 (= F198), K198 (= K199), Y199 (= Y200), N245 (= N246), S247 (= S248), R319 (= R321), S327 (= S329), R329 (= R331)
- binding l-methionine-s-sulfoximine phosphate: E130 (= E131), E132 (= E133), E187 (= E188), E194 (= E195), N238 (= N239), G239 (= G240), H243 (= H244), R296 (= R298), E302 (= E304), R314 (= R316), R333 (= R335)
7tf6A Glutamine synthetase (see paper)
62% identity, 99% coverage: 4:444/444 of query aligns to 2:438/438 of 7tf6A
- binding glutamine: E128 (= E133), E183 (= E188), G235 (= G240), H239 (= H244), R292 (= R298), E298 (= E304)
- binding magnesium ion: E126 (= E131), E128 (= E133), E183 (= E188), E190 (= E195), H239 (= H244), E327 (= E333)
- binding : F58 (= F60), R60 (= R62), G232 (= G237), N234 (= N239), G296 (= G302), Y297 (= Y303), R310 (= R316), Y367 (= Y373), Y421 (≠ R427), Q433 (≠ E439), Q437 (≠ K443)
8ufjB Glutamine synthetase (see paper)
58% identity, 98% coverage: 5:441/444 of query aligns to 6:441/444 of 8ufjB
8tfkA Glutamine synthetase (see paper)
58% identity, 98% coverage: 5:441/444 of query aligns to 2:437/440 of 8tfkA
- binding adenosine-5'-diphosphate: E128 (= E131), D194 (= D197), F195 (= F198), F197 (≠ Y200), N243 (= N246), R312 (= R316), R317 (= R321), G325 (≠ S329), R327 (= R331)
- binding magnesium ion: E128 (= E131), E128 (= E131), E130 (= E133), E185 (= E188), E192 (= E195), E192 (= E195), H241 (= H244), E329 (= E333)
- binding l-methionine-s-sulfoximine phosphate: E128 (= E131), E130 (= E133), E185 (= E188), E192 (= E195), G237 (= G240), H241 (= H244), R294 (= R298), E300 (= E304), R312 (= R316), R331 (= R335)
8ooxB Glutamine synthetase (see paper)
59% identity, 99% coverage: 7:444/444 of query aligns to 4:438/438 of 8ooxB
8oozA Glutamine synthetase (see paper)
58% identity, 99% coverage: 7:444/444 of query aligns to 4:430/430 of 8oozA
- binding adenosine-5'-triphosphate: G117 (= G129), E170 (= E183), F185 (= F198), K186 (= K199), Y187 (= Y200), N233 (= N246), S235 (= S248), S315 (= S329), R317 (= R331)
- binding magnesium ion: E119 (= E131), H231 (= H244), E319 (= E333)
8ooqB Glutamine synthetase from Methanothermococcus thermolithotrophicus (see paper)
55% identity, 99% coverage: 5:442/444 of query aligns to 1:445/446 of 8ooqB
- binding 2-oxoglutaric acid: F16 (= F20), R18 (= R22), A32 (= A36), R86 (≠ K83), V92 (= V89), P169 (≠ E165), R172 (= R168), R173 (= R169), S189 (= S185)
- binding magnesium ion: E137 (= E133), E192 (= E188), E199 (= E195)
8oooA Glutamine synthetase from methanothermococcus thermolithotrophicus in complex with 2-oxoglutarate and mgatp at 2.15 a resolution (see paper)
55% identity, 99% coverage: 5:442/444 of query aligns to 2:446/447 of 8oooA
- binding 2-oxoglutaric acid: F17 (= F20), R19 (= R22), A33 (= A36), R87 (≠ K83), V93 (= V89), P170 (≠ E165), R173 (= R168), R174 (= R169), S190 (= S185)
- binding adenosine-5'-triphosphate: E136 (= E131), E188 (= E183), F203 (= F198), K204 (= K199), F205 (≠ Y200), H251 (≠ N246), S253 (= S248), R325 (= R321), R335 (= R331)
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)
47% identity, 98% coverage: 9:441/444 of query aligns to 8:444/446 of A0R083
- K363 (= K360) 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)
46% identity, 98% coverage: 9:441/444 of query aligns to 8:444/446 of P9WN37
- K363 (= K360) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
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)
42% identity, 98% coverage: 4:440/444 of query aligns to 1:466/469 of P0A9C5
- M1 (≠ L4) modified: Initiator methionine, Removed
- Y398 (= Y373) 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)
42% identity, 98% coverage: 4:440/444 of query aligns to 1:466/469 of P0A1P6
- E130 (= E131) binding Mn(2+)
- E132 (= E133) binding Mn(2+)
- E208 (= E183) binding ATP
- E213 (= E188) binding Mn(2+)
- E221 (= E195) binding Mn(2+)
- NG 265:266 (= NG 239:240) binding L-glutamate
- H270 (= H244) binding Mn(2+)
- HMS 272:274 (≠ NQS 246:248) binding ATP
- R322 (= R298) binding L-glutamate
- E358 (= E333) binding Mn(2+)
- R360 (= R335) binding L-glutamate
Query Sequence
>WP_013840878.1 NCBI__GCF_000215085.1:WP_013840878.1
MTKLTNDDVRQMCKDLNVKFIRLQFTDIFGVLKNVAITVEQLDKALDGEMMFDGSSIEGF
VRIEESDMYLRPDPSTFVVFPWKPREGGVARLICDIYNPDGTPFFGDPRYALKRALAEAE
QMGYVMNVGPEAEFFLFHVDNEGRPTTKTHDKAGYFDMTPIDLGENARRDMVLTLEQMGF
EIEASHHEVAPGQHEIDFKYADALDMADKIMTFKLVVRTIAQRHGLHATFMPKPVFGING
SGMHVNQSLITLDGKNAFYDPDAPMGLSKVCMNYIAGLMNHADAITAIANPTVNSYKRLV
AGYEAPVYVAWSGRNRSPLIRIPAKRGMSTRVELRSPDPSCNPYLALAACLHAGLDGIKK
GMTPPPATDRNIYEMTLAERQELGISNLPENLSEALKVLAADNVIKEALGPHIFERFIEA
KSIEWDRYRMQVSSWELDEYLEKF
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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