SitesBLAST
Comparing WP_013840509.1 NCBI__GCF_000215085.1:WP_013840509.1 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)
7tdpA Structure of paenibacillus polymyxa gs bound to met-sox-p-adp (transition state complex) to 1.98 angstom (see paper)
45% identity, 99% coverage: 5:432/432 of query aligns to 3:439/439 of 7tdpA
- binding adenosine-5'-diphosphate: N123 (≠ T127), G125 (= G129), E127 (= E131), E179 (≠ V183), D193 (≠ V197), Y196 (≠ E200), N242 (= N246), S244 (≠ C248), R316 (= R320), R326 (= R330)
- binding magnesium ion: E127 (= E131), E127 (= E131), E129 (= E133), E184 (= E188), E191 (= E195), E191 (= E195), H240 (≠ A244), E328 (≠ V332)
- binding l-methionine-s-sulfoximine phosphate: E127 (= E131), E129 (= E133), E184 (= E188), E191 (= E195), G236 (= G240), H240 (≠ A244), R293 (= R297), E299 (≠ L303), R311 (= R315), R330 (= R334)
7tfaB Glutamine synthetase (see paper)
45% identity, 99% coverage: 5:432/432 of query aligns to 3:441/441 of 7tfaB
- binding glutamine: E131 (= E133), Y153 (≠ L155), E186 (= E188), G238 (= G240), H242 (≠ A244), R295 (= R297), E301 (≠ L303)
- binding magnesium ion: E129 (= E131), E131 (= E133), E186 (= E188), E193 (= E195), H242 (≠ A244), E330 (≠ V332)
- binding : Y58 (≠ Q60), R60 (≠ G62), V187 (≠ S189), N237 (= N239), G299 (≠ S301), Y300 (≠ H302), R313 (= R315), M424 (≠ E415)
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)
44% identity, 100% coverage: 1:432/432 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 (≠ G62) 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 (≠ S189) 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 (≠ A244) binding Mg(2+)
- G302 (≠ S301) 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 (≠ L303) 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 (≠ R305) 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 (≠ V332) binding Mg(2+)
- E424 (= E412) 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.
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)
45% identity, 99% coverage: 6:432/432 of query aligns to 4:443/443 of 4lnkA
- active site: D52 (= D53), E131 (= E131), E133 (= E133), E188 (= E188), E195 (= E195), H244 (≠ A244), R315 (= R315), E332 (≠ V332), R334 (= R334)
- binding adenosine-5'-diphosphate: K43 (≠ R44), M50 (≠ S51), F198 (≠ L198), Y200 (≠ E200), N246 (= N246), S248 (≠ C248), S324 (≠ Q324), S328 (≠ D328), R330 (= R330)
- binding glutamic acid: E133 (= E133), E188 (= E188), V189 (≠ S189), N239 (= N239), G240 (= G240), G242 (= G242), E303 (≠ L303)
- binding magnesium ion: E131 (= E131), E188 (= E188), E195 (= E195), H244 (≠ A244), E332 (≠ V332)
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)
45% identity, 99% coverage: 6:432/432 of query aligns to 4:443/443 of 4lniA
- active site: D52 (= D53), E131 (= E131), E133 (= E133), E188 (= E188), E195 (= E195), H244 (≠ A244), R315 (= R315), E332 (≠ V332), R334 (= R334)
- binding adenosine-5'-diphosphate: E131 (= E131), E183 (≠ V183), D197 (≠ V197), Y200 (≠ E200), N246 (= N246), S248 (≠ C248), R320 (= R320), R330 (= R330)
- binding magnesium ion: E131 (= E131), E131 (= E131), E133 (= E133), E188 (= E188), E195 (= E195), E195 (= E195), H244 (≠ A244), E332 (≠ V332)
- binding l-methionine-s-sulfoximine phosphate: E133 (= E133), E188 (= E188), H244 (≠ A244), R297 (= R297), E303 (≠ L303), R315 (= R315), R334 (= R334)
4s0rD Structure of gs-tnra complex (see paper)
44% identity, 100% coverage: 1:432/432 of query aligns to 4:447/447 of 4s0rD
- active site: D56 (= D53), E135 (= E131), E137 (= E133), E192 (= E188), E199 (= E195), H248 (≠ A244), R319 (= R315), E336 (≠ V332), R338 (= R334)
- binding glutamine: E137 (= E133), E192 (= E188), R301 (= R297), E307 (≠ L303)
- binding magnesium ion: I66 (≠ V63), E135 (= E131), E135 (= E131), E199 (= E195), H248 (≠ A244), H248 (≠ A244), E336 (≠ V332), H419 (≠ R404)
- binding : F63 (≠ Q60), V64 (≠ Y61), R65 (≠ G62), I66 (≠ V63), D161 (= D157), G241 (≠ E237), V242 (≠ H238), N243 (= N239), G305 (≠ S301), Y306 (≠ H302), Y376 (≠ V372), I426 (≠ R411), M430 (≠ E415)
7tenA Glutamine synthetase (see paper)
44% identity, 99% coverage: 5:432/432 of query aligns to 3:442/442 of 7tenA
- binding adenosine-5'-diphosphate: G128 (= G129), E130 (= E131), E182 (≠ V183), D196 (≠ V197), F197 (≠ L198), K198 (≠ R199), Y199 (≠ E200), N245 (= N246), S247 (≠ C248), R319 (= R320), S327 (≠ D328), R329 (= R330)
- binding l-methionine-s-sulfoximine phosphate: E130 (= E131), E132 (= E133), E187 (= E188), E194 (= E195), N238 (= N239), G239 (= G240), H243 (≠ A244), R296 (= R297), E302 (≠ L303), R314 (= R315), R333 (= R334)
7tf9S L. Monocytogenes gs(14)-q-glnr peptide (see paper)
44% identity, 99% coverage: 5:432/432 of query aligns to 4:443/443 of 7tf9S
- binding glutamine: E133 (= E133), Y155 (≠ L155), E188 (= E188), G240 (= G240), G242 (= G242), R297 (= R297), E303 (≠ L303)
- binding magnesium ion: E131 (= E131), E133 (= E133), E188 (= E188), E195 (= E195), H244 (≠ A244), E332 (≠ V332)
- binding : F59 (≠ Q60), V60 (≠ Y61), E418 (≠ D407), I422 (≠ R411), M426 (≠ E415)
8ufjB Glutamine synthetase (see paper)
44% identity, 99% coverage: 5:430/432 of query aligns to 6:442/444 of 8ufjB
8tfkA Glutamine synthetase (see paper)
43% identity, 99% coverage: 5:430/432 of query aligns to 2:438/440 of 8tfkA
- binding adenosine-5'-diphosphate: E128 (= E131), D194 (≠ V197), F195 (≠ L198), F197 (≠ E200), N243 (= N246), R312 (= R315), R317 (= R320), G325 (≠ D328), R327 (= R330)
- binding magnesium ion: E128 (= E131), E128 (= E131), E130 (= E133), E185 (= E188), E192 (= E195), E192 (= E195), H241 (≠ A244), E329 (≠ V332)
- binding l-methionine-s-sulfoximine phosphate: E128 (= E131), E130 (= E133), E185 (= E188), E192 (= E195), G237 (= G240), H241 (≠ A244), R294 (= R297), E300 (≠ L303), R312 (= R315), R331 (= R334)
7tdvC Glutamine synthetase (see paper)
42% identity, 99% coverage: 4:432/432 of query aligns to 3:443/443 of 7tdvC
- binding adenosine-5'-diphosphate: G129 (= G129), E131 (= E131), E183 (≠ V183), D197 (≠ V197), F198 (≠ L198), K199 (≠ R199), Y200 (≠ E200), N246 (= N246), V247 (≠ L247), S248 (≠ C248), R320 (= R320), S328 (≠ D328), R330 (= R330)
- binding magnesium ion: E131 (= E131), E131 (= E131), E133 (= E133), E188 (= E188), E195 (= E195), E195 (= E195), H244 (≠ A244), E332 (≠ V332)
- binding l-methionine-s-sulfoximine phosphate: E131 (= E131), E133 (= E133), E188 (= E188), E195 (= E195), G240 (= G240), H244 (≠ A244), R297 (= R297), E303 (≠ L303), R315 (= R315)
7tf6A Glutamine synthetase (see paper)
42% identity, 99% coverage: 4:432/432 of query aligns to 2:438/438 of 7tf6A
- binding glutamine: E128 (= E133), E183 (= E188), G235 (= G240), H239 (≠ A244), R292 (= R297), E298 (≠ L303)
- binding magnesium ion: E126 (= E131), E128 (= E133), E183 (= E188), E190 (= E195), H239 (≠ A244), E327 (≠ V332)
- binding : F58 (≠ Q60), R60 (≠ G62), G232 (≠ E237), N234 (= N239), G296 (≠ S301), Y297 (≠ H302), R310 (= R315), Y367 (≠ V372), Y421 (≠ E415), Q433 (≠ K427), Q437 (≠ N431)
8ooxB Glutamine synthetase (see paper)
42% identity, 98% coverage: 8:432/432 of query aligns to 5:438/438 of 8ooxB
8oozA Glutamine synthetase (see paper)
42% identity, 98% coverage: 8:432/432 of query aligns to 5:430/430 of 8oozA
- binding adenosine-5'-triphosphate: G117 (= G129), E170 (≠ V183), F185 (≠ L198), K186 (≠ R199), Y187 (≠ E200), N233 (= N246), S235 (≠ C248), S315 (≠ D328), R317 (= R330)
- binding magnesium ion: E119 (= E131), H231 (≠ A244), E319 (≠ V332)
8ooqB Glutamine synthetase from Methanothermococcus thermolithotrophicus (see paper)
41% identity, 98% coverage: 5:429/432 of query aligns to 1:444/446 of 8ooqB
- binding 2-oxoglutaric acid: F16 (= F20), R18 (= R22), A32 (= A36), R86 (= R83), 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)
41% identity, 98% coverage: 5:429/432 of query aligns to 2:445/447 of 8oooA
- binding 2-oxoglutaric acid: F17 (= F20), R19 (= R22), A33 (= A36), R87 (= R83), V93 (= V89), P170 (≠ E165), R173 (= R168), R174 (= R169), S190 (= S185)
- binding adenosine-5'-triphosphate: E136 (= E131), E188 (≠ V183), F203 (≠ L198), K204 (≠ R199), F205 (≠ E200), H251 (≠ N246), S253 (≠ C248), R325 (= R320), R335 (= R330)
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)
38% identity, 98% coverage: 9:430/432 of query aligns to 8:445/446 of A0R083
- K363 (≠ Q359) 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)
38% identity, 98% coverage: 9:430/432 of query aligns to 8:445/446 of P9WN37
- K363 (≠ Q359) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
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)
30% identity, 99% coverage: 4:430/432 of query aligns to 1:468/469 of P0A1P6
- E130 (= E131) binding Mn(2+)
- E132 (= E133) binding Mn(2+)
- E208 (≠ V183) binding ATP
- E213 (= E188) binding Mn(2+)
- E221 (= E195) binding Mn(2+)
- NG 265:266 (= NG 239:240) binding L-glutamate
- H270 (≠ A244) binding Mn(2+)
- HMS 272:274 (≠ NLC 246:248) binding ATP
- R322 (= R297) binding L-glutamate
- E358 (≠ V332) binding Mn(2+)
- R360 (= R334) binding L-glutamate
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)
30% identity, 99% coverage: 4:430/432 of query aligns to 1:468/469 of P0A9C5
- M1 (≠ L4) modified: Initiator methionine, Removed
- Y398 (≠ V372) modified: O-AMP-tyrosine
Query Sequence
>WP_013840509.1 NCBI__GCF_000215085.1:WP_013840509.1
MQPLTAREVMEKAQECHVKFVRLQFTDIQGSFKNVAVTVEELERALQAKISMDSAVLEGQ
YGVRQRDVFLKPDPSTFEVFPWRPREGAVARLICDVVDAAGNAYPGCVRSKLKDSLARLE
KNHFELTVGAEIEFFLFQTDPQGHPIPCTHDNAGLCDLSPADLGENARRDMVLTLEEMGF
QVVSSHHESAPGQHEIVLREEDPLGMADKIATFKFVVRTIAQRHGLHASFMPKPLAEHNG
SGMALNLCLWQEGNNALADETGPCGLSAQAGSFIAGITGHASALTAIVNPLVNSYKRLGC
SHLDRVLKGWSEGNRNSMIRVPGQRGNDTRIVLRNPDATCNPYLALNLIMQTGLRGIEQG
LPLPTSLDQDVVDRRVPGNLGEALAALLQDQYIKEALGEVIFERYVDYKKREWDEFHNYL
HPWELDKYLTNY
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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