SitesBLAST
Comparing WP_012977188.1 NCBI__GCF_000010725.1:WP_012977188.1 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)
35% identity, 96% coverage: 16:446/447 of query aligns to 40:471/472 of P78061
- H282 (= H257) mutation to N: Activity is impaired to 9% of wild-type.
- R357 (= R333) mutation to Q: Activity is impaired to 3% of wild-type.
8ufjB Glutamine synthetase (see paper)
30% identity, 98% coverage: 8:444/447 of query aligns to 14:441/444 of 8ufjB
8tfkA Glutamine synthetase (see paper)
30% identity, 98% coverage: 8:444/447 of query aligns to 10:437/440 of 8tfkA
- binding adenosine-5'-diphosphate: E128 (= E136), D194 (≠ N210), F195 (= F211), F197 (≠ H213), N243 (≠ H259), R312 (= R328), R317 (= R333), G325 (≠ A341), R327 (= R343)
- binding magnesium ion: E128 (= E136), E128 (= E136), E130 (= E138), E185 (= E201), E192 (= E208), E192 (= E208), H241 (= H257), E329 (= E345)
- binding l-methionine-s-sulfoximine phosphate: E128 (= E136), E130 (= E138), E185 (= E201), E192 (= E208), G237 (= G253), H241 (= H257), R294 (= R310), E300 (≠ D316), R312 (= R328), R331 (= R347)
8oozA Glutamine synthetase (see paper)
31% identity, 85% coverage: 66:444/447 of query aligns to 50:427/430 of 8oozA
- binding adenosine-5'-triphosphate: G117 (≠ A134), E170 (≠ D196), F185 (= F211), K186 (≠ N212), Y187 (≠ H213), N233 (≠ H259), S235 (= S261), S315 (≠ A341), R317 (= R343)
- binding magnesium ion: E119 (= E136), H231 (= H257), E319 (= E345)
8ooxB Glutamine synthetase (see paper)
31% identity, 84% coverage: 71:444/447 of query aligns to 61:435/438 of 8ooxB
8oooA Glutamine synthetase from methanothermococcus thermolithotrophicus in complex with 2-oxoglutarate and mgatp at 2.15 a resolution (see paper)
28% identity, 98% coverage: 6:444/447 of query aligns to 8:445/447 of 8oooA
- binding 2-oxoglutaric acid: F17 (≠ E15), R19 (≠ E17), A33 (≠ I31), R87 (vs. gap), V93 (≠ T94), P170 (≠ D178), R173 (≠ F181), R174 (≠ E182), S190 (≠ L198)
- binding adenosine-5'-triphosphate: E136 (= E136), E188 (≠ D196), F203 (= F211), K204 (≠ N212), F205 (≠ H213), H251 (= H259), S253 (= S261), R325 (= R333), R335 (= R343)
8ooqB Glutamine synthetase from Methanothermococcus thermolithotrophicus (see paper)
28% identity, 98% coverage: 6:444/447 of query aligns to 7:444/446 of 8ooqB
- binding 2-oxoglutaric acid: F16 (≠ E15), R18 (≠ E17), A32 (≠ I31), R86 (vs. gap), V92 (≠ T94), P169 (≠ D178), R172 (≠ F181), R173 (≠ E182), S189 (≠ L198)
- binding magnesium ion: E137 (= E138), E192 (= E201), E199 (= E208)
7tfaB Glutamine synthetase (see paper)
33% identity, 84% coverage: 71:444/447 of query aligns to 62:438/441 of 7tfaB
- binding glutamine: E131 (= E138), Y153 (≠ R161), E186 (= E201), G238 (= G253), H242 (= H257), R295 (= R310), E301 (≠ D316)
- binding magnesium ion: E129 (= E136), E131 (= E138), E186 (= E201), E193 (= E208), H242 (= H257), E330 (= E345)
- binding : V187 (≠ A202), N237 (≠ P252), G299 (≠ N314), Y300 (≠ S315), R313 (= R328), M424 (≠ A430)
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, 99% coverage: 4:444/447 of query aligns to 8:440/443 of 4lnkA
- active site: D52 (≠ L48), E131 (= E136), E133 (= E138), E188 (= E201), E195 (= E208), H244 (= H257), R315 (= R328), E332 (= E345), R334 (= R347)
- binding adenosine-5'-diphosphate: K43 (≠ R39), M50 (≠ L46), F198 (= F211), Y200 (≠ H213), N246 (≠ H259), S248 (= S261), S324 (= S337), S328 (≠ A341), R330 (= R343)
- binding glutamic acid: E133 (= E138), E188 (= E201), V189 (≠ A202), N239 (≠ P252), G240 (= G253), G242 (≠ A255), E303 (≠ D316)
- binding magnesium ion: E131 (= E136), E188 (= E201), E195 (= E208), H244 (= H257), E332 (= E345)
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, 99% coverage: 4:444/447 of query aligns to 8:440/443 of 4lniA
- active site: D52 (≠ L48), E131 (= E136), E133 (= E138), E188 (= E201), E195 (= E208), H244 (= H257), R315 (= R328), E332 (= E345), R334 (= R347)
- binding adenosine-5'-diphosphate: E131 (= E136), E183 (≠ D196), D197 (≠ N210), Y200 (≠ H213), N246 (≠ H259), S248 (= S261), R320 (= R333), R330 (= R343)
- binding magnesium ion: E131 (= E136), E131 (= E136), E133 (= E138), E188 (= E201), E195 (= E208), E195 (= E208), H244 (= H257), E332 (= E345)
- binding l-methionine-s-sulfoximine phosphate: E133 (= E138), E188 (= E201), H244 (= H257), R297 (= R310), E303 (≠ D316), R315 (= R328), R334 (= R347)
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, 99% coverage: 4:444/447 of query aligns to 9:441/444 of P12425
- G59 (≠ D66) 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 (≠ S69) 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 (= E136) binding Mg(2+)
- E134 (= E138) binding Mg(2+)
- E189 (= E201) binding Mg(2+)
- 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 Mg(2+)
- G241 (= G253) binding L-glutamate
- H245 (= H257) binding Mg(2+)
- G302 (≠ N314) 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 (≠ D316) 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 (= P318) 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 (= E345) binding Mg(2+)
- E424 (= E427) 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)
29% identity, 99% coverage: 4:444/447 of query aligns to 12:444/447 of 4s0rD
- active site: D56 (≠ L48), E135 (= E136), E137 (= E138), E192 (= E201), E199 (= E208), H248 (= H257), R319 (= R328), E336 (= E345), R338 (= R347)
- binding glutamine: E137 (= E138), E192 (= E201), R301 (= R310), E307 (≠ D316)
- binding magnesium ion: I66 (≠ D70), E135 (= E136), E135 (= E136), E199 (= E208), H248 (= H257), H248 (= H257), E336 (= E345), H419 (≠ A419)
- binding : F63 (≠ I67), V64 (≠ T68), R65 (≠ S69), I66 (≠ D70), D161 (≠ E163), G241 (= G250), V242 (≠ E251), N243 (≠ P252), G305 (≠ N314), Y306 (≠ S315), Y376 (= Y385), I426 (≠ A426), M430 (≠ A430)
7tdpA Structure of paenibacillus polymyxa gs bound to met-sox-p-adp (transition state complex) to 1.98 angstom (see paper)
33% identity, 84% coverage: 71:444/447 of query aligns to 62:436/439 of 7tdpA
- binding adenosine-5'-diphosphate: N123 (vs. gap), G125 (≠ A134), E127 (= E136), E179 (≠ D196), D193 (≠ N210), Y196 (≠ H213), N242 (≠ H259), S244 (= S261), R316 (= R333), R326 (= R343)
- binding magnesium ion: E127 (= E136), E127 (= E136), E129 (= E138), E184 (= E201), E191 (= E208), E191 (= E208), H240 (= H257), E328 (= E345)
- binding l-methionine-s-sulfoximine phosphate: E127 (= E136), E129 (= E138), E184 (= E201), E191 (= E208), G236 (= G253), H240 (= H257), R293 (= R310), E299 (≠ D316), R311 (= R328), R330 (= R347)
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, 83% coverage: 73:444/447 of query aligns to 65:444/446 of A0R083
- K363 (≠ Q372) 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)
32% identity, 88% coverage: 50:444/447 of query aligns to 42:444/446 of P9WN37
- K363 (≠ Q372) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
5dm3C Crystal structure of glutamine synthetase from chromohalobacter salexigens dsm 3043(csal_0679, target efi-550015) with bound adp
32% identity, 81% coverage: 77:439/447 of query aligns to 56:390/396 of 5dm3C
- active site: E115 (= E136), E117 (= E138), E162 (= E201), E169 (= E208), H218 (= H257), R286 (= R328), E303 (= E345), R305 (= R347)
- binding adenosine-5'-diphosphate: R173 (≠ N212), C174 (≠ H213), H220 (= H259), S222 (= S261), R301 (= R343)
7tenA Glutamine synthetase (see paper)
30% identity, 84% coverage: 71:444/447 of query aligns to 62:439/442 of 7tenA
- binding adenosine-5'-diphosphate: G128 (≠ A134), E130 (= E136), E182 (≠ D196), D196 (≠ N210), F197 (= F211), K198 (≠ N212), Y199 (≠ H213), N245 (≠ H259), S247 (= S261), R319 (= R333), S327 (≠ A341), R329 (= R343)
- binding l-methionine-s-sulfoximine phosphate: E130 (= E136), E132 (= E138), E187 (= E201), E194 (= E208), N238 (≠ P252), G239 (= G253), H243 (= H257), R296 (= R310), E302 (≠ D316), R314 (= R328), R333 (= R347)
7tf9S L. Monocytogenes gs(14)-q-glnr peptide (see paper)
30% identity, 84% coverage: 71:444/447 of query aligns to 63:440/443 of 7tf9S
- binding glutamine: E133 (= E138), Y155 (≠ R161), E188 (= E201), G240 (= G253), G242 (≠ A255), R297 (= R310), E303 (≠ D316)
- binding magnesium ion: E131 (= E136), E133 (= E138), E188 (= E201), E195 (= E208), H244 (= H257), E332 (= E345)
- binding : E418 (≠ C422), I422 (≠ A426), M426 (≠ A430)
Sites not aligning to the query:
7tdvC Glutamine synthetase (see paper)
27% identity, 98% coverage: 7:444/447 of query aligns to 11:440/443 of 7tdvC
- binding adenosine-5'-diphosphate: G129 (≠ A134), E131 (= E136), E183 (≠ D196), D197 (≠ N210), F198 (= F211), K199 (≠ N212), Y200 (≠ H213), N246 (≠ H259), V247 (≠ Q260), S248 (= S261), R320 (= R333), S328 (≠ A341), R330 (= R343)
- binding magnesium ion: E131 (= E136), E131 (= E136), E133 (= E138), E188 (= E201), E195 (= E208), E195 (= E208), H244 (= H257), E332 (= E345)
- binding l-methionine-s-sulfoximine phosphate: E131 (= E136), E133 (= E138), E188 (= E201), E195 (= E208), G240 (= G253), H244 (= H257), R297 (= R310), E303 (≠ D316), R315 (= R328)
7tf6A Glutamine synthetase (see paper)
30% identity, 84% coverage: 71:444/447 of query aligns to 62:435/438 of 7tf6A
- binding glutamine: E128 (= E138), E183 (= E201), G235 (= G253), H239 (= H257), R292 (= R310), E298 (≠ D316)
- binding magnesium ion: E126 (= E136), E128 (= E138), E183 (= E201), E190 (= E208), H239 (= H257), E327 (= E345)
- binding : G232 (= G250), N234 (≠ P252), G296 (≠ N314), Y297 (≠ S315), R310 (= R328), Y367 (= Y385), Y421 (≠ A430), Q433 (≠ N442)
Sites not aligning to the query:
Query Sequence
>WP_012977188.1 NCBI__GCF_000010725.1:WP_012977188.1
MGFMEDFIKKNRITEVECLVPDMSGIARGKIVPAEKFLRILRDRGLRLPEAIFVQTVTGE
FPDDEDITSDENSDIYMIPDERTIRFVPWYTEPTAQVITDCVYADGRPVDVSPRHVLKRV
LSLYEERGWKPLVAPELEFFLVQVNKDPDYPLVPPVGRNGRMESGRQAFGIDAVNEFDPI
FEAVYDFCEKQDIDIDTLTHEAGAAQIEINFNHGDALELADQAFLFKRTAREAAIRHQVY
ATFMAKPMQGEPGSAMHIHQSVVDADSGRNLFANPDGTDSPLFLSHIAGLQKYLPYAMPL
LAPNVNSYRRLVPNSDAPINVHWGRDNRTTGLRVPVSPPDARRVENRVAGADANPYLAIA
ASLACGYIGMTQGLEPNDPIKGSAYRLAFTLPRHQSEALSKFNACKPLKEILGERFIDAV
DCVKQAEYKAYNRVISSWERENLLLNV
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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