SitesBLAST
Comparing WP_057507762.1 NCBI__GCF_001431535.1:WP_057507762.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.
Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures
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)
36% identity, 93% coverage: 33:464/465 of query aligns to 40:471/472 of P78061
- H282 (= H272) mutation to N: Activity is impaired to 9% of wild-type.
- R357 (= R351) mutation to Q: Activity is impaired to 3% of wild-type.
8oozA Glutamine synthetase (see paper)
30% identity, 95% coverage: 16:457/465 of query aligns to 1:422/430 of 8oozA
- binding adenosine-5'-triphosphate: G117 (≠ A149), E170 (≠ D211), F185 (= F226), K186 (≠ T227), Y187 (≠ H228), N233 (≠ H274), S235 (= S276), S315 (≠ N359), R317 (= R361)
- binding magnesium ion: E119 (= E151), H231 (= H272), E319 (= E363)
8ooxB Glutamine synthetase (see paper)
30% identity, 95% coverage: 16:457/465 of query aligns to 1:430/438 of 8ooxB
5dm3C Crystal structure of glutamine synthetase from chromohalobacter salexigens dsm 3043(csal_0679, target efi-550015) with bound adp
35% identity, 79% coverage: 91:457/465 of query aligns to 55:390/396 of 5dm3C
- active site: E115 (= E151), E117 (= E153), E162 (= E216), E169 (= E223), H218 (= H272), R286 (= R346), E303 (= E363), R305 (= R365)
- binding adenosine-5'-diphosphate: R173 (≠ T227), C174 (≠ H228), H220 (= H274), S222 (= S276), R301 (= R361)
8oooA Glutamine synthetase from methanothermococcus thermolithotrophicus in complex with 2-oxoglutarate and mgatp at 2.15 a resolution (see paper)
31% identity, 94% coverage: 21:457/465 of query aligns to 6:440/447 of 8oooA
- binding 2-oxoglutaric acid: F17 (≠ E32), R19 (≠ E34), A33 (≠ I48), R87 (vs. gap), V93 (≠ T109), P170 (≠ D193), R173 (≠ L196), R174 (≠ D197), S190 (≠ L213)
- binding adenosine-5'-triphosphate: E136 (= E151), E188 (≠ D211), F203 (= F226), K204 (≠ T227), F205 (≠ H228), H251 (= H274), S253 (= S276), R325 (= R351), R335 (= R361)
8ooqB Glutamine synthetase from Methanothermococcus thermolithotrophicus (see paper)
31% identity, 94% coverage: 21:457/465 of query aligns to 5:439/446 of 8ooqB
- binding 2-oxoglutaric acid: F16 (≠ E32), R18 (≠ E34), A32 (≠ I48), R86 (vs. gap), V92 (≠ T109), P169 (≠ D193), R172 (≠ L196), R173 (≠ D197), S189 (≠ L213)
- binding magnesium ion: E137 (= E153), E192 (= E216), E199 (= E223)
8ufjB Glutamine synthetase (see paper)
30% identity, 97% coverage: 8:457/465 of query aligns to 2:436/444 of 8ufjB
8tfkA Glutamine synthetase (see paper)
30% identity, 96% coverage: 12:457/465 of query aligns to 2:432/440 of 8tfkA
- binding adenosine-5'-diphosphate: E128 (= E151), D194 (≠ N225), F195 (= F226), F197 (≠ H228), N243 (≠ H274), R312 (= R346), R317 (= R351), G325 (≠ N359), R327 (= R361)
- binding magnesium ion: E128 (= E151), E128 (= E151), E130 (= E153), E185 (= E216), E192 (= E223), E192 (= E223), H241 (= H272), E329 (= E363)
- binding l-methionine-s-sulfoximine phosphate: E128 (= E151), E130 (= E153), E185 (= E216), E192 (= E223), G237 (= G268), H241 (= H272), R294 (= R328), E300 (≠ V334), R312 (= R346), R331 (= R365)
4s0rD Structure of gs-tnra complex (see paper)
30% identity, 94% coverage: 23:459/465 of query aligns to 14:441/447 of 4s0rD
- active site: D56 (vs. gap), E135 (= E151), E137 (= E153), E192 (= E216), E199 (= E223), H248 (= H272), R319 (= R346), E336 (= E363), R338 (= R365)
- binding glutamine: E137 (= E153), E192 (= E216), R301 (= R328), E307 (≠ V334)
- binding magnesium ion: I66 (≠ P85), E135 (= E151), E135 (= E151), E199 (= E223), H248 (= H272), H248 (= H272), E336 (= E363), H419 (≠ A437)
- binding : F63 (≠ L82), V64 (≠ T83), R65 (≠ S84), I66 (≠ P85), D161 (≠ E178), G241 (≠ N265), V242 (≠ E266), N243 (≠ P267), G305 (= G332), Y306 (≠ E333), Y376 (≠ K403), I426 (≠ K444), M430 (≠ T448)
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)
30% identity, 94% coverage: 23:459/465 of query aligns to 11:438/444 of P12425
- G59 (= G73) 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 (≠ S84) 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 (= E151) binding
- E134 (= E153) binding
- E189 (= E216) binding
- V190 (≠ S217) 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 (= E223) binding
- G241 (= G268) binding
- H245 (= H272) binding
- G302 (= G332) 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 (≠ V334) 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 (= P336) 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 (= E363) binding
- E424 (= E445) 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
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)
30% identity, 94% coverage: 23:459/465 of query aligns to 10:437/443 of 4lnkA
- active site: D52 (vs. gap), E131 (= E151), E133 (= E153), E188 (= E216), E195 (= E223), H244 (= H272), R315 (= R346), E332 (= E363), R334 (= R365)
- binding adenosine-5'-diphosphate: K43 (≠ H56), M50 (≠ I66), F198 (= F226), Y200 (≠ H228), N246 (≠ H274), S248 (= S276), S324 (≠ D355), S328 (≠ N359), R330 (= R361)
- binding glutamic acid: E133 (= E153), E188 (= E216), V189 (≠ S217), N239 (≠ P267), G240 (= G268), G242 (≠ A270), E303 (≠ V334)
- binding magnesium ion: E131 (= E151), E188 (= E216), E195 (= E223), H244 (= H272), E332 (= E363)
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)
30% identity, 94% coverage: 23:459/465 of query aligns to 10:437/443 of 4lniA
- active site: D52 (vs. gap), E131 (= E151), E133 (= E153), E188 (= E216), E195 (= E223), H244 (= H272), R315 (= R346), E332 (= E363), R334 (= R365)
- binding adenosine-5'-diphosphate: E131 (= E151), E183 (≠ D211), D197 (≠ N225), Y200 (≠ H228), N246 (≠ H274), S248 (= S276), R320 (= R351), R330 (= R361)
- binding magnesium ion: E131 (= E151), E131 (= E151), E133 (= E153), E188 (= E216), E195 (= E223), E195 (= E223), H244 (= H272), E332 (= E363)
- binding l-methionine-s-sulfoximine phosphate: E133 (= E153), E188 (= E216), H244 (= H272), R297 (= R328), E303 (≠ V334), R315 (= R346), R334 (= R365)
7tfaB Glutamine synthetase (see paper)
34% identity, 81% coverage: 87:462/465 of query aligns to 63:438/441 of 7tfaB
- binding glutamine: E131 (= E153), Y153 (≠ R176), E186 (= E216), G238 (= G268), H242 (= H272), R295 (= R328), E301 (≠ V334)
- binding magnesium ion: E129 (= E151), E131 (= E153), E186 (= E216), E193 (= E223), H242 (= H272), E330 (= E363)
- binding : V187 (≠ S217), N237 (≠ P267), G299 (= G332), Y300 (≠ E333), R313 (= R346), M424 (≠ T448)
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)
34% identity, 81% coverage: 87:462/465 of query aligns to 63:436/439 of 7tdpA
- binding adenosine-5'-diphosphate: N123 (vs. gap), G125 (≠ A149), E127 (= E151), E179 (≠ D211), D193 (≠ N225), Y196 (≠ H228), N242 (≠ H274), S244 (= S276), R316 (= R351), R326 (= R361)
- binding magnesium ion: E127 (= E151), E127 (= E151), E129 (= E153), E184 (= E216), E191 (= E223), E191 (= E223), H240 (= H272), E328 (= E363)
- binding l-methionine-s-sulfoximine phosphate: E127 (= E151), E129 (= E153), E184 (= E216), E191 (= E223), G236 (= G268), H240 (= H272), R293 (= R328), E299 (≠ V334), R311 (= R346), R330 (= R365)
7tf9S L. Monocytogenes gs(14)-q-glnr peptide (see paper)
30% identity, 95% coverage: 18:459/465 of query aligns to 5:437/443 of 7tf9S
- binding glutamine: E133 (= E153), Y155 (≠ R173), E188 (= E216), G240 (= G268), G242 (≠ A270), R297 (= R328), E303 (≠ V334)
- binding magnesium ion: E131 (= E151), E133 (= E153), E188 (= E216), E195 (= E223), H244 (= H272), E332 (= E363)
- binding : F59 (≠ L82), V60 (≠ T83), E418 (≠ S440), I422 (≠ K444), M426 (≠ T448)
7tenA Glutamine synthetase (see paper)
30% identity, 95% coverage: 18:459/465 of query aligns to 4:436/442 of 7tenA
- binding adenosine-5'-diphosphate: G128 (≠ A149), E130 (= E151), E182 (≠ D211), D196 (≠ N225), F197 (= F226), K198 (≠ T227), Y199 (≠ H228), N245 (≠ H274), S247 (= S276), R319 (= R351), S327 (≠ N359), R329 (= R361)
- binding l-methionine-s-sulfoximine phosphate: E130 (= E151), E132 (= E153), E187 (= E216), E194 (= E223), N238 (≠ P267), G239 (= G268), H243 (= H272), R296 (= R328), E302 (≠ V334), R314 (= R346), R333 (= R365)
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, 95% coverage: 15:457/465 of query aligns to 2:439/446 of A0R083
- K363 (vs. gap) 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, 97% coverage: 15:463/465 of query aligns to 2:446/446 of P9WN37
- K363 (≠ G390) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
5dm3A Crystal structure of glutamine synthetase from chromohalobacter salexigens dsm 3043(csal_0679, target efi-550015) with bound adp
33% identity, 80% coverage: 87:457/465 of query aligns to 47:368/374 of 5dm3A
- active site: E107 (= E151), E109 (= E153), E146 (≠ A219), E150 (= E223), H199 (= H272), R265 (= R346), E282 (= E363), R284 (= R365)
- binding adenosine-5'-diphosphate: I103 (≠ V147), E141 (≠ D211), R154 (≠ T227), C155 (≠ H228), H201 (= H274), S203 (= S276), R280 (= R361)
8wwvA Glutamine synthetase
31% identity, 82% coverage: 70:450/465 of query aligns to 82:464/490 of 8wwvA
- binding adenosine-5'-diphosphate: G155 (≠ A149), E157 (= E151), R224 (≠ D211), F239 (= F226), D240 (≠ T227), V241 (≠ H228), H288 (= H274), S290 (= S276), R374 (= R361), E376 (= E363)
- binding magnesium ion: E157 (= E151), E236 (= E223)
- binding manganese (ii) ion: E157 (= E151), E159 (= E153), E229 (= E216), E236 (= E223), H286 (= H272), E376 (= E363)
- binding l-methionine-s-sulfoximine phosphate: E157 (= E151), E159 (= E153), E229 (= E216), E236 (= E223), A282 (≠ G268), H286 (= H272), R340 (= R328), K358 (≠ R346)
Query Sequence
>WP_057507762.1 NCBI__GCF_001431535.1:WP_057507762.1
MSTDSRTRRMPTEEDAQESSLLRWLKDRRITEVECLVPDITGIARGKIIPADKFSHDYGT
RLPEGIFATTVTGDYPDDYYELTSPSDSDMVLRPDPETVRMVPWATDPTAQIIHDCYTKS
GQPHELAPRNVLRRVLDAYTELGLRPVVAPELEFFLVQKNTDPDFPLLPPAGRSGRPETA
RQSYSIDAVNEFDPILDLMYDYADAMKLDVDTLIHESGAAQLEVNFTHAGAMNLADQVFL
FKRTMREAAMRHGVYATFLAKPMENEPGSAMHIHQSLLRISDGANVFAGDGDGEGEFSPV
FGHYLGGLQKFAPQAMAFFAPNVNSYRRLVFGEVSPSNVHWGFDNRTCGLRVPMDTPDNM
RVESRFAGSDANPYLAMAATLACGLLGLRGQLAPDAPVSGSAKELGYDLPRSLGEALDGL
EQCAELQALLGERFCRAYISVKRKEYETFFRVISSWEREFLLLNV
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