SitesBLAST
Comparing WP_028321524.1 NCBI__GCF_000422285.1:WP_028321524.1 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)
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)
53% identity, 99% coverage: 4:440/442 of query aligns to 3:445/446 of A0R083
- K363 (≠ N358) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
8ufjB Glutamine synthetase (see paper)
52% identity, 100% coverage: 3:442/442 of query aligns to 4:444/444 of 8ufjB
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)
52% identity, 99% coverage: 4:440/442 of query aligns to 3:445/446 of P9WN37
- K363 (≠ N358) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
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)
51% identity, 99% coverage: 5:441/442 of query aligns to 5:443/444 of P12425
- 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
- E134 (= E133) binding
- E189 (= E184) binding
- V190 (= V185) 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 (= E191) binding
- G241 (= G236) binding
- H245 (= H240) binding
- G302 (= G297) 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 (= E299) 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 (= P301) 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 (= E331) binding
- E424 (= E422) 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)
51% identity, 100% coverage: 1:441/442 of query aligns to 4:446/447 of 4s0rD
- active site: D56 (= D53), E135 (= E131), E137 (= E133), E192 (= E184), E199 (= E191), H248 (= H240), R319 (= R311), E336 (= E331), R338 (= R333)
- binding glutamine: E137 (= E133), E192 (= E184), R301 (= R293), E307 (= E299)
- binding magnesium ion: I66 (= I63), E135 (= E131), E135 (= E131), E199 (= E191), H248 (= H240), H248 (= H240), E336 (= E331), H419 (≠ K414)
- binding : F63 (= F60), V64 (≠ A61), R65 (= R62), I66 (= I63), D161 (= D153), G241 (= G233), V242 (≠ Q234), N243 (= N235), G305 (= G297), Y306 (= Y298), Y376 (≠ F371), I426 (= I421), M430 (= M425)
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)
51% identity, 99% coverage: 5:441/442 of query aligns to 4:442/443 of 4lnkA
- active site: D52 (= D53), E131 (= E131), E133 (= E133), E188 (= E184), E195 (= E191), H244 (= H240), R315 (= R311), E332 (= E331), R334 (= R333)
- binding adenosine-5'-diphosphate: K43 (≠ E44), M50 (≠ G51), F198 (≠ L194), Y200 (= Y196), N246 (≠ H242), S248 (= S244), S324 (≠ G323), S328 (≠ A327), R330 (= R329)
- binding glutamic acid: E133 (= E133), E188 (= E184), V189 (= V185), N239 (= N235), G240 (= G236), G242 (= G238), E303 (= E299)
- binding magnesium ion: E131 (= E131), E188 (= E184), E195 (= E191), H244 (= H240), E332 (= E331)
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)
51% identity, 99% coverage: 5:441/442 of query aligns to 4:442/443 of 4lniA
- active site: D52 (= D53), E131 (= E131), E133 (= E133), E188 (= E184), E195 (= E191), H244 (= H240), R315 (= R311), E332 (= E331), R334 (= R333)
- binding adenosine-5'-diphosphate: E131 (= E131), E183 (= E179), D197 (= D193), Y200 (= Y196), N246 (≠ H242), S248 (= S244), R320 (= R316), R330 (= R329)
- binding magnesium ion: E131 (= E131), E131 (= E131), E133 (= E133), E188 (= E184), E195 (= E191), E195 (= E191), H244 (= H240), E332 (= E331)
- binding l-methionine-s-sulfoximine phosphate: E133 (= E133), E188 (= E184), H244 (= H240), R297 (= R293), E303 (= E299), R315 (= R311), R334 (= R333)
7tfaB Glutamine synthetase (see paper)
51% identity, 99% coverage: 5:440/442 of query aligns to 3:439/441 of 7tfaB
- binding glutamine: E131 (= E133), Y153 (= Y151), E186 (= E184), G238 (= G236), H242 (= H240), R295 (= R293), E301 (= E299)
- binding magnesium ion: E129 (= E131), E131 (= E133), E186 (= E184), E193 (= E191), H242 (= H240), E330 (= E331)
- binding : Y58 (≠ F60), R60 (= R62), V187 (= V185), N237 (= N235), G299 (= G297), Y300 (= Y298), R313 (= R311), M424 (= M425)
8tfkA Glutamine synthetase (see paper)
52% identity, 99% coverage: 5:442/442 of query aligns to 2:440/440 of 8tfkA
- binding adenosine-5'-diphosphate: E128 (= E131), D194 (= D193), F195 (≠ L194), F197 (≠ Y196), N243 (≠ H242), R312 (= R311), R317 (= R316), G325 (≠ A327), R327 (= R329)
- binding magnesium ion: E128 (= E131), E128 (= E131), E130 (= E133), E185 (= E184), E192 (= E191), E192 (= E191), H241 (= H240), E329 (= E331)
- binding l-methionine-s-sulfoximine phosphate: E128 (= E131), E130 (= E133), E185 (= E184), E192 (= E191), G237 (= G236), H241 (= H240), R294 (= R293), E300 (= E299), R312 (= R311), R331 (= R333)
7tdvC Glutamine synthetase (see paper)
50% identity, 99% coverage: 5:441/442 of query aligns to 4:442/443 of 7tdvC
- binding adenosine-5'-diphosphate: G129 (= G129), E131 (= E131), E183 (= E179), D197 (= D193), F198 (≠ L194), K199 (≠ R195), Y200 (= Y196), N246 (≠ H242), V247 (≠ Q243), S248 (= S244), R320 (= R316), S328 (≠ A327), R330 (= R329)
- binding magnesium ion: E131 (= E131), E131 (= E131), E133 (= E133), E188 (= E184), E195 (= E191), E195 (= E191), H244 (= H240), E332 (= E331)
- binding l-methionine-s-sulfoximine phosphate: E131 (= E131), E133 (= E133), E188 (= E184), E195 (= E191), G240 (= G236), H244 (= H240), R297 (= R293), E303 (= E299), R315 (= R311)
7tdpA Structure of paenibacillus polymyxa gs bound to met-sox-p-adp (transition state complex) to 1.98 angstom (see paper)
51% identity, 99% coverage: 5:440/442 of query aligns to 3:437/439 of 7tdpA
- binding adenosine-5'-diphosphate: N123 (≠ Y127), G125 (= G129), E127 (= E131), E179 (= E179), D193 (= D193), Y196 (= Y196), N242 (≠ H242), S244 (= S244), R316 (= R316), R326 (= R329)
- binding magnesium ion: E127 (= E131), E127 (= E131), E129 (= E133), E184 (= E184), E191 (= E191), E191 (= E191), H240 (= H240), E328 (= E331)
- binding l-methionine-s-sulfoximine phosphate: E127 (= E131), E129 (= E133), E184 (= E184), E191 (= E191), G236 (= G236), H240 (= H240), R293 (= R293), E299 (= E299), R311 (= R311), R330 (= R333)
7tf6A Glutamine synthetase (see paper)
50% identity, 99% coverage: 5:441/442 of query aligns to 3:437/438 of 7tf6A
- binding glutamine: E128 (= E133), E183 (= E184), G235 (= G236), H239 (= H240), R292 (= R293), E298 (= E299)
- binding magnesium ion: E126 (= E131), E128 (= E133), E183 (= E184), E190 (= E191), H239 (= H240), E327 (= E331)
- binding : F58 (= F60), R60 (= R62), G232 (= G233), N234 (= N235), G296 (= G297), Y297 (= Y298), R310 (= R311), Y367 (≠ F371), Y421 (≠ M425), Q433 (≠ R437), Q437 (≠ K441)
7tf9S L. Monocytogenes gs(14)-q-glnr peptide (see paper)
50% identity, 98% coverage: 5:439/442 of query aligns to 4:440/443 of 7tf9S
- binding glutamine: E133 (= E133), Y155 (= Y151), E188 (= E184), G240 (= G236), G242 (= G238), R297 (= R293), E303 (= E299)
- binding magnesium ion: E131 (= E131), E133 (= E133), E188 (= E184), E195 (= E191), H244 (= H240), E332 (= E331)
- binding : F59 (= F60), V60 (≠ A61), E418 (= E417), I422 (= I421), M426 (= M425)
7tenA Glutamine synthetase (see paper)
50% identity, 98% coverage: 5:439/442 of query aligns to 3:439/442 of 7tenA
- binding adenosine-5'-diphosphate: G128 (= G129), E130 (= E131), E182 (= E179), D196 (= D193), F197 (≠ L194), K198 (≠ R195), Y199 (= Y196), N245 (≠ H242), S247 (= S244), R319 (= R316), S327 (≠ A327), R329 (= R329)
- binding l-methionine-s-sulfoximine phosphate: E130 (= E131), E132 (= E133), E187 (= E184), E194 (= E191), N238 (= N235), G239 (= G236), H243 (= H240), R296 (= R293), E302 (= E299), R314 (= R311), R333 (= R333)
8oooA Glutamine synthetase from methanothermococcus thermolithotrophicus in complex with 2-oxoglutarate and mgatp at 2.15 a resolution (see paper)
50% identity, 99% coverage: 4:439/442 of query aligns to 1:445/447 of 8oooA
- binding 2-oxoglutaric acid: F17 (= F20), R19 (≠ Q22), A33 (= A36), R87 (= R83), V93 (= V89), P170 (≠ S161), R173 (= R164), R174 (= R165), S190 (= S181)
- binding adenosine-5'-triphosphate: E136 (= E131), E188 (= E179), F203 (≠ L194), K204 (≠ R195), F205 (≠ Y196), H251 (= H242), S253 (= S244), R325 (= R316), R335 (= R329)
8ooqB Glutamine synthetase from Methanothermococcus thermolithotrophicus (see paper)
50% identity, 98% coverage: 5:439/442 of query aligns to 1:444/446 of 8ooqB
- binding 2-oxoglutaric acid: F16 (= F20), R18 (≠ Q22), A32 (= A36), R86 (= R83), V92 (= V89), P169 (≠ S161), R172 (= R164), R173 (= R165), S189 (= S181)
- binding magnesium ion: E137 (= E133), E192 (= E184), E199 (= E191)
8ooxB Glutamine synthetase (see paper)
49% identity, 98% coverage: 6:439/442 of query aligns to 3:435/438 of 8ooxB
8oozA Glutamine synthetase (see paper)
48% identity, 98% coverage: 6:439/442 of query aligns to 3:427/430 of 8oozA
- binding adenosine-5'-triphosphate: G117 (= G129), E170 (= E179), F185 (≠ L194), K186 (≠ R195), Y187 (= Y196), N233 (≠ H242), S235 (= S244), S315 (≠ A327), R317 (= R329)
- binding magnesium ion: E119 (= E131), H231 (= H240), E319 (= E331)
A0R079 Glutamine synthetase; GS; Glutamate--ammonia ligase; Glutamine synthetase I beta; GSI beta; EC 6.3.1.2 from Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis) (see paper)
37% identity, 95% coverage: 1:420/442 of query aligns to 1:456/478 of A0R079
- K14 (= K14) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
P9WN39 Glutamine synthetase; GS; Glutamate--ammonia ligase; Glutamine synthetase I beta; GSI beta; EC 6.3.1.2 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 5 papers)
38% identity, 88% coverage: 1:390/442 of query aligns to 1:423/478 of P9WN39
- M1 (= M1) modified: Initiator methionine, Removed
- E133 (= E131) binding
- E135 (= E133) binding
- E219 (= E184) binding
- E227 (= E191) binding
- H276 (= H240) binding
- E366 (= E331) binding
- Y406 (≠ F371) modified: O-AMP-tyrosine; mutation to F: Unable to be adenylylated.
Query Sequence
>WP_028321524.1 NCBI__GCF_000422285.1:WP_028321524.1
MICQTEEDVKRIVKEKNISFIQFWFTDVLGVLKSFAVTPSELEEGLSEGMGFDGSSIEGF
ARIQESDMIAKPDVTTFQLVPWRSGDRPVARMFCDVMNPDGTPYEGDPRYVLKRLLKKVA
EKGYTFYVGPELEYFYFRNNCGTECLDTGGYFDSRPIDMGSDLRRETIFALQDMGIQVEY
SHHEVAPSQHEIDLRYDEGLRMADKTMTYRLVVKEVARKNGFYATFMPKPIFGQNGSGMH
VHQSLFKGERNAFYDPSDRYNLSDVAKHYIAGIMRHAPEITVVTNQWVNSYKRLVPGYEA
PVYVAWARRNRSAMIRVPMYKPGKEAATRIEFRSPDPSCNPYLAFAVMLGAGLEGIENKY
EMPDPIEEDIFEMNPAERKAHGITDLPGNLYAATLEAEKSSLVKKVLGEHVFNKFIENKK
IEWDMYRTHVSAFELERYLAKL
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