SitesBLAST
Comparing WP_011885444.1 NCBI__GCF_000016205.1:WP_011885444.1 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, 99% coverage: 3:442/445 of query aligns to 25:469/472 of P78061
- H282 (= H255) mutation to N: Activity is impaired to 9% of wild-type.
- R357 (= R331) mutation to Q: Activity is impaired to 3% of wild-type.
8ooqB Glutamine synthetase from Methanothermococcus thermolithotrophicus (see paper)
30% identity, 98% coverage: 4:437/445 of query aligns to 4:439/446 of 8ooqB
- binding 2-oxoglutaric acid: F16 (≠ E16), R18 (≠ E18), A32 (≠ I32), R86 (vs. gap), V92 (≠ T92), P169 (≠ D176), R172 (≠ F179), R173 (≠ E180), S189 (≠ L196)
- binding magnesium ion: E137 (= E136), E192 (= E199), E199 (= E206)
8oooA Glutamine synthetase from methanothermococcus thermolithotrophicus in complex with 2-oxoglutarate and mgatp at 2.15 a resolution (see paper)
30% identity, 97% coverage: 7:437/445 of query aligns to 8:440/447 of 8oooA
- binding 2-oxoglutaric acid: F17 (≠ E16), R19 (≠ E18), A33 (≠ I32), R87 (vs. gap), V93 (≠ T92), P170 (≠ D176), R173 (≠ F179), R174 (≠ E180), S190 (≠ L196)
- binding adenosine-5'-triphosphate: E136 (= E134), E188 (= E194), F203 (= F209), K204 (≠ M210), F205 (≠ H211), H251 (= H257), S253 (= S259), R325 (= R331), R335 (= R341)
8tfkA Glutamine synthetase (see paper)
31% identity, 98% coverage: 2:437/445 of query aligns to 3:432/440 of 8tfkA
- binding adenosine-5'-diphosphate: E128 (= E134), D194 (≠ N208), F195 (= F209), F197 (≠ H211), N243 (≠ H257), R312 (= R326), R317 (= R331), G325 (≠ A339), R327 (= R341)
- binding magnesium ion: E128 (= E134), E128 (= E134), E130 (= E136), E185 (= E199), E192 (= E206), E192 (= E206), H241 (= H255), E329 (= E343)
- binding l-methionine-s-sulfoximine phosphate: E128 (= E134), E130 (= E136), E185 (= E199), E192 (= E206), G237 (= G251), H241 (= H255), R294 (= R308), E300 (≠ A314), R312 (= R326), R331 (= R345)
8ufjB Glutamine synthetase (see paper)
31% identity, 98% coverage: 2:437/445 of query aligns to 7:436/444 of 8ufjB
7tdpA Structure of paenibacillus polymyxa gs bound to met-sox-p-adp (transition state complex) to 1.98 angstom (see paper)
34% identity, 84% coverage: 68:442/445 of query aligns to 61:436/439 of 7tdpA
- binding adenosine-5'-diphosphate: N123 (vs. gap), G125 (≠ A132), E127 (= E134), E179 (= E194), D193 (≠ N208), Y196 (≠ H211), N242 (≠ H257), S244 (= S259), R316 (= R331), R326 (= R341)
- binding magnesium ion: E127 (= E134), E127 (= E134), E129 (= E136), E184 (= E199), E191 (= E206), E191 (= E206), H240 (= H255), E328 (= E343)
- binding l-methionine-s-sulfoximine phosphate: E127 (= E134), E129 (= E136), E184 (= E199), E191 (= E206), G236 (= G251), H240 (= H255), R293 (= R308), E299 (≠ A314), R311 (= R326), R330 (= R345)
7tfaB Glutamine synthetase (see paper)
34% identity, 84% coverage: 68:442/445 of query aligns to 61:438/441 of 7tfaB
- binding glutamine: E131 (= E136), Y153 (≠ S166), E186 (= E199), G238 (= G251), H242 (= H255), R295 (= R308), E301 (≠ A314)
- binding magnesium ion: E129 (= E134), E131 (= E136), E186 (= E199), E193 (= E206), H242 (= H255), E330 (= E343)
- binding : V187 (= V200), N237 (≠ P250), G299 (≠ F312), Y300 (≠ M313), R313 (= R326), M424 (≠ A428)
Sites not aligning to the query:
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, 84% coverage: 68:442/445 of query aligns to 62:444/446 of P9WN37
- K363 (≠ Q370) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
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, 84% coverage: 68:442/445 of query aligns to 62:444/446 of A0R083
- K363 (≠ Q370) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
8oozA Glutamine synthetase (see paper)
31% identity, 84% coverage: 62:437/445 of query aligns to 50:422/430 of 8oozA
- binding adenosine-5'-triphosphate: G117 (≠ A132), E170 (= E194), F185 (= F209), K186 (≠ M210), Y187 (≠ H211), N233 (≠ H257), S235 (= S259), S315 (≠ A339), R317 (= R341)
- binding magnesium ion: E119 (= E134), H231 (= H255), E319 (= E343)
8ooxB Glutamine synthetase (see paper)
28% identity, 98% coverage: 2:437/445 of query aligns to 3:430/438 of 8ooxB
5dm3C Crystal structure of glutamine synthetase from chromohalobacter salexigens dsm 3043(csal_0679, target efi-550015) with bound adp
35% identity, 81% coverage: 77:437/445 of query aligns to 58:390/396 of 5dm3C
- active site: E115 (= E134), E117 (= E136), E162 (= E199), E169 (= E206), H218 (= H255), R286 (= R326), E303 (= E343), R305 (= R345)
- binding adenosine-5'-diphosphate: R173 (≠ M210), C174 (≠ H211), H220 (= H257), S222 (= S259), R301 (= R341)
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, 90% coverage: 42:442/445 of query aligns to 32:440/443 of 4lnkA
- active site: D52 (= D62), E131 (= E134), E133 (= E136), E188 (= E199), E195 (= E206), H244 (= H255), R315 (= R326), E332 (= E343), R334 (= R345)
- binding adenosine-5'-diphosphate: K43 (≠ Q53), M50 (≠ P60), F198 (= F209), Y200 (≠ H211), N246 (≠ H257), S248 (= S259), S324 (= S335), S328 (≠ A339), R330 (= R341)
- binding glutamic acid: E133 (= E136), E188 (= E199), V189 (= V200), N239 (≠ P250), G240 (= G251), G242 (≠ A253), E303 (≠ A314)
- binding magnesium ion: E131 (= E134), E188 (= E199), E195 (= E206), H244 (= H255), E332 (= E343)
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, 90% coverage: 42:442/445 of query aligns to 32:440/443 of 4lniA
- active site: D52 (= D62), E131 (= E134), E133 (= E136), E188 (= E199), E195 (= E206), H244 (= H255), R315 (= R326), E332 (= E343), R334 (= R345)
- binding adenosine-5'-diphosphate: E131 (= E134), E183 (= E194), D197 (≠ N208), Y200 (≠ H211), N246 (≠ H257), S248 (= S259), R320 (= R331), R330 (= R341)
- binding magnesium ion: E131 (= E134), E131 (= E134), E133 (= E136), E188 (= E199), E195 (= E206), E195 (= E206), H244 (= H255), E332 (= E343)
- binding l-methionine-s-sulfoximine phosphate: E133 (= E136), E188 (= E199), H244 (= H255), R297 (= R308), E303 (≠ A314), R315 (= R326), R334 (= R345)
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, 90% coverage: 42:442/445 of query aligns to 33:441/444 of P12425
- G59 (vs. gap) 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 (≠ G67) 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 (= E134) binding Mg(2+)
- E134 (= E136) binding Mg(2+)
- E189 (= E199) binding Mg(2+)
- V190 (= V200) 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 (= E206) binding Mg(2+)
- G241 (= G251) binding L-glutamate
- H245 (= H255) binding Mg(2+)
- G302 (≠ F312) 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 (≠ A314) 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 (= P316) 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 (= E343) binding Mg(2+)
- E424 (= E425) 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)
30% identity, 90% coverage: 42:442/445 of query aligns to 36:444/447 of 4s0rD
- active site: D56 (= D62), E135 (= E134), E137 (= E136), E192 (= E199), E199 (= E206), H248 (= H255), R319 (= R326), E336 (= E343), R338 (= R345)
- binding glutamine: E137 (= E136), E192 (= E199), R301 (= R308), E307 (≠ A314)
- binding magnesium ion: I66 (≠ V68), E135 (= E134), E135 (= E134), E199 (= E206), H248 (= H255), H248 (= H255), E336 (= E343), H419 (≠ A417)
- binding : F63 (≠ L65), V64 (≠ T66), R65 (≠ G67), I66 (≠ V68), D161 (≠ G158), G241 (≠ D248), V242 (≠ E249), N243 (≠ P250), G305 (≠ F312), Y306 (≠ M313), Y376 (= Y383), I426 (≠ T424), M430 (≠ A428)
7tdvC Glutamine synthetase (see paper)
28% identity, 99% coverage: 2:442/445 of query aligns to 5:440/443 of 7tdvC
- binding adenosine-5'-diphosphate: G129 (≠ A132), E131 (= E134), E183 (= E194), D197 (≠ N208), F198 (= F209), K199 (≠ M210), Y200 (≠ H211), N246 (≠ H257), V247 (≠ Q258), S248 (= S259), R320 (= R331), S328 (≠ A339), R330 (= R341)
- binding magnesium ion: E131 (= E134), E131 (= E134), E133 (= E136), E188 (= E199), E195 (= E206), E195 (= E206), H244 (= H255), E332 (= E343)
- binding l-methionine-s-sulfoximine phosphate: E131 (= E134), E133 (= E136), E188 (= E199), E195 (= E206), G240 (= G251), H244 (= H255), R297 (= R308), E303 (≠ A314), R315 (= R326)
7tf6A Glutamine synthetase (see paper)
30% identity, 90% coverage: 42:442/445 of query aligns to 31:435/438 of 7tf6A
- binding glutamine: E128 (= E136), E183 (= E199), G235 (= G251), H239 (= H255), R292 (= R308), E298 (≠ A314)
- binding magnesium ion: E126 (= E134), E128 (= E136), E183 (= E199), E190 (= E206), H239 (= H255), E327 (= E343)
- binding : F58 (≠ L65), R60 (≠ G67), G232 (≠ D248), N234 (≠ P250), G296 (≠ F312), Y297 (≠ M313), R310 (= R326), Y367 (= Y383), Y421 (≠ A428), Q433 (≠ H440)
Sites not aligning to the query:
7tf9S L. Monocytogenes gs(14)-q-glnr peptide (see paper)
28% identity, 99% coverage: 2:442/445 of query aligns to 5:440/443 of 7tf9S
- binding glutamine: E133 (= E136), Y155 (≠ S166), E188 (= E199), G240 (= G251), G242 (≠ A253), R297 (= R308), E303 (≠ A314)
- binding magnesium ion: E131 (= E134), E133 (= E136), E188 (= E199), E195 (= E206), H244 (= H255), E332 (= E343)
- binding : F59 (≠ L65), V60 (≠ T66), E418 (≠ A420), I422 (≠ T424), M426 (≠ A428)
7tenA Glutamine synthetase (see paper)
28% identity, 99% coverage: 2:442/445 of query aligns to 4:439/442 of 7tenA
- binding adenosine-5'-diphosphate: G128 (≠ A132), E130 (= E134), E182 (= E194), D196 (≠ N208), F197 (= F209), K198 (≠ M210), Y199 (≠ H211), N245 (≠ H257), S247 (= S259), R319 (= R331), S327 (≠ A339), R329 (= R341)
- binding l-methionine-s-sulfoximine phosphate: E130 (= E134), E132 (= E136), E187 (= E199), E194 (= E206), N238 (≠ P250), G239 (= G251), H243 (= H255), R296 (= R308), E302 (≠ A314), R314 (= R326), R333 (= R345)
Query Sequence
>WP_011885444.1 NCBI__GCF_000016205.1:WP_011885444.1
MQSELSEFLRQHRITEVEAIIPDMAGIARGKIIPRNKFESGESMRLPQAVMVQTVTGDYP
EDGSLTGVTDPDMVCVPDPSTICLIPWAVDPTAQVIHDCVHFDGSPVEISPRYVLRRVLD
LYEAKGWKPVVAPELEFYLVDMNADPDLPLRPPVGRTGRAETGRQSYSIEAVNEFDPLFE
DIYEYCEMQGLDIETLIHEVGAAQMEINFMHGDALSLADQVFLFKRTVREAALRHNMYAT
FMAKPMEDEPGSAMHIHQSLADARTGRNLFADEGGDVSPMFQSYLAGLQKYTPALMPIFA
PYINSYRRLSRFMAAPINVQWGYDNRTVGFRIPQSAPAARRIENRIPGVDCNPYLAFAAT
LAAGYLGLTQQLAPTEPIASDGYDLPYQLPRNLEEGISLMAACTPLAGILGDKFVKAYLA
LKETEYEAFFRVISSWERRHLLLHV
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