SitesBLAST
Comparing WP_011780791.1 NCBI__GCF_000015305.1:WP_011780791.1 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)
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)
95% identity, 100% coverage: 1:446/446 of query aligns to 1:446/446 of A0R083
- K363 (= K363) 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)
89% identity, 100% coverage: 1:446/446 of query aligns to 1:446/446 of P9WN37
- K363 (= K363) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
8ooxB Glutamine synthetase (see paper)
49% identity, 98% coverage: 8:445/446 of query aligns to 6:436/438 of 8ooxB
8tfkA Glutamine synthetase (see paper)
48% identity, 99% coverage: 6:446/446 of query aligns to 4:439/440 of 8tfkA
- binding adenosine-5'-diphosphate: E128 (= E132), D194 (= D198), F195 (≠ L199), F197 (≠ Y201), N243 (≠ H247), R312 (= R316), R317 (= R321), G325 (≠ S332), R327 (= R334)
- binding magnesium ion: E128 (= E132), E128 (= E132), E130 (= E134), E185 (= E189), E192 (= E196), E192 (= E196), H241 (= H245), E329 (= E336)
- binding l-methionine-s-sulfoximine phosphate: E128 (= E132), E130 (= E134), E185 (= E189), E192 (= E196), G237 (= G241), H241 (= H245), R294 (= R298), E300 (= E304), R312 (= R316), R331 (= R338)
8ufjB Glutamine synthetase (see paper)
48% identity, 99% coverage: 6:446/446 of query aligns to 8:443/444 of 8ufjB
8oozA Glutamine synthetase (see paper)
48% identity, 98% coverage: 8:445/446 of query aligns to 6:428/430 of 8oozA
- binding adenosine-5'-triphosphate: G117 (≠ H130), E170 (= E184), F185 (≠ L199), K186 (≠ R200), Y187 (= Y201), N233 (≠ H247), S235 (= S249), S315 (= S332), R317 (= R334)
- binding magnesium ion: E119 (= E132), H231 (= H245), E319 (= E336)
7tfaB Glutamine synthetase (see paper)
46% identity, 99% coverage: 6:446/446 of query aligns to 5:440/441 of 7tfaB
- binding glutamine: E131 (= E134), Y153 (= Y156), E186 (= E189), G238 (= G241), H242 (= H245), R295 (= R298), E301 (= E304)
- binding magnesium ion: E129 (= E132), E131 (= E134), E186 (= E189), E193 (= E196), H242 (= H245), E330 (= E336)
- binding : Y58 (≠ F59), R60 (= R61), V187 (≠ G190), N237 (≠ P240), G299 (= G302), Y300 (≠ G303), R313 (= R316), M424 (≠ N430)
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)
46% identity, 99% coverage: 6:445/446 of query aligns to 6:441/443 of 4lnkA
- active site: D52 (= D52), E131 (= E132), E133 (= E134), E188 (= E189), E195 (= E196), H244 (= H245), R315 (= R316), E332 (= E336), R334 (= R338)
- binding adenosine-5'-diphosphate: K43 (≠ G43), M50 (≠ G50), F198 (≠ L199), Y200 (= Y201), N246 (≠ H247), S248 (= S249), S324 (≠ H328), S328 (= S332), R330 (= R334)
- binding glutamic acid: E133 (= E134), E188 (= E189), V189 (≠ G190), N239 (≠ P240), G240 (= G241), G242 (≠ A243), E303 (= E304)
- binding magnesium ion: E131 (= E132), E188 (= E189), E195 (= E196), H244 (= H245), E332 (= E336)
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)
46% identity, 99% coverage: 6:445/446 of query aligns to 6:441/443 of 4lniA
- active site: D52 (= D52), E131 (= E132), E133 (= E134), E188 (= E189), E195 (= E196), H244 (= H245), R315 (= R316), E332 (= E336), R334 (= R338)
- binding adenosine-5'-diphosphate: E131 (= E132), E183 (= E184), D197 (= D198), Y200 (= Y201), N246 (≠ H247), S248 (= S249), R320 (= R321), R330 (= R334)
- binding magnesium ion: E131 (= E132), E131 (= E132), E133 (= E134), E188 (= E189), E195 (= E196), E195 (= E196), H244 (= H245), E332 (= E336)
- binding l-methionine-s-sulfoximine phosphate: E133 (= E134), E188 (= E189), H244 (= H245), R297 (= R298), E303 (= E304), R315 (= R316), R334 (= R338)
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)
46% identity, 99% coverage: 6:445/446 of query aligns to 7:442/444 of P12425
- G59 (= G58) 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 (= R61) 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 (= E132) binding Mg(2+)
- E134 (= E134) binding Mg(2+)
- E189 (= E189) binding Mg(2+)
- V190 (≠ G190) 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 (= E196) binding Mg(2+)
- G241 (= G241) binding L-glutamate
- H245 (= H245) binding Mg(2+)
- G302 (= G302) 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 (= E304) 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 (= P306) 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 (= E336) 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)
46% identity, 99% coverage: 6:445/446 of query aligns to 10:445/447 of 4s0rD
- active site: D56 (= D52), E135 (= E132), E137 (= E134), E192 (= E189), E199 (= E196), H248 (= H245), R319 (= R316), E336 (= E336), R338 (= R338)
- binding glutamine: E137 (= E134), E192 (= E189), R301 (= R298), E307 (= E304)
- binding magnesium ion: I66 (≠ V62), E135 (= E132), E135 (= E132), E199 (= E196), H248 (= H245), H248 (= H245), E336 (= E336), H419 (≠ F419)
- binding : F63 (= F59), V64 (≠ A60), R65 (= R61), I66 (≠ V62), D161 (= D158), G241 (≠ E238), V242 (≠ H239), N243 (≠ P240), G305 (= G302), Y306 (≠ G303), Y376 (≠ W376), I426 (≠ S426), M430 (≠ N430)
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: 6:446/446 of query aligns to 5:438/439 of 7tdpA
- binding adenosine-5'-diphosphate: N123 (≠ Y128), G125 (≠ H130), E127 (= E132), E179 (= E184), D193 (= D198), Y196 (= Y201), N242 (≠ H247), S244 (= S249), R316 (= R321), R326 (= R334)
- binding magnesium ion: E127 (= E132), E127 (= E132), E129 (= E134), E184 (= E189), E191 (= E196), E191 (= E196), H240 (= H245), E328 (= E336)
- binding l-methionine-s-sulfoximine phosphate: E127 (= E132), E129 (= E134), E184 (= E189), E191 (= E196), G236 (= G241), H240 (= H245), R293 (= R298), E299 (= E304), R311 (= R316), R330 (= R338)
8oooA Glutamine synthetase from methanothermococcus thermolithotrophicus in complex with 2-oxoglutarate and mgatp at 2.15 a resolution (see paper)
43% identity, 99% coverage: 5:446/446 of query aligns to 3:447/447 of 8oooA
- binding 2-oxoglutaric acid: F17 (= F19), R19 (= R21), A33 (= A35), R87 (≠ T82), V93 (≠ S90), P170 (= P166), R173 (= R169), R174 (= R170), S190 (= S186)
- binding adenosine-5'-triphosphate: E136 (= E132), E188 (= E184), F203 (≠ L199), K204 (≠ R200), F205 (≠ Y201), H251 (= H247), S253 (= S249), R325 (= R321), R335 (= R334)
8ooqB Glutamine synthetase from Methanothermococcus thermolithotrophicus (see paper)
43% identity, 99% coverage: 5:446/446 of query aligns to 2:446/446 of 8ooqB
- binding 2-oxoglutaric acid: F16 (= F19), R18 (= R21), A32 (= A35), R86 (≠ T82), V92 (≠ S90), P169 (= P166), R172 (= R169), R173 (= R170), S189 (= S186)
- binding magnesium ion: E137 (= E134), E192 (= E189), E199 (= E196)
7tf9S L. Monocytogenes gs(14)-q-glnr peptide (see paper)
45% identity, 99% coverage: 6:446/446 of query aligns to 6:442/443 of 7tf9S
- binding glutamine: E133 (= E134), Y155 (= Y156), E188 (= E189), G240 (= G241), G242 (≠ A243), R297 (= R298), E303 (= E304)
- binding magnesium ion: E131 (= E132), E133 (= E134), E188 (= E189), E195 (= E196), H244 (= H245), E332 (= E336)
- binding : F59 (= F59), V60 (≠ A60), E418 (≠ R422), I422 (≠ S426), M426 (≠ N430)
7tenA Glutamine synthetase (see paper)
45% identity, 99% coverage: 6:446/446 of query aligns to 5:441/442 of 7tenA
- binding adenosine-5'-diphosphate: G128 (≠ H130), E130 (= E132), E182 (= E184), D196 (= D198), F197 (≠ L199), K198 (≠ R200), Y199 (= Y201), N245 (≠ H247), S247 (= S249), R319 (= R321), S327 (= S332), R329 (= R334)
- binding l-methionine-s-sulfoximine phosphate: E130 (= E132), E132 (= E134), E187 (= E189), E194 (= E196), N238 (≠ P240), G239 (= G241), H243 (= H245), R296 (= R298), E302 (= E304), R314 (= R316), R333 (= R338)
7tdvC Glutamine synthetase (see paper)
43% identity, 99% coverage: 6:445/446 of query aligns to 6:441/443 of 7tdvC
- binding adenosine-5'-diphosphate: G129 (≠ H130), E131 (= E132), E183 (= E184), D197 (= D198), F198 (≠ L199), K199 (≠ R200), Y200 (= Y201), N246 (≠ H247), V247 (≠ M248), S248 (= S249), R320 (= R321), S328 (= S332), R330 (= R334)
- binding magnesium ion: E131 (= E132), E131 (= E132), E133 (= E134), E188 (= E189), E195 (= E196), E195 (= E196), H244 (= H245), E332 (= E336)
- binding l-methionine-s-sulfoximine phosphate: E131 (= E132), E133 (= E134), E188 (= E189), E195 (= E196), G240 (= G241), H244 (= H245), R297 (= R298), E303 (= E304), R315 (= R316)
7tf6A Glutamine synthetase (see paper)
42% identity, 99% coverage: 6:445/446 of query aligns to 5:436/438 of 7tf6A
- binding glutamine: E128 (= E134), E183 (= E189), G235 (= G241), H239 (= H245), R292 (= R298), E298 (= E304)
- binding magnesium ion: E126 (= E132), E128 (= E134), E183 (= E189), E190 (= E196), H239 (= H245), E327 (= E336)
- binding : F58 (= F59), R60 (= R61), G232 (≠ E238), N234 (≠ P240), G296 (= G302), Y297 (≠ G303), R310 (= R316), Y367 (≠ W376), Y421 (≠ N430), Q433 (≠ N442)
Sites not aligning to the query:
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)
35% identity, 99% coverage: 6:446/446 of query aligns to 4:469/469 of P0A9C5
- Y398 (≠ W376) modified: O-AMP-tyrosine
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
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)
35% identity, 99% coverage: 6:446/446 of query aligns to 4:469/469 of P0A1P6
- E130 (= E132) binding Mn(2+)
- E132 (= E134) binding Mn(2+)
- E208 (= E184) binding ATP
- E213 (= E189) binding Mn(2+)
- E221 (= E196) binding Mn(2+)
- NG 265:266 (≠ PG 240:241) binding L-glutamate
- H270 (= H245) binding Mn(2+)
- HMS 272:274 (= HMS 247:249) binding ATP
- R322 (= R298) binding L-glutamate
- E358 (= E336) binding Mn(2+)
- R360 (= R338) binding L-glutamate
Query Sequence
>WP_011780791.1 NCBI__GCF_000015305.1:WP_011780791.1
MDRQMEFVLRTLEERDIRFVRLWFTDVLGYLKSVAIAPAELEGAFEEGIGFDGSSIEGFA
RVSEADMVARPDPSTFQVLPWTTSAGNHYSARMFCDITMPDGSPSWADSRHVLRRQLSKA
SDLGFSCYVHPEIEFFLLKPGPDDGTQPIPADNGGYFDQAVHDAAPNFRRHAIDALEQMG
ISVEFSHHEGAPGQQEIDLRYADALSMADNVMTFRYLVKEVALADGVRASFMPKPFAEHP
GSAMHTHMSLFEGDTNAFHSPDDPLQLSDVGKSFIAGILEHANEISAVTNQWVNSYKRLV
HGGEAPTAASWGAANRSALVRVPMYTPHKVSSRRVEVRSPDSACNPYLTFAVLLAAGLRG
IEKNYVLGPQAEDNVWSLTPEERRAMGYKELPGSLGVALTEMENSELVAEALGEHVFDFF
LRNKRSEWENYRSHVTPFELKNYLSL
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