SitesBLAST
Comparing WP_004045354.1 NCBI__GCF_000337315.1:WP_004045354.1 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)
8ooxB Glutamine synthetase (see paper)
58% identity, 95% coverage: 23:456/456 of query aligns to 10:438/438 of 8ooxB
7tfaB Glutamine synthetase (see paper)
57% identity, 96% coverage: 19:456/456 of query aligns to 7:441/441 of 7tfaB
- binding glutamine: E131 (= E145), Y153 (= Y167), E186 (= E200), G238 (= G252), H242 (= H256), R295 (= R309), E301 (= E315)
- binding magnesium ion: E129 (= E143), E131 (= E145), E186 (= E200), E193 (= E207), H242 (= H256), E330 (= E345)
- binding : Y58 (≠ F70), R60 (= R72), V187 (= V201), N237 (= N251), G299 (= G313), Y300 (= Y314), R313 (= R327), M424 (≠ D439)
7tdvC Glutamine synthetase (see paper)
56% identity, 95% coverage: 23:456/456 of query aligns to 12:443/443 of 7tdvC
- binding adenosine-5'-diphosphate: G129 (≠ A141), E131 (= E143), E183 (= E195), D197 (≠ N209), F198 (= F210), K199 (≠ T211), Y200 (= Y212), N246 (≠ H258), V247 (≠ I259), S248 (= S260), R320 (= R332), S328 (≠ A341), R330 (= R343)
- binding magnesium ion: E131 (= E143), E131 (= E143), E133 (= E145), E188 (= E200), E195 (= E207), E195 (= E207), H244 (= H256), E332 (= E345)
- binding l-methionine-s-sulfoximine phosphate: E131 (= E143), E133 (= E145), E188 (= E200), E195 (= E207), G240 (= G252), H244 (= H256), R297 (= R309), E303 (= E315), R315 (= R327)
7tdpA Structure of paenibacillus polymyxa gs bound to met-sox-p-adp (transition state complex) to 1.98 angstom (see paper)
57% identity, 96% coverage: 19:456/456 of query aligns to 7:439/439 of 7tdpA
- binding adenosine-5'-diphosphate: N123 (= N139), G125 (≠ A141), E127 (= E143), E179 (= E195), D193 (≠ N209), Y196 (= Y212), N242 (≠ H258), S244 (= S260), R316 (= R332), R326 (= R343)
- binding magnesium ion: E127 (= E143), E127 (= E143), E129 (= E145), E184 (= E200), E191 (= E207), E191 (= E207), H240 (= H256), E328 (= E345)
- binding l-methionine-s-sulfoximine phosphate: E127 (= E143), E129 (= E145), E184 (= E200), E191 (= E207), G236 (= G252), H240 (= H256), R293 (= R309), E299 (= E315), R311 (= R327), R330 (= R347)
7tf6A Glutamine synthetase (see paper)
56% identity, 95% coverage: 24:456/456 of query aligns to 12:438/438 of 7tf6A
- binding glutamine: E128 (= E145), E183 (= E200), G235 (= G252), H239 (= H256), R292 (= R309), E298 (= E315)
- binding magnesium ion: E126 (= E143), E128 (= E145), E183 (= E200), E190 (= E207), H239 (= H256), E327 (= E345)
- binding : F58 (= F70), R60 (= R72), G232 (≠ R249), N234 (= N251), G296 (= G313), Y297 (= Y314), R310 (= R327), Y367 (= Y385), Y421 (≠ D439), Q433 (≠ R451), Q437 (≠ T455)
8oooA Glutamine synthetase from methanothermococcus thermolithotrophicus in complex with 2-oxoglutarate and mgatp at 2.15 a resolution (see paper)
54% identity, 96% coverage: 16:454/456 of query aligns to 3:446/447 of 8oooA
- binding 2-oxoglutaric acid: F17 (= F30), R19 (= R32), A33 (≠ S46), R87 (= R93), V93 (≠ A99), P170 (≠ S177), R173 (= R180), R174 (= R181), S190 (= S197)
- binding adenosine-5'-triphosphate: E136 (= E143), E188 (= E195), F203 (= F210), K204 (≠ T211), F205 (≠ Y212), H251 (= H258), S253 (= S260), R325 (= R332), R335 (= R343)
8ooqB Glutamine synthetase from Methanothermococcus thermolithotrophicus (see paper)
54% identity, 96% coverage: 16:454/456 of query aligns to 2:445/446 of 8ooqB
- binding 2-oxoglutaric acid: F16 (= F30), R18 (= R32), A32 (≠ S46), R86 (= R93), V92 (≠ A99), P169 (≠ S177), R172 (= R180), R173 (= R181), S189 (= S197)
- binding magnesium ion: E137 (= E145), E192 (= E200), E199 (= E207)
8oozA Glutamine synthetase (see paper)
56% identity, 95% coverage: 23:456/456 of query aligns to 10:430/430 of 8oozA
- binding adenosine-5'-triphosphate: G117 (≠ A141), E170 (= E195), F185 (= F210), K186 (≠ T211), Y187 (= Y212), N233 (≠ H258), S235 (= S260), S315 (≠ A341), R317 (= R343)
- binding magnesium ion: E119 (= E143), H231 (= H256), E319 (= E345)
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)
54% identity, 95% coverage: 23:456/456 of query aligns to 13:444/444 of P12425
- G59 (= G69) 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 (= R72) 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 (= E143) binding Mg(2+)
- E134 (= E145) binding Mg(2+)
- E189 (= E200) binding Mg(2+)
- V190 (= V201) 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 (= E207) binding Mg(2+)
- G241 (= G252) binding L-glutamate
- H245 (= H256) binding Mg(2+)
- G302 (= G313) 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 (= E315) 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 (= P317) 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 (= E436) 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)
54% identity, 95% coverage: 23:456/456 of query aligns to 12:443/443 of 4lnkA
- active site: D52 (= D63), E131 (= E143), E133 (= E145), E188 (= E200), E195 (= E207), H244 (= H256), R315 (= R327), E332 (= E345), R334 (= R347)
- binding adenosine-5'-diphosphate: K43 (= K54), M50 (≠ Y61), F198 (= F210), Y200 (= Y212), N246 (≠ H258), S248 (= S260), S324 (≠ A336), S328 (≠ A341), R330 (= R343)
- binding glutamic acid: E133 (= E145), E188 (= E200), V189 (= V201), N239 (= N251), G240 (= G252), G242 (= G254), E303 (= E315)
- binding magnesium ion: E131 (= E143), E188 (= E200), E195 (= E207), H244 (= H256), 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)
54% identity, 95% coverage: 23:456/456 of query aligns to 12:443/443 of 4lniA
- active site: D52 (= D63), E131 (= E143), E133 (= E145), E188 (= E200), E195 (= E207), H244 (= H256), R315 (= R327), E332 (= E345), R334 (= R347)
- binding adenosine-5'-diphosphate: E131 (= E143), E183 (= E195), D197 (≠ N209), Y200 (= Y212), N246 (≠ H258), S248 (= S260), R320 (= R332), R330 (= R343)
- binding magnesium ion: E131 (= E143), E131 (= E143), E133 (= E145), E188 (= E200), E195 (= E207), E195 (= E207), H244 (= H256), E332 (= E345)
- binding l-methionine-s-sulfoximine phosphate: E133 (= E145), E188 (= E200), H244 (= H256), R297 (= R309), E303 (= E315), R315 (= R327), R334 (= R347)
4s0rD Structure of gs-tnra complex (see paper)
54% identity, 95% coverage: 23:456/456 of query aligns to 16:447/447 of 4s0rD
- active site: D56 (= D63), E135 (= E143), E137 (= E145), E192 (= E200), E199 (= E207), H248 (= H256), R319 (= R327), E336 (= E345), R338 (= R347)
- binding glutamine: E137 (= E145), E192 (= E200), R301 (= R309), E307 (= E315)
- binding magnesium ion: I66 (= I73), E135 (= E143), E135 (= E143), E199 (= E207), H248 (= H256), H248 (= H256), E336 (= E345), H419 (≠ K428)
- binding : F63 (= F70), V64 (= V71), R65 (= R72), I66 (= I73), D161 (= D169), G241 (≠ R249), V242 (≠ I250), N243 (= N251), G305 (= G313), Y306 (= Y314), Y376 (= Y385), I426 (≠ S435), M430 (≠ D439)
7tf9S L. Monocytogenes gs(14)-q-glnr peptide (see paper)
55% identity, 95% coverage: 24:456/456 of query aligns to 13:443/443 of 7tf9S
- binding glutamine: E133 (= E145), Y155 (= Y167), E188 (= E200), G240 (= G252), G242 (= G254), R297 (= R309), E303 (= E315)
- binding magnesium ion: E131 (= E143), E133 (= E145), E188 (= E200), E195 (= E207), H244 (= H256), E332 (= E345)
- binding : F59 (= F70), V60 (= V71), E418 (= E431), I422 (≠ S435), M426 (≠ D439)
7tenA Glutamine synthetase (see paper)
55% identity, 95% coverage: 24:456/456 of query aligns to 12:442/442 of 7tenA
- binding adenosine-5'-diphosphate: G128 (≠ A141), E130 (= E143), E182 (= E195), D196 (≠ N209), F197 (= F210), K198 (≠ T211), Y199 (= Y212), N245 (≠ H258), S247 (= S260), R319 (= R332), S327 (≠ A341), R329 (= R343)
- binding l-methionine-s-sulfoximine phosphate: E130 (= E143), E132 (= E145), E187 (= E200), E194 (= E207), N238 (= N251), G239 (= G252), H243 (= H256), R296 (= R309), E302 (= E315), R314 (= R327), R333 (= R347)
8ufjB Glutamine synthetase (see paper)
54% identity, 96% coverage: 19:456/456 of query aligns to 10:444/444 of 8ufjB
8tfkA Glutamine synthetase (see paper)
54% identity, 96% coverage: 19:456/456 of query aligns to 6:440/440 of 8tfkA
- binding adenosine-5'-diphosphate: E128 (= E143), D194 (≠ N209), F195 (= F210), F197 (≠ Y212), N243 (≠ H258), R312 (= R327), R317 (= R332), G325 (≠ A341), R327 (= R343)
- binding magnesium ion: E128 (= E143), E128 (= E143), E130 (= E145), E185 (= E200), E192 (= E207), E192 (= E207), H241 (= H256), E329 (= E345)
- binding l-methionine-s-sulfoximine phosphate: E128 (= E143), E130 (= E145), E185 (= E200), E192 (= E207), G237 (= G252), H241 (= H256), R294 (= R309), E300 (= E315), R312 (= R327), R331 (= 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)
48% identity, 96% coverage: 15:453/456 of query aligns to 4:444/446 of A0R083
- K363 (= K372) 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)
47% identity, 96% coverage: 15:453/456 of query aligns to 4:444/446 of P9WN37
- K363 (= K372) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
1fpyA Crystal structure of glutamine synthetase from salmonella typhimurium with inhibitor phosphinothricin (see paper)
40% identity, 92% coverage: 16:436/456 of query aligns to 2:449/468 of 1fpyA
- binding adenosine-5'-diphosphate: G127 (≠ A141), E129 (= E143), E207 (= E195), T223 (≠ F210), F225 (≠ Y212), H271 (= H258), S273 (= S260), R355 (= R343), E357 (= E345)
- binding manganese (ii) ion: E129 (= E143), E131 (= E145), E212 (= E200), E220 (= E207), H269 (= H256), E357 (= E345)
- binding phosphinothricin: E131 (= E145), E212 (= E200), G265 (= G252), H269 (= H256), R321 (= R309), E327 (= E315), R359 (= R347)
1f1hA Crystal structure of glutamine synthetase from salmonella typhimurium with thallium ions (see paper)
40% identity, 92% coverage: 16:436/456 of query aligns to 2:449/468 of 1f1hA
- binding adenosine-5'-diphosphate: E129 (= E143), E207 (= E195), H210 (= H198), E220 (= E207), T223 (≠ F210), F225 (≠ Y212), H271 (= H258), S273 (= S260), R355 (= R343)
- binding manganese (ii) ion: E129 (= E143), E131 (= E145), E212 (= E200), E220 (= E207), H269 (= H256), E357 (= E345)
Query Sequence
>WP_004045354.1 NCBI__GCF_000337315.1:WP_004045354.1
MTEDNALTDGGLSDEAQAVIDEIEEKNVDFLRLQFTDILGTVKNVSIPASQAEKAFTEGI
YFDGSSIDGFVRIQESDMRLEPDPSTFAVLPWRKKENSAAGRLICDVFNTSTGEPFSGDP
RGVLKRAIERAEELGYDVNVAPEPEFFLFEEDEDGRATTVTNDAGGYFDLAPKDLASDVR
RDIIYGLESMGFDIEASHHEVAEGQHEINFTYDDALSTADNVATFRSVVRAIAAEHDLHA
TFMPKPIPRINGSGMHTHISLFKDGENAFHDGDDEFDLSDTAKSFVAGILDHAPAITAVA
DPTVNSYKRLVPGYEAPVYIAWSDRNRSALIRKPAARTPAASRIEARFPDPSCNPYLAFA
ALIHAGLDGVEKGLDCPDPVRENIYEFDEAKREEYGIETLPKDLGGAVDALEEDEVIQEA
LGDHVFEKFVEAKRSEFKDYLVDVSQWELDRYLETF
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