SitesBLAST
Comparing GFF3214 FitnessBrowser__Marino:GFF3214 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)
7cqwA Gmas/adp complex-conformation 1 (see paper)
40% identity, 95% coverage: 16:444/452 of query aligns to 10:423/430 of 7cqwA
7cquA Gmas/adp/metsox-p complex (see paper)
40% identity, 95% coverage: 16:444/452 of query aligns to 9:422/429 of 7cquA
- binding adenosine-5'-diphosphate: E121 (= E129), Y173 (= Y184), N187 (≠ D198), W188 (≠ F199), D189 (≠ K200), Y190 (= Y201), H236 (≠ N247), L237 (≠ M248), S238 (= S249), R316 (= R332), R322 (= R339)
- binding magnesium ion: E121 (= E129), E121 (= E129), E123 (= E131), E178 (= E189), E185 (= E196), E185 (= E196), H234 (= H245), E324 (= E341)
- binding l-methionine-s-sulfoximine phosphate: E121 (= E129), E123 (= E131), E178 (= E189), E185 (= E196), T229 (= T240), G230 (= G241), H234 (= H245), R287 (= R303), W299 (= W315), R311 (= R327), R326 (= R343)
7cqqA Gmas in complex with amppnp and metsox (see paper)
40% identity, 95% coverage: 16:444/452 of query aligns to 9:422/429 of 7cqqA
- binding phosphoaminophosphonic acid-adenylate ester: E121 (= E129), Y173 (= Y184), E185 (= E196), N187 (≠ D198), D189 (≠ K200), Y190 (= Y201), H234 (= H245), H236 (≠ N247), S238 (= S249), R311 (= R327), R316 (= R332), R322 (= R339), E324 (= E341)
- binding magnesium ion: E121 (= E129), E121 (= E129), E123 (= E131), E178 (= E189), E185 (= E196), E185 (= E196), H234 (= H245), E324 (= E341)
- binding (2s)-2-amino-4-(methylsulfonimidoyl)butanoic acid: E123 (= E131), E178 (= E189), T229 (= T240), H234 (= H245), R287 (= R303), W299 (= W315), R311 (= R327), R326 (= R343)
7cqnA Gmas in complex with amppcp (see paper)
40% identity, 95% coverage: 16:444/452 of query aligns to 9:422/429 of 7cqnA
- binding phosphomethylphosphonic acid adenylate ester: G45 (≠ L52), D61 (≠ E69), E121 (= E129), Y173 (= Y184), Q174 (≠ S185), W188 (≠ F199), D189 (≠ K200), Y190 (= Y201), H236 (≠ N247), S238 (= S249), R311 (= R327), R316 (= R332), R322 (= R339)
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)
38% identity, 98% coverage: 12:452/452 of query aligns to 10:444/444 of P12425
- G59 (= G60) 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 (≠ Q63) 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 (= E129) binding
- E134 (= E131) binding
- E189 (= E189) binding
- V190 (≠ D190) 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
- G241 (= G241) binding
- H245 (= H245) binding
- G302 (≠ S313) 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 (≠ W315) 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 (= E341) binding
- E424 (= E432) 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)
38% identity, 98% coverage: 12:452/452 of query aligns to 13:447/447 of 4s0rD
- active site: D56 (≠ T54), E135 (= E129), E137 (= E131), E192 (= E189), E199 (= E196), H248 (= H245), R319 (= R327), E336 (= E341), R338 (= R343)
- binding glutamine: E137 (= E131), E192 (= E189), R301 (= R303), E307 (≠ W315)
- binding magnesium ion: I66 (= I65), E135 (= E129), E135 (= E129), E199 (= E196), H248 (= H245), H248 (= H245), E336 (= E341), H419 (≠ S424)
- binding : F63 (≠ V61), V64 (≠ P62), R65 (≠ Q63), I66 (= I65), D161 (≠ C156), G241 (≠ D238), V242 (≠ R239), N243 (≠ T240), G305 (≠ S313), Y306 (≠ T314), Y376 (= Y381), I426 (≠ G431), M430 (≠ S435)
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)
38% identity, 98% coverage: 12:452/452 of query aligns to 9:443/443 of 4lnkA
- active site: D52 (≠ T54), E131 (= E129), E133 (= E131), E188 (= E189), E195 (= E196), H244 (= H245), R315 (= R327), E332 (= E341), R334 (= R343)
- binding adenosine-5'-diphosphate: K43 (≠ Q45), M50 (≠ L52), F198 (= F199), Y200 (= Y201), N246 (= N247), S248 (= S249), S324 (vs. gap), S328 (≠ G337), R330 (= R339)
- binding glutamic acid: E133 (= E131), E188 (= E189), V189 (≠ D190), N239 (≠ T240), G240 (= G241), G242 (= G243), E303 (≠ W315)
- binding magnesium ion: E131 (= E129), E188 (= E189), E195 (= E196), H244 (= H245), E332 (= E341)
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)
38% identity, 98% coverage: 12:452/452 of query aligns to 9:443/443 of 4lniA
- active site: D52 (≠ T54), E131 (= E129), E133 (= E131), E188 (= E189), E195 (= E196), H244 (= H245), R315 (= R327), E332 (= E341), R334 (= R343)
- binding adenosine-5'-diphosphate: E131 (= E129), E183 (≠ Y184), D197 (= D198), Y200 (= Y201), N246 (= N247), S248 (= S249), R320 (= R332), R330 (= R339)
- binding magnesium ion: E131 (= E129), E131 (= E129), E133 (= E131), E188 (= E189), E195 (= E196), E195 (= E196), H244 (= H245), E332 (= E341)
- binding l-methionine-s-sulfoximine phosphate: E133 (= E131), E188 (= E189), H244 (= H245), R297 (= R303), E303 (≠ W315), R315 (= R327), R334 (= R343)
7tf6A Glutamine synthetase (see paper)
37% identity, 97% coverage: 16:452/452 of query aligns to 13:438/438 of 7tf6A
- binding glutamine: E128 (= E131), E183 (= E189), G235 (= G241), H239 (= H245), R292 (= R303), E298 (≠ W315)
- binding magnesium ion: E126 (= E129), E128 (= E131), E183 (= E189), E190 (= E196), H239 (= H245), E327 (= E341)
- binding : F58 (≠ V61), R60 (≠ Q63), G232 (≠ D238), N234 (≠ T240), G296 (≠ S313), Y297 (≠ T314), R310 (= R327), Y367 (= Y381), Y421 (≠ S435), Q433 (≠ R447), Q437 (≠ M451)
7tdvC Glutamine synthetase (see paper)
36% identity, 98% coverage: 10:452/452 of query aligns to 8:443/443 of 7tdvC
- binding adenosine-5'-diphosphate: G129 (= G127), E131 (= E129), E183 (≠ Y184), D197 (= D198), F198 (= F199), K199 (= K200), Y200 (= Y201), N246 (= N247), V247 (≠ M248), S248 (= S249), R320 (= R332), S328 (≠ G337), R330 (= R339)
- binding magnesium ion: E131 (= E129), E131 (= E129), E133 (= E131), E188 (= E189), E195 (= E196), E195 (= E196), H244 (= H245), E332 (= E341)
- binding l-methionine-s-sulfoximine phosphate: E131 (= E129), E133 (= E131), E188 (= E189), E195 (= E196), G240 (= G241), H244 (= H245), R297 (= R303), E303 (≠ W315), R315 (= R327)
7tdpA Structure of paenibacillus polymyxa gs bound to met-sox-p-adp (transition state complex) to 1.98 angstom (see paper)
36% identity, 97% coverage: 16:452/452 of query aligns to 13:439/439 of 7tdpA
- binding adenosine-5'-diphosphate: N123 (= N125), G125 (= G127), E127 (= E129), E179 (≠ Y184), D193 (= D198), Y196 (= Y201), N242 (= N247), S244 (= S249), R316 (= R332), R326 (= R339)
- binding magnesium ion: E127 (= E129), E127 (= E129), E129 (= E131), E184 (= E189), E191 (= E196), E191 (= E196), H240 (= H245), E328 (= E341)
- binding l-methionine-s-sulfoximine phosphate: E127 (= E129), E129 (= E131), E184 (= E189), E191 (= E196), G236 (= G241), H240 (= H245), R293 (= R303), E299 (≠ W315), R311 (= R327), R330 (= R343)
7tfaB Glutamine synthetase (see paper)
36% identity, 97% coverage: 16:452/452 of query aligns to 13:441/441 of 7tfaB
- binding glutamine: E131 (= E131), Y153 (≠ C156), E186 (= E189), G238 (= G241), H242 (= H245), R295 (= R303), E301 (≠ W315)
- binding magnesium ion: E129 (= E129), E131 (= E131), E186 (= E189), E193 (= E196), H242 (= H245), E330 (= E341)
- binding : Y58 (≠ V61), R60 (≠ Q63), V187 (≠ D190), N237 (≠ T240), G299 (≠ S313), Y300 (≠ T314), R313 (= R327), M424 (≠ S435)
8ooxB Glutamine synthetase (see paper)
36% identity, 97% coverage: 14:452/452 of query aligns to 10:438/438 of 8ooxB
8oozA Glutamine synthetase (see paper)
36% identity, 97% coverage: 14:452/452 of query aligns to 10:430/430 of 8oozA
- binding adenosine-5'-triphosphate: G117 (= G127), E170 (≠ Y184), F185 (= F199), K186 (= K200), Y187 (= Y201), N233 (= N247), S235 (= S249), S315 (≠ G337), R317 (= R339)
- binding magnesium ion: E119 (= E129), H231 (= H245), E319 (= E341)
8ufjB Glutamine synthetase (see paper)
35% identity, 100% coverage: 1:452/452 of query aligns to 1:444/444 of 8ufjB
8tfkA Glutamine synthetase (see paper)
35% identity, 99% coverage: 5:452/452 of query aligns to 1:440/440 of 8tfkA
- binding adenosine-5'-diphosphate: E128 (= E129), D194 (= D198), F195 (= F199), F197 (≠ Y201), N243 (= N247), R312 (= R327), R317 (= R332), G325 (= G337), R327 (= R339)
- binding magnesium ion: E128 (= E129), E128 (= E129), E130 (= E131), E185 (= E189), E192 (= E196), E192 (= E196), H241 (= H245), E329 (= E341)
- binding l-methionine-s-sulfoximine phosphate: E128 (= E129), E130 (= E131), E185 (= E189), E192 (= E196), G237 (= G241), H241 (= H245), R294 (= R303), E300 (≠ W315), R312 (= R327), R331 (= R343)
7tenA Glutamine synthetase (see paper)
34% identity, 97% coverage: 16:452/452 of query aligns to 13:442/442 of 7tenA
- binding adenosine-5'-diphosphate: G128 (= G127), E130 (= E129), E182 (≠ Y184), D196 (= D198), F197 (= F199), K198 (= K200), Y199 (= Y201), N245 (= N247), S247 (= S249), R319 (= R332), S327 (≠ G337), R329 (= R339)
- binding l-methionine-s-sulfoximine phosphate: E130 (= E129), E132 (= E131), E187 (= E189), E194 (= E196), N238 (≠ T240), G239 (= G241), H243 (= H245), R296 (= R303), E302 (≠ W315), R314 (= R327), R333 (= R343)
7tf9S L. Monocytogenes gs(14)-q-glnr peptide (see paper)
34% identity, 97% coverage: 16:452/452 of query aligns to 14:443/443 of 7tf9S
- binding glutamine: E133 (= E131), Y155 (≠ F143), E188 (= E189), G240 (= G241), G242 (= G243), R297 (= R303), E303 (≠ W315)
- binding magnesium ion: E131 (= E129), E133 (= E131), E188 (= E189), E195 (= E196), H244 (= H245), E332 (= E341)
- binding : F59 (≠ V61), V60 (≠ P62), E418 (≠ D427), I422 (≠ G431), M426 (≠ S435)
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)
35% identity, 97% coverage: 14:451/452 of query aligns to 12:446/446 of A0R083
- K363 (≠ E368) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
8oooA Glutamine synthetase from methanothermococcus thermolithotrophicus in complex with 2-oxoglutarate and mgatp at 2.15 a resolution (see paper)
33% identity, 99% coverage: 5:451/452 of query aligns to 1:447/447 of 8oooA
- binding 2-oxoglutaric acid: F17 (≠ Y21), R19 (≠ I23), A33 (≠ F37), R87 (≠ N85), V93 (≠ L88), P170 (= P167), R173 (≠ M169), R174 (≠ D170), S190 (≠ F186)
- binding adenosine-5'-triphosphate: E136 (= E129), E188 (≠ Y184), F203 (= F199), K204 (= K200), F205 (≠ Y201), H251 (≠ N247), S253 (= S249), R325 (= R332), R335 (= R339)
Query Sequence
>GFF3214 FitnessBrowser__Marino:GFF3214
MTELTNTQALKEKLTEEGVKYAIASYVDIHGVTKGKFVPVAHLGQMMEGSELYTGAALDG
VPQDISDDEVASMPDADGLAICPWNRQLAWFPGNLFLNGTPFEACSRNILRRQLSAAADM
GYRFNLGIETEFFLFRDTEDGGFAPLSDRDNLGKPCYDPRTLMDNLPIMDELVDAMNELG
WDVYSFDHEDANGQFETDFKYADALTMSDRLVFFRMMANEIARKHGAFASFMPKPFADRT
GSGAHYNMSLADLKTGENLFEPRGDDLHNCGISKIAYHFTAGVLKHGAAISAVIAPTVNS
YKRLVRQGSMSGSTWAPVFMCYGSNNRTNMIRIPGMGGRIECRAADIACNPYLGSALILA
AGLEGIREGLDAGAPHHENMYNYSDAEIAEQGIEYLPRNLGEAVEAFEADPLAKEVFGEA
MFNSFIDFKKGEWESYQNHVSSWEVDRYLKMF
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