SitesBLAST
Comparing 6937000 FitnessBrowser__SB2B:6937000 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)
P78061 Gamma-glutamylputrescine synthetase PuuA; Gamma-Glu-Put synthetase; Glutamate--putrescine ligase; EC 6.3.1.11 from Escherichia coli (strain K12) (see paper)
38% identity, 99% coverage: 7:455/455 of query aligns to 25:472/472 of P78061
- H282 (= H265) mutation to N: Activity is impaired to 9% of wild-type.
- R357 (= R340) mutation to Q: Activity is impaired to 3% of wild-type.
8wwuB Glutamine synthetase
27% identity, 94% coverage: 19:446/455 of query aligns to 31:472/492 of 8wwuB
- binding phosphoaminophosphonic acid-adenylate ester: G157 (≠ A141), E159 (= E143), R226 (= R203), F241 (≠ L218), V243 (≠ R221), H290 (= H267), S292 (= S269), K360 (≠ R335), R365 (= R340), R376 (≠ H350)
- binding magnesium ion: E159 (= E143), E238 (= E215)
- binding manganese (ii) ion: E159 (= E143), E161 (= E145), E231 (= E208), E238 (= E215), H288 (= H265), E378 (= E352)
8wwvA Glutamine synthetase
27% identity, 94% coverage: 19:446/455 of query aligns to 29:470/490 of 8wwvA
- binding adenosine-5'-diphosphate: G155 (≠ A141), E157 (= E143), R224 (= R203), F239 (≠ L218), D240 (≠ E219), V241 (≠ R221), H288 (= H267), S290 (= S269), R374 (≠ H350), E376 (= E352)
- binding magnesium ion: E157 (= E143), E236 (= E215)
- binding manganese (ii) ion: E157 (= E143), E159 (= E145), E229 (= E208), E236 (= E215), H286 (= H265), E376 (= E352)
- binding l-methionine-s-sulfoximine phosphate: E157 (= E143), E159 (= E145), E229 (= E208), E236 (= E215), A282 (≠ G261), H286 (= H265), R340 (= R317), K358 (≠ R335)
8tfkA Glutamine synthetase (see paper)
31% identity, 79% coverage: 94:453/455 of query aligns to 78:438/440 of 8tfkA
- binding adenosine-5'-diphosphate: E128 (= E143), D194 (≠ E219), F195 (≠ H220), F197 (= F222), N243 (≠ H267), R312 (= R335), R317 (= R340), G325 (≠ S348), R327 (≠ H350)
- binding magnesium ion: E128 (= E143), E128 (= E143), E130 (= E145), E185 (= E208), E192 (= E215), E192 (= E215), H241 (= H265), E329 (= E352)
- binding l-methionine-s-sulfoximine phosphate: E128 (= E143), E130 (= E145), E185 (= E208), E192 (= E215), G237 (= G261), H241 (= H265), R294 (= R317), E300 (≠ Y323), R312 (= R335), R331 (= R354)
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)
30% identity, 87% coverage: 59:453/455 of query aligns to 48:445/446 of A0R083
- K363 (≠ N379) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
8ooqB Glutamine synthetase from Methanothermococcus thermolithotrophicus (see paper)
29% identity, 86% coverage: 59:449/455 of query aligns to 52:439/446 of 8ooqB
Sites not aligning to the query:
8oooA Glutamine synthetase from methanothermococcus thermolithotrophicus in complex with 2-oxoglutarate and mgatp at 2.15 a resolution (see paper)
29% identity, 86% coverage: 59:449/455 of query aligns to 53:440/447 of 8oooA
- binding 2-oxoglutaric acid: R87 (= R96), V93 (≠ T100), P170 (≠ L188), R173 (vs. gap), R174 (vs. gap), S190 (≠ A205)
- binding adenosine-5'-triphosphate: E136 (= E143), E188 (≠ R203), F203 (≠ L218), K204 (≠ E219), F205 (≠ H220), H251 (= H267), S253 (= S269), R325 (= R340), R335 (≠ H350)
Sites not aligning to the query:
8ufjB Glutamine synthetase (see paper)
31% identity, 79% coverage: 94:453/455 of query aligns to 82:442/444 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)
30% identity, 87% coverage: 59:453/455 of query aligns to 48:445/446 of P9WN37
- K363 (≠ N379) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
7tenA Glutamine synthetase (see paper)
30% identity, 83% coverage: 76:452/455 of query aligns to 61:439/442 of 7tenA
- binding adenosine-5'-diphosphate: G128 (≠ A141), E130 (= E143), E182 (≠ R203), D196 (≠ T217), F197 (≠ L218), K198 (≠ E219), Y199 (≠ H220), N245 (≠ H267), S247 (= S269), R319 (= R340), S327 (= S348), R329 (≠ H350)
- binding l-methionine-s-sulfoximine phosphate: E130 (= E143), E132 (= E145), E187 (= E208), E194 (= E215), N238 (≠ A260), G239 (= G261), H243 (= H265), R296 (= R317), E302 (≠ Y323), R314 (= R335), R333 (= R354)
7tf9S L. Monocytogenes gs(14)-q-glnr peptide (see paper)
30% identity, 83% coverage: 76:452/455 of query aligns to 62:440/443 of 7tf9S
- binding glutamine: E133 (= E145), Y155 (≠ V175), E188 (= E208), G240 (= G261), G242 (= G263), R297 (= R317), E303 (≠ Y323)
- binding magnesium ion: E131 (= E143), E133 (= E145), E188 (= E208), E195 (= E215), H244 (= H265), E332 (= E352)
- binding : E418 (≠ R430), I422 (≠ A434), M426 (≠ E438)
Sites not aligning to the query:
7tdvC Glutamine synthetase (see paper)
28% identity, 83% coverage: 76:454/455 of query aligns to 62:442/443 of 7tdvC
- binding adenosine-5'-diphosphate: G129 (≠ A141), E131 (= E143), E183 (≠ R203), D197 (≠ T217), F198 (≠ L218), K199 (≠ E219), Y200 (≠ H220), N246 (≠ H267), V247 (= V268), S248 (= S269), R320 (= R340), S328 (= S348), R330 (≠ H350)
- binding magnesium ion: E131 (= E143), E131 (= E143), E133 (= E145), E188 (= E208), E195 (= E215), E195 (= E215), H244 (= H265), E332 (= E352)
- binding l-methionine-s-sulfoximine phosphate: E131 (= E143), E133 (= E145), E188 (= E208), E195 (= E215), G240 (= G261), H244 (= H265), R297 (= R317), E303 (≠ Y323), R315 (= R335)
7tf6A Glutamine synthetase (see paper)
28% identity, 83% coverage: 76:454/455 of query aligns to 61:437/438 of 7tf6A
- binding glutamine: E128 (= E145), E183 (= E208), G235 (= G261), H239 (= H265), R292 (= R317), E298 (≠ Y323)
- binding magnesium ion: E126 (= E143), E128 (= E145), E183 (= E208), E190 (= E215), H239 (= H265), E327 (= E352)
- binding : G232 (≠ E258), N234 (≠ A260), G296 (≠ A321), Y297 (≠ S322), R310 (= R335), Y367 (= Y392), Y421 (≠ E438), Q433 (≠ W450), Q437 (≠ H454)
Sites not aligning to the query:
7cquA Gmas/adp/metsox-p complex (see paper)
30% identity, 86% coverage: 22:414/455 of query aligns to 12:390/429 of 7cquA
- binding adenosine-5'-diphosphate: E121 (= E143), Y173 (≠ R203), N187 (≠ T217), W188 (≠ L218), D189 (≠ E219), Y190 (≠ H220), H236 (= H267), L237 (≠ V268), S238 (= S269), R316 (= R340), R322 (≠ H350)
- binding magnesium ion: E121 (= E143), E121 (= E143), E123 (= E145), E178 (= E208), E185 (= E215), E185 (= E215), H234 (= H265), E324 (= E352)
- binding l-methionine-s-sulfoximine phosphate: E121 (= E143), E123 (= E145), E178 (= E208), E185 (= E215), T229 (≠ A260), G230 (= G261), H234 (= H265), R287 (= R317), W299 (≠ Y323), R311 (= R335), R326 (= R354)
7cqqA Gmas in complex with amppnp and metsox (see paper)
30% identity, 86% coverage: 22:414/455 of query aligns to 12:390/429 of 7cqqA
- binding phosphoaminophosphonic acid-adenylate ester: E121 (= E143), Y173 (≠ R203), E185 (= E215), N187 (≠ T217), D189 (≠ E219), Y190 (≠ H220), H234 (= H265), H236 (= H267), S238 (= S269), R311 (= R335), R316 (= R340), R322 (≠ H350), E324 (= E352)
- binding magnesium ion: E121 (= E143), E121 (= E143), E123 (= E145), E178 (= E208), E185 (= E215), E185 (= E215), H234 (= H265), E324 (= E352)
- binding (2s)-2-amino-4-(methylsulfonimidoyl)butanoic acid: E123 (= E145), E178 (= E208), T229 (≠ A260), H234 (= H265), R287 (= R317), W299 (≠ Y323), R311 (= R335), R326 (= R354)
7cqnA Gmas in complex with amppcp (see paper)
30% identity, 86% coverage: 22:414/455 of query aligns to 12:390/429 of 7cqnA
- binding phosphomethylphosphonic acid adenylate ester: G45 (≠ P52), D61 (= D80), E121 (= E143), Y173 (≠ R203), Q174 (≠ T204), W188 (≠ L218), D189 (≠ E219), Y190 (≠ H220), H236 (= H267), S238 (= S269), R311 (= R335), R316 (= R340), R322 (≠ H350)
7cqwA Gmas/adp complex-conformation 1 (see paper)
30% identity, 86% coverage: 22:414/455 of query aligns to 13:391/430 of 7cqwA
4s0rD Structure of gs-tnra complex (see paper)
26% identity, 98% coverage: 7:454/455 of query aligns to 9:446/447 of 4s0rD
- active site: D56 (≠ Q63), E135 (= E143), E137 (= E145), E192 (= E208), E199 (= E215), H248 (= H265), R319 (= R335), E336 (= E352), R338 (= R354)
- binding glutamine: E137 (= E145), E192 (= E208), R301 (= R317), E307 (≠ Y323)
- binding magnesium ion: I66 (≠ V76), E135 (= E143), E135 (= E143), E199 (= E215), H248 (= H265), H248 (= H265), E336 (= E352), H419 (≠ I427)
- binding : F63 (≠ L72), V64 (= V73), R65 (≠ E75), I66 (≠ V76), D161 (≠ G177), G241 (≠ E258), V242 (≠ L259), N243 (≠ A260), G305 (≠ A321), Y306 (≠ S322), Y376 (= Y392), I426 (≠ A434), M430 (≠ E438)
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)
26% identity, 98% coverage: 7:454/455 of query aligns to 6:443/444 of P12425
- G59 (= G71) 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 (≠ E75) 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
- E134 (= E145) binding
- E189 (= E208) binding
- V190 (≠ Y209) 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 (= E215) binding
- G241 (= G261) binding
- H245 (= H265) binding
- G302 (≠ A321) 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 (≠ Y323) 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 (= P325) 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 (= E352) binding
- E424 (= E435) 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)
26% identity, 98% coverage: 7:454/455 of query aligns to 5:442/443 of 4lnkA
- active site: D52 (≠ Q63), E131 (= E143), E133 (= E145), E188 (= E208), E195 (= E215), H244 (= H265), R315 (= R335), E332 (= E352), R334 (= R354)
- binding adenosine-5'-diphosphate: K43 (≠ R51), M50 (≠ L58), F198 (≠ L218), Y200 (≠ H220), N246 (≠ H267), S248 (= S269), S324 (≠ G344), S328 (= S348), R330 (≠ H350)
- binding glutamic acid: E133 (= E145), E188 (= E208), V189 (≠ Y209), N239 (≠ A260), G240 (= G261), G242 (= G263), E303 (≠ Y323)
- binding magnesium ion: E131 (= E143), E188 (= E208), E195 (= E215), H244 (= H265), E332 (= E352)
Query Sequence
>6937000 FitnessBrowser__SB2B:6937000
MPFANPQEAIDFLDKHPQVQHVEVFIIDPNGIPRGKLLHRQEVLSMYRHGRPLPSTILGL
TVQGDDVEDTGLVWEVGDADCLAFPIEGGLLMQPWRAQPTAQVHLTMHPEAGMPAAVADP
RLVLSKVIDSLQADGFYPVMAAELEFFLLDQRFDANGRPQPAMQSDGHRPHQTQVYGILE
LERLQPFLDDLYHACEVQGIPARTAISEYAPGQVEITLEHRFDALQAMDEAVRYKRLVKG
VAAKHGMQACFMAKPFGELAGSGMHMHVSLADADGNNRFASDNPEGTPELTQSIAGMMAT
LEDAQLLFCPNANSFRRFQSASYAPIAKTWGVNNRTVSFRVPGGPAPSRHVEHRICGADA
NPYLAAAAILAACHHGIRNQLSPGQAIVGNGYEGKHQTLPTDWLSALTNFERSEWMKSVL
GEDFHRIYGRIKRAEYQEFMAEVGQQDWHWYLTHA
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