SitesBLAST
Comparing Pf6N2E2_5686 FitnessBrowser__pseudo6_N2E2:Pf6N2E2_5686 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)
31% identity, 98% coverage: 2:439/447 of query aligns to 24:464/472 of P78061
- H282 (= H256) mutation to N: Activity is impaired to 9% of wild-type.
- R357 (= R332) mutation to Q: Activity is impaired to 3% of wild-type.
8tfkA Glutamine synthetase (see paper)
31% identity, 83% coverage: 70:439/447 of query aligns to 61:432/440 of 8tfkA
- binding adenosine-5'-diphosphate: E128 (= E135), D194 (≠ N209), F195 (≠ L210), F197 (≠ H212), N243 (≠ H258), R312 (= R327), R317 (= R332), G325 (≠ A340), R327 (= R342)
- binding magnesium ion: E128 (= E135), E128 (= E135), E130 (= E137), E185 (= E200), E192 (= E207), E192 (= E207), H241 (= H256), E329 (= E344)
- binding l-methionine-s-sulfoximine phosphate: E128 (= E135), E130 (= E137), E185 (= E200), E192 (= E207), G237 (= G252), H241 (= H256), R294 (= R309), E300 (≠ A315), R312 (= R327), R331 (= R346)
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)
31% identity, 83% coverage: 71:439/447 of query aligns to 64:439/446 of A0R083
- K363 (vs. gap) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
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)
30% identity, 89% coverage: 47:446/447 of query aligns to 40:442/443 of 4lnkA
- active site: D52 (≠ G59), E131 (= E135), E133 (= E137), E188 (= E200), E195 (= E207), H244 (= H256), R315 (= R327), E332 (= E344), R334 (= R346)
- binding adenosine-5'-diphosphate: K43 (≠ R50), M50 (≠ I57), F198 (≠ L210), Y200 (≠ H212), N246 (≠ H258), S248 (= S260), S324 (= S336), S328 (≠ A340), R330 (= R342)
- binding glutamic acid: E133 (= E137), E188 (= E200), V189 (≠ M201), N239 (≠ P251), G240 (= G252), G242 (≠ S254), E303 (≠ A315)
- binding magnesium ion: E131 (= E135), E188 (= E200), E195 (= E207), H244 (= H256), E332 (= E344)
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)
30% identity, 89% coverage: 47:446/447 of query aligns to 40:442/443 of 4lniA
- active site: D52 (≠ G59), E131 (= E135), E133 (= E137), E188 (= E200), E195 (= E207), H244 (= H256), R315 (= R327), E332 (= E344), R334 (= R346)
- binding adenosine-5'-diphosphate: E131 (= E135), E183 (≠ D195), D197 (≠ N209), Y200 (≠ H212), N246 (≠ H258), S248 (= S260), R320 (= R332), R330 (= R342)
- binding magnesium ion: E131 (= E135), E131 (= E135), E133 (= E137), E188 (= E200), E195 (= E207), E195 (= E207), H244 (= H256), E332 (= E344)
- binding l-methionine-s-sulfoximine phosphate: E133 (= E137), E188 (= E200), H244 (= H256), R297 (= R309), E303 (≠ A315), R315 (= R327), R334 (= R346)
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, 89% coverage: 47:446/447 of query aligns to 41:443/444 of P12425
- G59 (≠ R65) 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 (≠ G68) 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 (= E135) binding
- E134 (= E137) binding
- E189 (= E200) binding
- V190 (≠ M201) 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
- G241 (= G252) binding
- H245 (= H256) binding
- G302 (≠ P313) 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 (≠ A315) 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 (= E344) binding
- 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)
30% identity, 89% coverage: 47:446/447 of query aligns to 44:446/447 of 4s0rD
- active site: D56 (≠ G59), E135 (= E135), E137 (= E137), E192 (= E200), E199 (= E207), H248 (= H256), R319 (= R327), E336 (= E344), R338 (= R346)
- binding glutamine: E137 (= E137), E192 (= E200), R301 (= R309), E307 (≠ A315)
- binding magnesium ion: I66 (≠ S69), E135 (= E135), E135 (= E135), E199 (= E207), H248 (= H256), H248 (= H256), E336 (= E344), H419 (≠ G419)
- binding : F63 (= F66), V64 (≠ Y67), R65 (≠ G68), I66 (≠ S69), D161 (≠ S169), G241 (≠ H249), V242 (≠ T250), N243 (≠ P251), G305 (≠ P313), Y306 (≠ F314), Y376 (≠ E384), I426 (≠ L426), M430 (≠ S430)
8ufjB Glutamine synthetase (see paper)
31% identity, 83% coverage: 70:439/447 of query aligns to 65:436/444 of 8ufjB
8ooqB Glutamine synthetase from Methanothermococcus thermolithotrophicus (see paper)
29% identity, 93% coverage: 25:439/447 of query aligns to 23:439/446 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, 93% coverage: 25:439/447 of query aligns to 24:440/447 of 8oooA
- binding 2-oxoglutaric acid: A33 (vs. gap), R87 (vs. gap), V93 (≠ R93), P170 (≠ R177), R173 (≠ F180), R174 (≠ S181), S190 (≠ F197)
- binding adenosine-5'-triphosphate: E136 (= E135), E188 (≠ D195), F203 (≠ L210), K204 (≠ L211), F205 (≠ H212), H251 (= H258), S253 (= S260), R325 (= R332), R335 (= R342)
Sites not aligning to the query:
3ng0A Crystal structure of glutamine synthetase from synechocystis sp. Pcc 6803
32% identity, 79% coverage: 70:424/447 of query aligns to 62:442/465 of 3ng0A
- active site: E130 (= E135), E132 (= E137), E213 (= E200), E221 (= E207), H270 (= H256), R340 (= R327), E359 (= E344), R361 (= R346)
- binding phosphoaminophosphonic acid-adenylate ester: Y126 (vs. gap), E130 (= E135), K209 (≠ T196), I224 (≠ L210), F226 (≠ H212), H272 (= H258), S274 (= S260), R340 (= R327), R345 (= R332), R357 (= R342)
- binding manganese (ii) ion: E130 (= E135), E132 (= E137), E213 (= E200), E221 (= E207), H270 (= H256), E359 (= E344), R361 (= R346)
Sites not aligning to the query:
8ooxB Glutamine synthetase (see paper)
29% identity, 84% coverage: 66:439/447 of query aligns to 57:430/438 of 8ooxB
8oozA Glutamine synthetase (see paper)
30% identity, 85% coverage: 62:439/447 of query aligns to 45:422/430 of 8oozA
- binding adenosine-5'-triphosphate: G117 (≠ A133), E170 (≠ D195), F185 (≠ L210), K186 (≠ L211), Y187 (≠ H212), N233 (≠ H258), S235 (= S260), S315 (≠ A340), R317 (= R342)
- binding magnesium ion: E119 (= E135), H231 (= H256), E319 (= E344)
5dm3C Crystal structure of glutamine synthetase from chromohalobacter salexigens dsm 3043(csal_0679, target efi-550015) with bound adp
33% identity, 79% coverage: 86:439/447 of query aligns to 66:390/396 of 5dm3C
- active site: E115 (= E135), E117 (= E137), E162 (= E200), E169 (= E207), H218 (= H256), R286 (= R327), E303 (= E344), R305 (= R346)
- binding adenosine-5'-diphosphate: R173 (≠ L211), C174 (≠ H212), H220 (= H258), S222 (= S260), R301 (= R342)
7tdpA Structure of paenibacillus polymyxa gs bound to met-sox-p-adp (transition state complex) to 1.98 angstom (see paper)
30% identity, 88% coverage: 47:440/447 of query aligns to 39:432/439 of 7tdpA
- binding adenosine-5'-diphosphate: N123 (vs. gap), G125 (≠ A133), E127 (= E135), E179 (≠ D195), D193 (≠ N209), Y196 (≠ H212), N242 (≠ H258), S244 (= S260), R316 (= R332), R326 (= R342)
- binding magnesium ion: E127 (= E135), E127 (= E135), E129 (= E137), E184 (= E200), E191 (= E207), E191 (= E207), H240 (= H256), E328 (= E344)
- binding l-methionine-s-sulfoximine phosphate: E127 (= E135), E129 (= E137), E184 (= E200), E191 (= E207), G236 (= G252), H240 (= H256), R293 (= R309), E299 (≠ A315), R311 (= R327), R330 (= R346)
7tfaB Glutamine synthetase (see paper)
30% identity, 88% coverage: 47:440/447 of query aligns to 39:434/441 of 7tfaB
- binding glutamine: E131 (= E137), Y153 (≠ A167), E186 (= E200), G238 (= G252), H242 (= H256), R295 (= R309), E301 (≠ A315)
- binding magnesium ion: E129 (= E135), E131 (= E137), E186 (= E200), E193 (= E207), H242 (= H256), E330 (= E344)
- binding : Y58 (≠ F66), R60 (≠ G68), V187 (≠ M201), N237 (≠ P251), G299 (≠ P313), Y300 (≠ F314), R313 (= R327), M424 (≠ S430)
7tf9S L. Monocytogenes gs(14)-q-glnr peptide (see paper)
29% identity, 88% coverage: 47:440/447 of query aligns to 40:436/443 of 7tf9S
- binding glutamine: E133 (= E137), Y155 (≠ A167), E188 (= E200), G240 (= G252), G242 (≠ S254), R297 (= R309), E303 (≠ A315)
- binding magnesium ion: E131 (= E135), E133 (= E137), E188 (= E200), E195 (= E207), H244 (= H256), E332 (= E344)
- binding : F59 (= F66), V60 (≠ Y67), E418 (≠ A422), I422 (≠ L426), M426 (≠ S430)
7tenA Glutamine synthetase (see paper)
29% identity, 88% coverage: 47:440/447 of query aligns to 39:435/442 of 7tenA
- binding adenosine-5'-diphosphate: G128 (≠ A133), E130 (= E135), E182 (≠ D195), D196 (≠ N209), F197 (≠ L210), K198 (≠ L211), Y199 (≠ H212), N245 (≠ H258), S247 (= S260), R319 (= R332), S327 (≠ A340), R329 (= R342)
- binding l-methionine-s-sulfoximine phosphate: E130 (= E135), E132 (= E137), E187 (= E200), E194 (= E207), N238 (≠ P251), G239 (= G252), H243 (= H256), R296 (= R309), E302 (≠ A315), R314 (= R327), R333 (= R346)
P77961 Glutamine synthetase; GS; Glutamate--ammonia ligase; Glutamine synthetase I beta; GSI beta; EC 6.3.1.2 from Synechocystis sp. (strain PCC 6803 / Kazusa)
31% identity, 79% coverage: 70:424/447 of query aligns to 64:450/473 of P77961
- E134 (= E137) binding
- E215 (= E200) binding
- E223 (= E207) binding
- E361 (= E344) binding
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, 81% coverage: 79:442/447 of query aligns to 72:442/446 of P9WN37
- K363 (vs. gap) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
Query Sequence
>Pf6N2E2_5686 FitnessBrowser__pseudo6_N2E2:Pf6N2E2_5686
MTTDGQRSLAQRLTGIDEIECVTPDLNGVPRGKVMTAEGFLEGRRLQLARGVLLQCIMGG
YPPSRFYGSDDGDLALVADPKQIHRLPWSQQPRALAICDADELTGESSRLSTRGQLKAVV
ARYAALGLAPVVATELEFFVFAPNPDPTQPFQPPMGLDGRREDGHSAFSVSSNNGLRPFF
SEVYACMAALGLPRDTFMHEMGVSQFEINLLHGDPLLLADQTFLFKHLLKEVALKHGLTV
VCMAKPLAHTPGSSMHIHQSVVEEGSGRNVFSDEAGEPTAAFRHFIGGQQACLADFTALF
APNVNSYQRLCHPFASPNNACWSHDNRSAGLRIPASSPVARRVENRLPGADANPYLAIAA
SLAAGLYGIEHRLEPSAAIQGEFEVPDNLSLPCTLHAALERLKRSHLAKELFGTEFIEGY
IASKTLELTSFFDEITPWERRVLAAQA
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