SitesBLAST
Comparing H281DRAFT_01081 FitnessBrowser__Burk376:H281DRAFT_01081 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)
34% identity, 99% coverage: 2:441/444 of query aligns to 25:469/472 of P78061
- H282 (= H254) mutation to N: Activity is impaired to 9% of wild-type.
- R357 (= R330) mutation to Q: Activity is impaired to 3% of wild-type.
8oooA Glutamine synthetase from methanothermococcus thermolithotrophicus in complex with 2-oxoglutarate and mgatp at 2.15 a resolution (see paper)
31% identity, 97% coverage: 6:436/444 of query aligns to 8:440/447 of 8oooA
- binding 2-oxoglutaric acid: F17 (≠ E15), R19 (≠ E17), A33 (≠ I31), R87 (vs. gap), V93 (≠ T91), P170 (≠ D175), R173 (≠ F178), R174 (≠ E179), S190 (≠ L195)
- binding adenosine-5'-triphosphate: E136 (= E133), E188 (≠ D193), F203 (= F208), K204 (≠ M209), F205 (≠ H210), H251 (= H256), S253 (= S258), R325 (= R330), R335 (= R340)
8ooqB Glutamine synthetase from Methanothermococcus thermolithotrophicus (see paper)
31% identity, 97% coverage: 6:436/444 of query aligns to 7:439/446 of 8ooqB
- binding 2-oxoglutaric acid: F16 (≠ E15), R18 (≠ E17), A32 (≠ I31), R86 (vs. gap), V92 (≠ T91), P169 (≠ D175), R172 (≠ F178), R173 (≠ E179), S189 (≠ L195)
- binding magnesium ion: E137 (= E135), E192 (= E198), E199 (= E205)
8tfkA Glutamine synthetase (see paper)
31% identity, 99% coverage: 3:441/444 of query aligns to 5:437/440 of 8tfkA
- binding adenosine-5'-diphosphate: E128 (= E133), D194 (≠ N207), F195 (= F208), F197 (≠ H210), N243 (≠ H256), R312 (= R325), R317 (= R330), G325 (≠ A338), R327 (= R340)
- binding magnesium ion: E128 (= E133), E128 (= E133), E130 (= E135), E185 (= E198), E192 (= E205), E192 (= E205), H241 (= H254), E329 (= E342)
- binding l-methionine-s-sulfoximine phosphate: E128 (= E133), E130 (= E135), E185 (= E198), E192 (= E205), G237 (= G250), H241 (= H254), R294 (= R307), E300 (≠ A313), R312 (= R325), R331 (= R344)
8ufjB Glutamine synthetase (see paper)
31% identity, 99% coverage: 3:441/444 of query aligns to 9:441/444 of 8ufjB
7tdpA Structure of paenibacillus polymyxa gs bound to met-sox-p-adp (transition state complex) to 1.98 angstom (see paper)
31% identity, 99% coverage: 3:441/444 of query aligns to 6:436/439 of 7tdpA
- binding adenosine-5'-diphosphate: N123 (vs. gap), G125 (≠ A131), E127 (= E133), E179 (≠ D193), D193 (≠ N207), Y196 (≠ H210), N242 (≠ H256), S244 (= S258), R316 (= R330), R326 (= R340)
- binding magnesium ion: E127 (= E133), E127 (= E133), E129 (= E135), E184 (= E198), E191 (= E205), E191 (= E205), H240 (= H254), E328 (= E342)
- binding l-methionine-s-sulfoximine phosphate: E127 (= E133), E129 (= E135), E184 (= E198), E191 (= E205), G236 (= G250), H240 (= H254), R293 (= R307), E299 (≠ A313), R311 (= R325), R330 (= R344)
7tfaB Glutamine synthetase (see paper)
31% identity, 99% coverage: 3:441/444 of query aligns to 6:438/441 of 7tfaB
- binding glutamine: E131 (= E135), Y153 (≠ R155), E186 (= E198), G238 (= G250), H242 (= H254), R295 (= R307), E301 (≠ A313)
- binding magnesium ion: E129 (= E133), E131 (= E135), E186 (= E198), E193 (= E205), H242 (= H254), E330 (= E342)
- binding : Y58 (vs. gap), R60 (vs. gap), V187 (= V199), N237 (≠ P249), G299 (≠ F311), Y300 (≠ M312), R313 (= R325), M424 (≠ A427)
4s0rD Structure of gs-tnra complex (see paper)
30% identity, 99% coverage: 3:441/444 of query aligns to 11:444/447 of 4s0rD
- active site: D56 (= D60), E135 (= E133), E137 (= E135), E192 (= E198), E199 (= E205), H248 (= H254), R319 (= R325), E336 (= E342), R338 (= R344)
- binding glutamine: E137 (= E135), E192 (= E198), R301 (= R307), E307 (≠ A313)
- binding magnesium ion: I66 (≠ V67), E135 (= E133), E135 (= E133), E199 (= E205), H248 (= H254), H248 (= H254), E336 (= E342), H419 (≠ A416)
- binding : F63 (vs. gap), V64 (vs. gap), R65 (vs. gap), I66 (≠ V67), D161 (= D175), G241 (= G247), V242 (≠ E248), N243 (≠ P249), G305 (≠ F311), Y306 (≠ M312), Y376 (= Y382), I426 (≠ T423), M430 (≠ A427)
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)
33% identity, 86% coverage: 60:441/444 of query aligns to 52:444/446 of P9WN37
- K363 (≠ Q369) 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, 99% coverage: 3:441/444 of query aligns to 7:440/443 of 4lnkA
- active site: D52 (= D60), E131 (= E133), E133 (= E135), E188 (= E198), E195 (= E205), H244 (= H254), R315 (= R325), E332 (= E342), R334 (= R344)
- binding adenosine-5'-diphosphate: K43 (≠ S39), M50 (= M50), F198 (= F208), Y200 (≠ H210), N246 (≠ H256), S248 (= S258), S324 (= S334), S328 (≠ A338), R330 (= R340)
- binding glutamic acid: E133 (= E135), E188 (= E198), V189 (= V199), N239 (≠ P249), G240 (= G250), G242 (≠ A252), E303 (≠ A313)
- binding magnesium ion: E131 (= E133), E188 (= E198), E195 (= E205), H244 (= H254), E332 (= E342)
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, 99% coverage: 3:441/444 of query aligns to 7:440/443 of 4lniA
- active site: D52 (= D60), E131 (= E133), E133 (= E135), E188 (= E198), E195 (= E205), H244 (= H254), R315 (= R325), E332 (= E342), R334 (= R344)
- binding adenosine-5'-diphosphate: E131 (= E133), E183 (≠ D193), D197 (≠ N207), Y200 (≠ H210), N246 (≠ H256), S248 (= S258), R320 (= R330), R330 (= R340)
- binding magnesium ion: E131 (= E133), E131 (= E133), E133 (= E135), E188 (= E198), E195 (= E205), E195 (= E205), H244 (= H254), E332 (= E342)
- binding l-methionine-s-sulfoximine phosphate: E133 (= E135), E188 (= E198), H244 (= H254), R297 (= R307), E303 (≠ A313), R315 (= R325), R334 (= R344)
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, 99% coverage: 3:441/444 of query aligns to 8:441/444 of P12425
- G59 (= G66) 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 (vs. gap) 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 (= E133) binding
- E134 (= E135) binding
- E189 (= E198) binding
- V190 (= V199) 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 (= E205) binding
- G241 (= G250) binding
- H245 (= H254) binding
- G302 (≠ F311) 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 (≠ A313) 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 (= P315) 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 (= E342) binding
- E424 (= E424) 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
8ooxB Glutamine synthetase (see paper)
28% identity, 98% coverage: 3:436/444 of query aligns to 5:430/438 of 8ooxB
8oozA Glutamine synthetase (see paper)
28% identity, 98% coverage: 3:436/444 of query aligns to 5:422/430 of 8oozA
- binding adenosine-5'-triphosphate: G117 (≠ A131), E170 (≠ D193), F185 (= F208), K186 (≠ M209), Y187 (≠ H210), N233 (≠ H256), S235 (= S258), S315 (≠ A338), R317 (= R340)
- binding magnesium ion: E119 (= E133), H231 (= H254), E319 (= E342)
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)
32% identity, 86% coverage: 60:441/444 of query aligns to 52:444/446 of A0R083
- K363 (vs. gap) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
7tdvC Glutamine synthetase (see paper)
29% identity, 99% coverage: 2:441/444 of query aligns to 6:440/443 of 7tdvC
- binding adenosine-5'-diphosphate: G129 (≠ A131), E131 (= E133), E183 (≠ D193), D197 (≠ N207), F198 (= F208), K199 (≠ M209), Y200 (≠ H210), N246 (≠ H256), V247 (≠ Q257), S248 (= S258), R320 (= R330), S328 (≠ A338), R330 (= R340)
- binding magnesium ion: E131 (= E133), E131 (= E133), E133 (= E135), E188 (= E198), E195 (= E205), E195 (= E205), H244 (= H254), E332 (= E342)
- binding l-methionine-s-sulfoximine phosphate: E131 (= E133), E133 (= E135), E188 (= E198), E195 (= E205), G240 (= G250), H244 (= H254), R297 (= R307), E303 (≠ A313), R315 (= R325)
7tf6A Glutamine synthetase (see paper)
29% identity, 99% coverage: 2:441/444 of query aligns to 5:435/438 of 7tf6A
- binding glutamine: E128 (= E135), E183 (= E198), G235 (= G250), H239 (= H254), R292 (= R307), E298 (≠ A313)
- binding magnesium ion: E126 (= E133), E128 (= E135), E183 (= E198), E190 (= E205), H239 (= H254), E327 (= E342)
- binding : F58 (vs. gap), R60 (vs. gap), G232 (= G247), N234 (≠ P249), G296 (≠ F311), Y297 (≠ M312), R310 (= R325), Y367 (= Y382), Y421 (≠ A427), Q433 (≠ H439)
Sites not aligning to the query:
5dm3C Crystal structure of glutamine synthetase from chromohalobacter salexigens dsm 3043(csal_0679, target efi-550015) with bound adp
34% identity, 81% coverage: 76:436/444 of query aligns to 58:390/396 of 5dm3C
- active site: E115 (= E133), E117 (= E135), E162 (= E198), E169 (= E205), H218 (= H254), R286 (= R325), E303 (= E342), R305 (= R344)
- binding adenosine-5'-diphosphate: R173 (≠ M209), C174 (≠ H210), H220 (= H256), S222 (= S258), R301 (= R340)
7tenA Glutamine synthetase (see paper)
30% identity, 99% coverage: 3:441/444 of query aligns to 6:439/442 of 7tenA
- binding adenosine-5'-diphosphate: G128 (≠ A131), E130 (= E133), E182 (≠ D193), D196 (≠ N207), F197 (= F208), K198 (≠ M209), Y199 (≠ H210), N245 (≠ H256), S247 (= S258), R319 (= R330), S327 (≠ A338), R329 (= R340)
- binding l-methionine-s-sulfoximine phosphate: E130 (= E133), E132 (= E135), E187 (= E198), E194 (= E205), N238 (≠ P249), G239 (= G250), H243 (= H254), R296 (= R307), E302 (≠ A313), R314 (= R325), R333 (= R344)
7tf9S L. Monocytogenes gs(14)-q-glnr peptide (see paper)
30% identity, 99% coverage: 3:441/444 of query aligns to 7:440/443 of 7tf9S
- binding glutamine: E133 (= E135), Y155 (≠ R155), E188 (= E198), G240 (= G250), G242 (≠ A252), R297 (= R307), E303 (≠ A313)
- binding magnesium ion: E131 (= E133), E133 (= E135), E188 (= E198), E195 (= E205), H244 (= H254), E332 (= E342)
- binding : F59 (vs. gap), V60 (vs. gap), E418 (≠ A419), I422 (≠ T423), M426 (≠ A427)
Query Sequence
>H281DRAFT_01081 FitnessBrowser__Burk376:H281DRAFT_01081
MHDIDEFLKKNHVTEIEAIIPDMAGIARGKIIPRSKFESGESMRLPQAVMIQTVTGDYPD
GGTLTGVTDPDMVCVPDSSTIRMIPWAVDPTAQVIHDCVHFDGTPVAISPRRVLRRVLEL
YKAKGWKPVIAPELEFYLVDMNKDPDLPLQPPIGRTGRAETGRQAYSIEAVNEFDPLFED
IYEYCDVQELEVDTLIHEVGAAQMEINFMHGDPLKLADSVFLFKRTVREAALRHKMYATF
MAKPMEGEPGSAMHMHQSLVDGRTGHNLFTGADGKPTSLFTSYIAGLQKYTPALMPIFAP
YINSYRRLSRFMAAPINVAWGYDNRTVGFRIPHSGPAARRIENRIPGVDCNPYLAIAATL
AAGYLGMTQKLDATEPLLSDGYELPYQLPRNLEEGLTLMGACEPIAEVLGDKFVQAYLAL
KETEYEAFFRVISSWERRHLLLHV
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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