SitesBLAST
Comparing CCNA_03240 FitnessBrowser__Caulo:CCNA_03240 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)
39% identity, 98% coverage: 9:460/460 of query aligns to 25:472/472 of P78061
- H282 (= H267) mutation to N: Activity is impaired to 9% of wild-type.
- R357 (= R342) mutation to Q: Activity is impaired to 3% of wild-type.
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)
29% identity, 95% coverage: 21:457/460 of query aligns to 17:444/446 of A0R083
- K363 (≠ N381) 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)
29% identity, 95% coverage: 21:457/460 of query aligns to 17:444/446 of P9WN37
- K363 (≠ N381) 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)
27% identity, 98% coverage: 6:458/460 of query aligns to 1:446/447 of 8oooA
- binding 2-oxoglutaric acid: F17 (= F23), R19 (≠ E25), A33 (≠ R39), R87 (≠ L98), V93 (= V102), P170 (≠ A187), R173 (≠ L190), R174 (= R191), S190 (≠ A207)
- binding adenosine-5'-triphosphate: E136 (= E144), E188 (= E205), F203 (≠ L220), K204 (= K221), F205 (≠ H222), H251 (= H269), S253 (= S271), R325 (= R342), R335 (≠ H352)
8ooqB Glutamine synthetase from Methanothermococcus thermolithotrophicus (see paper)
28% identity, 95% coverage: 20:458/460 of query aligns to 13:445/446 of 8ooqB
- binding 2-oxoglutaric acid: F16 (= F23), R18 (≠ E25), A32 (≠ R39), R86 (≠ L98), V92 (= V102), P169 (≠ A187), R172 (≠ L190), R173 (= R191), S189 (≠ A207)
- binding magnesium ion: E137 (= E146), E192 (= E210), E199 (= E217)
8ooxB Glutamine synthetase (see paper)
28% identity, 97% coverage: 15:459/460 of query aligns to 9:437/438 of 8ooxB
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)
29% identity, 93% coverage: 15:444/460 of query aligns to 12:428/444 of P12425
- G59 (= G73) 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 (≠ W76) 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 (= E144) binding
- E134 (= E146) binding
- E189 (= E210) binding
- V190 (≠ F211) 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 (= E217) binding
- G241 (= G263) binding
- H245 (= H267) binding
- G302 (≠ N323) 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 (≠ Y325) 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 (= P327) 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 (= E354) binding
- E424 (= E440) 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)
29% identity, 93% coverage: 15:444/460 of query aligns to 15:431/447 of 4s0rD
- active site: D56 (≠ N65), E135 (= E144), E137 (= E146), E192 (= E210), E199 (= E217), H248 (= H267), R319 (= R337), E336 (= E354), R338 (= R356)
- binding glutamine: E137 (= E146), E192 (= E210), R301 (= R319), E307 (≠ Y325)
- binding magnesium ion: I66 (≠ E77), E135 (= E144), E135 (= E144), E199 (= E217), H248 (= H267), H248 (= H267), E336 (= E354), H419 (≠ M432)
- binding : F63 (≠ L74), V64 (= V75), R65 (≠ W76), I66 (≠ E77), D161 (≠ G169), G241 (≠ D260), V242 (≠ R261), N243 (≠ A262), G305 (≠ N323), Y306 (≠ S324), Y376 (≠ A395), I426 (≠ T439), M430 (≠ R443)
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)
29% identity, 93% coverage: 15:444/460 of query aligns to 11:427/443 of 4lnkA
- active site: D52 (≠ N65), E131 (= E144), E133 (= E146), E188 (= E210), E195 (= E217), H244 (= H267), R315 (= R337), E332 (= E354), R334 (= R356)
- binding adenosine-5'-diphosphate: K43 (≠ R53), M50 (≠ L60), F198 (≠ L220), Y200 (≠ H222), N246 (≠ H269), S248 (= S271), S324 (≠ G346), S328 (≠ T350), R330 (≠ H352)
- binding glutamic acid: E133 (= E146), E188 (= E210), V189 (≠ F211), N239 (≠ A262), G240 (= G263), G242 (= G265), E303 (≠ Y325)
- binding magnesium ion: E131 (= E144), E188 (= E210), E195 (= E217), H244 (= H267), E332 (= E354)
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)
29% identity, 93% coverage: 15:444/460 of query aligns to 11:427/443 of 4lniA
- active site: D52 (≠ N65), E131 (= E144), E133 (= E146), E188 (= E210), E195 (= E217), H244 (= H267), R315 (= R337), E332 (= E354), R334 (= R356)
- binding adenosine-5'-diphosphate: E131 (= E144), E183 (= E205), D197 (≠ T219), Y200 (≠ H222), N246 (≠ H269), S248 (= S271), R320 (= R342), R330 (≠ H352)
- binding magnesium ion: E131 (= E144), E131 (= E144), E133 (= E146), E188 (= E210), E195 (= E217), E195 (= E217), H244 (= H267), E332 (= E354)
- binding l-methionine-s-sulfoximine phosphate: E133 (= E146), E188 (= E210), H244 (= H267), R297 (= R319), E303 (≠ Y325), R315 (= R337), R334 (= R356)
8oozA Glutamine synthetase (see paper)
27% identity, 97% coverage: 15:459/460 of query aligns to 9:429/430 of 8oozA
- binding adenosine-5'-triphosphate: G117 (≠ A142), E170 (= E205), F185 (≠ L220), K186 (= K221), Y187 (≠ H222), N233 (≠ H269), S235 (= S271), S315 (≠ T350), R317 (≠ H352)
- binding magnesium ion: E119 (= E144), H231 (= H267), E319 (= E354)
8wwvA Glutamine synthetase
29% identity, 93% coverage: 21:446/460 of query aligns to 29:465/490 of 8wwvA
- binding adenosine-5'-diphosphate: G155 (≠ A142), E157 (= E144), R224 (≠ E205), F239 (≠ L220), D240 (≠ K221), V241 (≠ H222), H288 (= H269), S290 (= S271), R374 (= R351), E376 (= E354)
- binding magnesium ion: E157 (= E144), E236 (= E217)
- binding manganese (ii) ion: E157 (= E144), E159 (= E146), E229 (= E210), E236 (= E217), H286 (= H267), E376 (= E354)
- binding l-methionine-s-sulfoximine phosphate: E157 (= E144), E159 (= E146), E229 (= E210), E236 (= E217), A282 (vs. gap), H286 (= H267), R340 (= R319), K358 (≠ R337)
7tfaB Glutamine synthetase (see paper)
28% identity, 96% coverage: 15:457/460 of query aligns to 10:438/441 of 7tfaB
- binding glutamine: E131 (= E159), Y153 (vs. gap), E186 (= E210), G238 (= G263), H242 (= H267), R295 (= R319), E301 (≠ Y325)
- binding magnesium ion: E129 (≠ N157), E131 (= E159), E186 (= E210), E193 (= E217), H242 (= H267), E330 (= E354)
- binding : Y58 (≠ L74), R60 (≠ W76), V187 (≠ F211), N237 (≠ A262), G299 (≠ N323), Y300 (≠ S324), R313 (= R337), M424 (≠ R443)
8wwuB Glutamine synthetase
29% identity, 93% coverage: 21:446/460 of query aligns to 31:467/492 of 8wwuB
- binding phosphoaminophosphonic acid-adenylate ester: G157 (≠ A142), E159 (= E144), R226 (≠ E205), F241 (≠ L220), V243 (≠ H222), H290 (= H269), S292 (= S271), K360 (≠ R337), R365 (= R342), R376 (= R351)
- binding magnesium ion: E159 (= E144), E238 (= E217)
- binding manganese (ii) ion: E159 (= E144), E161 (= E146), E231 (= E210), E238 (= E217), H288 (= H267), E378 (= E354)
8ufjB Glutamine synthetase (see paper)
27% identity, 95% coverage: 21:457/460 of query aligns to 19:441/444 of 8ufjB
8tfkA Glutamine synthetase (see paper)
27% identity, 95% coverage: 21:457/460 of query aligns to 15:437/440 of 8tfkA
- binding adenosine-5'-diphosphate: E128 (= E144), D194 (≠ T219), F195 (≠ L220), F197 (≠ H222), N243 (≠ H269), R312 (= R337), R317 (= R342), G325 (≠ T350), R327 (≠ H352)
- binding magnesium ion: E128 (= E144), E128 (= E144), E130 (= E146), E185 (= E210), E192 (= E217), E192 (= E217), H241 (= H267), E329 (= E354)
- binding l-methionine-s-sulfoximine phosphate: E128 (= E144), E130 (= E146), E185 (= E210), E192 (= E217), G237 (= G263), H241 (= H267), R294 (= R319), E300 (≠ Y325), R312 (= R337), R331 (= R356)
7tdpA Structure of paenibacillus polymyxa gs bound to met-sox-p-adp (transition state complex) to 1.98 angstom (see paper)
28% identity, 96% coverage: 15:457/460 of query aligns to 10:436/439 of 7tdpA
- binding adenosine-5'-diphosphate: N123 (≠ Q153), G125 (= G155), E127 (≠ N157), E179 (= E205), D193 (≠ T219), Y196 (≠ H222), N242 (≠ H269), S244 (= S271), R316 (= R342), R326 (≠ H352)
- binding magnesium ion: E127 (≠ N157), E127 (≠ N157), E129 (= E159), E184 (= E210), E191 (= E217), E191 (= E217), H240 (= H267), E328 (= E354)
- binding l-methionine-s-sulfoximine phosphate: E127 (≠ N157), E129 (= E159), E184 (= E210), E191 (= E217), G236 (= G263), H240 (= H267), R293 (= R319), E299 (≠ Y325), R311 (= R337), R330 (= R356)
7tenA Glutamine synthetase (see paper)
26% identity, 97% coverage: 15:458/460 of query aligns to 10:440/442 of 7tenA
- binding adenosine-5'-diphosphate: G128 (= G155), E130 (≠ N157), E182 (= E205), D196 (≠ T219), F197 (≠ L220), K198 (= K221), Y199 (≠ H222), N245 (≠ H269), S247 (= S271), R319 (= R342), S327 (≠ T350), R329 (≠ H352)
- binding l-methionine-s-sulfoximine phosphate: E130 (≠ N157), E132 (= E159), E187 (= E210), E194 (= E217), N238 (≠ A262), G239 (= G263), H243 (= H267), R296 (= R319), E302 (≠ Y325), R314 (= R337), R333 (= R356)
7tf9S L. Monocytogenes gs(14)-q-glnr peptide (see paper)
26% identity, 97% coverage: 15:458/460 of query aligns to 11:441/443 of 7tf9S
- binding glutamine: E133 (= E159), Y155 (≠ V177), E188 (= E210), G240 (= G263), G242 (= G265), R297 (= R319), E303 (≠ Y325)
- binding magnesium ion: E131 (≠ N157), E133 (= E159), E188 (= E210), E195 (= E217), H244 (= H267), E332 (= E354)
- binding : F59 (≠ L74), V60 (= V75), E418 (≠ S435), I422 (≠ T439), M426 (≠ R443)
7tf6A Glutamine synthetase (see paper)
25% identity, 98% coverage: 9:458/460 of query aligns to 5:436/438 of 7tf6A
- binding glutamine: E128 (= E159), E183 (= E210), G235 (= G263), H239 (= H267), R292 (= R319), E298 (≠ Y325)
- binding magnesium ion: E126 (≠ N157), E128 (= E159), E183 (= E210), E190 (= E217), H239 (= H267), E327 (= E354)
- binding : F58 (≠ L74), R60 (≠ W76), G232 (≠ D260), N234 (≠ A262), G296 (≠ N323), Y297 (≠ S324), R310 (= R337), Y367 (= Y394), Y421 (≠ R443), Q433 (≠ W455)
Sites not aligning to the query:
Query Sequence
>CCNA_03240 FitnessBrowser__Caulo:CCNA_03240
MMSAVADIQECRDFLAAHPQVKFVEVFFTSMTGVPRGKRLRVHELEAIYEYGRFLPGSVL
VVDTNGADCEDTGLVWEDGDADRRARPVPGTLTLAPWLGPDVAQVMLSLYELDGTPNDLD
PRHVLQRVLDRYAADGLTPVAACELEYYLVDLQRGPNGELLPAKSLQTGLRPTGIQVYGL
PELEAHAPFLRELWDVADTLGVPLEGAISEFAPAQVELTLKHKPDALRAADDAVLYKRAA
KGVALRHGMEATFMAKPWSDRAGNGFHVHLSVNDAAGNNLCASEDIEGSDLLKHAIGGMK
VLLGEGMAILAPNANSYRRFKANSYAPVAPTWGVNNRTVSLRVPAGPPKTRHVEHRVAGA
DGNPYLVLAVLLASAHHGITNKIDPGPAVIGDGYAAAAKENIRLPNNWFAAVDLFEQSSV
LRDYLGDRFVDMFVSVKRTEQARFFEVVTELDFDWYLRNA
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