SitesBLAST
Comparing CCNA_03230 FitnessBrowser__Caulo:CCNA_03230 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)
35% identity, 97% coverage: 16:464/465 of query aligns to 19:471/472 of P78061
- H282 (= H276) mutation to N: Activity is impaired to 9% of wild-type.
- R357 (= R351) 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)
30% identity, 94% coverage: 19:457/465 of query aligns to 1:440/447 of 8oooA
- binding 2-oxoglutaric acid: F17 (≠ E35), R19 (≠ E37), A33 (≠ I51), R87 (vs. gap), V93 (≠ T113), P170 (≠ D197), R173 (≠ F200), R174 (≠ E201), S190 (≠ L217)
- binding adenosine-5'-triphosphate: E136 (= E155), E188 (≠ D215), F203 (≠ L230), K204 (≠ Q231), F205 (≠ H232), H251 (= H278), S253 (= S280), R325 (= R351), R335 (= R361)
8ooqB Glutamine synthetase from Methanothermococcus thermolithotrophicus (see paper)
30% identity, 94% coverage: 20:457/465 of query aligns to 1:439/446 of 8ooqB
- binding 2-oxoglutaric acid: F16 (≠ E35), R18 (≠ E37), A32 (≠ I51), R86 (vs. gap), V92 (≠ T113), P169 (≠ D197), R172 (≠ F200), R173 (≠ E201), S189 (≠ L217)
- binding magnesium ion: E137 (= E157), E192 (= E220), E199 (= E227)
8ooxB Glutamine synthetase (see paper)
31% identity, 79% coverage: 91:457/465 of query aligns to 62:430/438 of 8ooxB
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, 85% coverage: 68:463/465 of query aligns to 43:446/446 of P9WN37
- K363 (≠ Q390) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
8oozA Glutamine synthetase (see paper)
32% identity, 79% coverage: 92:457/465 of query aligns to 57:422/430 of 8oozA
- binding adenosine-5'-triphosphate: G117 (≠ A153), E170 (≠ D215), F185 (≠ L230), K186 (≠ Q231), Y187 (≠ H232), N233 (≠ H278), S235 (= S280), S315 (≠ N359), R317 (= R361)
- binding magnesium ion: E119 (= E155), H231 (= H276), E319 (= E363)
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)
33% identity, 84% coverage: 68:457/465 of query aligns to 43:439/446 of A0R083
- K363 (≠ Q390) 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)
29% identity, 95% coverage: 20:459/465 of query aligns to 4:437/443 of 4lnkA
- active site: D52 (= D77), E131 (= E155), E133 (= E157), E188 (= E220), E195 (= E227), H244 (= H276), R315 (= R346), E332 (= E363), R334 (= R365)
- binding adenosine-5'-diphosphate: K43 (≠ S60), M50 (≠ T75), F198 (≠ L230), Y200 (≠ H232), N246 (≠ H278), S248 (= S280), S324 (= S355), S328 (≠ N359), R330 (= R361)
- binding glutamic acid: E133 (= E157), E188 (= E220), V189 (≠ S221), N239 (≠ P271), G240 (= G272), G242 (≠ A274), E303 (≠ G334)
- binding magnesium ion: E131 (= E155), E188 (= E220), E195 (= E227), H244 (= H276), E332 (= E363)
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, 95% coverage: 20:459/465 of query aligns to 4:437/443 of 4lniA
- active site: D52 (= D77), E131 (= E155), E133 (= E157), E188 (= E220), E195 (= E227), H244 (= H276), R315 (= R346), E332 (= E363), R334 (= R365)
- binding adenosine-5'-diphosphate: E131 (= E155), E183 (≠ D215), D197 (≠ N229), Y200 (≠ H232), N246 (≠ H278), S248 (= S280), R320 (= R351), R330 (= R361)
- binding magnesium ion: E131 (= E155), E131 (= E155), E133 (= E157), E188 (= E220), E195 (= E227), E195 (= E227), H244 (= H276), E332 (= E363)
- binding l-methionine-s-sulfoximine phosphate: E133 (= E157), E188 (= E220), H244 (= H276), R297 (= R328), E303 (≠ G334), R315 (= R346), R334 (= R365)
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, 95% coverage: 20:459/465 of query aligns to 5:438/444 of P12425
- G59 (= G83) 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 (≠ N86) 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 (= E155) binding
- E134 (= E157) binding
- E189 (= E220) binding
- V190 (≠ S221) 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 (= E227) binding
- G241 (= G272) binding
- H245 (= H276) binding
- G302 (≠ D332) 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 (≠ G334) 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 (= P336) 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 (= E363) binding
- E424 (= E445) 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, 95% coverage: 20:459/465 of query aligns to 8:441/447 of 4s0rD
- active site: D56 (= D77), E135 (= E155), E137 (= E157), E192 (= E220), E199 (= E227), H248 (= H276), R319 (= R346), E336 (= E363), R338 (= R365)
- binding glutamine: E137 (= E157), E192 (= E220), R301 (= R328), E307 (≠ G334)
- binding magnesium ion: I66 (≠ A87), E135 (= E155), E135 (= E155), E199 (= E227), H248 (= H276), H248 (= H276), E336 (= E363), H419 (≠ A437)
- binding : F63 (≠ A84), V64 (= V85), R65 (≠ N86), I66 (≠ A87), D161 (≠ S189), G241 (≠ N269), V242 (≠ E270), N243 (≠ P271), G305 (≠ D332), Y306 (≠ S333), Y376 (≠ G403), I426 (≠ A444), M430 (≠ T448)
8tfkA Glutamine synthetase (see paper)
30% identity, 83% coverage: 70:457/465 of query aligns to 43:432/440 of 8tfkA
- binding adenosine-5'-diphosphate: E128 (= E155), D194 (≠ N229), F195 (≠ L230), F197 (≠ H232), N243 (≠ H278), R312 (= R346), R317 (= R351), G325 (≠ N359), R327 (= R361)
- binding magnesium ion: E128 (= E155), E128 (= E155), E130 (= E157), E185 (= E220), E192 (= E227), E192 (= E227), H241 (= H276), E329 (= E363)
- binding l-methionine-s-sulfoximine phosphate: E128 (= E155), E130 (= E157), E185 (= E220), E192 (= E227), G237 (= G272), H241 (= H276), R294 (= R328), E300 (≠ G334), R312 (= R346), R331 (= R365)
8ufjB Glutamine synthetase (see paper)
28% identity, 95% coverage: 16:457/465 of query aligns to 2:436/444 of 8ufjB
5dm3C Crystal structure of glutamine synthetase from chromohalobacter salexigens dsm 3043(csal_0679, target efi-550015) with bound adp
33% identity, 78% coverage: 95:457/465 of query aligns to 55:390/396 of 5dm3C
- active site: E115 (= E155), E117 (= E157), E162 (= E220), E169 (= E227), H218 (= H276), R286 (= R346), E303 (= E363), R305 (= R365)
- binding adenosine-5'-diphosphate: R173 (≠ Q231), C174 (≠ H232), H220 (= H278), S222 (= S280), R301 (= R361)
7tdpA Structure of paenibacillus polymyxa gs bound to met-sox-p-adp (transition state complex) to 1.98 angstom (see paper)
30% identity, 83% coverage: 77:462/465 of query aligns to 51:436/439 of 7tdpA
- binding adenosine-5'-diphosphate: N123 (vs. gap), G125 (≠ A153), E127 (= E155), E179 (≠ D215), D193 (≠ N229), Y196 (≠ H232), N242 (≠ H278), S244 (= S280), R316 (= R351), R326 (= R361)
- binding magnesium ion: E127 (= E155), E127 (= E155), E129 (= E157), E184 (= E220), E191 (= E227), E191 (= E227), H240 (= H276), E328 (= E363)
- binding l-methionine-s-sulfoximine phosphate: E127 (= E155), E129 (= E157), E184 (= E220), E191 (= E227), G236 (= G272), H240 (= H276), R293 (= R328), E299 (≠ G334), R311 (= R346), R330 (= R365)
7tfaB Glutamine synthetase (see paper)
30% identity, 83% coverage: 77:462/465 of query aligns to 51:438/441 of 7tfaB
- binding glutamine: E131 (= E157), Y153 (≠ R177), E186 (= E220), G238 (= G272), H242 (= H276), R295 (= R328), E301 (≠ G334)
- binding magnesium ion: E129 (= E155), E131 (= E157), E186 (= E220), E193 (= E227), H242 (= H276), E330 (= E363)
- binding : Y58 (≠ A84), R60 (≠ N86), V187 (≠ S221), N237 (≠ P271), G299 (≠ D332), Y300 (≠ S333), R313 (= R346), M424 (≠ T448)
5dm3A Crystal structure of glutamine synthetase from chromohalobacter salexigens dsm 3043(csal_0679, target efi-550015) with bound adp
31% identity, 79% coverage: 91:457/465 of query aligns to 47:368/374 of 5dm3A
- active site: E107 (= E155), E109 (= E157), E146 (≠ Y188), E150 (= E227), H199 (= H276), R265 (= R346), E282 (= E363), R284 (= R365)
- binding adenosine-5'-diphosphate: I103 (= I151), E141 (≠ T183), R154 (≠ Q231), C155 (≠ H232), H201 (= H278), S203 (= S280), R280 (= R361)
7tenA Glutamine synthetase (see paper)
29% identity, 92% coverage: 31:459/465 of query aligns to 14:436/442 of 7tenA
- binding adenosine-5'-diphosphate: G128 (≠ A153), E130 (= E155), E182 (≠ D215), D196 (≠ N229), F197 (≠ L230), K198 (≠ Q231), Y199 (≠ H232), N245 (≠ H278), S247 (= S280), R319 (= R351), S327 (≠ N359), R329 (= R361)
- binding l-methionine-s-sulfoximine phosphate: E130 (= E155), E132 (= E157), E187 (= E220), E194 (= E227), N238 (≠ P271), G239 (= G272), H243 (= H276), R296 (= R328), E302 (≠ G334), R314 (= R346), R333 (= R365)
7tf9S L. Monocytogenes gs(14)-q-glnr peptide (see paper)
29% identity, 92% coverage: 31:459/465 of query aligns to 15:437/443 of 7tf9S
- binding glutamine: E133 (= E157), Y155 (≠ R177), E188 (= E220), G240 (= G272), G242 (≠ A274), R297 (= R328), E303 (≠ G334)
- binding magnesium ion: E131 (= E155), E133 (= E157), E188 (= E220), E195 (= E227), H244 (= H276), E332 (= E363)
- binding : F59 (≠ A84), V60 (= V85), E418 (≠ R440), I422 (≠ A444), M426 (≠ T448)
7tdvC Glutamine synthetase (see paper)
27% identity, 95% coverage: 20:459/465 of query aligns to 4:437/443 of 7tdvC
- binding adenosine-5'-diphosphate: G129 (≠ A153), E131 (= E155), E183 (≠ D215), D197 (≠ N229), F198 (≠ L230), K199 (≠ Q231), Y200 (≠ H232), N246 (≠ H278), V247 (≠ Q279), S248 (= S280), R320 (= R351), S328 (≠ N359), R330 (= R361)
- binding magnesium ion: E131 (= E155), E131 (= E155), E133 (= E157), E188 (= E220), E195 (= E227), E195 (= E227), H244 (= H276), E332 (= E363)
- binding l-methionine-s-sulfoximine phosphate: E131 (= E155), E133 (= E157), E188 (= E220), E195 (= E227), G240 (= G272), H244 (= H276), R297 (= R328), E303 (≠ G334), R315 (= R346)
Query Sequence
>CCNA_03230 FitnessBrowser__Caulo:CCNA_03230
MKPKHNKAKRDQILDRGVSTIEEAKDWFARQHIEEIECVVPDLAGVARGKIMPVRKFLGS
PSMNLPLAVFYQTITGDFPEFEGAVNAVQSDTDIFLTPDFATLAAVPWAQDPTAQVIHDA
FHPDGRPVEEAPRQVLRRVLALYADKGWHPIVAPEIEFYLVDRNTDPDYPLKPPIGRSGR
PETGRQGYSISAVNEFDALFEDMYEYSERQGLEIDTLIHESGVAQMEINLQHGHPLELAD
QVFMMKRTIREAALEHEIYATFMAKPMANEPGSAMHIHQSIVDKKGRNLFSDEDGAESAM
FHGFIAGQQTYLPAIMAILAPYVNSYRRISRDSGAPVNTQWGYDNRTCGLRVPPSGPNNR
RVENRIPSSDANPYLAIAASLAAGYLGMVQGLKPSEPVSIDAGARGIELPRSLSDSLRLF
VACQPLVEILGPTFCAAYDRVKQAEYETFMRTISPWEREFLLLNV
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