SitesBLAST
Comparing AO356_30085 FitnessBrowser__pseudo5_N2C3_1:AO356_30085 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)
7cqwA Gmas/adp complex-conformation 1 (see paper)
41% identity, 96% coverage: 9:436/444 of query aligns to 7:423/430 of 7cqwA
7cquA Gmas/adp/metsox-p complex (see paper)
41% identity, 96% coverage: 9:436/444 of query aligns to 6:422/429 of 7cquA
- binding adenosine-5'-diphosphate: E121 (= E125), Y173 (= Y180), N187 (= N194), W188 (≠ Y195), D189 (≠ T196), Y190 (= Y197), H236 (= H243), L237 (= L244), S238 (= S245), R316 (= R326), R322 (= R331)
- binding magnesium ion: E121 (= E125), E121 (= E125), E123 (= E127), E178 (= E185), E185 (= E192), E185 (= E192), H234 (= H241), E324 (= E333)
- binding l-methionine-s-sulfoximine phosphate: E121 (= E125), E123 (= E127), E178 (= E185), E185 (= E192), T229 (≠ A236), G230 (= G237), H234 (= H241), R287 (= R297), W299 (= W309), R311 (= R321), R326 (= R335)
7cqqA Gmas in complex with amppnp and metsox (see paper)
41% identity, 96% coverage: 9:436/444 of query aligns to 6:422/429 of 7cqqA
- binding phosphoaminophosphonic acid-adenylate ester: E121 (= E125), Y173 (= Y180), E185 (= E192), N187 (= N194), D189 (≠ T196), Y190 (= Y197), H234 (= H241), H236 (= H243), S238 (= S245), R311 (= R321), R316 (= R326), R322 (= R331), E324 (= E333)
- binding magnesium ion: E121 (= E125), E121 (= E125), E123 (= E127), E178 (= E185), E185 (= E192), E185 (= E192), H234 (= H241), E324 (= E333)
- binding (2s)-2-amino-4-(methylsulfonimidoyl)butanoic acid: E123 (= E127), E178 (= E185), T229 (≠ A236), H234 (= H241), R287 (= R297), W299 (= W309), R311 (= R321), R326 (= R335)
7cqnA Gmas in complex with amppcp (see paper)
41% identity, 96% coverage: 9:436/444 of query aligns to 6:422/429 of 7cqnA
- binding phosphomethylphosphonic acid adenylate ester: G45 (= G48), D61 (= D65), E121 (= E125), Y173 (= Y180), Q174 (= Q181), W188 (≠ Y195), D189 (≠ T196), Y190 (= Y197), H236 (= H243), S238 (= S245), R311 (= R321), R316 (= R326), R322 (= R331)
7tdpA Structure of paenibacillus polymyxa gs bound to met-sox-p-adp (transition state complex) to 1.98 angstom (see paper)
35% identity, 98% coverage: 8:444/444 of query aligns to 9:439/439 of 7tdpA
- binding adenosine-5'-diphosphate: N123 (= N121), G125 (= G123), E127 (= E125), E179 (≠ Y180), D193 (≠ N194), Y196 (= Y197), N242 (≠ H243), S244 (= S245), R316 (= R326), R326 (vs. gap)
- binding magnesium ion: E127 (= E125), E127 (= E125), E129 (= E127), E184 (= E185), E191 (= E192), E191 (= E192), H240 (= H241), E328 (= E333)
- binding l-methionine-s-sulfoximine phosphate: E127 (= E125), E129 (= E127), E184 (= E185), E191 (= E192), G236 (= G237), H240 (= H241), R293 (= R297), E299 (≠ S303), R311 (= R321), R330 (= R335)
7tfaB Glutamine synthetase (see paper)
35% identity, 98% coverage: 8:444/444 of query aligns to 9:441/441 of 7tfaB
- binding glutamine: E131 (= E127), Y153 (≠ N147), E186 (= E185), G238 (= G237), H242 (= H241), R295 (= R297), E301 (≠ S303)
- binding magnesium ion: E129 (= E125), E131 (= E127), E186 (= E185), E193 (= E192), H242 (= H241), E330 (= E333)
- binding : Y58 (≠ M57), R60 (≠ E60), V187 (≠ D186), N237 (≠ A236), G299 (= G301), Y300 (≠ N302), R313 (= R321), M424 (≠ E427)
7tdvC Glutamine synthetase (see paper)
35% identity, 98% coverage: 5:440/444 of query aligns to 7:439/443 of 7tdvC
- binding adenosine-5'-diphosphate: G129 (= G123), E131 (= E125), E183 (≠ Y180), D197 (≠ N194), F198 (≠ Y195), K199 (≠ T196), Y200 (= Y197), N246 (≠ H243), V247 (≠ L244), S248 (= S245), R320 (= R326), S328 (vs. gap), R330 (vs. gap)
- binding magnesium ion: E131 (= E125), E131 (= E125), E133 (= E127), E188 (= E185), E195 (= E192), E195 (= E192), H244 (= H241), E332 (= E333)
- binding l-methionine-s-sulfoximine phosphate: E131 (= E125), E133 (= E127), E188 (= E185), E195 (= E192), G240 (= G237), H244 (= H241), R297 (= R297), E303 (≠ S303), R315 (= R321)
7tf6A Glutamine synthetase (see paper)
35% identity, 98% coverage: 5:440/444 of query aligns to 6:434/438 of 7tf6A
- binding glutamine: E128 (= E127), E183 (= E185), G235 (= G237), H239 (= H241), R292 (= R297), E298 (≠ S303)
- binding magnesium ion: E126 (= E125), E128 (= E127), E183 (= E185), E190 (= E192), H239 (= H241), E327 (= E333)
- binding : F58 (≠ M57), R60 (≠ E60), G232 (≠ K234), N234 (≠ A236), G296 (= G301), Y297 (≠ N302), R310 (= R321), Y367 (= Y373), Y421 (≠ E427), Q433 (≠ R439)
Sites not aligning to the query:
8tfkA Glutamine synthetase (see paper)
35% identity, 97% coverage: 10:440/444 of query aligns to 10:436/440 of 8tfkA
- binding adenosine-5'-diphosphate: E128 (= E125), D194 (≠ N194), F195 (≠ Y195), F197 (≠ Y197), N243 (≠ H243), R312 (= R321), R317 (= R326), G325 (vs. gap), R327 (vs. gap)
- binding magnesium ion: E128 (= E125), E128 (= E125), E130 (= E127), E185 (= E185), E192 (= E192), E192 (= E192), H241 (= H241), E329 (= E333)
- binding l-methionine-s-sulfoximine phosphate: E128 (= E125), E130 (= E127), E185 (= E185), E192 (= E192), G237 (= G237), H241 (= H241), R294 (= R297), E300 (≠ S303), R312 (= R321), R331 (= R335)
8oozA Glutamine synthetase (see paper)
33% identity, 99% coverage: 5:444/444 of query aligns to 5:430/430 of 8oozA
- binding adenosine-5'-triphosphate: G117 (= G123), E170 (≠ Y180), F185 (≠ Y195), K186 (≠ T196), Y187 (= Y197), N233 (≠ H243), S235 (= S245), S315 (≠ Y329), R317 (= R331)
- binding magnesium ion: E119 (= E125), H231 (= H241), E319 (= E333)
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)
36% identity, 98% coverage: 8:440/444 of query aligns to 10:443/446 of A0R083
- K363 (≠ R360) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
8ufjB Glutamine synthetase (see paper)
34% identity, 97% coverage: 10:440/444 of query aligns to 14:440/444 of 8ufjB
8ooxB Glutamine synthetase (see paper)
33% identity, 99% coverage: 5:444/444 of query aligns to 5:438/438 of 8ooxB
8oooA Glutamine synthetase from methanothermococcus thermolithotrophicus in complex with 2-oxoglutarate and mgatp at 2.15 a resolution (see paper)
34% identity, 97% coverage: 10:440/444 of query aligns to 10:444/447 of 8oooA
- binding 2-oxoglutaric acid: F17 (≠ Y17), R19 (≠ L19), A33 (≠ S33), R87 (≠ Q81), V93 (≠ Y84), P170 (≠ R162), R173 (≠ L165), R174 (≠ E166), S190 (≠ I182)
- binding adenosine-5'-triphosphate: E136 (= E125), E188 (≠ Y180), F203 (≠ Y195), K204 (≠ T196), F205 (≠ Y197), H251 (= H243), S253 (= S245), R325 (= R326), R335 (vs. gap)
8ooqB Glutamine synthetase from Methanothermococcus thermolithotrophicus (see paper)
34% identity, 97% coverage: 10:440/444 of query aligns to 9:443/446 of 8ooqB
- binding 2-oxoglutaric acid: F16 (≠ Y17), R18 (≠ L19), A32 (≠ S33), R86 (≠ Q81), V92 (≠ Y84), P169 (≠ R162), R172 (≠ L165), R173 (≠ E166), S189 (≠ I182)
- binding magnesium ion: E137 (= E127), E192 (= E185), E199 (= E192)
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)
35% identity, 98% coverage: 8:440/444 of query aligns to 10:443/446 of P9WN37
- K363 (≠ R360) 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)
33% identity, 98% coverage: 5:440/444 of query aligns to 7:439/443 of 4lnkA
- active site: D52 (≠ A50), E131 (= E125), E133 (= E127), E188 (= E185), E195 (= E192), H244 (= H241), R315 (= R321), E332 (= E333), R334 (= R335)
- binding adenosine-5'-diphosphate: K43 (≠ T41), M50 (≠ G48), F198 (≠ Y195), Y200 (= Y197), N246 (≠ H243), S248 (= S245), S324 (≠ G330), S328 (vs. gap), R330 (vs. gap)
- binding glutamic acid: E133 (= E127), E188 (= E185), V189 (≠ D186), N239 (≠ A236), G240 (= G237), G242 (= G239), E303 (≠ S303)
- binding magnesium ion: E131 (= E125), E188 (= E185), E195 (= E192), H244 (= H241), E332 (= E333)
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)
33% identity, 98% coverage: 5:440/444 of query aligns to 7:439/443 of 4lniA
- active site: D52 (≠ A50), E131 (= E125), E133 (= E127), E188 (= E185), E195 (= E192), H244 (= H241), R315 (= R321), E332 (= E333), R334 (= R335)
- binding adenosine-5'-diphosphate: E131 (= E125), E183 (≠ Y180), D197 (≠ N194), Y200 (= Y197), N246 (≠ H243), S248 (= S245), R320 (= R326), R330 (vs. gap)
- binding magnesium ion: E131 (= E125), E131 (= E125), E133 (= E127), E188 (= E185), E195 (= E192), E195 (= E192), H244 (= H241), E332 (= E333)
- binding l-methionine-s-sulfoximine phosphate: E133 (= E127), E188 (= E185), H244 (= H241), R297 (= R297), E303 (≠ S303), R315 (= R321), R334 (= R335)
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)
33% identity, 98% coverage: 5:440/444 of query aligns to 8:440/444 of P12425
- G59 (= G56) 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 (≠ E60) 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 (= E125) binding
- E134 (= E127) binding
- E189 (= E185) binding
- V190 (≠ D186) 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 (= E192) binding
- G241 (= G237) binding
- H245 (= H241) binding
- G302 (= G301) 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 (≠ S303) 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 (= P311) 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 (= E333) 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
4s0rD Structure of gs-tnra complex (see paper)
33% identity, 98% coverage: 5:440/444 of query aligns to 11:443/447 of 4s0rD
- active site: D56 (≠ A50), E135 (= E125), E137 (= E127), E192 (= E185), E199 (= E192), H248 (= H241), R319 (= R321), E336 (= E333), R338 (= R335)
- binding glutamine: E137 (= E127), E192 (= E185), R301 (= R297), E307 (≠ S303)
- binding magnesium ion: I66 (≠ P61), E135 (= E125), E135 (= E125), E199 (= E192), H248 (= H241), H248 (= H241), E336 (= E333), H419 (≠ E416)
- binding : F63 (≠ M57), V64 (≠ M59), R65 (≠ E60), I66 (≠ P61), D161 (= D149), G241 (≠ K234), V242 (≠ R235), N243 (≠ A236), G305 (= G301), Y306 (≠ N302), Y376 (= Y373), I426 (≠ M423), M430 (≠ E427)
Query Sequence
>AO356_30085 FitnessBrowser__pseudo5_N2C3_1:AO356_30085
MLPAETQRIIDKHGIKYVLAQFVDIHGAAKTKSVPICGLKTVAEEGAGFAGFAISGMGME
PHGPDFMARGDLSTLTPVPWQPGYGRVVCVGHVDGKPHPYDSRYVLGQQVQRLAEKGWTL
NTGLEPEFNLMRRDESGKLQLVDPSDNLDKPCYDYKGLSRSRVFLERLTEALQAVDFEVY
QIDHEDANGQFEINYTYSDAMTSADRFTFFRMAAGEIANDLGMICSFMPKPDPKRAGNGM
HFHLSISSADNKNLFHDASDPSGMGLSKLAYHFAAGLLAHGPALCAFAAPTVNSYKRLVV
GNSLSGATWAPAFIAFGANNRSAMVRVPYGRLEFRLPDAGCNPYLVSAAIIAAGLDGIDR
QLEIDHVCNENLYSLSLEQIAARGIKTLPQSLKEACDALEADPLFAEMLGPQIVDEFIKL
KRMEWVEYSRHVSDWEIQRYTEFF
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