SitesBLAST
Comparing WP_013257968.1 NCBI__GCF_000143965.1:WP_013257968.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.
Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures
Found 20 (the maximum) hits to proteins with known functional sites (download)
8tfkA Glutamine synthetase (see paper)
56% identity, 99% coverage: 5:443/443 of query aligns to 2:440/440 of 8tfkA
- binding adenosine-5'-diphosphate: E128 (= E132), D194 (= D194), F195 (≠ L195), F197 (≠ Y197), N243 (≠ H243), R312 (= R312), R317 (= R317), G325 (≠ A328), R327 (= R330)
- binding magnesium ion: E128 (= E132), E128 (= E132), E130 (= E134), E185 (= E185), E192 (= E192), E192 (= E192), H241 (= H241), E329 (= E332)
- binding l-methionine-s-sulfoximine phosphate: E128 (= E132), E130 (= E134), E185 (= E185), E192 (= E192), G237 (= G237), H241 (= H241), R294 (= R294), E300 (= E300), R312 (= R312), R331 (= R334)
8ufjB Glutamine synthetase (see paper)
56% identity, 99% coverage: 5:443/443 of query aligns to 6:444/444 of 8ufjB
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)
54% identity, 99% coverage: 3:442/443 of query aligns to 2:446/446 of A0R083
- K363 (≠ E359) 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)
53% identity, 99% coverage: 3:442/443 of query aligns to 2:446/446 of P9WN37
- K363 (≠ E359) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
7tfaB Glutamine synthetase (see paper)
49% identity, 99% coverage: 5:442/443 of query aligns to 3:440/441 of 7tfaB
- binding glutamine: E131 (= E134), Y153 (= Y152), E186 (= E185), G238 (= G237), H242 (= H241), R295 (= R294), E301 (= E300)
- binding magnesium ion: E129 (= E132), E131 (= E134), E186 (= E185), E193 (= E192), H242 (= H241), E330 (= E332)
- binding : Y58 (≠ F60), R60 (= R62), V187 (= V186), N237 (= N236), G299 (= G298), Y300 (= Y299), R313 (= R312), M424 (≠ A426)
7tdpA Structure of paenibacillus polymyxa gs bound to met-sox-p-adp (transition state complex) to 1.98 angstom (see paper)
49% identity, 99% coverage: 5:442/443 of query aligns to 3:438/439 of 7tdpA
- binding adenosine-5'-diphosphate: N123 (≠ Y128), G125 (= G130), E127 (= E132), E179 (= E180), D193 (= D194), Y196 (= Y197), N242 (≠ H243), S244 (= S245), R316 (= R317), R326 (= R330)
- binding magnesium ion: E127 (= E132), E127 (= E132), E129 (= E134), E184 (= E185), E191 (= E192), E191 (= E192), H240 (= H241), E328 (= E332)
- binding l-methionine-s-sulfoximine phosphate: E127 (= E132), E129 (= E134), E184 (= E185), E191 (= E192), G236 (= G237), H240 (= H241), R293 (= R294), E299 (= E300), R311 (= R312), R330 (= R334)
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)
50% identity, 99% coverage: 1:440/443 of query aligns to 1:441/444 of P12425
- M1 (= M1) modified: Initiator methionine, Removed
- G59 (= G59) 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 (= R62) 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 (= E132) binding Mg(2+)
- E134 (= E134) binding Mg(2+)
- E189 (= E185) binding Mg(2+)
- V190 (= V186) 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 Mg(2+)
- G241 (= G237) binding L-glutamate
- H245 (= H241) binding Mg(2+)
- G302 (= G298) 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 (= E300) 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 (= P302) 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 (= E332) binding Mg(2+)
- E424 (= E423) 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.
4s0rD Structure of gs-tnra complex (see paper)
50% identity, 99% coverage: 1:440/443 of query aligns to 4:444/447 of 4s0rD
- active site: D56 (= D53), E135 (= E132), E137 (= E134), E192 (= E185), E199 (= E192), H248 (= H241), R319 (= R312), E336 (= E332), R338 (= R334)
- binding glutamine: E137 (= E134), E192 (= E185), R301 (= R294), E307 (= E300)
- binding magnesium ion: I66 (= I63), E135 (= E132), E135 (= E132), E199 (= E192), H248 (= H241), H248 (= H241), E336 (= E332), H419 (≠ K415)
- binding : F63 (= F60), V64 (≠ A61), R65 (= R62), I66 (= I63), D161 (= D154), G241 (= G234), V242 (≠ E235), N243 (= N236), G305 (= G298), Y306 (= Y299), Y376 (≠ F372), I426 (≠ A422), M430 (≠ A426)
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)
51% identity, 98% coverage: 6:440/443 of query aligns to 5:440/443 of 4lnkA
- active site: D52 (= D53), E131 (= E132), E133 (= E134), E188 (= E185), E195 (= E192), H244 (= H241), R315 (= R312), E332 (= E332), R334 (= R334)
- binding adenosine-5'-diphosphate: K43 (≠ L44), M50 (≠ G51), F198 (≠ L195), Y200 (= Y197), N246 (≠ H243), S248 (= S245), S324 (≠ G324), S328 (≠ A328), R330 (= R330)
- binding glutamic acid: E133 (= E134), E188 (= E185), V189 (= V186), N239 (= N236), G240 (= G237), G242 (= G239), E303 (= E300)
- binding magnesium ion: E131 (= E132), E188 (= E185), E195 (= E192), H244 (= H241), E332 (= E332)
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)
51% identity, 98% coverage: 6:440/443 of query aligns to 5:440/443 of 4lniA
- active site: D52 (= D53), E131 (= E132), E133 (= E134), E188 (= E185), E195 (= E192), H244 (= H241), R315 (= R312), E332 (= E332), R334 (= R334)
- binding adenosine-5'-diphosphate: E131 (= E132), E183 (= E180), D197 (= D194), Y200 (= Y197), N246 (≠ H243), S248 (= S245), R320 (= R317), R330 (= R330)
- binding magnesium ion: E131 (= E132), E131 (= E132), E133 (= E134), E188 (= E185), E195 (= E192), E195 (= E192), H244 (= H241), E332 (= E332)
- binding l-methionine-s-sulfoximine phosphate: E133 (= E134), E188 (= E185), H244 (= H241), R297 (= R294), E303 (= E300), R315 (= R312), R334 (= R334)
8ooqB Glutamine synthetase from Methanothermococcus thermolithotrophicus (see paper)
51% identity, 98% coverage: 7:442/443 of query aligns to 3:446/446 of 8ooqB
- binding 2-oxoglutaric acid: F16 (= F20), R18 (= R22), A32 (= A36), R86 (= R83), V92 (= V90), P169 (≠ S162), R172 (= R165), R173 (= R166), S189 (= S182)
- binding magnesium ion: E137 (= E134), E192 (= E185), E199 (= E192)
8oooA Glutamine synthetase from methanothermococcus thermolithotrophicus in complex with 2-oxoglutarate and mgatp at 2.15 a resolution (see paper)
51% identity, 98% coverage: 7:442/443 of query aligns to 4:447/447 of 8oooA
- binding 2-oxoglutaric acid: F17 (= F20), R19 (= R22), A33 (= A36), R87 (= R83), V93 (= V90), P170 (≠ S162), R173 (= R165), R174 (= R166), S190 (= S182)
- binding adenosine-5'-triphosphate: E136 (= E132), E188 (= E180), F203 (≠ L195), K204 (≠ R196), F205 (≠ Y197), H251 (= H243), S253 (= S245), R325 (= R317), R335 (= R330)
7tenA Glutamine synthetase (see paper)
50% identity, 99% coverage: 5:442/443 of query aligns to 3:441/442 of 7tenA
- binding adenosine-5'-diphosphate: G128 (= G130), E130 (= E132), E182 (= E180), D196 (= D194), F197 (≠ L195), K198 (≠ R196), Y199 (= Y197), N245 (≠ H243), S247 (= S245), R319 (= R317), S327 (≠ A328), R329 (= R330)
- binding l-methionine-s-sulfoximine phosphate: E130 (= E132), E132 (= E134), E187 (= E185), E194 (= E192), N238 (= N236), G239 (= G237), H243 (= H241), R296 (= R294), E302 (= E300), R314 (= R312), R333 (= R334)
7tf9S L. Monocytogenes gs(14)-q-glnr peptide (see paper)
50% identity, 99% coverage: 5:442/443 of query aligns to 4:442/443 of 7tf9S
- binding glutamine: E133 (= E134), Y155 (= Y152), E188 (= E185), G240 (= G237), G242 (= G239), R297 (= R294), E303 (= E300)
- binding magnesium ion: E131 (= E132), E133 (= E134), E188 (= E185), E195 (= E192), H244 (= H241), E332 (= E332)
- binding : F59 (= F60), V60 (≠ A61), E418 (= E418), I422 (≠ A422), M426 (≠ A426)
8ooxB Glutamine synthetase (see paper)
47% identity, 98% coverage: 6:440/443 of query aligns to 3:435/438 of 8ooxB
7tdvC Glutamine synthetase (see paper)
47% identity, 98% coverage: 6:440/443 of query aligns to 5:440/443 of 7tdvC
- binding adenosine-5'-diphosphate: G129 (= G130), E131 (= E132), E183 (= E180), D197 (= D194), F198 (≠ L195), K199 (≠ R196), Y200 (= Y197), N246 (≠ H243), V247 (≠ Q244), S248 (= S245), R320 (= R317), S328 (≠ A328), R330 (= R330)
- binding magnesium ion: E131 (= E132), E131 (= E132), E133 (= E134), E188 (= E185), E195 (= E192), E195 (= E192), H244 (= H241), E332 (= E332)
- binding l-methionine-s-sulfoximine phosphate: E131 (= E132), E133 (= E134), E188 (= E185), E195 (= E192), G240 (= G237), H244 (= H241), R297 (= R294), E303 (= E300), R315 (= R312)
7tf6A Glutamine synthetase (see paper)
47% identity, 98% coverage: 6:440/443 of query aligns to 4:435/438 of 7tf6A
- binding glutamine: E128 (= E134), E183 (= E185), G235 (= G237), H239 (= H241), R292 (= R294), E298 (= E300)
- binding magnesium ion: E126 (= E132), E128 (= E134), E183 (= E185), E190 (= E192), H239 (= H241), E327 (= E332)
- binding : F58 (= F60), R60 (= R62), G232 (= G234), N234 (= N236), G296 (= G298), Y297 (= Y299), R310 (= R312), Y367 (≠ F372), Y421 (≠ A426), Q433 (≠ R438)
Sites not aligning to the query:
8oozA Glutamine synthetase (see paper)
46% identity, 98% coverage: 6:440/443 of query aligns to 3:427/430 of 8oozA
- binding adenosine-5'-triphosphate: G117 (= G130), E170 (= E180), F185 (≠ L195), K186 (≠ R196), Y187 (= Y197), N233 (≠ H243), S235 (= S245), S315 (≠ A328), R317 (= R330)
- binding magnesium ion: E119 (= E132), H231 (= H241), E319 (= E332)
A0R079 Glutamine synthetase; GS; Glutamate--ammonia ligase; Glutamine synthetase I beta; GSI beta; EC 6.3.1.2 from Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis) (see paper)
35% identity, 95% coverage: 1:421/443 of query aligns to 1:456/478 of A0R079
- K14 (≠ R14) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
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)
38% identity, 98% coverage: 7:439/443 of query aligns to 6:470/473 of P77961
- E134 (= E134) binding Mg(2+)
- E215 (= E185) binding Mg(2+)
- E223 (= E192) binding Mg(2+)
- E361 (= E332) binding Mn(2+)
Query Sequence
>WP_013257968.1 NCBI__GCF_000143965.1:WP_013257968.1
MSDMNKEQVLKAVRDNNVKFIRLWFTDILGMLKSFAISPAELELAMEEGMGFDGSSIQGF
ARIDESDMVAMPDPNTFAILPWRPADKGAVARMFTDVLNPDLTPYVGDPRYVLKRQLKKA
ADKGYTMYVGPELEFFYFKNSEGTEVLDRGGYFDLTPLDVASDLRRDTIFALESMGIKVE
YSHHEVAPSQHEIDLRYQESLKMADAAMTYRLTVKEIAMKHGYYASFMPKPIFGENGSGM
HTHQSLFKDGRNVFFDGSDKYNLSAAGKSYIAGLLKHAPEFCSIIAQWINSYKRLVPGYE
APVYVAWARRNRSALVRVPMYKPGKEMATRCELRCPDPACNPYLSFAVQLAAGLKGIEEN
YVLPEPVEEDIFEMSKKELAEHGITSLPSTLGEAIAITEKSAFVKEVLGDHVFEKFIENK
KAEWDAFRLHVTDFELERYLPIL
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