SitesBLAST
Comparing GFF543 FitnessBrowser__Phaeo:GFF543 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)
8wwuB Glutamine synthetase
36% identity, 98% coverage: 10:482/483 of query aligns to 5:491/492 of 8wwuB
- binding phosphoaminophosphonic acid-adenylate ester: G157 (= G163), E159 (= E165), R226 (= R229), F241 (= F244), V243 (≠ P246), H290 (= H293), S292 (= S295), K360 (≠ R363), R365 (= R368), R376 (= R379)
- binding magnesium ion: E159 (= E165), E238 (= E241)
- binding manganese (ii) ion: E159 (= E165), E161 (= E167), E231 (= E234), E238 (= E241), H288 (= H291), E378 (= E381)
8wwvA Glutamine synthetase
36% identity, 98% coverage: 10:482/483 of query aligns to 3:489/490 of 8wwvA
- binding adenosine-5'-diphosphate: G155 (= G163), E157 (= E165), R224 (= R229), F239 (= F244), D240 (= D245), V241 (≠ P246), H288 (= H293), S290 (= S295), R374 (= R379), E376 (= E381)
- binding magnesium ion: E157 (= E165), E236 (= E241)
- binding manganese (ii) ion: E157 (= E165), E159 (= E167), E229 (= E234), E236 (= E241), H286 (= H291), E376 (= E381)
- binding l-methionine-s-sulfoximine phosphate: E157 (= E165), E159 (= E167), E229 (= E234), E236 (= E241), A282 (= A287), H286 (= H291), R340 (= R345), K358 (≠ R363)
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, 95% coverage: 25:482/483 of query aligns to 6:446/446 of A0R083
- K363 (≠ A408) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
8ufjB Glutamine synthetase (see paper)
29% identity, 96% coverage: 19:482/483 of query aligns to 2:443/444 of 8ufjB
7tdpA Structure of paenibacillus polymyxa gs bound to met-sox-p-adp (transition state complex) to 1.98 angstom (see paper)
33% identity, 79% coverage: 103:483/483 of query aligns to 64:439/439 of 7tdpA
- binding adenosine-5'-diphosphate: N123 (vs. gap), G125 (= G163), E127 (= E165), E179 (≠ R229), D193 (≠ T243), Y196 (≠ P246), N242 (≠ H293), S244 (= S295), R316 (= R368), R326 (= R379)
- binding magnesium ion: E127 (= E165), E127 (= E165), E129 (= E167), E184 (= E234), E191 (= E241), E191 (= E241), H240 (= H291), E328 (= E381)
- binding l-methionine-s-sulfoximine phosphate: E127 (= E165), E129 (= E167), E184 (= E234), E191 (= E241), G236 (≠ A287), H240 (= H291), R293 (= R345), E299 (≠ L351), R311 (= R363), R330 (= R383)
8tfkA Glutamine synthetase (see paper)
30% identity, 95% coverage: 25:482/483 of query aligns to 4:439/440 of 8tfkA
- binding adenosine-5'-diphosphate: E128 (= E165), D194 (≠ T243), F195 (= F244), F197 (≠ P246), N243 (≠ H293), R312 (= R363), R317 (= R368), G325 (≠ P376), R327 (= R379)
- binding magnesium ion: E128 (= E165), E128 (= E165), E130 (= E167), E185 (= E234), E192 (= E241), E192 (= E241), H241 (= H291), E329 (= E381)
- binding l-methionine-s-sulfoximine phosphate: E128 (= E165), E130 (= E167), E185 (= E234), E192 (= E241), G237 (≠ A287), H241 (= H291), R294 (= R345), E300 (≠ L351), R312 (= R363), R331 (= R383)
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)
31% identity, 95% coverage: 25:482/483 of query aligns to 6:446/446 of P9WN37
- K363 (≠ A408) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
8oozA Glutamine synthetase (see paper)
31% identity, 79% coverage: 102:483/483 of query aligns to 56:430/430 of 8oozA
- binding adenosine-5'-triphosphate: G117 (= G163), E170 (≠ R229), F185 (= F244), K186 (≠ D245), Y187 (≠ P246), N233 (≠ H293), S235 (= S295), S315 (≠ T377), R317 (= R379)
- binding magnesium ion: E119 (= E165), H231 (= H291), E319 (= E381)
7tfaB Glutamine synthetase (see paper)
32% identity, 79% coverage: 103:483/483 of query aligns to 64:441/441 of 7tfaB
- binding glutamine: E131 (= E167), Y153 (= Y199), E186 (= E234), G238 (≠ A287), H242 (= H291), R295 (= R345), E301 (≠ L351)
- binding magnesium ion: E129 (= E165), E131 (= E167), E186 (= E234), E193 (= E241), H242 (= H291), E330 (= E381)
- binding : V187 (≠ M235), N237 (≠ M286), G299 (≠ Y349), Y300 (≠ Q350), R313 (= R363), M424 (≠ R466)
Sites not aligning to the query:
8ooxB Glutamine synthetase (see paper)
31% identity, 79% coverage: 103:483/483 of query aligns to 63:438/438 of 8ooxB
5dm3C Crystal structure of glutamine synthetase from chromohalobacter salexigens dsm 3043(csal_0679, target efi-550015) with bound adp
30% identity, 93% coverage: 32:481/483 of query aligns to 10:396/396 of 5dm3C
- active site: E115 (= E165), E117 (= E167), E162 (= E234), E169 (= E241), H218 (= H291), R286 (= R363), E303 (= E381), R305 (= R383)
- binding adenosine-5'-diphosphate: R173 (≠ D245), C174 (≠ P246), H220 (= H293), S222 (= S295), R301 (= R379)
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)
31% identity, 79% coverage: 103:483/483 of query aligns to 66:444/444 of P12425
- E132 (= E165) binding
- E134 (= E167) binding
- E189 (= E234) binding
- V190 (≠ M235) 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 (= E241) binding
- G241 (= G289) binding
- H245 (= H293) binding
- G302 (≠ Y349) 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 (≠ L351) 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 (= P353) 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 (= E381) binding
- E424 (= E463) 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
- 59 G→R: Unable to form stable complex with TnrA. In the presence of glutamine, this mutant derepresses amtB-lacZ fusion and glnRA-lacZ fusion.
- 62 Important for inhibition by glutamine; R→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.
4s0rD Structure of gs-tnra complex (see paper)
31% identity, 79% coverage: 103:483/483 of query aligns to 69:447/447 of 4s0rD
- active site: E135 (= E165), E137 (= E167), E192 (= E234), E199 (= E241), H248 (= H293), R319 (= R363), E336 (= E381), R338 (= R383)
- binding glutamine: E137 (= E167), E192 (= E234), R301 (= R345), E307 (≠ L351)
- binding magnesium ion: E135 (= E165), E135 (= E165), E199 (= E241), H248 (= H293), H248 (= H293), E336 (= E381), H419 (≠ Y455)
- binding : D161 (≠ Y201), G241 (≠ M286), V242 (≠ A287), N243 (= N288), G305 (≠ Y349), Y306 (≠ Q350), Y376 (= Y420), I426 (≠ V462), M430 (≠ R466)
Sites not aligning to the query:
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)
31% identity, 79% coverage: 103:483/483 of query aligns to 65:443/443 of 4lnkA
- active site: E131 (= E165), E133 (= E167), E188 (= E234), E195 (= E241), H244 (= H293), R315 (= R363), E332 (= E381), R334 (= R383)
- binding adenosine-5'-diphosphate: F198 (= F244), Y200 (≠ P246), N246 (≠ S295), S248 (≠ I297), S324 (≠ R372), S328 (≠ P376), R330 (= R379)
- binding glutamic acid: E133 (= E167), E188 (= E234), V189 (≠ M235), N239 (= N288), G240 (= G289), G242 (≠ H291), E303 (≠ L351)
- binding magnesium ion: E131 (= E165), E188 (= E234), E195 (= E241), H244 (= H293), E332 (= E381)
Sites not aligning to the query:
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)
31% identity, 79% coverage: 103:483/483 of query aligns to 65:443/443 of 4lniA
- active site: E131 (= E165), E133 (= E167), E188 (= E234), E195 (= E241), H244 (= H293), R315 (= R363), E332 (= E381), R334 (= R383)
- binding adenosine-5'-diphosphate: E131 (= E165), E183 (≠ R229), D197 (≠ T243), Y200 (≠ P246), N246 (≠ S295), S248 (≠ I297), R320 (= R368), R330 (= R379)
- binding magnesium ion: E131 (= E165), E131 (= E165), E133 (= E167), E188 (= E234), E195 (= E241), E195 (= E241), H244 (= H293), E332 (= E381)
- binding l-methionine-s-sulfoximine phosphate: E133 (= E167), E188 (= E234), H244 (= H293), R297 (= R345), E303 (≠ L351), R315 (= R363), R334 (= R383)
Sites not aligning to the query:
8ooqB Glutamine synthetase from Methanothermococcus thermolithotrophicus (see paper)
30% identity, 79% coverage: 103:482/483 of query aligns to 69:446/446 of 8ooqB
Sites not aligning to the query:
8oooA Glutamine synthetase from methanothermococcus thermolithotrophicus in complex with 2-oxoglutarate and mgatp at 2.15 a resolution (see paper)
30% identity, 79% coverage: 103:482/483 of query aligns to 70:447/447 of 8oooA
- binding 2-oxoglutaric acid: R87 (≠ S120), V93 (vs. gap), P170 (≠ E211), R173 (≠ L214), R174 (≠ D215), S190 (≠ V231)
- binding adenosine-5'-triphosphate: E136 (= E165), E188 (≠ R229), F203 (= F244), K204 (≠ D245), F205 (≠ P246), H251 (= H293), S253 (= S295), R325 (= R368), R335 (= R379)
Sites not aligning to the query:
7tf6A Glutamine synthetase (see paper)
30% identity, 79% coverage: 103:483/483 of query aligns to 64:438/438 of 7tf6A
- binding glutamine: E128 (= E167), E183 (= E234), G235 (≠ A287), H239 (= H291), R292 (= R345), E298 (≠ L351)
- binding magnesium ion: E126 (= E165), E128 (= E167), E183 (= E234), E190 (= E241), H239 (= H291), E327 (= E381)
- binding : G232 (≠ D283), N234 (≠ M286), G296 (≠ Y349), Y297 (≠ Q350), R310 (= R363), Y367 (= Y420), Y421 (≠ R466), Q433 (≠ E478), Q437 (≠ L482)
Sites not aligning to the query:
7tdvC Glutamine synthetase (see paper)
29% identity, 79% coverage: 103:483/483 of query aligns to 65:443/443 of 7tdvC
- binding adenosine-5'-diphosphate: G129 (= G163), E131 (= E165), E183 (≠ R229), D197 (≠ T243), F198 (= F244), K199 (≠ D245), Y200 (≠ P246), N246 (≠ H293), V247 (≠ Q294), S248 (= S295), R320 (= R368), S328 (≠ T377), R330 (= R379)
- binding magnesium ion: E131 (= E165), E131 (= E165), E133 (= E167), E188 (= E234), E195 (= E241), E195 (= E241), H244 (= H291), E332 (= E381)
- binding l-methionine-s-sulfoximine phosphate: E131 (= E165), E133 (= E167), E188 (= E234), E195 (= E241), G240 (≠ A287), H244 (= H291), R297 (= R345), E303 (≠ L351), R315 (= R363)
5dm3A Crystal structure of glutamine synthetase from chromohalobacter salexigens dsm 3043(csal_0679, target efi-550015) with bound adp
28% identity, 94% coverage: 30:481/483 of query aligns to 10:374/374 of 5dm3A
- active site: E107 (= E165), E109 (= E167), E146 (≠ P237), E150 (= E241), H199 (= H291), R265 (= R363), E282 (= E381), R284 (= R383)
- binding adenosine-5'-diphosphate: I103 (≠ V161), E141 (≠ R229), R154 (≠ D245), C155 (≠ P246), H201 (= H293), S203 (= S295), R280 (= R379)
Query Sequence
>GFF543 FitnessBrowser__Phaeo:GFF543
MTTSLNRGALARNGLLSDQACHDAEVVLAQCEAARVETVRVLFADQHGILRGKTLVAAGL
RSLFEQGIAVPSTLLLKDTAHRTVFPVWSENPEEVVTPMQGASDVLLVPRPETFRVLPWS
PHSAWIFCHVAFHDGATVPFGSAHVLERAVATLAEQGLQTVVGLEVEFQIFERVDPALGH
AQQGMPGAPIETRNLIQGYQYLTETRYAEAEGILDALRRHAQALGLPVRTVEIEMGPSQF
EFTFDPADPMTQADAMVMFRTMAKEVCAANGLHASFMAKPRQDHAMANGWHIHQSLIDTV
SGRNLFMPEVAGELTAEASGWIAGLLAHAEAASILVAPTVNSYKRYLPYQLAPNRVQWGE
DNRGAMLRGLMRPGDPTSRVENRAPDSTANPYFALAAQIIAGSEGMMAGRRAPAPTASPY
SDDAEKLPRSLGQALQAFSSSELFRSALGEDVVDYLTHLKEVEWARYLDTVSEWEQAEYF
NLY
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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