SitesBLAST
Comparing BWI76_RS10710 FitnessBrowser__Koxy:BWI76_RS10710 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)
94% identity, 100% coverage: 1:472/472 of query aligns to 1:472/472 of P78061
- H282 (= H282) mutation to N: Activity is impaired to 9% of wild-type.
- R357 (= R357) mutation to Q: Activity is impaired to 3% of wild-type.
4s0rD Structure of gs-tnra complex (see paper)
30% identity, 95% coverage: 20:467/472 of query aligns to 4:428/447 of 4s0rD
- active site: D56 (≠ P71), E135 (= E159), E137 (= E161), E192 (= E225), E199 (= E232), H248 (= H282), R319 (= R352), E336 (= E369), R338 (= R371)
- binding glutamine: E137 (= E161), E192 (= E225), R301 (= R334), E307 (≠ Y340)
- binding magnesium ion: I66 (≠ M93), E135 (= E159), E135 (= E159), E199 (= E232), H248 (= H282), H248 (= H282), E336 (= E369), H419 (≠ R458)
- binding : F63 (≠ N82), V64 (= V83), R65 (≠ E92), I66 (≠ M93), D161 (≠ Q191), G241 (≠ E275), V242 (≠ H276), N243 (≠ A277), G305 (= G338), Y306 (≠ M339), Y376 (vs. gap), I426 (= I465)
Sites not aligning to the query:
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)
30% identity, 95% coverage: 20:467/472 of query aligns to 1:425/444 of P12425
- M1 (≠ V20) modified: Initiator methionine, Removed
- G59 (= G81) 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 (≠ E92) 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 (= E159) binding
- E134 (= E161) binding
- E189 (= E225) binding
- V190 (≠ A226) 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 (= E232) binding
- G241 (= G278) binding
- H245 (= H282) binding
- G302 (= G338) 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 (≠ Y340) 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 (= P342) 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 (= E369) binding
- E424 (= E466) 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.
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)
30% identity, 95% coverage: 21:467/472 of query aligns to 1:424/443 of 4lnkA
- active site: D52 (≠ P71), E131 (= E159), E133 (= E161), E188 (= E225), E195 (= E232), H244 (= H282), R315 (= R352), E332 (= E369), R334 (= R371)
- binding adenosine-5'-diphosphate: K43 (= K63), M50 (≠ Y69), F198 (≠ L235), Y200 (≠ H237), N246 (≠ H284), S248 (= S286), S324 (≠ G361), S328 (≠ N365), R330 (= R367)
- binding glutamic acid: E133 (= E161), E188 (= E225), V189 (≠ A226), N239 (≠ A277), G240 (= G278), G242 (= G280), E303 (≠ Y340)
- binding magnesium ion: E131 (= E159), E188 (= E225), E195 (= E232), H244 (= H282), E332 (= E369)
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)
30% identity, 95% coverage: 21:467/472 of query aligns to 1:424/443 of 4lniA
- active site: D52 (≠ P71), E131 (= E159), E133 (= E161), E188 (= E225), E195 (= E232), H244 (= H282), R315 (= R352), E332 (= E369), R334 (= R371)
- binding adenosine-5'-diphosphate: E131 (= E159), E183 (≠ D220), D197 (≠ N234), Y200 (≠ H237), N246 (≠ H284), S248 (= S286), R320 (= R357), R330 (= R367)
- binding magnesium ion: E131 (= E159), E131 (= E159), E133 (= E161), E188 (= E225), E195 (= E232), E195 (= E232), H244 (= H282), E332 (= E369)
- binding l-methionine-s-sulfoximine phosphate: E133 (= E161), E188 (= E225), H244 (= H282), R297 (= R334), E303 (≠ Y340), R315 (= R352), R334 (= R371)
7tf9S L. Monocytogenes gs(14)-q-glnr peptide (see paper)
29% identity, 92% coverage: 36:470/472 of query aligns to 16:441/443 of 7tf9S
- binding glutamine: E133 (= E161), Y155 (= Y174), E188 (= E225), G240 (= G278), G242 (= G280), R297 (= R334), E303 (≠ Y340)
- binding magnesium ion: E131 (= E159), E133 (= E161), E188 (= E225), E195 (= E232), H244 (= H282), E332 (= E369)
- binding : F59 (≠ N82), V60 (= V83), E418 (≠ A447), I422 (≠ D451), M426 (≠ Q455)
7tenA Glutamine synthetase (see paper)
29% identity, 92% coverage: 36:470/472 of query aligns to 15:440/442 of 7tenA
- binding adenosine-5'-diphosphate: G128 (≠ A157), E130 (= E159), E182 (≠ D220), D196 (≠ N234), F197 (≠ L235), K198 (≠ H236), Y199 (≠ H237), N245 (≠ H284), S247 (= S286), R319 (= R357), S327 (≠ N365), R329 (= R367)
- binding l-methionine-s-sulfoximine phosphate: E130 (= E159), E132 (= E161), E187 (= E225), E194 (= E232), N238 (≠ A277), G239 (= G278), H243 (= H282), R296 (= R334), E302 (≠ Y340), R314 (= R352), R333 (= R371)
8ooqB Glutamine synthetase from Methanothermococcus thermolithotrophicus (see paper)
27% identity, 92% coverage: 36:470/472 of query aligns to 13:445/446 of 8ooqB
- binding 2-oxoglutaric acid: F16 (≠ Y39), R18 (≠ D41), A32 (≠ R55), R86 (≠ A111), V92 (≠ I117), P169 (≠ A202), R172 (≠ L205), R173 (≠ N206), S189 (≠ A222)
- binding magnesium ion: E137 (= E161), E192 (= E225), E199 (= E232)
8oooA Glutamine synthetase from methanothermococcus thermolithotrophicus in complex with 2-oxoglutarate and mgatp at 2.15 a resolution (see paper)
27% identity, 92% coverage: 36:470/472 of query aligns to 14:446/447 of 8oooA
- binding 2-oxoglutaric acid: F17 (≠ Y39), R19 (≠ D41), A33 (≠ R55), R87 (≠ A111), V93 (≠ I117), P170 (≠ A202), R173 (≠ L205), R174 (≠ N206), S190 (≠ A222)
- binding adenosine-5'-triphosphate: E136 (= E159), E188 (≠ D220), F203 (≠ L235), K204 (≠ H236), F205 (≠ H237), H251 (= H284), S253 (= S286), R325 (= R357), R335 (= R367)
7tdvC Glutamine synthetase (see paper)
29% identity, 94% coverage: 22:467/472 of query aligns to 2:434/443 of 7tdvC
- binding adenosine-5'-diphosphate: G129 (≠ A157), E131 (= E159), E183 (≠ D220), D197 (≠ N234), F198 (≠ L235), K199 (≠ H236), Y200 (≠ H237), N246 (≠ H284), V247 (≠ I285), S248 (= S286), R320 (= R357), S328 (≠ N365), R330 (= R367)
- binding magnesium ion: E131 (= E159), E131 (= E159), E133 (= E161), E188 (= E225), E195 (= E232), E195 (= E232), H244 (= H282), E332 (= E369)
- binding l-methionine-s-sulfoximine phosphate: E131 (= E159), E133 (= E161), E188 (= E225), E195 (= E232), G240 (= G278), H244 (= H282), R297 (= R334), E303 (≠ Y340), R315 (= R352)
7tf6A Glutamine synthetase (see paper)
28% identity, 94% coverage: 22:467/472 of query aligns to 1:429/438 of 7tf6A
- binding glutamine: E128 (= E161), E183 (= E225), G235 (= G278), H239 (= H282), R292 (= R334), E298 (≠ Y340)
- binding magnesium ion: E126 (= E159), E128 (= E161), E183 (= E225), E190 (= E232), H239 (= H282), E327 (= E369)
- binding : F58 (≠ N82), R60 (≠ E92), G232 (≠ E275), N234 (≠ A277), G296 (= G338), Y297 (≠ M339), R310 (= R352), Y367 (vs. gap), Y421 (≠ R458)
Sites not aligning to the query:
7tfaB Glutamine synthetase (see paper)
28% identity, 88% coverage: 36:452/472 of query aligns to 15:421/441 of 7tfaB
- binding glutamine: E131 (= E161), Y153 (≠ V192), E186 (= E225), G238 (= G278), H242 (= H282), R295 (= R334), E301 (≠ Y340)
- binding magnesium ion: E129 (= E159), E131 (= E161), E186 (= E225), E193 (= E232), H242 (= H282), E330 (= E369)
- binding : Y58 (≠ N82), R60 (≠ E92), V187 (≠ A226), N237 (≠ A277), G299 (= G338), Y300 (≠ M339), R313 (= R352)
Sites not aligning to the query:
7tdpA Structure of paenibacillus polymyxa gs bound to met-sox-p-adp (transition state complex) to 1.98 angstom (see paper)
28% identity, 88% coverage: 36:452/472 of query aligns to 15:419/439 of 7tdpA
- binding adenosine-5'-diphosphate: N123 (vs. gap), G125 (≠ A157), E127 (= E159), E179 (≠ D220), D193 (≠ N234), Y196 (≠ H237), N242 (≠ H284), S244 (= S286), R316 (= R357), R326 (= R367)
- binding magnesium ion: E127 (= E159), E127 (= E159), E129 (= E161), E184 (= E225), E191 (= E232), E191 (= E232), H240 (= H282), E328 (= E369)
- binding l-methionine-s-sulfoximine phosphate: E127 (= E159), E129 (= E161), E184 (= E225), E191 (= E232), G236 (= G278), H240 (= H282), R293 (= R334), E299 (≠ Y340), R311 (= R352), R330 (= R371)
8ooxB Glutamine synthetase (see paper)
29% identity, 94% coverage: 26:469/472 of query aligns to 5:431/438 of 8ooxB
8oozA Glutamine synthetase (see paper)
29% identity, 94% coverage: 26:469/472 of query aligns to 5:423/430 of 8oozA
- binding adenosine-5'-triphosphate: G117 (≠ A157), E170 (≠ D220), F185 (≠ L235), K186 (≠ H236), Y187 (≠ H237), N233 (≠ H284), S235 (= S286), S315 (≠ N365), R317 (= R367)
- binding magnesium ion: E119 (= E159), H231 (= H282), E319 (= E369)
5dm3C Crystal structure of glutamine synthetase from chromohalobacter salexigens dsm 3043(csal_0679, target efi-550015) with bound adp
29% identity, 70% coverage: 136:465/472 of query aligns to 92:391/396 of 5dm3C
- active site: E115 (= E159), E117 (= E161), E162 (= E225), E169 (= E232), H218 (= H282), R286 (= R352), E303 (= E369), R305 (= R371)
- binding adenosine-5'-diphosphate: R173 (≠ H236), C174 (≠ T238), H220 (= H284), S222 (= S286), R301 (= R367)
8tfkA Glutamine synthetase (see paper)
27% identity, 92% coverage: 36:469/472 of query aligns to 14:437/440 of 8tfkA
- binding adenosine-5'-diphosphate: E128 (= E159), D194 (≠ N234), F195 (≠ L235), F197 (≠ H237), N243 (≠ H284), R312 (= R352), R317 (= R357), G325 (≠ N365), R327 (= R367)
- binding magnesium ion: E128 (= E159), E128 (= E159), E130 (= E161), E185 (= E225), E192 (= E232), E192 (= E232), H241 (= H282), E329 (= E369)
- binding l-methionine-s-sulfoximine phosphate: E128 (= E159), E130 (= E161), E185 (= E225), E192 (= E232), G237 (= G278), H241 (= H282), R294 (= R334), E300 (≠ Y340), R312 (= R352), R331 (= R371)
8ufjB Glutamine synthetase (see paper)
27% identity, 92% coverage: 36:469/472 of query aligns to 18:441/444 of 8ufjB
8wwuB Glutamine synthetase
28% identity, 87% coverage: 46:456/472 of query aligns to 40:465/492 of 8wwuB
- binding phosphoaminophosphonic acid-adenylate ester: G157 (≠ A157), E159 (= E159), R226 (≠ D220), F241 (≠ L235), V243 (≠ H237), H290 (= H284), S292 (= S286), K360 (≠ R352), R365 (= R357), R376 (= R367)
- binding magnesium ion: E159 (= E159), E238 (= E232)
- binding manganese (ii) ion: E159 (= E159), E161 (= E161), E231 (= E225), E238 (= E232), H288 (= H282), E378 (= E369)
8wwvA Glutamine synthetase
28% identity, 87% coverage: 46:456/472 of query aligns to 38:463/490 of 8wwvA
- binding adenosine-5'-diphosphate: G155 (≠ A157), E157 (= E159), R224 (≠ D220), F239 (≠ L235), D240 (≠ H236), V241 (≠ H237), H288 (= H284), S290 (= S286), R374 (= R367), E376 (= E369)
- binding magnesium ion: E157 (= E159), E236 (= E232)
- binding manganese (ii) ion: E157 (= E159), E159 (= E161), E229 (= E225), E236 (= E232), H286 (= H282), E376 (= E369)
- binding l-methionine-s-sulfoximine phosphate: E157 (= E159), E159 (= E161), E229 (= E225), E236 (= E232), A282 (≠ G278), H286 (= H282), R340 (= R334), K358 (≠ R352)
Query Sequence
>BWI76_RS10710 FitnessBrowser__Koxy:BWI76_RS10710
METNIVEVENFVQQSEERRVSAFTWEVKRYLERYPNTQYVDVLLTDLNGCFRGKRIPVSG
LSKLEKGCYFPASVFAMDILGNVVEEAGLGQEMGEPDRTCVPVLGTLTPSAADPEYIGQV
LLTMVDEDGAPFDVEPRNVLNRLWQQLRQRGLFPVVAVELEFYLLDRKRDAEGYLQPPCA
PGTGDRNTQSQVYSVDNLNHFADVLNEIDEIAQLQLIPADGAVAEASPGQFEINLHHTDN
VLDACDDALALKRLVRLMAEKHKMHATFMAKPYEEHAGSGMHIHISMQNNKGENVLADAD
GEDSAMLKRALAGMIDLMPASMALLAPNVNSYRRFQPGMYVPTQASWGHNNRTVALRIPC
GDRHNHRVEYRVAGADANPYLVMAAIFAGILHGLDNPLPLQEEVEGNGLEQEGLPFPIRQ
SDALWEFMQNDHLRERLGERFCHVYHACKNDELLQFERLITETEIEWMLKNA
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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