SitesBLAST
Comparing Pf6N2E2_2730 FitnessBrowser__pseudo6_N2E2:Pf6N2E2_2730 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)
37% identity, 98% coverage: 9:460/460 of query aligns to 22:472/472 of P78061
- H282 (= H270) mutation to N: Activity is impaired to 9% of wild-type.
- R357 (= R345) mutation to Q: Activity is impaired to 3% of wild-type.
8wwvA Glutamine synthetase
30% identity, 93% coverage: 24:451/460 of query aligns to 29:470/490 of 8wwvA
- binding adenosine-5'-diphosphate: G155 (≠ A146), E157 (= E148), R224 (= R208), F239 (≠ L223), D240 (≠ E224), V241 (≠ H225), H288 (= H272), S290 (= S274), R374 (≠ H355), E376 (= E357)
- binding magnesium ion: E157 (= E148), E236 (= E220)
- binding manganese (ii) ion: E157 (= E148), E159 (= E150), E229 (= E213), E236 (= E220), H286 (= H270), E376 (= E357)
- binding l-methionine-s-sulfoximine phosphate: E157 (= E148), E159 (= E150), E229 (= E213), E236 (= E220), A282 (≠ G266), H286 (= H270), R340 (= R322), K358 (≠ R340)
8wwuB Glutamine synthetase
30% identity, 93% coverage: 24:451/460 of query aligns to 31:472/492 of 8wwuB
- binding phosphoaminophosphonic acid-adenylate ester: G157 (≠ A146), E159 (= E148), R226 (= R208), F241 (≠ L223), V243 (≠ H225), H290 (= H272), S292 (= S274), K360 (≠ R340), R365 (= R345), R376 (≠ H355)
- binding magnesium ion: E159 (= E148), E238 (= E220)
- binding manganese (ii) ion: E159 (= E148), E161 (= E150), E231 (= E213), E238 (= E220), H288 (= H270), E378 (= E357)
8oooA Glutamine synthetase from methanothermococcus thermolithotrophicus in complex with 2-oxoglutarate and mgatp at 2.15 a resolution (see paper)
29% identity, 86% coverage: 64:457/460 of query aligns to 53:445/447 of 8oooA
- binding 2-oxoglutaric acid: R87 (= R101), V93 (≠ A107), P170 (≠ E190), R173 (≠ L193), R174 (≠ A194), S190 (≠ A210)
- binding adenosine-5'-triphosphate: E136 (= E148), E188 (≠ R208), F203 (≠ L223), K204 (≠ E224), F205 (≠ H225), H251 (= H272), S253 (= S274), R325 (= R345), R335 (≠ H355)
Sites not aligning to the query:
8ooqB Glutamine synthetase from Methanothermococcus thermolithotrophicus (see paper)
29% identity, 86% coverage: 64:457/460 of query aligns to 52:444/446 of 8ooqB
Sites not aligning to the query:
8tfkA Glutamine synthetase (see paper)
27% identity, 95% coverage: 23:458/460 of query aligns to 14:438/440 of 8tfkA
- binding adenosine-5'-diphosphate: E128 (= E148), D194 (≠ T222), F195 (≠ L223), F197 (≠ H225), N243 (≠ H272), R312 (= R340), R317 (= R345), G325 (≠ S353), R327 (≠ H355)
- binding magnesium ion: E128 (= E148), E128 (= E148), E130 (= E150), E185 (= E213), E192 (= E220), E192 (= E220), H241 (= H270), E329 (= E357)
- binding l-methionine-s-sulfoximine phosphate: E128 (= E148), E130 (= E150), E185 (= E213), E192 (= E220), G237 (= G266), H241 (= H270), R294 (= R322), E300 (≠ Y328), R312 (= R340), R331 (= R359)
8ufjB Glutamine synthetase (see paper)
27% identity, 95% coverage: 23:458/460 of query aligns to 18:442/444 of 8ufjB
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)
29% identity, 95% coverage: 23:458/460 of query aligns to 16:445/446 of P9WN37
- K363 (≠ E384) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
7tdpA Structure of paenibacillus polymyxa gs bound to met-sox-p-adp (transition state complex) to 1.98 angstom (see paper)
28% identity, 82% coverage: 81:458/460 of query aligns to 61:437/439 of 7tdpA
- binding adenosine-5'-diphosphate: N123 (vs. gap), G125 (≠ A146), E127 (= E148), E179 (≠ R208), D193 (≠ T222), Y196 (≠ H225), N242 (≠ H272), S244 (= S274), R316 (= R345), R326 (≠ H355)
- binding magnesium ion: E127 (= E148), E127 (= E148), E129 (= E150), E184 (= E213), E191 (= E220), E191 (= E220), H240 (= H270), E328 (= E357)
- binding l-methionine-s-sulfoximine phosphate: E127 (= E148), E129 (= E150), E184 (= E213), E191 (= E220), G236 (= G266), H240 (= H270), R293 (= R322), E299 (≠ Y328), R311 (= R340), R330 (= R359)
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)
28% identity, 95% coverage: 23:458/460 of query aligns to 16:445/446 of A0R083
- K363 (≠ E384) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
7tfaB Glutamine synthetase (see paper)
28% identity, 82% coverage: 81:458/460 of query aligns to 61:439/441 of 7tfaB
- binding glutamine: E131 (= E150), Y153 (≠ V180), E186 (= E213), G238 (= G266), H242 (= H270), R295 (= R322), E301 (≠ Y328)
- binding magnesium ion: E129 (= E148), E131 (= E150), E186 (= E213), E193 (= E220), H242 (= H270), E330 (= E357)
- binding : V187 (≠ Y214), N237 (≠ A265), G299 (≠ N326), Y300 (≠ S327), R313 (= R340), M424 (≠ Q443)
Sites not aligning to the query:
7tf6A Glutamine synthetase (see paper)
28% identity, 78% coverage: 100:459/460 of query aligns to 75:437/438 of 7tf6A
- binding glutamine: E128 (= E150), E183 (= E213), G235 (= G266), H239 (= H270), R292 (= R322), E298 (≠ Y328)
- binding magnesium ion: E126 (= E148), E128 (= E150), E183 (= E213), E190 (= E220), H239 (= H270), E327 (= E357)
- binding : G232 (≠ H263), N234 (≠ A265), G296 (≠ N326), Y297 (≠ S327), R310 (= R340), Y367 (= Y397), Y421 (≠ Q443), Q433 (≠ W455), Q437 (= Q459)
Sites not aligning to the query:
7cqwA Gmas/adp complex-conformation 1 (see paper)
30% identity, 87% coverage: 16:417/460 of query aligns to 5:389/430 of 7cqwA
7cquA Gmas/adp/metsox-p complex (see paper)
30% identity, 87% coverage: 16:417/460 of query aligns to 4:388/429 of 7cquA
- binding adenosine-5'-diphosphate: E121 (= E148), Y173 (≠ R208), N187 (≠ T222), W188 (≠ L223), D189 (≠ E224), Y190 (≠ H225), H236 (= H272), L237 (≠ V273), S238 (= S274), R316 (= R345), R322 (≠ H355)
- binding magnesium ion: E121 (= E148), E121 (= E148), E123 (= E150), E178 (= E213), E185 (= E220), E185 (= E220), H234 (= H270), E324 (= E357)
- binding l-methionine-s-sulfoximine phosphate: E121 (= E148), E123 (= E150), E178 (= E213), E185 (= E220), T229 (≠ A265), G230 (= G266), H234 (= H270), R287 (= R322), W299 (≠ Y328), R311 (= R340), R326 (= R359)
7cqqA Gmas in complex with amppnp and metsox (see paper)
30% identity, 87% coverage: 16:417/460 of query aligns to 4:388/429 of 7cqqA
- binding phosphoaminophosphonic acid-adenylate ester: E121 (= E148), Y173 (≠ R208), E185 (= E220), N187 (≠ T222), D189 (≠ E224), Y190 (≠ H225), H234 (= H270), H236 (= H272), S238 (= S274), R311 (= R340), R316 (= R345), R322 (≠ H355), E324 (= E357)
- binding magnesium ion: E121 (= E148), E121 (= E148), E123 (= E150), E178 (= E213), E185 (= E220), E185 (= E220), H234 (= H270), E324 (= E357)
- binding (2s)-2-amino-4-(methylsulfonimidoyl)butanoic acid: E123 (= E150), E178 (= E213), T229 (≠ A265), H234 (= H270), R287 (= R322), W299 (≠ Y328), R311 (= R340), R326 (= R359)
7cqnA Gmas in complex with amppcp (see paper)
30% identity, 87% coverage: 16:417/460 of query aligns to 4:388/429 of 7cqnA
- binding phosphomethylphosphonic acid adenylate ester: G45 (≠ D71), D61 (= D85), E121 (= E148), Y173 (≠ R208), Q174 (≠ T209), W188 (≠ L223), D189 (≠ E224), Y190 (≠ H225), H236 (= H272), S238 (= S274), R311 (= R340), R316 (= R345), R322 (≠ H355)
7tdvC Glutamine synthetase (see paper)
28% identity, 78% coverage: 100:459/460 of query aligns to 76:442/443 of 7tdvC
- binding adenosine-5'-diphosphate: G129 (≠ A146), E131 (= E148), E183 (≠ R208), D197 (≠ T222), F198 (≠ L223), K199 (≠ E224), Y200 (≠ H225), N246 (≠ H272), V247 (= V273), S248 (= S274), R320 (= R345), S328 (= S353), R330 (≠ H355)
- binding magnesium ion: E131 (= E148), E131 (= E148), E133 (= E150), E188 (= E213), E195 (= E220), E195 (= E220), H244 (= H270), E332 (= E357)
- binding l-methionine-s-sulfoximine phosphate: E131 (= E148), E133 (= E150), E188 (= E213), E195 (= E220), G240 (= G266), H244 (= H270), R297 (= R322), E303 (≠ Y328), R315 (= R340)
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)
26% identity, 89% coverage: 49:459/460 of query aligns to 36:442/443 of 4lnkA
- active site: D52 (≠ N68), E131 (= E148), E133 (= E150), E188 (= E213), E195 (= E220), H244 (= H270), R315 (= R340), E332 (= E357), R334 (= R359)
- binding adenosine-5'-diphosphate: K43 (≠ R56), M50 (≠ L63), F198 (≠ L223), Y200 (≠ H225), N246 (≠ H272), S248 (= S274), S324 (≠ G349), S328 (= S353), R330 (≠ H355)
- binding glutamic acid: E133 (= E150), E188 (= E213), V189 (≠ Y214), N239 (≠ A265), G240 (= G266), G242 (= G268), E303 (≠ Y328)
- binding magnesium ion: E131 (= E148), E188 (= E213), E195 (= E220), H244 (= H270), E332 (= E357)
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)
26% identity, 89% coverage: 49:459/460 of query aligns to 36:442/443 of 4lniA
- active site: D52 (≠ N68), E131 (= E148), E133 (= E150), E188 (= E213), E195 (= E220), H244 (= H270), R315 (= R340), E332 (= E357), R334 (= R359)
- binding adenosine-5'-diphosphate: E131 (= E148), E183 (≠ R208), D197 (≠ T222), Y200 (≠ H225), N246 (≠ H272), S248 (= S274), R320 (= R345), R330 (≠ H355)
- binding magnesium ion: E131 (= E148), E131 (= E148), E133 (= E150), E188 (= E213), E195 (= E220), E195 (= E220), H244 (= H270), E332 (= E357)
- binding l-methionine-s-sulfoximine phosphate: E133 (= E150), E188 (= E213), H244 (= H270), R297 (= R322), E303 (≠ Y328), R315 (= R340), R334 (= R359)
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)
26% identity, 89% coverage: 49:459/460 of query aligns to 37:443/444 of P12425
- G59 (= G76) 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 (≠ D80) 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 (= E148) binding
- E134 (= E150) binding
- E189 (= E213) binding
- V190 (≠ Y214) 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 (= E220) binding
- G241 (= G266) binding
- H245 (= H270) binding
- G302 (≠ N326) 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 (≠ Y328) 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 (= P330) 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 (= E357) binding
- E424 (= E440) 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
Query Sequence
>Pf6N2E2_2730 FitnessBrowser__pseudo6_N2E2:Pf6N2E2_2730
MSLAKISFAPVQHAEAFLAQNPDIELFELFILDNNGVPRGKLLHRDELLAVFESGRPLPS
TILGLTVNGDDVENSGLVWDIGDIDCRAYPLSGSLQRMPWRLIPTAAVQVSMHPQEGMPA
TIADPRYLLSQVIEALQADGYYPVMAAELEFYLLDAQRDSQGRPQPARDADGGRPRATQV
YGLRELEQIEPFLADLYAACKLQGIAARTAISEYAPGQVEITLEHRSDALQAMDEAVRYK
RLVKGVAHKHGMQACFMAKPFDHLAGSGMHMHVSLADRDGHNLFASEAADGTPLLRHAVG
GMLDTLLDSLLMFCPNANSYRRFQSNSYAPLAATWGVDNRTVSLRVPGGPALSRHIEHRI
CGADANPYLAAAAILAGIHRGLREQCDPGKPVEGNGYAQAAELLPTDWLTTLRALEASAW
AREAFGDEFLGVYLAVKRAEYRQFMAEVGEQDWRWYLNQA
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