SitesBLAST
Comparing WP_218017304.1 NCBI__GCF_001592305.1:WP_218017304.1 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)
P78061 Gamma-glutamylputrescine synthetase PuuA; Gamma-Glu-Put synthetase; Glutamate--putrescine ligase; EC 6.3.1.11 from Escherichia coli (strain K12) (see paper)
35% identity, 93% coverage: 35:461/461 of query aligns to 40:472/472 of P78061
- H282 (= H272) mutation to N: Activity is impaired to 9% of wild-type.
- R357 (= R347) mutation to Q: Activity is impaired to 3% of wild-type.
8ooqB Glutamine synthetase from Methanothermococcus thermolithotrophicus (see paper)
29% identity, 94% coverage: 22:453/461 of query aligns to 4:439/446 of 8ooqB
- binding 2-oxoglutaric acid: F16 (≠ D34), R18 (≠ E36), A32 (≠ L50), R86 (≠ A105), V92 (≠ L111), P169 (≠ A193), R172 (≠ W196), R173 (≠ D197), S189 (≠ W213)
- binding magnesium ion: E137 (= E153), E192 (= E216), E199 (= E223)
8oooA Glutamine synthetase from methanothermococcus thermolithotrophicus in complex with 2-oxoglutarate and mgatp at 2.15 a resolution (see paper)
29% identity, 94% coverage: 22:453/461 of query aligns to 5:440/447 of 8oooA
- binding 2-oxoglutaric acid: F17 (≠ D34), R19 (≠ E36), A33 (≠ L50), R87 (≠ A105), V93 (≠ L111), P170 (≠ A193), R173 (≠ W196), R174 (≠ D197), S190 (≠ W213)
- binding adenosine-5'-triphosphate: E136 (= E151), E188 (≠ D211), F203 (≠ L226), K204 (≠ L227), F205 (≠ H228), H251 (= H274), S253 (= S276), R325 (= R347), R335 (= R357)
8tfbA Glutamine synthetase (see paper)
32% identity, 81% coverage: 86:457/461 of query aligns to 64:440/443 of 8tfbA
8s59O Glutamine synthetase
32% identity, 81% coverage: 86:457/461 of query aligns to 67:443/446 of 8s59O
Sites not aligning to the query:
8tfkA Glutamine synthetase (see paper)
32% identity, 81% coverage: 86:457/461 of query aligns to 61:437/440 of 8tfkA
- binding adenosine-5'-diphosphate: E128 (= E151), D194 (≠ N225), F195 (≠ L226), F197 (≠ H228), N243 (≠ H274), R312 (= R342), R317 (= R347), G325 (≠ A355), R327 (= R357)
- binding magnesium ion: E128 (= E151), E128 (= E151), E130 (= E153), E185 (= E216), E192 (= E223), E192 (= E223), H241 (= H272), E329 (= E359)
- binding l-methionine-s-sulfoximine phosphate: E128 (= E151), E130 (= E153), E185 (= E216), E192 (= E223), G237 (= G268), H241 (= H272), R294 (= R324), E300 (≠ Q330), R312 (= R342), R331 (= R361)
7tf6A Glutamine synthetase (see paper)
31% identity, 81% coverage: 86:460/461 of query aligns to 62:437/438 of 7tf6A
- binding glutamine: E128 (= E153), E183 (= E216), G235 (= G268), H239 (= H272), R292 (= R324), E298 (≠ Q330)
- binding magnesium ion: E126 (= E151), E128 (= E153), E183 (= E216), E190 (= E223), H239 (= H272), E327 (= E359)
- binding : G232 (= G265), N234 (≠ A267), G296 (= G328), Y297 (≠ S329), R310 (= R342), Y367 (= Y399), Y421 (≠ H444), Q433 (≠ Y456), Q437 (= Q460)
Sites not aligning to the query:
4s0rD Structure of gs-tnra complex (see paper)
28% identity, 96% coverage: 20:460/461 of query aligns to 9:446/447 of 4s0rD
- active site: D56 (≠ G75), E135 (= E151), E137 (= E153), E192 (= E216), E199 (= E223), H248 (= H272), R319 (= R342), E336 (= E359), R338 (= R361)
- binding glutamine: E137 (= E153), E192 (= E216), R301 (= R324), E307 (≠ Q330)
- binding magnesium ion: I66 (≠ D85), E135 (= E151), E135 (= E151), E199 (= E223), H248 (= H272), H248 (= H272), E336 (= E359), H419 (≠ G433)
- binding : F63 (≠ I82), V64 (≠ F83), R65 (≠ P84), I66 (≠ D85), D161 (≠ E178), G241 (= G265), V242 (≠ Q266), N243 (≠ A267), G305 (= G328), Y306 (≠ S329), Y376 (= Y399), I426 (≠ L440), M430 (≠ H444)
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)
28% identity, 96% coverage: 20:460/461 of query aligns to 5:442/443 of 4lnkA
- active site: D52 (≠ G75), E131 (= E151), E133 (= E153), E188 (= E216), E195 (= E223), H244 (= H272), R315 (= R342), E332 (= E359), R334 (= R361)
- binding adenosine-5'-diphosphate: K43 (≠ Q66), M50 (≠ V73), F198 (≠ L226), Y200 (≠ H228), N246 (≠ H274), S248 (= S276), S324 (= S351), S328 (≠ A355), R330 (= R357)
- binding glutamic acid: E133 (= E153), E188 (= E216), V189 (= V217), N239 (≠ A267), G240 (= G268), G242 (≠ S270), E303 (≠ Q330)
- binding magnesium ion: E131 (= E151), E188 (= E216), E195 (= E223), H244 (= H272), E332 (= E359)
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)
28% identity, 96% coverage: 20:460/461 of query aligns to 5:442/443 of 4lniA
- active site: D52 (≠ G75), E131 (= E151), E133 (= E153), E188 (= E216), E195 (= E223), H244 (= H272), R315 (= R342), E332 (= E359), R334 (= R361)
- binding adenosine-5'-diphosphate: E131 (= E151), E183 (≠ D211), D197 (≠ N225), Y200 (≠ H228), N246 (≠ H274), S248 (= S276), R320 (= R347), R330 (= R357)
- binding magnesium ion: E131 (= E151), E131 (= E151), E133 (= E153), E188 (= E216), E195 (= E223), E195 (= E223), H244 (= H272), E332 (= E359)
- binding l-methionine-s-sulfoximine phosphate: E133 (= E153), E188 (= E216), H244 (= H272), R297 (= R324), E303 (≠ Q330), R315 (= R342), R334 (= R361)
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)
28% identity, 96% coverage: 20:460/461 of query aligns to 6:443/444 of P12425
- G59 (≠ P81) 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 (≠ P84) 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 (= E151) binding Mg(2+)
- E134 (= E153) binding Mg(2+)
- E189 (= E216) binding Mg(2+)
- V190 (= V217) 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 (= E223) binding Mg(2+)
- G241 (= G268) binding L-glutamate
- H245 (= H272) binding Mg(2+)
- G302 (= G328) 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 (≠ Q330) 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 (= P332) 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 (= E359) binding Mg(2+)
- E424 (= E441) 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
7tfaB Glutamine synthetase (see paper)
30% identity, 92% coverage: 31:454/461 of query aligns to 15:434/441 of 7tfaB
- binding glutamine: E131 (= E153), Y153 (≠ R176), E186 (= E216), G238 (= G268), H242 (= H272), R295 (= R324), E301 (≠ Q330)
- binding magnesium ion: E129 (= E151), E131 (= E153), E186 (= E216), E193 (= E223), H242 (= H272), E330 (= E359)
- binding : Y58 (≠ I82), R60 (≠ P84), V187 (= V217), N237 (≠ A267), G299 (= G328), Y300 (≠ S329), R313 (= R342), M424 (≠ H444)
7tdvC Glutamine synthetase (see paper)
28% identity, 96% coverage: 20:460/461 of query aligns to 5:442/443 of 7tdvC
- binding adenosine-5'-diphosphate: G129 (≠ A149), E131 (= E151), E183 (≠ D211), D197 (≠ N225), F198 (≠ L226), K199 (≠ L227), Y200 (≠ H228), N246 (≠ H274), V247 (≠ Q275), S248 (= S276), R320 (= R347), S328 (≠ A355), R330 (= R357)
- binding magnesium ion: E131 (= E151), E131 (= E151), E133 (= E153), E188 (= E216), E195 (= E223), E195 (= E223), H244 (= H272), E332 (= E359)
- binding l-methionine-s-sulfoximine phosphate: E131 (= E151), E133 (= E153), E188 (= E216), E195 (= E223), G240 (= G268), H244 (= H272), R297 (= R324), E303 (≠ Q330), R315 (= R342)
7tdpA Structure of paenibacillus polymyxa gs bound to met-sox-p-adp (transition state complex) to 1.98 angstom (see paper)
30% identity, 92% coverage: 31:454/461 of query aligns to 15:432/439 of 7tdpA
- binding adenosine-5'-diphosphate: N123 (vs. gap), G125 (≠ A149), E127 (= E151), E179 (≠ D211), D193 (≠ N225), Y196 (≠ H228), N242 (≠ H274), S244 (= S276), R316 (= R347), R326 (= R357)
- binding magnesium ion: E127 (= E151), E127 (= E151), E129 (= E153), E184 (= E216), E191 (= E223), E191 (= E223), H240 (= H272), E328 (= E359)
- binding l-methionine-s-sulfoximine phosphate: E127 (= E151), E129 (= E153), E184 (= E216), E191 (= E223), G236 (= G268), H240 (= H272), R293 (= R324), E299 (≠ Q330), R311 (= R342), R330 (= R361)
7tenA Glutamine synthetase (see paper)
28% identity, 93% coverage: 31:458/461 of query aligns to 15:439/442 of 7tenA
- binding adenosine-5'-diphosphate: G128 (≠ A149), E130 (= E151), E182 (≠ D211), D196 (≠ N225), F197 (≠ L226), K198 (≠ L227), Y199 (≠ H228), N245 (≠ H274), S247 (= S276), R319 (= R347), S327 (≠ A355), R329 (= R357)
- binding l-methionine-s-sulfoximine phosphate: E130 (= E151), E132 (= E153), E187 (= E216), E194 (= E223), N238 (≠ A267), G239 (= G268), H243 (= H272), R296 (= R324), E302 (≠ Q330), R314 (= R342), R333 (= R361)
7tf9S L. Monocytogenes gs(14)-q-glnr peptide (see paper)
28% identity, 93% coverage: 31:458/461 of query aligns to 16:440/443 of 7tf9S
- binding glutamine: E133 (= E153), Y155 (≠ R176), E188 (= E216), G240 (= G268), G242 (≠ S270), R297 (= R324), E303 (≠ Q330)
- binding magnesium ion: E131 (= E151), E133 (= E153), E188 (= E216), E195 (= E223), H244 (= H272), E332 (= E359)
- binding : F59 (≠ I82), V60 (≠ F83), E418 (≠ A436), I422 (≠ L440), M426 (≠ H444)
8oozA Glutamine synthetase (see paper)
30% identity, 93% coverage: 28:457/461 of query aligns to 11:427/430 of 8oozA
- binding adenosine-5'-triphosphate: G117 (≠ A149), E170 (≠ D211), F185 (≠ L226), K186 (≠ L227), Y187 (≠ H228), N233 (≠ H274), S235 (= S276), S315 (≠ A355), R317 (= R357)
- binding magnesium ion: E119 (= E151), H231 (= H272), E319 (= E359)
8ooxB Glutamine synthetase (see paper)
30% identity, 93% coverage: 28:457/461 of query aligns to 11:435/438 of 8ooxB
5dm3C Crystal structure of glutamine synthetase from chromohalobacter salexigens dsm 3043(csal_0679, target efi-550015) with bound adp
34% identity, 79% coverage: 92:453/461 of query aligns to 56:390/396 of 5dm3C
- active site: E115 (= E151), E117 (= E153), E162 (= E216), E169 (= E223), H218 (= H272), R286 (= R342), E303 (= E359), R305 (= R361)
- binding adenosine-5'-diphosphate: R173 (≠ L227), C174 (≠ H228), H220 (= H274), S222 (= S276), R301 (= R357)
5dm3A Crystal structure of glutamine synthetase from chromohalobacter salexigens dsm 3043(csal_0679, target efi-550015) with bound adp
32% identity, 79% coverage: 92:453/461 of query aligns to 52:368/374 of 5dm3A
- active site: E107 (= E151), E109 (= E153), E146 (≠ Q219), E150 (= E223), H199 (= H272), R265 (= R342), E282 (= E359), R284 (= R361)
- binding adenosine-5'-diphosphate: I103 (≠ V147), E141 (≠ R209), R154 (≠ L227), C155 (≠ H228), H201 (= H274), S203 (= S276), R280 (= R357)
Query Sequence
>WP_218017304.1 NCBI__GCF_001592305.1:WP_218017304.1
MTLPASPSWSHLNLSQDADRAQLAAHFKAAGVRDVECLFADVTGYPRGKLMPAASFAAGG
ELRICQAIPMQCVTGEYSYDPIFPDSDPDVRLVPDLATLKPTPWASVPRYLAVHDCFELD
GSLCEFAPRSVLKQVVARYRARGLTPVIAPEIEFYLTAAMTDPAQPLAYPVGRGGRPEVG
QSAFSMNLLNELAPFWDALHAAIDGLGIRADTWLHEVGQSQYEINLLHGDPVAVADQAFL
FKTAAREIALQHGLNAVFMAKPISGQAGSSMHLHQSVVDAQGRNIFSQADGSASEAFLHY
LGGLQAYTPDLALVYAPSVNSYRRYVAGSQAPINVAWGHDNRTTGLRVPDSPPAARRVEN
RLAGADANPYLAMAATLAAGLAGIDERLPPSEPVQGNGYDLARGLPRTFSTAHDQMAHSE
HAPRLLGERFVRGYLAVKALEHDHYLNEVSAWERRYLLPQA
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