SitesBLAST
Comparing WP_027180554.1 NCBI__GCF_000429985.1:WP_027180554.1 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)
3o6xA Crystal structure of the type iii glutamine synthetase from bacteroides fragilis (see paper)
38% identity, 97% coverage: 23:725/727 of query aligns to 15:637/638 of 3o6xA
- binding adenosine-5'-diphosphate: E180 (= E224), E244 (= E302), F249 (≠ Y307), N295 (= N353), S297 (= S355), R388 (= R476), E390 (= E478)
- binding magnesium ion: E180 (= E224), E182 (= E226), E237 (= E295), E244 (= E302), H293 (= H351), E390 (= E478)
- binding l-methionine-s-sulfoximine phosphate: E180 (= E224), E182 (= E226), E237 (= E295), G289 (= G347), G291 (= G349), H293 (= H351), R349 (= R407), E354 (= E412), R378 (= R466)
8oooA Glutamine synthetase from methanothermococcus thermolithotrophicus in complex with 2-oxoglutarate and mgatp at 2.15 a resolution (see paper)
26% identity, 46% coverage: 203:538/727 of query aligns to 117:382/447 of 8oooA
- binding 2-oxoglutaric acid: P170 (≠ L272), R173 (≠ M275), R174 (≠ M276), S190 (≠ R292)
- binding adenosine-5'-triphosphate: E136 (= E224), E188 (≠ K290), F203 (≠ P305), K204 (≠ L306), F205 (≠ Y307), H251 (≠ N353), S253 (= S355), R325 (≠ K437), R335 (= R476)
Sites not aligning to the query:
8ooqB Glutamine synthetase from Methanothermococcus thermolithotrophicus (see paper)
26% identity, 46% coverage: 203:538/727 of query aligns to 116:381/446 of 8ooqB
Sites not aligning to the query:
7tf9S L. Monocytogenes gs(14)-q-glnr peptide (see paper)
37% identity, 20% coverage: 220:366/727 of query aligns to 127:259/443 of 7tf9S
Sites not aligning to the query:
7tenA Glutamine synthetase (see paper)
37% identity, 20% coverage: 220:366/727 of query aligns to 126:258/442 of 7tenA
- binding adenosine-5'-diphosphate: G128 (= G222), E130 (= E224), E182 (≠ K290), D196 (≠ A304), F197 (≠ P305), K198 (≠ L306), Y199 (= Y307), N245 (= N353), S247 (= S355)
- binding l-methionine-s-sulfoximine phosphate: E130 (= E224), E132 (= E226), E187 (= E295), E194 (= E302), N238 (= N346), G239 (= G347), H243 (= H351)
Sites not aligning to the query:
7tf6A Glutamine synthetase (see paper)
32% identity, 20% coverage: 220:367/727 of query aligns to 122:255/438 of 7tf6A
Sites not aligning to the query:
7tdvC Glutamine synthetase (see paper)
32% identity, 20% coverage: 220:367/727 of query aligns to 127:260/443 of 7tdvC
- binding adenosine-5'-diphosphate: G129 (= G222), E131 (= E224), E183 (≠ K290), D197 (≠ A304), F198 (≠ P305), K199 (≠ L306), Y200 (= Y307), N246 (= N353), V247 (≠ Y354), S248 (= S355)
- binding magnesium ion: E131 (= E224), E131 (= E224), E133 (= E226), E188 (= E295), E195 (= E302), E195 (= E302), H244 (= H351)
- binding l-methionine-s-sulfoximine phosphate: E131 (= E224), E133 (= E226), E188 (= E295), E195 (= E302), G240 (= G347), H244 (= H351)
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)
34% identity, 18% coverage: 277:407/727 of query aligns to 170:296/443 of 4lnkA
- active site: E188 (= E295), E195 (= E302), H244 (= H351)
- binding adenosine-5'-diphosphate: F198 (≠ P305), Y200 (= Y307), N246 (= N353), S248 (= S355)
- binding glutamic acid: E188 (= E295), V189 (= V296), N239 (= N346), G240 (= G347), G242 (= G349)
- binding magnesium ion: E188 (= E295), E195 (= E302), H244 (= H351)
Sites not aligning to the query:
- active site: 52, 131, 133, 315, 332, 334
- binding adenosine-5'-diphosphate: 43, 50, 324, 328, 330
- binding glutamic acid: 133, 303
- binding magnesium ion: 131, 332
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)
34% identity, 18% coverage: 277:407/727 of query aligns to 170:296/443 of 4lniA
- active site: E188 (= E295), E195 (= E302), H244 (= H351)
- binding adenosine-5'-diphosphate: E183 (≠ K290), D197 (≠ A304), Y200 (= Y307), N246 (= N353), S248 (= S355)
- binding magnesium ion: E188 (= E295), E195 (= E302), E195 (= E302), H244 (= H351)
- binding l-methionine-s-sulfoximine phosphate: E188 (= E295), H244 (= H351)
Sites not aligning to the query:
- active site: 52, 131, 133, 315, 332, 334
- binding adenosine-5'-diphosphate: 131, 320, 330
- binding magnesium ion: 131, 131, 133, 332
- binding l-methionine-s-sulfoximine phosphate: 133, 297, 303, 315, 334
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)
34% identity, 18% coverage: 277:407/727 of query aligns to 171:297/444 of P12425
- E189 (= E295) binding Mg(2+)
- V190 (= V296) 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 (= E302) binding Mg(2+)
- G241 (= G347) binding L-glutamate
- H245 (= H351) binding Mg(2+)
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.
- 132 binding Mg(2+)
- 134 binding Mg(2+)
- 302 G→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.
- 304 E→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.
- 306 P→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.
- 333 binding Mg(2+)
- 424 E→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)
34% identity, 18% coverage: 277:407/727 of query aligns to 174:300/447 of 4s0rD
Sites not aligning to the query:
- active site: 56, 135, 137, 319, 336, 338
- binding glutamine: 137, 301, 307
- binding magnesium ion: 66, 135, 135, 336, 419
- binding : 63, 64, 65, 66, 161, 305, 306, 376, 426, 430
7tfaB Glutamine synthetase (see paper)
31% identity, 21% coverage: 220:369/727 of query aligns to 125:260/441 of 7tfaB
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)
31% identity, 21% coverage: 220:369/727 of query aligns to 123:258/439 of 7tdpA
- binding adenosine-5'-diphosphate: N123 (= N220), G125 (= G222), E127 (= E224), E179 (≠ K290), D193 (≠ A304), Y196 (= Y307), N242 (= N353), S244 (= S355)
- binding magnesium ion: E127 (= E224), E127 (= E224), E129 (= E226), E184 (= E295), E191 (= E302), E191 (= E302), H240 (= H351)
- binding l-methionine-s-sulfoximine phosphate: E127 (= E224), E129 (= E226), E184 (= E295), E191 (= E302), G236 (= G347), H240 (= H351)
Sites not aligning to the query:
8ooxB Glutamine synthetase (see paper)
32% identity, 21% coverage: 218:373/727 of query aligns to 121:260/438 of 8ooxB
8oozA Glutamine synthetase (see paper)
32% identity, 21% coverage: 218:373/727 of query aligns to 113:252/430 of 8oozA
Sites not aligning to the query:
8tfkA Glutamine synthetase (see paper)
27% identity, 25% coverage: 220:401/727 of query aligns to 124:291/440 of 8tfkA
- binding adenosine-5'-diphosphate: E128 (= E224), D194 (≠ A304), F195 (≠ P305), F197 (≠ Y307), N243 (= N353)
- binding magnesium ion: E128 (= E224), E128 (= E224), E130 (= E226), E185 (= E295), E192 (= E302), E192 (= E302), H241 (= H351)
- binding l-methionine-s-sulfoximine phosphate: E128 (= E224), E130 (= E226), E185 (= E295), E192 (= E302), G237 (= G347), H241 (= H351)
Sites not aligning to the query:
8ufjB Glutamine synthetase (see paper)
27% identity, 25% coverage: 220:401/727 of query aligns to 128:295/444 of 8ufjB
Sites not aligning to the query:
3ng0A Crystal structure of glutamine synthetase from synechocystis sp. Pcc 6803
29% identity, 19% coverage: 222:356/727 of query aligns to 128:275/465 of 3ng0A
- active site: E130 (= E224), E132 (= E226), E213 (= E295), E221 (= E302), H270 (= H351)
- binding phosphoaminophosphonic acid-adenylate ester: E130 (= E224), K209 (≠ T291), I224 (≠ P305), F226 (≠ Y307), H272 (≠ N353), S274 (= S355)
- binding manganese (ii) ion: E130 (= E224), E132 (= E226), E213 (= E295), E221 (= E302), H270 (= H351)
Sites not aligning to the query:
7cquA Gmas/adp/metsox-p complex (see paper)
27% identity, 19% coverage: 230:366/727 of query aligns to 120:249/429 of 7cquA
- binding adenosine-5'-diphosphate: E121 (≠ D231), Y173 (= Y283), N187 (≠ A304), W188 (≠ P305), D189 (≠ L306), Y190 (= Y307), H236 (≠ N353), L237 (≠ Y354), S238 (= S355)
- binding magnesium ion: E121 (≠ D231), E121 (≠ D231), E123 (≠ N233), E178 (= E295), E185 (= E302), E185 (= E302), H234 (= H351)
- binding l-methionine-s-sulfoximine phosphate: E121 (≠ D231), E123 (≠ N233), E178 (= E295), E185 (= E302), T229 (≠ N346), G230 (= G347), H234 (= H351)
Sites not aligning to the query:
7cqqA Gmas in complex with amppnp and metsox (see paper)
27% identity, 19% coverage: 230:366/727 of query aligns to 120:249/429 of 7cqqA
- binding phosphoaminophosphonic acid-adenylate ester: E121 (≠ D231), Y173 (= Y283), E185 (= E302), N187 (≠ A304), D189 (≠ L306), Y190 (= Y307), H234 (= H351), H236 (≠ N353), S238 (= S355)
- binding magnesium ion: E121 (≠ D231), E121 (≠ D231), E123 (≠ N233), E178 (= E295), E185 (= E302), E185 (= E302), H234 (= H351)
- binding (2s)-2-amino-4-(methylsulfonimidoyl)butanoic acid: E123 (≠ N233), E178 (= E295), T229 (≠ N346), H234 (= H351)
Sites not aligning to the query:
Query Sequence
>WP_027180554.1 NCBI__GCF_000429985.1:WP_027180554.1
MSGYQSRQNAINAVNNYKRTTAPLNFTETPPTEVFGSNVFSEKVMRKMLPKDIFKSIKKT
IKHGTKLDPAVADYVAAAMKEWAVSKGATHYTHVFYPLTGLTAEKHDGFLSPDGEGGAIA
EFSGKLLIQGEPDASSFPNGGIRTTFEARGYTAWDVTNPAYILENPNGTFLCIPTCFVSW
TGEALDKKTPLMRSSQAMNKQAQRILKLFGNDNGELVVSNAGPEQEYFLIDRNFFFSRPD
LLVSGRTVFGSKPAKGQEFDDHYFGAIPRRVLSFMMDVEHELYKLGVPIKTRHNEVAPGQ
FEIAPLYEQSNLATDHNQMVMTTLKTVAKKHGMACLLHEKPFAGINGSGKHLNYSLSTPS
LGSLYDPGDTPHENAQFLLVCAATIRAVHKYGKLLRAVVASAGNDHRLGANEAPPAILSV
YLGDQLTSILNQIKEGKVSESKCKENLKIGVDTIPPLPRDAGDRNRTSPFAFTGNRFEFR
AVGSNMSIAGPQVALNTMVAESLDYCATKIEEITGGDCKKLHDAVEQVIRDIMKEHEAVV
FNGDGYSEEWHKEAEKRGLPNLRNSAEALPVLNDPEVIELFTKYEVFTERELDSRREIYL
EQYSQTLRTEAAVCIKMGTTQIFPAAVRYQNELAQTCANLKAIGKDSVSLTLDDVTAKLR
GLQTSLTELESILAKEDFADALEEAKYLCYTLLPAMGKVREYADALEEVVADDLWPLPSY
QEMLFIK
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