SitesBLAST
Comparing WP_011840249.1 NCBI__GCF_000015985.1:WP_011840249.1 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)
P78061 Gamma-glutamylputrescine synthetase PuuA; Gamma-Glu-Put synthetase; Glutamate--putrescine ligase; EC 6.3.1.11 from Escherichia coli (strain K12) (see paper)
38% identity, 97% coverage: 13:463/464 of query aligns to 25:471/472 of P78061
- H282 (= H271) mutation to N: Activity is impaired to 9% of wild-type.
- R357 (= R347) mutation to Q: Activity is impaired to 3% of wild-type.
8tfkA Glutamine synthetase (see paper)
30% identity, 81% coverage: 71:445/464 of query aligns to 40:421/440 of 8tfkA
- binding adenosine-5'-diphosphate: E128 (= E148), D194 (≠ T223), F195 (≠ L224), F197 (≠ Y226), N243 (≠ H273), R312 (= R342), R317 (= R347), G325 (≠ A355), R327 (= R357)
- binding magnesium ion: E128 (= E148), E128 (= E148), E130 (= E150), E185 (= E214), E192 (= E221), E192 (= E221), H241 (= H271), E329 (= E359)
- binding l-methionine-s-sulfoximine phosphate: E128 (= E148), E130 (= E150), E185 (= E214), E192 (= E221), G237 (= G267), H241 (= H271), R294 (= R324), E300 (≠ Y330), R312 (= R342), R331 (= R361)
8ufjB Glutamine synthetase (see paper)
30% identity, 81% coverage: 71:445/464 of query aligns to 44:425/444 of 8ufjB
8ooqB Glutamine synthetase from Methanothermococcus thermolithotrophicus (see paper)
26% identity, 84% coverage: 72:461/464 of query aligns to 47:444/446 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)
26% identity, 84% coverage: 72:461/464 of query aligns to 48:445/447 of 8oooA
- binding 2-oxoglutaric acid: R87 (≠ H100), V93 (≠ R106), P170 (≠ M191), R173 (≠ F194), R174 (≠ S195), S190 (≠ M211)
- binding adenosine-5'-triphosphate: E136 (= E148), E188 (= E209), F203 (≠ L224), K204 (≠ H225), F205 (≠ Y226), H251 (= H273), S253 (= S275), R325 (= R347), R335 (= R357)
Sites not aligning to the query:
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)
30% identity, 74% coverage: 117:461/464 of query aligns to 101:444/446 of A0R083
- K363 (≠ Q386) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
8ooxB Glutamine synthetase (see paper)
28% identity, 83% coverage: 81:463/464 of query aligns to 61:437/438 of 8ooxB
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, 78% coverage: 84:445/464 of query aligns to 65:425/444 of P12425
- E132 (= E148) binding Mg(2+)
- E134 (= E150) binding Mg(2+)
- E189 (= E214) binding Mg(2+)
- V190 (≠ Y215) 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 (= E221) binding Mg(2+)
- G241 (= G267) binding L-glutamate
- H245 (= H271) binding Mg(2+)
- G302 (≠ Q328) 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 (≠ Y330) 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 (= E444) 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)
29% identity, 78% coverage: 84:445/464 of query aligns to 68:428/447 of 4s0rD
- active site: E135 (vs. gap), E137 (= E150), E192 (= E214), E199 (= E221), H248 (= H271), R319 (= R342), E336 (= E359), R338 (= R361)
- binding glutamine: E137 (= E150), E192 (= E214), R301 (= R324), E307 (≠ Y330)
- binding magnesium ion: E135 (vs. gap), E135 (vs. gap), E199 (= E221), H248 (= H271), H248 (= H271), E336 (= E359), H419 (≠ T436)
- binding : D161 (≠ E180), G241 (≠ S264), V242 (≠ Y265), N243 (≠ A266), G305 (≠ Q328), Y306 (≠ S329), Y376 (vs. gap), I426 (≠ A443)
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)
29% identity, 78% coverage: 84:445/464 of query aligns to 64:424/443 of 4lnkA
- active site: E131 (vs. gap), E133 (= E150), E188 (= E214), E195 (= E221), H244 (= H271), R315 (= R342), E332 (= E359), R334 (= R361)
- binding adenosine-5'-diphosphate: F198 (≠ L224), Y200 (= Y226), N246 (≠ H273), S248 (= S275), S324 (≠ G351), S328 (≠ A355), R330 (= R357)
- binding glutamic acid: E133 (= E150), E188 (= E214), V189 (≠ Y215), N239 (≠ A266), G240 (= G267), G242 (= G269), E303 (≠ Y330)
- binding magnesium ion: E131 (vs. gap), E188 (= E214), E195 (= E221), H244 (= H271), E332 (= E359)
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)
29% identity, 78% coverage: 84:445/464 of query aligns to 64:424/443 of 4lniA
- active site: E131 (vs. gap), E133 (= E150), E188 (= E214), E195 (= E221), H244 (= H271), R315 (= R342), E332 (= E359), R334 (= R361)
- binding adenosine-5'-diphosphate: E131 (vs. gap), E183 (= E209), D197 (≠ T223), Y200 (= Y226), N246 (≠ H273), S248 (= S275), R320 (= R347), R330 (= R357)
- binding magnesium ion: E131 (vs. gap), E131 (vs. gap), E133 (= E150), E188 (= E214), E195 (= E221), E195 (= E221), H244 (= H271), E332 (= E359)
- binding l-methionine-s-sulfoximine phosphate: E133 (= E150), E188 (= E214), H244 (= H271), R297 (= R324), E303 (≠ Y330), R315 (= R342), R334 (= R361)
Sites not aligning to the query:
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, 74% coverage: 117:461/464 of query aligns to 101:444/446 of P9WN37
- K363 (≠ Q386) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
8oozA Glutamine synthetase (see paper)
28% identity, 76% coverage: 110:463/464 of query aligns to 80:429/430 of 8oozA
- binding adenosine-5'-triphosphate: G117 (≠ A146), E170 (= E209), F185 (≠ L224), K186 (≠ H225), Y187 (= Y226), N233 (≠ H273), S235 (= S275), S315 (≠ A355), R317 (= R357)
- binding magnesium ion: E119 (= E148), H231 (= H271), E319 (= E359)
7tf9S L. Monocytogenes gs(14)-q-glnr peptide (see paper)
28% identity, 74% coverage: 103:444/464 of query aligns to 82:423/443 of 7tf9S
- binding glutamine: E133 (= E150), Y155 (≠ L187), E188 (= E214), G240 (= G267), G242 (= G269), R297 (= R324), E303 (≠ Y330)
- binding magnesium ion: E131 (vs. gap), E133 (= E150), E188 (= E214), E195 (= E221), H244 (= H271), E332 (= E359)
- binding : E418 (≠ A439), I422 (≠ A443)
Sites not aligning to the query:
7tf6A Glutamine synthetase (see paper)
27% identity, 77% coverage: 105:461/464 of query aligns to 79:435/438 of 7tf6A
- binding glutamine: E128 (= E150), E183 (= E214), G235 (= G267), H239 (= H271), R292 (= R324), E298 (≠ Y330)
- binding magnesium ion: E126 (= E148), E128 (= E150), E183 (= E214), E190 (= E221), H239 (= H271), E327 (= E359)
- binding : G232 (≠ S264), N234 (≠ A266), G296 (≠ Q328), Y297 (≠ S329), R310 (= R342), Y367 (= Y399), Y421 (≠ R447), Q433 (≠ L459)
Sites not aligning to the query:
7tenA Glutamine synthetase (see paper)
28% identity, 74% coverage: 103:444/464 of query aligns to 81:422/442 of 7tenA
- binding adenosine-5'-diphosphate: G128 (vs. gap), E130 (vs. gap), E182 (= E209), D196 (≠ T223), F197 (≠ L224), K198 (≠ H225), Y199 (= Y226), N245 (≠ H273), S247 (= S275), R319 (= R347), S327 (≠ A355), R329 (= R357)
- binding l-methionine-s-sulfoximine phosphate: E130 (vs. gap), E132 (= E150), E187 (= E214), E194 (= E221), N238 (≠ A266), G239 (= G267), H243 (= H271), R296 (= R324), E302 (≠ Y330), R314 (= R342), R333 (= R361)
7tdvC Glutamine synthetase (see paper)
27% identity, 76% coverage: 110:461/464 of query aligns to 91:440/443 of 7tdvC
- binding adenosine-5'-diphosphate: G129 (≠ A146), E131 (= E148), E183 (= E209), D197 (≠ T223), F198 (≠ L224), K199 (≠ H225), Y200 (= Y226), N246 (≠ H273), V247 (= V274), S248 (= S275), R320 (= R347), S328 (≠ A355), R330 (= R357)
- binding magnesium ion: E131 (= E148), E131 (= E148), E133 (= E150), E188 (= E214), E195 (= E221), E195 (= E221), H244 (= H271), E332 (= E359)
- binding l-methionine-s-sulfoximine phosphate: E131 (= E148), E133 (= E150), E188 (= E214), E195 (= E221), G240 (= G267), H244 (= H271), R297 (= R324), E303 (≠ Y330), R315 (= R342)
7tfaB Glutamine synthetase (see paper)
29% identity, 81% coverage: 84:461/464 of query aligns to 63:438/441 of 7tfaB
- binding glutamine: E131 (= E150), Y153 (≠ K178), E186 (= E214), G238 (= G267), H242 (= H271), R295 (= R324), E301 (≠ Y330)
- binding magnesium ion: E129 (= E148), E131 (= E150), E186 (= E214), E193 (= E221), H242 (= H271), E330 (= E359)
- binding : V187 (≠ Y215), N237 (≠ A266), G299 (≠ Q328), Y300 (≠ S329), R313 (= R342), M424 (≠ R447)
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)
29% identity, 76% coverage: 110:461/464 of query aligns to 87:436/439 of 7tdpA
- binding adenosine-5'-diphosphate: N123 (≠ S144), G125 (≠ A146), E127 (= E148), E179 (= E209), D193 (≠ T223), Y196 (= Y226), N242 (≠ H273), S244 (= S275), R316 (= R347), R326 (= R357)
- binding magnesium ion: E127 (= E148), E127 (= E148), E129 (= E150), E184 (= E214), E191 (= E221), E191 (= E221), H240 (= H271), E328 (= E359)
- binding l-methionine-s-sulfoximine phosphate: E127 (= E148), E129 (= E150), E184 (= E214), E191 (= E221), G236 (= G267), H240 (= H271), R293 (= R324), E299 (≠ Y330), R311 (= R342), R330 (= R361)
5dm3C Crystal structure of glutamine synthetase from chromohalobacter salexigens dsm 3043(csal_0679, target efi-550015) with bound adp
31% identity, 72% coverage: 125:456/464 of query aligns to 92:390/396 of 5dm3C
- active site: E115 (= E148), E117 (= E150), E162 (= E214), E169 (= E221), H218 (= H271), R286 (= R342), E303 (= E359), R305 (= R361)
- binding adenosine-5'-diphosphate: R173 (≠ H225), C174 (≠ Y226), H220 (= H273), S222 (= S275), R301 (= R357)
Query Sequence
>WP_011840249.1 NCBI__GCF_000015985.1:WP_011840249.1
MTDQPSPSGSTLSEAETFLAAHPEIEAFDIVLHDANGIGRGKIIRRHELLSFYKGGRHLP
ISILGLDICGEDVHETGLIWDQGDGDLRAWPIPGTLVPLHGTTPPRGEVFMCMYDLDGRP
MSSDPRHALARQVEALAELGLHPSAAFELEFFLLANERGPDGRVQPAADVLDGRRSAKTE
VYSVDHLHGMMPLFSDIYAGAEAAGIKAETMISEYAPGQYELTLHYRTDVLQAADDLMRL
KRIVRAQARRHGVTACFMAKPVESYAGSGMHLHVSLCDAEGRNIFVEETEGQWSRPILHA
LGGLRETMGESMLVFAPHANSWRRFASQSYAPVSPSWGVNNRSVALRIPAGDIRARRIEH
RPAGVDANPYLVAATVLAGIRRGLEQQIDPGPETTGNGYEDPGDTQPIPTCWRSAIAAAQ
HSAFLREALGPDMHRTFTAIKAAEYARVARTIPDVDYDLYLHTV
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