SitesBLAST
Comparing WP_013419765.1 NCBI__GCF_000166055.1:WP_013419765.1 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)
5dm3C Crystal structure of glutamine synthetase from chromohalobacter salexigens dsm 3043(csal_0679, target efi-550015) with bound adp
32% identity, 96% coverage: 14:428/433 of query aligns to 16:393/396 of 5dm3C
- active site: E115 (= E134), E117 (= E136), E162 (= E187), E169 (= E194), H218 (= H243), R286 (= R311), E303 (= E328), R305 (= R330)
- binding adenosine-5'-diphosphate: R173 (= R198), C174 (≠ H199), H220 (= H245), S222 (= S247), R301 (= R326)
5dm3A Crystal structure of glutamine synthetase from chromohalobacter salexigens dsm 3043(csal_0679, target efi-550015) with bound adp
32% identity, 96% coverage: 14:428/433 of query aligns to 18:371/374 of 5dm3A
- active site: E107 (= E134), E109 (= E136), E146 (= E187), E150 (= E194), H199 (= H243), R265 (= R311), E282 (= E328), R284 (= R330)
- binding adenosine-5'-diphosphate: I103 (≠ E130), E141 (= E182), R154 (= R198), C155 (≠ H199), H201 (= H245), S203 (= S247), R280 (= R326)
P78061 Gamma-glutamylputrescine synthetase PuuA; Gamma-Glu-Put synthetase; Glutamate--putrescine ligase; EC 6.3.1.11 from Escherichia coli (strain K12) (see paper)
30% identity, 97% coverage: 11:432/433 of query aligns to 36:471/472 of P78061
- H282 (= H243) mutation to N: Activity is impaired to 9% of wild-type.
- R357 (= R316) mutation to Q: Activity is impaired to 3% of wild-type.
8tfkA Glutamine synthetase (see paper)
32% identity, 80% coverage: 86:430/433 of query aligns to 77:437/440 of 8tfkA
- binding adenosine-5'-diphosphate: E128 (= E134), D194 (≠ N196), F195 (≠ I197), F197 (≠ H199), N243 (≠ H245), R312 (= R311), R317 (= R316), G325 (≠ Q324), R327 (= R326)
- binding magnesium ion: E128 (= E134), E128 (= E134), E130 (= E136), E185 (= E187), E192 (= E194), E192 (= E194), H241 (= H243), E329 (= E328)
- binding l-methionine-s-sulfoximine phosphate: E128 (= E134), E130 (= E136), E185 (= E187), E192 (= E194), G237 (= G239), H241 (= H243), R294 (= R293), E300 (≠ F299), R312 (= R311), R331 (= R330)
8ufjB Glutamine synthetase (see paper)
33% identity, 80% coverage: 86:430/433 of query aligns to 81:441/444 of 8ufjB
7tdpA Structure of paenibacillus polymyxa gs bound to met-sox-p-adp (transition state complex) to 1.98 angstom (see paper)
32% identity, 83% coverage: 73:433/433 of query aligns to 65:439/439 of 7tdpA
- binding adenosine-5'-diphosphate: N123 (≠ E130), G125 (= G132), E127 (= E134), E179 (= E182), D193 (≠ N196), Y196 (≠ H199), N242 (≠ H245), S244 (= S247), R316 (= R316), R326 (= R326)
- binding magnesium ion: E127 (= E134), E127 (= E134), E129 (= E136), E184 (= E187), E191 (= E194), E191 (= E194), H240 (= H243), E328 (= E328)
- binding l-methionine-s-sulfoximine phosphate: E127 (= E134), E129 (= E136), E184 (= E187), E191 (= E194), G236 (= G239), H240 (= H243), R293 (= R293), E299 (≠ F299), R311 (= R311), R330 (= R330)
8wwuB Glutamine synthetase
29% identity, 97% coverage: 11:430/433 of query aligns to 30:489/492 of 8wwuB
- binding phosphoaminophosphonic acid-adenylate ester: G157 (= G132), E159 (= E134), R226 (≠ E182), F241 (≠ I197), V243 (≠ H199), H290 (= H245), S292 (= S247), K360 (≠ R311), R365 (= R316), R376 (= R326)
- binding magnesium ion: E159 (= E134), E238 (= E194)
- binding manganese (ii) ion: E159 (= E134), E161 (= E136), E231 (= E187), E238 (= E194), H288 (= H243), E378 (= E328)
8wwvA Glutamine synthetase
29% identity, 97% coverage: 11:430/433 of query aligns to 28:487/490 of 8wwvA
- binding adenosine-5'-diphosphate: G155 (= G132), E157 (= E134), R224 (≠ E182), F239 (≠ I197), D240 (≠ R198), V241 (≠ H199), H288 (= H245), S290 (= S247), R374 (= R326), E376 (= E328)
- binding magnesium ion: E157 (= E134), E236 (= E194)
- binding manganese (ii) ion: E157 (= E134), E159 (= E136), E229 (= E187), E236 (= E194), H286 (= H243), E376 (= E328)
- binding l-methionine-s-sulfoximine phosphate: E157 (= E134), E159 (= E136), E229 (= E187), E236 (= E194), A282 (≠ G239), H286 (= H243), R340 (= R293), K358 (≠ R311)
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, 98% coverage: 10:433/433 of query aligns to 15:443/443 of 4lnkA
- active site: D52 (= D42), E131 (= E134), E133 (= E136), E188 (= E187), E195 (= E194), H244 (= H243), R315 (= R311), E332 (= E328), R334 (= R330)
- binding adenosine-5'-diphosphate: K43 (≠ T38), M50 (vs. gap), F198 (≠ I197), Y200 (≠ H199), N246 (≠ H245), S248 (= S247), S324 (≠ G320), S328 (≠ Q324), R330 (= R326)
- binding glutamic acid: E133 (= E136), E188 (= E187), V189 (≠ Y188), N239 (≠ S238), G240 (= G239), G242 (= G241), E303 (≠ F299)
- binding magnesium ion: E131 (= E134), E188 (= E187), E195 (= E194), H244 (= H243), E332 (= E328)
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, 98% coverage: 10:433/433 of query aligns to 15:443/443 of 4lniA
- active site: D52 (= D42), E131 (= E134), E133 (= E136), E188 (= E187), E195 (= E194), H244 (= H243), R315 (= R311), E332 (= E328), R334 (= R330)
- binding adenosine-5'-diphosphate: E131 (= E134), E183 (= E182), D197 (≠ N196), Y200 (≠ H199), N246 (≠ H245), S248 (= S247), R320 (= R316), R330 (= R326)
- binding magnesium ion: E131 (= E134), E131 (= E134), E133 (= E136), E188 (= E187), E195 (= E194), E195 (= E194), H244 (= H243), E332 (= E328)
- binding l-methionine-s-sulfoximine phosphate: E133 (= E136), E188 (= E187), H244 (= H243), R297 (= R293), E303 (≠ F299), R315 (= R311), R334 (= R330)
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, 98% coverage: 10:433/433 of query aligns to 16:444/444 of P12425
- G59 (≠ A48) 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 (≠ L53) 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 (= E134) binding Mg(2+)
- E134 (= E136) binding Mg(2+)
- E189 (= E187) binding Mg(2+)
- V190 (≠ Y188) 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 (= E194) binding Mg(2+)
- G241 (= G239) binding L-glutamate
- H245 (= H243) binding Mg(2+)
- G302 (≠ Y297) 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 (≠ F299) 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 (= P301) 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 (= E328) binding Mg(2+)
- E424 (= E413) 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
4s0rD Structure of gs-tnra complex (see paper)
30% identity, 98% coverage: 10:433/433 of query aligns to 19:447/447 of 4s0rD
- active site: D56 (= D42), E135 (= E134), E137 (= E136), E192 (= E187), E199 (= E194), H248 (= H243), R319 (= R311), E336 (= E328), R338 (= R330)
- binding glutamine: E137 (= E136), E192 (= E187), R301 (= R293), E307 (≠ F299)
- binding magnesium ion: I66 (≠ D54), E135 (= E134), E135 (= E134), E199 (= E194), H248 (= H243), H248 (= H243), E336 (= E328), H419 (≠ I405)
- binding : F63 (= F51), V64 (≠ A52), R65 (≠ L53), I66 (≠ D54), D161 (vs. gap), G241 (≠ D236), V242 (≠ Q237), N243 (≠ S238), G305 (≠ Y297), Y306 (≠ T298), Y376 (= Y369), I426 (≠ R412), M430 (≠ F416)
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)
35% identity, 76% coverage: 103:430/433 of query aligns to 101:444/446 of P9WN37
- K363 (≠ E355) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
7tfaB Glutamine synthetase (see paper)
32% identity, 83% coverage: 73:433/433 of query aligns to 65:441/441 of 7tfaB
- binding glutamine: E131 (= E136), Y153 (vs. gap), E186 (= E187), G238 (= G239), H242 (= H243), R295 (= R293), E301 (≠ F299)
- binding magnesium ion: E129 (= E134), E131 (= E136), E186 (= E187), E193 (= E194), H242 (= H243), E330 (= E328)
- binding : V187 (≠ Y188), N237 (≠ S238), G299 (≠ Y297), Y300 (≠ T298), R313 (= R311), M424 (≠ F416)
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)
33% identity, 76% coverage: 103:430/433 of query aligns to 101:444/446 of A0R083
- K363 (≠ E355) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
8oooA Glutamine synthetase from methanothermococcus thermolithotrophicus in complex with 2-oxoglutarate and mgatp at 2.15 a resolution (see paper)
30% identity, 83% coverage: 73:430/433 of query aligns to 71:445/447 of 8oooA
- binding 2-oxoglutaric acid: R87 (≠ E89), V93 (= V92), P170 (≠ E164), R173 (≠ L167), R174 (≠ G168), S190 (= S184)
- binding adenosine-5'-triphosphate: E136 (= E134), E188 (= E182), F203 (≠ I197), K204 (≠ R198), F205 (≠ H199), H251 (= H245), S253 (= S247), R325 (= R316), R335 (= R326)
Sites not aligning to the query:
8ooqB Glutamine synthetase from Methanothermococcus thermolithotrophicus (see paper)
30% identity, 83% coverage: 73:430/433 of query aligns to 70:444/446 of 8ooqB
Sites not aligning to the query:
8oozA Glutamine synthetase (see paper)
30% identity, 80% coverage: 86:433/433 of query aligns to 71:430/430 of 8oozA
- binding adenosine-5'-triphosphate: G117 (= G132), E170 (= E182), F185 (≠ I197), K186 (≠ R198), Y187 (≠ H199), N233 (≠ H245), S235 (= S247), S315 (≠ Q324), R317 (= R326)
- binding magnesium ion: E119 (= E134), H231 (= H243), E319 (= E328)
7tenA Glutamine synthetase (see paper)
31% identity, 83% coverage: 73:430/433 of query aligns to 65:439/442 of 7tenA
- binding adenosine-5'-diphosphate: G128 (= G132), E130 (= E134), E182 (= E182), D196 (≠ N196), F197 (≠ I197), K198 (≠ R198), Y199 (≠ H199), N245 (≠ H245), S247 (= S247), R319 (= R316), S327 (≠ Q324), R329 (= R326)
- binding l-methionine-s-sulfoximine phosphate: E130 (= E134), E132 (= E136), E187 (= E187), E194 (= E194), N238 (≠ S238), G239 (= G239), H243 (= H243), R296 (= R293), E302 (≠ F299), R314 (= R311), R333 (= R330)
7tf9S L. Monocytogenes gs(14)-q-glnr peptide (see paper)
31% identity, 83% coverage: 73:430/433 of query aligns to 66:440/443 of 7tf9S
- binding glutamine: E133 (= E136), Y155 (vs. gap), E188 (= E187), G240 (= G239), G242 (= G241), R297 (= R293), E303 (≠ F299)
- binding magnesium ion: E131 (= E134), E133 (= E136), E188 (= E187), E195 (= E194), H244 (= H243), E332 (= E328)
- binding : E418 (≠ R408), I422 (≠ R412), M426 (≠ F416)
Sites not aligning to the query:
Query Sequence
>WP_013419765.1 NCBI__GCF_000166055.1:WP_013419765.1
MSGSLLPLPEGTHTIVLGVGDVNGVMRGKRIPASNWATTCEDGKAICAAIFALDMTSDIW
DTPFCSFDNGYPDVHLFPLAAPPVAVPWEPGVAITLGRTETLDHKPVPIDPRVALLTQVE
RAARLGLTIEVGTELEFYLLDPETKRPKDKGISVYGIGRSAQFEPVLGPIRRHLEAIGIP
IEQSNPEYAPGRVEVNIRHAGALTGADRVVLFRTAIKEIAALHGYLATFMAKPFIDQSGS
GFHAHYSVWREGVNLFADGGRLSRFGRSFLAGLERRIAESALAVSTTPNAFRRRRPYTFC
PTNVSWGFDNRTIAFRVIEGKDHQVRIEKRDGSADANPYYLLAADIAAGLDGIEEGLELT
SAPISSNAYEQPDLPPLPRDLPTAVRLARSSEFLRRVIGEDRLSILVRQAEREIDFLEAQ
VTPVETKRYLVNF
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