SitesBLAST
Comparing PP_5299 FitnessBrowser__Putida:PP_5299 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)
44% identity, 98% coverage: 8:457/460 of query aligns to 21:469/472 of P78061
- H282 (= H269) mutation to N: Activity is impaired to 9% of wild-type.
- R357 (= R345) mutation to Q: Activity is impaired to 3% of wild-type.
8wwuB Glutamine synthetase
30% identity, 91% coverage: 25:444/460 of query aligns to 32:465/492 of 8wwuB
- binding phosphoaminophosphonic acid-adenylate ester: G157 (≠ A145), E159 (= E147), R226 (≠ D207), F241 (≠ L222), V243 (= V225), H290 (= H271), S292 (= S273), K360 (≠ R340), R365 (= R345), R376 (= R355)
- binding magnesium ion: E159 (= E147), E238 (= E219)
- binding manganese (ii) ion: E159 (= E147), E161 (= E149), E231 (= E212), E238 (= E219), H288 (= H269), E378 (= E357)
8wwvA Glutamine synthetase
30% identity, 91% coverage: 25:444/460 of query aligns to 30:463/490 of 8wwvA
- binding adenosine-5'-diphosphate: G155 (≠ A145), E157 (= E147), R224 (≠ D207), F239 (≠ L222), D240 (≠ H223), V241 (= V225), H288 (= H271), S290 (= S273), R374 (= R355), E376 (= E357)
- binding magnesium ion: E157 (= E147), E236 (= E219)
- binding manganese (ii) ion: E157 (= E147), E159 (= E149), E229 (= E212), E236 (= E219), H286 (= H269), E376 (= E357)
- binding l-methionine-s-sulfoximine phosphate: E157 (= E147), E159 (= E149), E229 (= E212), E236 (= E219), A282 (≠ G265), H286 (= H269), R340 (= R322), K358 (≠ R340)
8oooA Glutamine synthetase from methanothermococcus thermolithotrophicus in complex with 2-oxoglutarate and mgatp at 2.15 a resolution (see paper)
29% identity, 94% coverage: 25:457/460 of query aligns to 21:445/447 of 8oooA
- binding 2-oxoglutaric acid: A33 (≠ V37), R87 (≠ Q101), V93 (≠ T105), P170 (≠ A189), R173 (≠ L192), R174 (≠ Q193), S190 (≠ I209)
- binding adenosine-5'-triphosphate: E136 (= E147), E188 (≠ D207), F203 (≠ L222), K204 (≠ H223), F205 (≠ V225), H251 (= H271), S253 (= S273), R325 (= R345), R335 (= R355)
Sites not aligning to the query:
8ooqB Glutamine synthetase from Methanothermococcus thermolithotrophicus (see paper)
29% identity, 94% coverage: 25:457/460 of query aligns to 20:444/446 of 8ooqB
Sites not aligning to the query:
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: 18:457/460 of query aligns to 12:441/444 of P12425
- G59 (≠ S74) 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 (= E147) binding
- E134 (= E149) binding
- E189 (= E212) binding
- V190 (≠ S213) 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 (= E219) binding
- G241 (= G265) binding
- H245 (= H269) binding
- G302 (≠ Q326) 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
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: 18:457/460 of query aligns to 11:440/443 of 4lnkA
- active site: D52 (≠ N68), E131 (= E147), E133 (= E149), E188 (= E212), E195 (= E219), H244 (= H269), R315 (= R340), E332 (= E357), R334 (= R359)
- binding adenosine-5'-diphosphate: K43 (= K50), M50 (≠ N57), F198 (≠ L222), Y200 (≠ H224), N246 (≠ H271), S248 (= S273), S324 (≠ D349), S328 (≠ N353), R330 (= R355)
- binding glutamic acid: E133 (= E149), E188 (= E212), V189 (≠ S213), N239 (≠ A264), G240 (= G265), G242 (= G267), E303 (≠ Y328)
- binding magnesium ion: E131 (= E147), E188 (= E212), E195 (= E219), H244 (= H269), 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)
28% identity, 96% coverage: 18:457/460 of query aligns to 11:440/443 of 4lniA
- active site: D52 (≠ N68), E131 (= E147), E133 (= E149), E188 (= E212), E195 (= E219), H244 (= H269), R315 (= R340), E332 (= E357), R334 (= R359)
- binding adenosine-5'-diphosphate: E131 (= E147), E183 (≠ D207), D197 (≠ N221), Y200 (≠ H224), N246 (≠ H271), S248 (= S273), R320 (= R345), R330 (= R355)
- binding magnesium ion: E131 (= E147), E131 (= E147), E133 (= E149), E188 (= E212), E195 (= E219), E195 (= E219), H244 (= H269), E332 (= E357)
- binding l-methionine-s-sulfoximine phosphate: E133 (= E149), E188 (= E212), H244 (= H269), R297 (= R322), E303 (≠ Y328), R315 (= R340), R334 (= R359)
4s0rD Structure of gs-tnra complex (see paper)
28% identity, 96% coverage: 18:457/460 of query aligns to 15:444/447 of 4s0rD
- active site: D56 (≠ N68), E135 (= E147), E137 (= E149), E192 (= E212), E199 (= E219), H248 (= H269), R319 (= R340), E336 (= E357), R338 (= R359)
- binding glutamine: E137 (= E149), E192 (= E212), R301 (= R322), E307 (≠ Y328)
- binding magnesium ion: I66 (= I81), E135 (= E147), E135 (= E147), E199 (= E219), H248 (= H269), H248 (= H269), E336 (= E357), H419 (≠ I432)
- binding : F63 (≠ T75), V64 (≠ L79), R65 (≠ D80), I66 (= I81), D161 (≠ L181), G241 (= G262), V242 (≠ Q263), N243 (≠ A264), G305 (≠ Q326), Y306 (≠ F327), Y376 (= Y397), I426 (≠ S439), M430 (≠ E443)
8ooxB Glutamine synthetase (see paper)
29% identity, 95% coverage: 23:459/460 of query aligns to 14:437/438 of 8ooxB
7tdpA Structure of paenibacillus polymyxa gs bound to met-sox-p-adp (transition state complex) to 1.98 angstom (see paper)
28% identity, 95% coverage: 23:457/460 of query aligns to 15:436/439 of 7tdpA
- binding adenosine-5'-diphosphate: N123 (≠ C143), G125 (≠ A145), E127 (= E147), E179 (≠ D207), D193 (≠ N221), Y196 (≠ H224), N242 (≠ H271), S244 (= S273), R316 (= R345), R326 (= R355)
- binding magnesium ion: E127 (= E147), E127 (= E147), E129 (= E149), E184 (= E212), E191 (= E219), E191 (= E219), H240 (= H269), E328 (= E357)
- binding l-methionine-s-sulfoximine phosphate: E127 (= E147), E129 (= E149), E184 (= E212), E191 (= E219), G236 (= G265), H240 (= H269), 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)
29% identity, 95% coverage: 23:457/460 of query aligns to 16:444/446 of A0R083
- K363 (≠ H380) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
8oozA Glutamine synthetase (see paper)
29% identity, 95% coverage: 23:459/460 of query aligns to 14:429/430 of 8oozA
- binding adenosine-5'-triphosphate: G117 (≠ A145), E170 (≠ D207), F185 (≠ L222), K186 (≠ H223), Y187 (≠ H224), N233 (≠ H271), S235 (= S273), S315 (≠ N353), R317 (= R355)
- binding magnesium ion: E119 (= E147), H231 (= H269), E319 (= E357)
7tf6A Glutamine synthetase (see paper)
27% identity, 95% coverage: 23:457/460 of query aligns to 15:435/438 of 7tf6A
- binding glutamine: E128 (= E149), E183 (= E212), G235 (= G265), H239 (= H269), R292 (= R322), E298 (≠ Y328)
- binding magnesium ion: E126 (= E147), E128 (= E149), E183 (= E212), E190 (= E219), H239 (= H269), E327 (= E357)
- binding : F58 (≠ T75), R60 (≠ D80), G232 (= G262), N234 (≠ A264), G296 (≠ Q326), Y297 (≠ F327), R310 (= R340), Y367 (= Y397), Y421 (≠ E443), Q433 (≠ W455)
Sites not aligning to the query:
7tfaB Glutamine synthetase (see paper)
28% identity, 95% coverage: 23:457/460 of query aligns to 15:438/441 of 7tfaB
- binding glutamine: E131 (= E149), Y153 (≠ V179), E186 (= E212), G238 (= G265), H242 (= H269), R295 (= R322), E301 (≠ Y328)
- binding magnesium ion: E129 (= E147), E131 (= E149), E186 (= E212), E193 (= E219), H242 (= H269), E330 (= E357)
- binding : Y58 (≠ T75), R60 (≠ D80), V187 (≠ S213), N237 (≠ A264), G299 (≠ Q326), Y300 (≠ F327), R313 (= R340), M424 (≠ E443)
7tf9S L. Monocytogenes gs(14)-q-glnr peptide (see paper)
28% identity, 95% coverage: 23:457/460 of query aligns to 16:440/443 of 7tf9S
- binding glutamine: E133 (= E149), Y155 (≠ V179), E188 (= E212), G240 (= G265), G242 (= G267), R297 (= R322), E303 (≠ Y328)
- binding magnesium ion: E131 (= E147), E133 (= E149), E188 (= E212), E195 (= E219), H244 (= H269), E332 (= E357)
- binding : F59 (≠ T75), V60 (≠ L79), E418 (≠ A435), I422 (≠ S439), M426 (≠ E443)
7tenA Glutamine synthetase (see paper)
28% identity, 95% coverage: 23:457/460 of query aligns to 15:439/442 of 7tenA
- binding adenosine-5'-diphosphate: G128 (≠ A145), E130 (= E147), E182 (≠ D207), D196 (≠ N221), F197 (≠ L222), K198 (≠ H223), Y199 (≠ H224), N245 (≠ H271), S247 (= S273), R319 (= R345), S327 (≠ N353), R329 (= R355)
- binding l-methionine-s-sulfoximine phosphate: E130 (= E147), E132 (= E149), E187 (= E212), E194 (= E219), N238 (≠ A264), G239 (= G265), H243 (= H269), R296 (= R322), E302 (≠ Y328), R314 (= R340), R333 (= R359)
7tdvC Glutamine synthetase (see paper)
27% identity, 95% coverage: 23:457/460 of query aligns to 16:440/443 of 7tdvC
- binding adenosine-5'-diphosphate: G129 (≠ A145), E131 (= E147), E183 (≠ D207), D197 (≠ N221), F198 (≠ L222), K199 (≠ H223), Y200 (≠ H224), N246 (≠ H271), V247 (≠ I272), S248 (= S273), R320 (= R345), S328 (≠ N353), R330 (= R355)
- binding magnesium ion: E131 (= E147), E131 (= E147), E133 (= E149), E188 (= E212), E195 (= E219), E195 (= E219), H244 (= H269), E332 (= E357)
- binding l-methionine-s-sulfoximine phosphate: E131 (= E147), E133 (= E149), E188 (= E212), E195 (= E219), G240 (= G265), H244 (= H269), R297 (= R322), E303 (≠ Y328), R315 (= R340)
8tfkA Glutamine synthetase (see paper)
27% identity, 95% coverage: 23:457/460 of query aligns to 14:437/440 of 8tfkA
- binding adenosine-5'-diphosphate: E128 (= E147), D194 (≠ N221), F195 (≠ L222), F197 (≠ V225), N243 (≠ H271), R312 (= R340), R317 (= R345), G325 (≠ N353), R327 (= R355)
- binding magnesium ion: E128 (= E147), E128 (= E147), E130 (= E149), E185 (= E212), E192 (= E219), E192 (= E219), H241 (= H269), E329 (= E357)
- binding l-methionine-s-sulfoximine phosphate: E128 (= E147), E130 (= E149), E185 (= E212), E192 (= E219), G237 (= G265), H241 (= H269), R294 (= R322), E300 (≠ Y328), R312 (= R340), R331 (= R359)
8ufjB Glutamine synthetase (see paper)
27% identity, 95% coverage: 23:457/460 of query aligns to 18:441/444 of 8ufjB
Query Sequence
>PP_5299 FitnessBrowser__Putida:PP_5299
MTSVTPCASSSSEMNDFLQAHPDTQYVDLLISDMNGVVRGKRIERASLHKVYEKGINLPA
SLFALDINGSTVESTGLGLDIGDADRICFPIPGTLSDEPWQKRPTAQLLMTMHELDGQPF
FADPREVLRQVVSKFDDLGLTICAAFELEFYLIDQDNLNGRPQPPRSPISGKRPQSTQVY
LIDDLDEYADCLQDMLEAAKEQGLPADAIVKESAPAQFEVNLHHVADPLKACDYAILLKR
LIKNVAYDHEMDTTFMAKPYPGQAGNGLHVHISLLDKKTGKNIFASDDPLQSDTLRHAIG
GVLETMPASMAFLCPNINSYRRFGAQFYVPNAPSWGLDNRTVAVRVPTDSSENVRLEHRV
AGADANPYLMLAAILAGVHHGLTNKVEPEAPIEGNSYEQLEQSLPNNLRDALRALDDSEV
LNQYISPDYIDIFVACKESELAEFEVSISDLEYNWYLHTV
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