SitesBLAST
Comparing Pf6N2E2_4509 FitnessBrowser__pseudo6_N2E2:Pf6N2E2_4509 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)
44% identity, 99% coverage: 3:420/423 of query aligns to 52:469/472 of P78061
- H282 (= H233) mutation to N: Activity is impaired to 9% of wild-type.
- R357 (= R308) mutation to Q: Activity is impaired to 3% of wild-type.
7tdpA Structure of paenibacillus polymyxa gs bound to met-sox-p-adp (transition state complex) to 1.98 angstom (see paper)
31% identity, 99% coverage: 2:420/423 of query aligns to 16:436/439 of 7tdpA
- binding adenosine-5'-diphosphate: N123 (≠ C107), G125 (≠ A109), E127 (= E111), E179 (≠ D171), D193 (≠ N185), Y196 (≠ H188), N242 (≠ H235), S244 (= S237), R316 (= R308), R326 (= R318)
- binding magnesium ion: E127 (= E111), E127 (= E111), E129 (= E113), E184 (= E176), E191 (= E183), E191 (= E183), H240 (= H233), E328 (= E320)
- binding l-methionine-s-sulfoximine phosphate: E127 (= E111), E129 (= E113), E184 (= E176), E191 (= E183), G236 (= G229), H240 (= H233), R293 (= R285), E299 (≠ Y291), R311 (= R303), R330 (= R322)
8ooqB Glutamine synthetase from Methanothermococcus thermolithotrophicus (see paper)
29% identity, 96% coverage: 14:420/423 of query aligns to 36:444/446 of 8ooqB
Sites not aligning to the query:
8wwvA Glutamine synthetase
31% identity, 96% coverage: 1:407/423 of query aligns to 42:463/490 of 8wwvA
- binding adenosine-5'-diphosphate: G155 (≠ A109), E157 (= E111), R224 (≠ D171), F239 (≠ L186), D240 (≠ H187), V241 (= V189), H288 (= H235), S290 (= S237), R374 (= R318), E376 (= E320)
- binding magnesium ion: E157 (= E111), E236 (= E183)
- binding manganese (ii) ion: E157 (= E111), E159 (= E113), E229 (= E176), E236 (= E183), H286 (= H233), E376 (= E320)
- binding l-methionine-s-sulfoximine phosphate: E157 (= E111), E159 (= E113), E229 (= E176), E236 (= E183), A282 (≠ G229), H286 (= H233), R340 (= R285), K358 (≠ R303)
8oooA Glutamine synthetase from methanothermococcus thermolithotrophicus in complex with 2-oxoglutarate and mgatp at 2.15 a resolution (see paper)
29% identity, 96% coverage: 14:420/423 of query aligns to 37:445/447 of 8oooA
- binding 2-oxoglutaric acid: R87 (≠ Q65), V93 (≠ T69), P170 (≠ V153), R173 (≠ L156), R174 (≠ Q157), S190 (≠ I173)
- binding adenosine-5'-triphosphate: E136 (= E111), E188 (≠ D171), F203 (≠ L186), K204 (≠ H187), F205 (≠ V189), H251 (= H235), S253 (= S237), R325 (= R308), R335 (= R318)
Sites not aligning to the query:
8wwuB Glutamine synthetase
31% identity, 96% coverage: 1:407/423 of query aligns to 44:465/492 of 8wwuB
- binding phosphoaminophosphonic acid-adenylate ester: G157 (≠ A109), E159 (= E111), R226 (≠ D171), F241 (≠ L186), V243 (= V189), H290 (= H235), S292 (= S237), K360 (≠ R303), R365 (= R308), R376 (= R318)
- binding magnesium ion: E159 (= E111), E238 (= E183)
- binding manganese (ii) ion: E159 (= E111), E161 (= E113), E231 (= E176), E238 (= E183), H288 (= H233), E378 (= E320)
7tfaB Glutamine synthetase (see paper)
30% identity, 99% coverage: 2:420/423 of query aligns to 16:438/441 of 7tfaB
- binding glutamine: E131 (= E113), Y153 (≠ V143), E186 (= E176), G238 (= G229), H242 (= H233), R295 (= R285), E301 (≠ Y291)
- binding magnesium ion: E129 (= E111), E131 (= E113), E186 (= E176), E193 (= E183), H242 (= H233), E330 (= E320)
- binding : Y58 (≠ T39), R60 (≠ D44), V187 (≠ S177), N237 (≠ A228), G299 (≠ Q289), Y300 (≠ F290), R313 (= R303), M424 (≠ E406)
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)
29% identity, 95% coverage: 18:420/423 of query aligns to 33:441/444 of P12425
- G59 (≠ S38) 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 (≠ D44) 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 (= E111) binding
- E134 (= E113) binding
- E189 (= E176) binding
- V190 (≠ S177) 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 (= E183) binding
- G241 (= G229) binding
- H245 (= H233) binding
- G302 (≠ Q289) 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 (≠ Y291) 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 (= P293) 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 (= E320) binding
- E424 (= E403) 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)
29% identity, 95% coverage: 18:420/423 of query aligns to 32:440/443 of 4lnkA
- active site: D52 (≠ N32), E131 (= E111), E133 (= E113), E188 (= E176), E195 (= E183), H244 (= H233), R315 (= R303), E332 (= E320), R334 (= R322)
- binding adenosine-5'-diphosphate: K43 (vs. gap), M50 (vs. gap), F198 (≠ L186), Y200 (≠ H188), N246 (≠ H235), S248 (= S237), S324 (≠ G312), S328 (≠ A316), R330 (= R318)
- binding glutamic acid: E133 (= E113), E188 (= E176), V189 (≠ S177), N239 (≠ A228), G240 (= G229), G242 (= G231), E303 (≠ Y291)
- binding magnesium ion: E131 (= E111), E188 (= E176), E195 (= E183), H244 (= H233), E332 (= E320)
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, 95% coverage: 18:420/423 of query aligns to 32:440/443 of 4lniA
- active site: D52 (≠ N32), E131 (= E111), E133 (= E113), E188 (= E176), E195 (= E183), H244 (= H233), R315 (= R303), E332 (= E320), R334 (= R322)
- binding adenosine-5'-diphosphate: E131 (= E111), E183 (≠ D171), D197 (≠ N185), Y200 (≠ H188), N246 (≠ H235), S248 (= S237), R320 (= R308), R330 (= R318)
- binding magnesium ion: E131 (= E111), E131 (= E111), E133 (= E113), E188 (= E176), E195 (= E183), E195 (= E183), H244 (= H233), E332 (= E320)
- binding l-methionine-s-sulfoximine phosphate: E133 (= E113), E188 (= E176), H244 (= H233), R297 (= R285), E303 (≠ Y291), R315 (= R303), R334 (= R322)
4s0rD Structure of gs-tnra complex (see paper)
29% identity, 95% coverage: 18:420/423 of query aligns to 36:444/447 of 4s0rD
- active site: D56 (≠ N32), E135 (= E111), E137 (= E113), E192 (= E176), E199 (= E183), H248 (= H233), R319 (= R303), E336 (= E320), R338 (= R322)
- binding glutamine: E137 (= E113), E192 (= E176), R301 (= R285), E307 (≠ Y291)
- binding magnesium ion: I66 (= I45), E135 (= E111), E135 (= E111), E199 (= E183), H248 (= H233), H248 (= H233), E336 (= E320), H419 (≠ I395)
- binding : F63 (≠ T39), V64 (≠ L43), R65 (≠ D44), I66 (= I45), D161 (≠ P138), G241 (= G226), V242 (≠ Q227), N243 (≠ A228), G305 (≠ Q289), Y306 (≠ F290), Y376 (= Y360), I426 (≠ S402), M430 (≠ E406)
7tf9S L. Monocytogenes gs(14)-q-glnr peptide (see paper)
30% identity, 99% coverage: 2:420/423 of query aligns to 17:440/443 of 7tf9S
- binding glutamine: E133 (= E113), Y155 (≠ K136), E188 (= E176), G240 (= G229), G242 (= G231), R297 (= R285), E303 (≠ Y291)
- binding magnesium ion: E131 (= E111), E133 (= E113), E188 (= E176), E195 (= E183), H244 (= H233), E332 (= E320)
- binding : F59 (≠ T39), V60 (≠ L43), E418 (≠ A398), I422 (≠ S402), M426 (≠ E406)
7tenA Glutamine synthetase (see paper)
30% identity, 95% coverage: 18:420/423 of query aligns to 31:439/442 of 7tenA
- binding adenosine-5'-diphosphate: G128 (≠ A109), E130 (= E111), E182 (≠ D171), D196 (≠ N185), F197 (≠ L186), K198 (≠ H187), Y199 (≠ H188), N245 (≠ H235), S247 (= S237), R319 (= R308), S327 (≠ A316), R329 (= R318)
- binding l-methionine-s-sulfoximine phosphate: E130 (= E111), E132 (= E113), E187 (= E176), E194 (= E183), N238 (≠ A228), G239 (= G229), H243 (= H233), R296 (= R285), E302 (≠ Y291), R314 (= R303), R333 (= R322)
8ooxB Glutamine synthetase (see paper)
29% identity, 93% coverage: 28:422/423 of query aligns to 46:437/438 of 8ooxB
7tf6A Glutamine synthetase (see paper)
30% identity, 92% coverage: 31:420/423 of query aligns to 50:435/438 of 7tf6A
- binding glutamine: E128 (= E113), E183 (= E176), G235 (= G229), H239 (= H233), R292 (= R285), E298 (≠ Y291)
- binding magnesium ion: E126 (= E111), E128 (= E113), E183 (= E176), E190 (= E183), H239 (= H233), E327 (= E320)
- binding : F58 (≠ T39), R60 (≠ D44), G232 (= G226), N234 (≠ A228), G296 (≠ Q289), Y297 (≠ F290), R310 (= R303), Y367 (= Y360), Y421 (≠ E406), Q433 (≠ W418)
Sites not aligning to the query:
8tfkA Glutamine synthetase (see paper)
28% identity, 99% coverage: 1:420/423 of query aligns to 28:437/440 of 8tfkA
- binding adenosine-5'-diphosphate: E128 (= E111), D194 (≠ N185), F195 (≠ L186), F197 (≠ V189), N243 (≠ H235), R312 (= R303), R317 (= R308), G325 (≠ A316), R327 (= R318)
- binding magnesium ion: E128 (= E111), E128 (= E111), E130 (= E113), E185 (= E176), E192 (= E183), E192 (= E183), H241 (= H233), E329 (= E320)
- binding l-methionine-s-sulfoximine phosphate: E128 (= E111), E130 (= E113), E185 (= E176), E192 (= E183), G237 (= G229), H241 (= H233), R294 (= R285), E300 (≠ Y291), R312 (= R303), R331 (= R322)
8oozA Glutamine synthetase (see paper)
30% identity, 90% coverage: 42:422/423 of query aligns to 51:429/430 of 8oozA
- binding adenosine-5'-triphosphate: G117 (≠ A109), E170 (≠ D171), F185 (≠ L186), K186 (≠ H187), Y187 (≠ H188), N233 (≠ H235), S235 (= S237), S315 (≠ A316), R317 (= R318)
- binding magnesium ion: E119 (= E111), H231 (= H233), E319 (= E320)
8ufjB Glutamine synthetase (see paper)
28% identity, 99% coverage: 1:420/423 of query aligns to 32:441/444 of 8ufjB
7tdvC Glutamine synthetase (see paper)
29% identity, 92% coverage: 31:420/423 of query aligns to 51:440/443 of 7tdvC
- binding adenosine-5'-diphosphate: G129 (≠ A109), E131 (= E111), E183 (≠ D171), D197 (≠ N185), F198 (≠ L186), K199 (≠ H187), Y200 (≠ H188), N246 (≠ H235), V247 (≠ I236), S248 (= S237), R320 (= R308), S328 (≠ A316), R330 (= R318)
- binding magnesium ion: E131 (= E111), E131 (= E111), E133 (= E113), E188 (= E176), E195 (= E183), E195 (= E183), H244 (= H233), E332 (= E320)
- binding l-methionine-s-sulfoximine phosphate: E131 (= E111), E133 (= E113), E188 (= E176), E195 (= E183), G240 (= G229), H244 (= H233), R297 (= R285), E303 (≠ Y291), R315 (= R303)
7cquA Gmas/adp/metsox-p complex (see paper)
33% identity, 86% coverage: 22:383/423 of query aligns to 31:391/429 of 7cquA
- binding adenosine-5'-diphosphate: E121 (= E111), Y173 (≠ D171), N187 (= N185), W188 (≠ L186), D189 (≠ H187), Y190 (≠ H188), H236 (= H235), L237 (≠ I236), S238 (= S237), R316 (= R308), R322 (= R318)
- binding magnesium ion: E121 (= E111), E121 (= E111), E123 (= E113), E178 (= E176), E185 (= E183), E185 (= E183), H234 (= H233), E324 (= E320)
- binding l-methionine-s-sulfoximine phosphate: E121 (= E111), E123 (= E113), E178 (= E176), E185 (= E183), T229 (≠ A228), G230 (= G229), H234 (= H233), R287 (= R285), W299 (vs. gap), R311 (= R303), R326 (= R322)
Query Sequence
>Pf6N2E2_4509 FitnessBrowser__pseudo6_N2E2:Pf6N2E2_4509
VVRGKRIERTSLHKVYEKGINLPASLFALDINGSTVESTGLGLDIGDADRICYPIPDTLC
NEPWQKRPTAQLLMTMHELEGEPFFADPREVLRQVVTKFDELGLTICAAFELEFYLIDQE
NVNGRPQPPRSPISGKRPHSTQVYLIDDLDEYVDCLQDILEGAKEQGIPADAIVKESAPA
QFEVNLHHVADPIKACDYAVLLKRLIKNIAYDHEMDTTFMAKPYPGQAGNGLHVHISILD
KDGKNIFASEDPEQNAALRHAIGGVLETLPAQMAFLCPNVNSYRRFGAQFYVPNSPTWGL
DNRTVALRVPTGSADAVRLEHRVAGADANPYLLMASVLAGVHHGLVNKIEPGAPVEGNSY
EQNEQSLPNNLRDALRELDDSEVMAKYIDPKYIDIFVACKESELEEFEHSISDLEYNWYL
HTV
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