SitesBLAST
Comparing 3608834 Dshi_2226 Glutamate--putrescine ligase (RefSeq) 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)
36% identity, 98% coverage: 7:455/456 of query aligns to 17:471/472 of P78061
- H282 (= H266) mutation to N: Activity is impaired to 9% of wild-type.
- R357 (= R342) mutation to Q: Activity is impaired to 3% of wild-type.
8oooA Glutamine synthetase from methanothermococcus thermolithotrophicus in complex with 2-oxoglutarate and mgatp at 2.15 a resolution (see paper)
30% identity, 96% coverage: 12:448/456 of query aligns to 1:440/447 of 8oooA
- binding 2-oxoglutaric acid: F17 (≠ E28), R19 (≠ E30), A33 (= A44), R87 (vs. gap), V93 (≠ T103), P170 (≠ G187), R173 (≠ I190), R174 (≠ D191), S190 (≠ I207)
- binding adenosine-5'-triphosphate: E136 (= E145), E188 (≠ D205), F203 (≠ L220), K204 (≠ R221), F205 (≠ H222), H251 (= H268), S253 (= S270), R325 (= R342), R335 (= R352)
8ooqB Glutamine synthetase from Methanothermococcus thermolithotrophicus (see paper)
30% identity, 95% coverage: 15:448/456 of query aligns to 3:439/446 of 8ooqB
- binding 2-oxoglutaric acid: F16 (≠ E28), R18 (≠ E30), A32 (= A44), R86 (vs. gap), V92 (≠ T103), P169 (≠ G187), R172 (≠ I190), R173 (≠ D191), S189 (≠ I207)
- binding magnesium ion: E137 (= E147), E192 (= E210), E199 (= E217)
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)
32% identity, 84% coverage: 70:453/456 of query aligns to 50:444/446 of A0R083
- K363 (≠ A381) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
8ooxB Glutamine synthetase (see paper)
28% identity, 95% coverage: 21:453/456 of query aligns to 10:435/438 of 8ooxB
8oozA Glutamine synthetase (see paper)
28% identity, 95% coverage: 21:453/456 of query aligns to 10:427/430 of 8oozA
- binding adenosine-5'-triphosphate: G117 (≠ A143), E170 (≠ D205), F185 (≠ L220), K186 (≠ R221), Y187 (≠ H222), N233 (≠ H268), S235 (= S270), S315 (≠ A350), R317 (= R352)
- binding magnesium ion: E119 (= E145), H231 (= H266), E319 (= E354)
8tfkA Glutamine synthetase (see paper)
29% identity, 94% coverage: 24:453/456 of query aligns to 13:437/440 of 8tfkA
- binding adenosine-5'-diphosphate: E128 (= E145), D194 (≠ N219), F195 (≠ L220), F197 (≠ H222), N243 (≠ H268), R312 (= R337), R317 (= R342), G325 (≠ A350), R327 (= R352)
- binding magnesium ion: E128 (= E145), E128 (= E145), E130 (= E147), E185 (= E210), E192 (= E217), E192 (= E217), H241 (= H266), E329 (= E354)
- binding l-methionine-s-sulfoximine phosphate: E128 (= E145), E130 (= E147), E185 (= E210), E192 (= E217), G237 (= G262), H241 (= H266), R294 (= R319), E300 (≠ A325), R312 (= R337), R331 (= R356)
8ufjB Glutamine synthetase (see paper)
29% identity, 94% coverage: 24:453/456 of query aligns to 17:441/444 of 8ufjB
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, 84% coverage: 70:454/456 of query aligns to 50:446/446 of P9WN37
- K363 (≠ A381) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
5dm3C Crystal structure of glutamine synthetase from chromohalobacter salexigens dsm 3043(csal_0679, target efi-550015) with bound adp
28% identity, 95% coverage: 18:448/456 of query aligns to 6:390/396 of 5dm3C
- active site: E115 (= E145), E117 (= E147), E162 (= E210), E169 (= E217), H218 (= H266), R286 (= R337), E303 (= E354), R305 (= R356)
- binding adenosine-5'-diphosphate: R173 (= R221), C174 (≠ H222), H220 (= H268), S222 (= S270), R301 (= R352)
7tfaB Glutamine synthetase (see paper)
28% identity, 92% coverage: 34:453/456 of query aligns to 24:438/441 of 7tfaB
- binding glutamine: E131 (= E147), Y153 (≠ A177), E186 (= E210), G238 (= G262), H242 (= H266), R295 (= R319), E301 (≠ A325)
- binding magnesium ion: E129 (= E145), E131 (= E147), E186 (= E210), E193 (= E217), H242 (= H266), E330 (= E354)
- binding : Y58 (≠ F79), R60 (vs. gap), V187 (≠ G211), N237 (≠ P261), G299 (≠ E323), Y300 (≠ N324), R313 (= R337), M424 (≠ E439)
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, 92% coverage: 34:453/456 of query aligns to 25:440/443 of 4lnkA
- active site: D52 (≠ Q65), E131 (= E145), E133 (= E147), E188 (= E210), E195 (= E217), H244 (= H266), R315 (= R337), E332 (= E354), R334 (= R356)
- binding adenosine-5'-diphosphate: K43 (≠ R52), M50 (≠ F63), F198 (≠ L220), Y200 (≠ H222), N246 (≠ H268), S248 (= S270), S324 (≠ A346), S328 (≠ A350), R330 (= R352)
- binding glutamic acid: E133 (= E147), E188 (= E210), V189 (≠ G211), N239 (≠ P261), G240 (= G262), G242 (≠ A264), E303 (≠ A325)
- binding magnesium ion: E131 (= E145), E188 (= E210), E195 (= E217), H244 (= H266), E332 (= E354)
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, 92% coverage: 34:453/456 of query aligns to 25:440/443 of 4lniA
- active site: D52 (≠ Q65), E131 (= E145), E133 (= E147), E188 (= E210), E195 (= E217), H244 (= H266), R315 (= R337), E332 (= E354), R334 (= R356)
- binding adenosine-5'-diphosphate: E131 (= E145), E183 (≠ D205), D197 (≠ N219), Y200 (≠ H222), N246 (≠ H268), S248 (= S270), R320 (= R342), R330 (= R352)
- binding magnesium ion: E131 (= E145), E131 (= E145), E133 (= E147), E188 (= E210), E195 (= E217), E195 (= E217), H244 (= H266), E332 (= E354)
- binding l-methionine-s-sulfoximine phosphate: E133 (= E147), E188 (= E210), H244 (= H266), R297 (= R319), E303 (≠ A325), R315 (= R337), R334 (= R356)
4s0rD Structure of gs-tnra complex (see paper)
28% identity, 92% coverage: 34:453/456 of query aligns to 29:444/447 of 4s0rD
- active site: D56 (≠ Q65), E135 (= E145), E137 (= E147), E192 (= E210), E199 (= E217), H248 (= H266), R319 (= R337), E336 (= E354), R338 (= R356)
- binding glutamine: E137 (= E147), E192 (= E210), R301 (= R319), E307 (≠ A325)
- binding magnesium ion: I66 (vs. gap), E135 (= E145), E135 (= E145), E199 (= E217), H248 (= H266), H248 (= H266), E336 (= E354), H419 (≠ V428)
- binding : F63 (= F79), V64 (≠ T80), R65 (vs. gap), I66 (vs. gap), D161 (≠ S179), G241 (≠ D259), V242 (≠ E260), N243 (≠ P261), G305 (≠ E323), Y306 (≠ N324), Y376 (= Y389), I426 (≠ H435), M430 (≠ E439)
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, 92% coverage: 34:453/456 of query aligns to 26:441/444 of P12425
- G59 (= G78) 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 (vs. gap) 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 (= E145) binding
- E134 (= E147) binding
- E189 (= E210) binding
- V190 (≠ G211) 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 (= E217) binding
- G241 (= G262) binding
- H245 (= H266) binding
- G302 (≠ E323) 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 (≠ A325) 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 (= P327) 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 (= E354) binding
- E424 (= E436) 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
7tdpA Structure of paenibacillus polymyxa gs bound to met-sox-p-adp (transition state complex) to 1.98 angstom (see paper)
28% identity, 92% coverage: 34:453/456 of query aligns to 24:436/439 of 7tdpA
- binding adenosine-5'-diphosphate: N123 (vs. gap), G125 (≠ A143), E127 (= E145), E179 (≠ D205), D193 (≠ N219), Y196 (≠ H222), N242 (≠ H268), S244 (= S270), R316 (= R342), R326 (= R352)
- binding magnesium ion: E127 (= E145), E127 (= E145), E129 (= E147), E184 (= E210), E191 (= E217), E191 (= E217), H240 (= H266), E328 (= E354)
- binding l-methionine-s-sulfoximine phosphate: E127 (= E145), E129 (= E147), E184 (= E210), E191 (= E217), G236 (= G262), H240 (= H266), R293 (= R319), E299 (≠ A325), R311 (= R337), R330 (= R356)
7tenA Glutamine synthetase (see paper)
28% identity, 92% coverage: 34:453/456 of query aligns to 24:439/442 of 7tenA
- binding adenosine-5'-diphosphate: G128 (≠ A143), E130 (= E145), E182 (≠ D205), D196 (≠ N219), F197 (≠ L220), K198 (≠ R221), Y199 (≠ H222), N245 (≠ H268), S247 (= S270), R319 (= R342), S327 (≠ A350), R329 (= R352)
- binding l-methionine-s-sulfoximine phosphate: E130 (= E145), E132 (= E147), E187 (= E210), E194 (= E217), N238 (≠ P261), G239 (= G262), H243 (= H266), R296 (= R319), E302 (≠ A325), R314 (= R337), R333 (= R356)
7tf9S L. Monocytogenes gs(14)-q-glnr peptide (see paper)
28% identity, 92% coverage: 34:453/456 of query aligns to 25:440/443 of 7tf9S
- binding glutamine: E133 (= E147), Y155 (≠ A177), E188 (= E210), G240 (= G262), G242 (≠ A264), R297 (= R319), E303 (≠ A325)
- binding magnesium ion: E131 (= E145), E133 (= E147), E188 (= E210), E195 (= E217), H244 (= H266), E332 (= E354)
- binding : F59 (= F79), V60 (≠ T80), E418 (≠ I431), I422 (≠ H435), M426 (≠ E439)
8wwvA Glutamine synthetase
29% identity, 93% coverage: 19:441/456 of query aligns to 22:464/490 of 8wwvA
- binding adenosine-5'-diphosphate: G155 (≠ A143), E157 (= E145), R224 (vs. gap), F239 (≠ L220), D240 (≠ R221), V241 (≠ H222), H288 (= H268), S290 (= S270), R374 (= R352), E376 (= E354)
- binding magnesium ion: E157 (= E145), E236 (= E217)
- binding manganese (ii) ion: E157 (= E145), E159 (= E147), E229 (= E210), E236 (= E217), H286 (= H266), E376 (= E354)
- binding l-methionine-s-sulfoximine phosphate: E157 (= E145), E159 (= E147), E229 (= E210), E236 (= E217), A282 (≠ G262), H286 (= H266), R340 (= R319), K358 (≠ R337)
8wwuB Glutamine synthetase
29% identity, 93% coverage: 19:441/456 of query aligns to 24:466/492 of 8wwuB
- binding phosphoaminophosphonic acid-adenylate ester: G157 (≠ A143), E159 (= E145), R226 (vs. gap), F241 (≠ L220), V243 (≠ H222), H290 (= H268), S292 (= S270), K360 (≠ R337), R365 (= R342), R376 (= R352)
- binding magnesium ion: E159 (= E145), E238 (= E217)
- binding manganese (ii) ion: E159 (= E145), E161 (= E147), E231 (= E210), E238 (= E217), H288 (= H266), E378 (= E354)
Query Sequence
>3608834 Dshi_2226 Glutamate--putrescine ligase (RefSeq)
MAETPLERMLASVPEPARAYLEGRRLDEVECIVADLAGVARGKAMPAAKFARQMSFYLPN
SIFFQTITGGWAEAALDGFTEPDMVLKPDFSTATPAPWTADWTLQIIHDIEDQSGAPMPV
APRNVLKRVIALYKARGWKPVVAPEMEFYLTARNIDPAIAIQPPMGRTGRRAAARQAYSM
SAVDEYGPVIDDIYDFAEAQGLEIDGITQEGGAGQIEINLRHGDPLKLADEVFYFKRLIR
EAALRHDCFATFMAKPIQDEPGSAMHIHHSVTDIATGENIFTAPDGTETPAFQHFIAGLQ
SHLGDVVPLYAPYVNSYRRYVPENAAPINLEWARDNRTAGLRVPVANPAARRVENRLAGM
DCNPYLGIAASLACGYLGLLAEKPPKPQYVGDAYSGSEDLAPELGAALDLFSEATAVHDI
LGPEFCRVYEIVKRHEYTEFLQVISPWEREHLLLNV
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