SitesBLAST

P0A1P6 Glutamine synthetase; GS; Glutamate--ammonia ligase; Glutamine synthetase I beta; GSI beta; EC 6.3.1.2 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) (see 4 papers)
34% identity, 16% coverage: 246:355/697 of query aligns to 195:304/469 of P0A1P6

query
sites
P0A1P6

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E208 (≠ K259) binding ATP
E213 (= E264) binding Mn(2+)
E221 (= E271) binding Mn(2+)
NG 265:266 (= NG 315:316) binding L-glutamate
H270 (= H320) binding Mn(2+)
HMS 272:274 (≠ NWS 322:324) binding ATP

Sites not aligning to the query:

130 binding Mn(2+)
132 binding Mn(2+)
322 binding L-glutamate
358 binding Mn(2+)
360 binding L-glutamate

2lgsA Feedback inhibition of fully unadenylylated glutamine synthetase from salmonella typhimurium by glycine, alanine, and serine (see paper)
34% identity, 16% coverage: 246:355/697 of query aligns to 188:297/445 of 2lgsA

query
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2lgsA

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binding glutamic acid: N258 (= N315), G259 (= G316), G261 (= G318), H263 (= H320)
binding manganese (ii) ion: E206 (= E264), E214 (= E271), H263 (= H320)

Sites not aligning to the query:

1lgrA Interactions of nucleotides with fully unadenylylated glutamine synthetase from salmonella typhimurium (see paper)
34% identity, 16% coverage: 246:355/697 of query aligns to 188:297/445 of 1lgrA

query
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1lgrA

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binding adenosine monophosphate: E201 (≠ K259), T217 (≠ P274), F219 (= F276), H265 (≠ N322), S267 (= S324)
binding manganese (ii) ion: E206 (= E264), E214 (= E271), H263 (= H320)

Sites not aligning to the query:

1fpyA Crystal structure of glutamine synthetase from salmonella typhimurium with inhibitor phosphinothricin (see paper)
34% identity, 16% coverage: 246:355/697 of query aligns to 194:303/468 of 1fpyA

query
sites
1fpyA

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binding adenosine-5'-diphosphate: E207 (≠ K259), T223 (≠ P274), F225 (= F276), H271 (≠ N322), S273 (= S324)
binding manganese (ii) ion: E212 (= E264), E220 (= E271), H269 (= H320)
binding phosphinothricin: E212 (= E264), G265 (= G316), H269 (= H320)

Sites not aligning to the query:

binding adenosine-5'-diphosphate: 127, 129, 355, 357
binding manganese (ii) ion: 129, 131, 357
binding phosphinothricin: 131, 321, 327, 359

1f1hA Crystal structure of glutamine synthetase from salmonella typhimurium with thallium ions (see paper)
34% identity, 16% coverage: 246:355/697 of query aligns to 194:303/468 of 1f1hA

query
sites
1f1hA

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binding adenosine-5'-diphosphate: E207 (≠ K259), H210 (= H262), E220 (= E271), T223 (≠ P274), F225 (= F276), H271 (≠ N322), S273 (= S324)
binding manganese (ii) ion: E212 (= E264), E220 (= E271), H269 (= H320)

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)
36% identity, 13% coverage: 245:332/697 of query aligns to 170:256/444 of P12425

query
sites
P12425

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E189 (= E264) binding Mg(2+)
V190 (≠ A265) 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 (= E271) binding Mg(2+)
G241 (= G316) binding L-glutamate
H245 (= H320) binding Mg(2+)

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.
132 binding Mg(2+)
134 binding Mg(2+)
302 G→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.
304 E→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.
306 P→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.
333 binding Mg(2+)
424 E→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.

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)
36% identity, 13% coverage: 245:332/697 of query aligns to 169:255/443 of 4lnkA

query
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4lnkA

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active site: E188 (= E264), E195 (= E271), H244 (= H320)
binding adenosine-5'-diphosphate: F198 (≠ P274), Y200 (≠ F276), N246 (= N322), S248 (= S324)
binding glutamic acid: E188 (= E264), V189 (≠ A265), N239 (= N315), G240 (= G316), G242 (= G318)
binding magnesium ion: E188 (= E264), E195 (= E271), H244 (= H320)

Sites not aligning to the query:

active site: 52, 131, 133, 315, 332, 334
binding adenosine-5'-diphosphate: 43, 50, 324, 328, 330
binding glutamic acid: 133, 303
binding magnesium ion: 131, 332

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)
36% identity, 13% coverage: 245:332/697 of query aligns to 169:255/443 of 4lniA

query
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4lniA

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active site: E188 (= E264), E195 (= E271), H244 (= H320)
binding adenosine-5'-diphosphate: E183 (≠ K259), D197 (≠ A273), Y200 (≠ F276), N246 (= N322), S248 (= S324)
binding magnesium ion: E188 (= E264), E195 (= E271), E195 (= E271), H244 (= H320)
binding l-methionine-s-sulfoximine phosphate: E188 (= E264), H244 (= H320)

Sites not aligning to the query:

active site: 52, 131, 133, 315, 332, 334
binding adenosine-5'-diphosphate: 131, 320, 330
binding magnesium ion: 131, 131, 133, 332
binding l-methionine-s-sulfoximine phosphate: 133, 297, 303, 315, 334

4s0rD Structure of gs-tnra complex (see paper)
36% identity, 13% coverage: 245:332/697 of query aligns to 173:259/447 of 4s0rD

query
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4s0rD

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active site: E192 (= E264), E199 (= E271), H248 (= H320)
binding glutamine: E192 (= E264)
binding magnesium ion: E199 (= E271), H248 (= H320), H248 (= H320)
binding : G241 (= G313), V242 (= V314), N243 (= N315)

Sites not aligning to the query:

active site: 56, 135, 137, 319, 336, 338
binding glutamine: 137, 301, 307
binding magnesium ion: 66, 135, 135, 336, 419
binding : 63, 64, 65, 66, 161, 305, 306, 376, 426, 430

7tdvC Glutamine synthetase (see paper)
36% identity, 12% coverage: 245:325/697 of query aligns to 169:249/443 of 7tdvC

query
sites
7tdvC

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N

V

I

L

E

E

L

L

W

E

K

D

L

M

G

G

V

F

L

D

A

I

K
x
E

T

A

Q

S

H

H

K

H

E
|
E

A

V

A

A

P

P

G

G

Q

Q

Y

H

E
|
E

I

I

A
x
D

P
x
F

I
x
K

F
x
Y

T

A

S

D

T

A

N

V

I

T

A

A

T

C

D

D

H

N

N

I

Q

Q

I

T

I

F

M

K

D

L

T

V

L

V

H

K

K

T

V

I

A

A

N

R

R

K

H

H

G

N

L

L

A

H

C

A

L

T

L

F

H

M

E

P

K

K

P

P

F

L

A

F

G

G

V

V

N

N

G
|
G

S

S

G

G

K

M

H
|
H

N

F

N
|
N

W
x
V

S
|
S

L

L

binding adenosine-5'-diphosphate: E183 (≠ K259), D197 (≠ A273), F198 (≠ P274), K199 (≠ I275), Y200 (≠ F276), N246 (= N322), V247 (≠ W323), S248 (= S324)
binding magnesium ion: E188 (= E264), E195 (= E271), E195 (= E271), H244 (= H320)
binding l-methionine-s-sulfoximine phosphate: E188 (= E264), E195 (= E271), G240 (= G316), H244 (= H320)

Sites not aligning to the query:

binding adenosine-5'-diphosphate: 129, 131, 320, 328, 330
binding magnesium ion: 131, 131, 133, 332
binding l-methionine-s-sulfoximine phosphate: 131, 133, 297, 303, 315

7tf6A Glutamine synthetase (see paper)
36% identity, 12% coverage: 245:325/697 of query aligns to 164:244/438 of 7tf6A

query
sites
7tf6A

Q

R

E

D

V

I

N

V

I

L

E

E

L

L

W

E

K

D

L

M

G

G

V

F

L

D

A

I

K

E

T

A

Q

S

H

H

K

H

E
|
E

A

V

A

A

P

P

G

G

Q

Q

Y

H

E
|
E

I

I

A

D

P

F

I

K

F

Y

T

A

S

D

T

A

N

V

I

T

A

A

T

C

D

D

H

N

N

I

Q

Q

I

T

I

F

M

K

D

L

T

V

L

V

H

K

K

T

V

I

A

A

N

R

R

K

H

H

G

N

L

L

A

H

C

A

L

T

L

F

H

M

E

P

K

K

P

P

F

L

A

F

G
|
G

V

V

N
|
N

G
|
G

S

S

G

G

K

M

H
|
H

N

F

N

N

W

V

S

S

L

L

binding glutamine: E183 (= E264), G235 (= G316), H239 (= H320)
binding magnesium ion: E183 (= E264), E190 (= E271), H239 (= H320)
binding : G232 (= G313), N234 (= N315)

Sites not aligning to the query:

binding glutamine: 128, 292, 298
binding magnesium ion: 126, 128, 327
binding : 58, 60, 296, 297, 310, 367, 421, 433, 437

8oooA Glutamine synthetase from methanothermococcus thermolithotrophicus in complex with 2-oxoglutarate and mgatp at 2.15 a resolution (see paper)
27% identity, 20% coverage: 190:325/697 of query aligns to 133:254/447 of 8oooA

query
sites
8oooA

V

V

G

G

A

P

E
|
E

Q

P

E

E

Y

F

F

F

L

L

I

L

E

K

K

K

K

D

Y

P

H

H

Q

N

K

P

R

H

L

K

D

Y

L

I

M

P

L

A

T

D

G

D

R

G

T

G

L

Y

F

F

G

D

V

L

L

E

P

P

P

-

K

-

G

-

Q

-

E

-

M

-

E

-

D

-

H

-

Y

-

F

-

G

-

I

-

N

M

E

D

R

E

V

A

T
x
P

A

D

F

I

M
x
R

Q
x
R

E

D

V

I

N

V

I

F

E

A

L

L

W

E

K

N

L

L

G

G

V

F

L

H

A

V

K
x
E

T

A

Q
x
S

H

H

K

H

E

E

A

V

A

A

P

P

G

G

Q

Q

Y

H

E

E

I

V

A

D

P
x
F

I
x
K

F
|
F

T

D

S

D

T

A

N

L

I

K

A

T

T

A

D

D

H

S

N

V

Q

I

I

T

I

F

M

K

D

T

T

T

L

I

H

K

K

T

V

I

A

A

N

E

R

Q

H

H

G

G

L

L

A

K

C

A

L

T

L

F

H

M

E

P

K

K

P

P

F

F

A

F

G

G

V

M

N

N

G

G

S

S

G

G

K

M

H

H

N

C

N
x
H

W

Q

S
|
S

L

I

binding 2-oxoglutaric acid: P170 (≠ T241), R173 (≠ M244), R174 (≠ Q245), S190 (≠ Q261)
binding adenosine-5'-triphosphate: E136 (= E193), E188 (≠ K259), F203 (≠ P274), K204 (≠ I275), F205 (= F276), H251 (≠ N322), S253 (= S324)

Sites not aligning to the query:

8ooqB Glutamine synthetase from Methanothermococcus thermolithotrophicus (see paper)
27% identity, 20% coverage: 190:325/697 of query aligns to 132:253/446 of 8ooqB

query
sites
8ooqB

V

V

G

G

A

P

E

E

Q

P

E
|
E

Y

F

F

F

L

L

I

L

E

K

K

K

K

D

Y

P

H

H

Q

N

K

P

R

H

L

K

D

Y

L

I

M

P

L

A

T

D

G

D

R

G

T

G

L

Y

F

F

G

D

V

L

L

E

P

P

P

-

K

-

G

-

Q

-

E

-

M

-

E

-

D

-

H

-

Y

-

F

-

G

-

I

-

N

M

E

D

R

E

V

A

T
x
P

A

D

F

I

M
x
R

Q
x
R

E

D

V

I

N

V

I

F

E

A

L

L

W

E

K

N

L

L

G

G

V

F

L

H

A

V

K

E

T

A

Q
x
S

H

H

K

H

E
|
E

A

V

A

A

P

P

G

G

Q

Q

Y

H

E
|
E

I

V

A

D

P

F

I

K

F

F

T

D

S

D

T

A

N

L

I

K

A

T

T

A

D

D

H

S

N

V

Q

I

I

T

I

F

M

K

D

T

T

T

L

I

H

K

K

T

V

I

A

A

N

E

R

Q

H

H

G

G

L

L

A

K

C

A

L

T

L

F

H

M

E

P

K

K

P

P

F

F

A

F

G

G

V

M

N

N

G

G

S

S

G

G

K

M

H

H

N

C

N

H

W

Q

S

S

L

I

binding 2-oxoglutaric acid: P169 (≠ T241), R172 (≠ M244), R173 (≠ Q245), S189 (≠ Q261)
binding magnesium ion: E137 (= E195), E192 (= E264), E199 (= E271)

Sites not aligning to the query:

binding 2-oxoglutaric acid: 16, 18, 32, 86, 92

8tfkA Glutamine synthetase (see paper)
28% identity, 18% coverage: 238:360/697 of query aligns to 159:281/440 of 8tfkA

query
sites
8tfkA

E

D

R

R

V

A

T

Q

A

D

F

V

M

R

Q

R

E

D

V

I

N

D

I

Y

E

A

L

L

W

E

K

H

L

M

G

G

V

F

L

Q

A

I

K

E

T

A

Q

S

H

H

K

H

E
|
E

A

V

A

A

P

P

G

S

Q

Q

Y

H

E
|
E

I

I

A
x
D

P
x
F

I

R

F
|
F

T

G

S

D

T

V

N

L

I

C

A

T

T

A

D

D

H

N

N

V

Q

V

I

T

I

F

M

K

D

Y

T

V

L

V

H

K

K

S

V

I

A

A

N

Y

R

H

H

K

G

G

L

Y

A

Y

C

A

L

S

L

F

H

M

E

P

K

K

P

P

F

L

A

F

G

G

V

V

N

N

G
|
G

S

S

G

G

K

M

H
|
H

N

S

N
|
N

W

Q

S

S

L

L

S

F

T

K

D

D

E

-

G

G

V

K

N

N

L

V

L

F

E

Y

P

D

G

P

K

D

T

T

P

P

H

T

E

K

N

L

A

S

Q

Q

-

D

F

A

L

M

T

Y

F

Y

I

I

C

G

A

G

V

L

I

L

K

K

A

H

V

I

D

R

E

E

Y

F

binding adenosine-5'-diphosphate: D194 (≠ A273), F195 (≠ P274), F197 (= F276), N243 (= N322)
binding magnesium ion: E185 (= E264), E192 (= E271), E192 (= E271), H241 (= H320)
binding l-methionine-s-sulfoximine phosphate: E185 (= E264), E192 (= E271), G237 (= G316), H241 (= H320)

Sites not aligning to the query:

binding adenosine-5'-diphosphate: 128, 312, 317, 325, 327
binding magnesium ion: 128, 128, 130, 329
binding l-methionine-s-sulfoximine phosphate: 128, 130, 294, 300, 312, 331

Query Sequence

>WP_005812354.1 NCBI__GCF_000021925.1:WP_005812354.1
MDFFGKNVFNDAVMRERLPKNTYKALHKTIDEGLPLQLEVAEVVANAMKDWAIENGATHY
THWFQPMTGFTAEKHDSFISPTSDGKVIMEFSGKELIKGEPDASSFPNGGIRSTFEARGY
TAWDCTSPAFLREDAGKVILCIPTAFCSYTGEALDKKTPLLRSMETISKQALRILRLFGN
TTAKRVTPTVGAEQEYFLIEKKYHQKRLDLMLTGRTLFGVLPPKGQEMEDHYFGIINERV
TAFMQEVNIELWKLGVLAKTQHKEAAPGQYEIAPIFTSTNIATDHNQIIMDTLHKVANRH
GLACLLHEKPFAGVNGSGKHNNWSLSTDEGVNLLEPGKTPHENAQFLTFICAVIKAVDEY
ADLLRASAANSGNDHRLGANEAPPAIISIFLGDELSDIIEQLKNGKPNSSKQGGELTIGV
STLPSLPKDSTDRNRTSPFAFTGNKFEFRMVPSSLSIAGPNVVINTIVAEVLSQMADRLE
KAEDFHGELQAILQEIAIHHSRVVFDGNGYSEEWVKEAARRGLPNLSSTVEAISALISEK
TIELFKHHGVFSATELHSRYEIYLEQYSKTINIEALTMVDVAKRQILPAVMRYSTELAHS
INTIRTADPEAEVLAQRSLLNEISPLLKELSFKTKALQDATCAAKQLHGDAYKQGIYYRD
VVFKAMNELRQTADQLEVLVDYDMWPLPSYTKMLFRL

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