SitesBLAST

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)
38% identity, 12% coverage: 268:354/730 of query aligns to 170:255/443 of 4lnkA

query
sites
4lnkA

D

D

F

I

E

V

K

L

E

E

A

L

Y

E

R

E

L

M

G

G

V

F

P

E

V

I

K

E

T

A

R

S

H

H

N

H

E
|
E

V
|
V

A

A

P

P

N

G

Q

Q

F

H

E
|
E

V

I

A

D

P
x
F

I

K

F
x
Y

E

A

E

G

A

A

N

V

L

R

A

S

N

C

D

D

H

D

N

I

Q

Q

M

T

V

F

M

K

D

L

L

V

M

V

K

K

R

T

V

I

A

A

R

R

R

K

H

H

K

G

F

L

R

H

V

A

L

T

F

F

H

M

E

P

K

K

P

P

F

L

K

F

G

G

I

V

N
|
N

G
|
G

S

S

G
|
G

K

M

H
|
H

S

C

N
|
N

W

L

S
|
S

L

L

S

F

T

K

N

N

T

-

G

G

V

V

N

N

active site: E188 (= E286), E195 (= E293), H244 (= H342)
binding adenosine-5'-diphosphate: F198 (≠ P296), Y200 (≠ F298), N246 (= N344), S248 (= S346)
binding glutamic acid: E188 (= E286), V189 (= V287), N239 (= N337), G240 (= G338), G242 (= G340)
binding magnesium ion: E188 (= E286), E195 (= E293), H244 (= H342)

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)
38% identity, 12% coverage: 268:354/730 of query aligns to 170:255/443 of 4lniA

query
sites
4lniA

D

D

F

I

E

V

K

L

E

E

A

L

Y

E

R

E

L

M

G

G

V

F

P

E

V

I

K
x
E

T

A

R

S

H

H

N

H

E
|
E

V

V

A

A

P

P

N

G

Q

Q

F

H

E
|
E

V

I

A
x
D

P

F

I

K

F
x
Y

E

A

E

G

A

A

N

V

L

R

A

S

N

C

D

D

H

D

N

I

Q

Q

M

T

V

F

M

K

D

L

L

V

M

V

K

K

R

T

V

I

A

A

R

R

R

K

H

H

K

G

F

L

R

H

V

A

L

T

F

F

H

M

E

P

K

K

P

P

F

L

K

F

G

G

I

V

N

N

G

G

S

S

G

G

K

M

H
|
H

S

C

N
|
N

W

L

S
|
S

L

L

S

F

T

K

N

N

T

-

G

G

V

V

N

N

active site: E188 (= E286), E195 (= E293), H244 (= H342)
binding adenosine-5'-diphosphate: E183 (≠ K281), D197 (≠ A295), Y200 (≠ F298), N246 (= N344), S248 (= S346)
binding magnesium ion: E188 (= E286), E195 (= E293), E195 (= E293), H244 (= H342)
binding l-methionine-s-sulfoximine phosphate: E188 (= E286), H244 (= H342)

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

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)
38% identity, 12% coverage: 268:354/730 of query aligns to 171:256/444 of P12425

query
sites
P12425

D

D

F

I

E

V

K

L

E

E

A

L

Y

E

R

E

L

M

G

G

V

F

P

E

V

I

K

E

T

A

R

S

H

H

N

H

E
|
E

V
|
V

A

A

P

P

N

G

Q

Q

F

H

E
|
E

V

I

A

D

P

F

I

K

F

Y

E

A

E

G

A

A

N

V

L

R

A

S

N

C

D

D

H

D

N

I

Q

Q

M

T

V

F

M

K

D

L

L

V

M

V

K

K

R

T

V

I

A

A

R

R

R

K

H

H

K

G

F

L

R

H

V

A

L

T

F

F

H

M

E

P

K

K

P

P

F

L

K

F

G

G

I

V

N

N

G
|
G

S

S

G

G

K

M

H
|
H

S

C

N

N

W

L

S

S

L

L

S

F

T

K

N

N

T

-

G

G

V

V

N

N

E189 (= E286) binding Mg(2+)
V190 (= V287) 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 (= E293) binding Mg(2+)
G241 (= G338) binding L-glutamate
H245 (= H342) 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.

7tfaB Glutamine synthetase (see paper)
39% identity, 10% coverage: 276:347/730 of query aligns to 176:247/441 of 7tfaB

query
sites
7tfaB

L

M

G

G

V

F

P

E

V

I

K

E

T

A

R

S

H

H

N

H

E
|
E

V
|
V

A

A

P

P

N

G

Q

Q

F

H

E
|
E

V

I

A

D

P

F

I

K

F

Y

E

A

E

D

A

A

N

V

L

K

A

A

N

A

D

D

H

Q

N

I

Q

Q

M

T

V

F

M

K

D

L

L

V

M

V

K

K

R

T

V

I

A

A

R

R

R

Q

H

H

K

G

F

L

R

H

V

A

L

T

F

F

H

M

E

P

K

K

P

P

F

L

K

F

G

G

I

V

N
|
N

G
|
G

S

S

G

G

K

M

H
|
H

S

C

N

N

W

Q

S

S

L

L

binding glutamine: E186 (= E286), G238 (= G338), H242 (= H342)
binding magnesium ion: E186 (= E286), E193 (= E293), H242 (= H342)
binding : V187 (= V287), N237 (= N337)

Sites not aligning to the query:

7tdpA Structure of paenibacillus polymyxa gs bound to met-sox-p-adp (transition state complex) to 1.98 angstom (see paper)
39% identity, 10% coverage: 276:347/730 of query aligns to 174:245/439 of 7tdpA

query
sites
7tdpA

L

M

G

G

V

F

P

E

V

I

K
x
E

T

A

R

S

H

H

N

H

E
|
E

V

V

A

A

P

P

N

G

Q

Q

F

H

E
|
E

V

I

A
x
D

P

F

I

K

F
x
Y

E

A

E

D

A

A

N

V

L

K

A

A

N

A

D

D

H

Q

N

I

Q

Q

M

T

V

F

M

K

D

L

L

V

M

V

K

K

R

T

V

I

A

A

R

R

R

Q

H

H

K

G

F

L

R

H

V

A

L

T

F

F

H

M

E

P

K

K

P

P

F

L

K

F

G

G

I

V

N

N

G
|
G

S

S

G

G

K

M

H
|
H

S

C

N
|
N

W

Q

S
|
S

L

L

binding adenosine-5'-diphosphate: E179 (≠ K281), D193 (≠ A295), Y196 (≠ F298), N242 (= N344), S244 (= S346)
binding magnesium ion: E184 (= E286), E191 (= E293), E191 (= E293), H240 (= H342)
binding l-methionine-s-sulfoximine phosphate: E184 (= E286), E191 (= E293), G236 (= G338), H240 (= H342)

Sites not aligning to the query:

binding adenosine-5'-diphosphate: 123, 125, 127, 316, 326
binding magnesium ion: 127, 127, 129, 328
binding l-methionine-s-sulfoximine phosphate: 127, 129, 293, 299, 311, 330

7tdvC Glutamine synthetase (see paper)
33% identity, 19% coverage: 211:347/730 of query aligns to 127:249/443 of 7tdvC

query
sites
7tdvC

N

N

L

L

G
|
G

W

P

E
|
E

Q

P

E
|
E

Y

F

F

F

L

L

-

F

-

K

V

L

D

D

E

E

A

-

L

-

F

-

N

K

A

G

R

E

P

P

D

T

L

L

V

E

L

L

T

N

G

D

R

-

T

-

L

-

M

-

G

-

H

-

S

-

A

-

K

-

D

-

Q

-

L

-

D

D

D

G

H

G

Y

Y

F

F

G

D

S

L

I

A

P

P

E

T

R

D

V

L

I

G

A

E

-

N

F

C

M

R

E

R

D

D

F

I

E

V

K

L

E

E

A

L

Y

E

R

D

L

M

G

G

V

F

P

D

V

I

K
x
E

T

A

R

S

H

H

N

H

E
|
E

V

V

A

A

P

P

N

G

Q

Q

F

H

E
|
E

V

I

A
x
D

P
x
F

I
x
K

F
x
Y

E

A

E

D

A

A

N

V

L

T

A

A

N

C

D

D

H

N

N

I

Q

Q

M

T

V

F

M

K

D

L

L

V

M

V

K

K

R

T

V

I

A

A

R

R

R

K

H

H

K

N

F

L

R

H

V

A

L

T

F

F

H

M

E

P

K

K

P

P

F

L

K

F

G

G

I

V

N

N

G
|
G

S

S

G

G

K

M

H
|
H

S

F

N
|
N

W
x
V

S
|
S

L

L

binding adenosine-5'-diphosphate: G129 (= G213), E131 (= E215), E183 (≠ K281), D197 (≠ A295), F198 (≠ P296), K199 (≠ I297), Y200 (≠ F298), N246 (= N344), V247 (≠ W345), S248 (= S346)
binding magnesium ion: E131 (= E215), E131 (= E215), E133 (= E217), E188 (= E286), E195 (= E293), E195 (= E293), H244 (= H342)
binding l-methionine-s-sulfoximine phosphate: E131 (= E215), E133 (= E217), E188 (= E286), E195 (= E293), G240 (= G338), H244 (= H342)

Sites not aligning to the query:

7tf6A Glutamine synthetase (see paper)
33% identity, 19% coverage: 211:347/730 of query aligns to 122:244/438 of 7tf6A

query
sites
7tf6A

N

N

L

L

G

G

W

P

E
|
E

Q

P

E
|
E

Y

F

F

F

L

L

-

F

-

K

V

L

D

D

E

E

A

-

L

-

F

-

N

K

A

G

R

E

P

P

D

T

L

L

V

E

L

L

T

N

G

D

R

-

T

-

L

-

M

-

G

-

H

-

S

-

A

-

K

-

D

-

Q

-

L

-

D

D

D

G

H

G

Y

Y

F

F

G

D

S

L

I

A

P

P

E

T

R

D

V

L

I

G

A

E

-

N

F

C

M

R

E

R

D

D

F

I

E

V

K

L

E

E

A

L

Y

E

R

D

L

M

G

G

V

F

P

D

V

I

K

E

T

A

R

S

H

H

N

H

E
|
E

V

V

A

A

P

P

N

G

Q

Q

F

H

E
|
E

V

I

A

D

P

F

I

K

F

Y

E

A

E

D

A

A

N

V

L

T

A

A

N

C

D

D

H

N

N

I

Q

Q

M

T

V

F

M

K

D

L

L

V

M

V

K

K

R

T

V

I

A

A

R

R

R

K

H

H

K

N

F

L

R

H

V

A

L

T

F

F

H

M

E

P

K

K

P

P

F

L

K

F

G
|
G

I

V

N
|
N

G
|
G

S

S

G

G

K

M

H
|
H

S

F

N

N

W

V

S

S

L

L

binding glutamine: E128 (= E217), E183 (= E286), G235 (= G338), H239 (= H342)
binding magnesium ion: E126 (= E215), E128 (= E217), E183 (= E286), E190 (= E293), H239 (= H342)
binding : G232 (= G335), N234 (= N337)

Sites not aligning to the query:

binding glutamine: 292, 298
binding magnesium ion: 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, 22% coverage: 276:435/730 of query aligns to 183:347/447 of 8oooA

query
sites
8oooA

L

L

G

G

V

F

P

H

V

V

K
x
E

T

A

R
x
S

H

H

N

H

E

E

V

V

A

A

P

P

N

G

Q

Q

F

H

E

E

V

V

A

D

P
x
F

I
x
K

F
|
F

E

D

A

A

N

L

L

K

A

T

N

A

D

D

H

S

N

V

Q

I

M

T

V

F

M

K

D

T

L

T

M

I

K

K

R

T

V

I

A

A

R

E

R

Q

H

H

K

G

F

L

R

K

V

A

L

T

F

F

H

M

E

P

K

K

P

P

F

F

K

F

G

G

I

M

N

N

G

G

S

S

G

G

K

M

H

H

S

C

N
x
H

W

Q

S
|
S

L

I

S

W

T

L

N

N

T

G

G

E

V

P

N

S

L

F

L

Y

S

D

P

E

G

N

K

A

N

P

P

Y

K

Q

T

L

N

S

L

E

Q

T

F

C

L

M

T

N

F

Y

L

V

V

A

N

G

V

I

L

L

K

K

A

-

V

-

Y

-

D

-

N

H

Q

A

D

K

I

A

L

I

L

V

A

A

S

I

I

T

M

N

T

P

A

T

S

V

N

N

S

S

H

Y

R

K

-

R

-

L

L

V

G

P

A

G

N

Y

E

E

A

A

P

P

P

V

S

N

I

I

L

-

S

-

V

A

F

W

L

A

G

N

S

S

Q

N

I

R

S

S

A

A

M

I

L

I

-
x
R

-

V

-

P

-

A

-

R

-

G

-

K

-

G

D

T

D
x
R

L

I

E

E

T

F

R

R

V

A

P

P

D

D

K

P

K

S

M

C

T

N

P

P

binding 2-oxoglutaric acid: S190 (≠ R283)
binding adenosine-5'-triphosphate: E188 (≠ K281), F203 (≠ P296), K204 (≠ I297), F205 (= F298), H251 (≠ N344), S253 (= S346), R325 (vs. gap), R335 (≠ D423)

Sites not aligning to the query:

binding 2-oxoglutaric acid: 17, 19, 33, 87, 93, 170, 173, 174
binding adenosine-5'-triphosphate: 136

8ooqB Glutamine synthetase from Methanothermococcus thermolithotrophicus (see paper)
27% identity, 22% coverage: 276:435/730 of query aligns to 182:346/446 of 8ooqB

query
sites
8ooqB

L

L

G

G

V

F

P

H

V

V

K

E

T

A

R
x
S

H

H

N

H

E
|
E

V

V

A

A

P

P

N

G

Q

Q

F

H

E
|
E

V

V

A

D

P

F

I

K

F

F

E

D

A

A

N

L

L

K

A

T

N

A

D

D

H

S

N

V

Q

I

M

T

V

F

M

K

D

T

L

T

M

I

K

K

R

T

V

I

A

A

R

E

R

Q

H

H

K

G

F

L

R

K

V

A

L

T

F

F

H

M

E

P

K

K

P

P

F

F

K

F

G

G

I

M

N

N

G

G

S

S

G

G

K

M

H

H

S

C

N

H

W

Q

S

S

L

I

S

W

T

L

N

N

T

G

G

E

V

P

N

S

L

F

L

Y

S

D

P

E

G

N

K

A

N

P

P

Y

K

Q

T

L

N

S

L

E

Q

T

F

C

L

M

T

N

F

Y

L

V

V

A

N

G

V

I

L

L

K

K

A

-

V

-

Y

-

D

-

N

H

Q

A

D

K

I

A

L

I

L

V

A

A

S

I

I

T

M

N

T

P

A

T

S

V

N

N

S

S

H

Y

R

K

-

R

-

L

L

V

G

P

A

G

N

Y

E

E

A

A

P

P

P

V

S

N

I

I

L

-

S

-

V

A

F

W

L

A

G

N

S

S

Q

N

I

R

S

S

A

A

M

I

L

I

-

R

-

V

-

P

-

A

-

R

-

G

-

K

-

G

D

T

D

R

L

I

E

E

T

F

R

R

V

A

P

P

D

D

K

P

K

S

M

C

T

N

P

P

binding 2-oxoglutaric acid: S189 (≠ R283)
binding magnesium ion: E192 (= E286), E199 (= E293)

Sites not aligning to the query:

binding 2-oxoglutaric acid: 16, 18, 32, 86, 92, 169, 172, 173
binding magnesium ion: 137

P0A9C5 Glutamine synthetase; GS; Glutamate--ammonia ligase; Glutamine synthetase I beta; GSI beta; EC 6.3.1.2 from Escherichia coli (strain K12) (see 3 papers)
37% identity, 14% coverage: 275:377/730 of query aligns to 202:304/469 of P0A9C5

query
sites
P0A9C5

R

Q

L

M

G

G

V

L

P

V

V

V

K

E

T

A

R

H

H

H

N

H

E

E

V

V

A

A

-

T

P

A

N

G

Q

Q

F

N

E

E

V

V

A

A

P

T

I

R

F

F

E

N

E

T

A

M

N

T

L

K

A

K

N

A

D

D

H

E

N

I

Q

Q

M

I

V

Y

M

K

D

Y

L

V

M

V

K

H

R

N

V

V

A

A

R

H

R

R

H

F

K

G

F

K

R

T

V

A

L

T

F

F

H

M

E

P

K

K

P

P

F

M

K

F

G

G

I

D

N

N

G

G

S

S

G

G

K

M

H

H

S

C

N

H

W

M

S

S

L

L

S

S

T

K

N

N

T

-

G

G

V

V

N

N

L

L

L

F

S

A

P

G

G

D

K

K

N

Y

P

A

K

G

T

L

N

S

L

E

Q

Q

F

A

L

L

T

Y

F

Y

L

I

V

G

N

G

V

V

L

I

K

K

Sites not aligning to the query:

1 modified: Initiator methionine, Removed
398 modified: O-AMP-tyrosine

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)
36% identity, 14% coverage: 275:377/730 of query aligns to 202:304/469 of P0A1P6

query
sites
P0A1P6

R

Q

L

M

G

G

V

L

P

V

V

V

K
x
E

T

A

R

H

H

H

N

H

E
|
E

V

V

A

A

-

T

P

A

N

G

Q

Q

F

N

E
|
E

V

V

A

A

P

T

I

R

F

F

E

N

E

T

A

M

N

T

L

K

A

K

N

A

D

D

H

E

N

I

Q

Q

M

I

V

Y

M

K

D

Y

L

V

M

V

K

H

R

N

V

V

A

A

R

H

R

R

H

F

K

G

F

K

R

T

V

A

L

T

F

F

H

M

E

P

K

K

P

P

F

M

K

F

G

G

I

D

N
|
N

G
|
G

S

S

G

G

K

M

H
|
H

S

C

N
x
H

W
x
M

S
|
S

L

L

S

A

T

K

N

N

T

-

G

G

V

T

N

N

L

L

L

F

S

S

P

G

G

D

K

K

N

Y

P

A

K

G

T

L

N

S

L

E

Q

Q

F

A

L

L

T

Y

F

Y

L

I

V

G

N

G

V

V

L

I

K

K

E208 (≠ K281) binding ATP
E213 (= E286) binding Mn(2+)
E221 (= E293) binding Mn(2+)
NG 265:266 (= NG 337:338) binding L-glutamate
H270 (= H342) binding Mn(2+)
HMS 272:274 (≠ NWS 344:346) 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

1fpyA Crystal structure of glutamine synthetase from salmonella typhimurium with inhibitor phosphinothricin (see paper)
36% identity, 14% coverage: 275:377/730 of query aligns to 201:303/468 of 1fpyA

query
sites
1fpyA

R

Q

L

M

G

G

V

L

P

V

V

V

K
x
E

T

A

R

H

H

H

N

H

E
|
E

V

V

A

A

-

T

P

A

N

G

Q

Q

F

N

E
|
E

V

V

A

A

P
x
T

I

R

F
|
F

E

N

E

T

A

M

N

T

L

K

A

K

N

A

D

D

H

E

N

I

Q

Q

M

I

V

Y

M

K

D

Y

L

V

M

V

K

H

R

N

V

V

A

A

R

H

R

R

H

F

K

G

F

K

R

T

V

A

L

T

F

F

H

M

E

P

K

K

P

P

F

M

K

F

G

G

I

D

N

N

G
|
G

S

S

G

G

K

M

H
|
H

S

C

N
x
H

W

M

S
|
S

L

L

S

A

T

K

N

N

T

-

G

G

V

T

N

N

L

L

L

F

S

S

P

G

G

D

K

K

N

Y

P

A

K

G

T

L

N

S

L

E

Q

Q

F

A

L

L

T

Y

F

Y

L

I

V

G

N

G

V

V

L

I

K

K

binding adenosine-5'-diphosphate: E207 (≠ K281), T223 (≠ P296), F225 (= F298), H271 (≠ N344), S273 (= S346)
binding manganese (ii) ion: E212 (= E286), E220 (= E293), H269 (= H342)
binding phosphinothricin: E212 (= E286), G265 (= G338), H269 (= H342)

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)
36% identity, 14% coverage: 275:377/730 of query aligns to 201:303/468 of 1f1hA

query
sites
1f1hA

R

Q

L

M

G

G

V

L

P

V

V

V

K
x
E

T

A

R

H

H
|
H

N

H

E
|
E

V

V

A

A

-

T

P

A

N

G

Q

Q

F

N

E
|
E

V

V

A

A

P
x
T

I

R

F
|
F

E

N

E

T

A

M

N

T

L

K

A

K

N

A

D

D

H

E

N

I

Q

Q

M

I

V

Y

M

K

D

Y

L

V

M

V

K

H

R

N

V

V

A

A

R

H

R

R

H

F

K

G

F

K

R

T

V

A

L

T

F

F

H

M

E

P

K

K

P

P

F

M

K

F

G

G

I

D

N

N

G

G

S

S

G

G

K

M

H
|
H

S

C

N
x
H

W

M

S
|
S

L

L

S

A

T

K

N

N

T

-

G

G

V

T

N

N

L

L

L

F

S

S

P

G

G

D

K

K

N

Y

P

A

K

G

T

L

N

S

L

E

Q

Q

F

A

L

L

T

Y

F

Y

L

I

V

G

N

G

V

V

L

I

K

K

binding adenosine-5'-diphosphate: E207 (≠ K281), H210 (= H284), E220 (= E293), T223 (≠ P296), F225 (= F298), H271 (≠ N344), S273 (= S346)
binding manganese (ii) ion: E212 (= E286), E220 (= E293), H269 (= H342)

Sites not aligning to the query:

2lgsA Feedback inhibition of fully unadenylylated glutamine synthetase from salmonella typhimurium by glycine, alanine, and serine (see paper)
36% identity, 14% coverage: 275:377/730 of query aligns to 195:297/445 of 2lgsA

query
sites
2lgsA

R

Q

L

M

G

G

V

L

P

V

V

V

K

E

T

A

R

H

H

H

N

H

E
|
E

V

V

A

A

-

T

P

A

N

G

Q

Q

F

N

E
|
E

V

V

A

A

P

T

I

R

F

F

E

N

E

T

A

M

N

T

L

K

A

K

N

A

D

D

H

E

N

I

Q

Q

M

I

V

Y

M

K

D

Y

L

V

M

V

K

H

R

N

V

V

A

A

R

H

R

R

H

F

K

G

F

K

R

T

V

A

L

T

F

F

H

M

E

P

K

K

P

P

F

M

K

F

G

G

I

D

N
|
N

G
|
G

S

S

G
|
G

K

M

H
|
H

S

C

N

H

W

M

S

S

L

L

S

A

T

K

N

N

T

-

G

G

V

T

N

N

L

L

L

F

S

S

P

G

G

D

K

K

N

Y

P

A

K

G

T

L

N

S

L

E

Q

Q

F

A

L

L

T

Y

F

Y

L

I

V

G

N

G

V

V

L

I

K

K

binding glutamic acid: N258 (= N337), G259 (= G338), G261 (= G340), H263 (= H342)
binding manganese (ii) ion: E206 (= E286), E214 (= E293), H263 (= H342)

Sites not aligning to the query:

1lgrA Interactions of nucleotides with fully unadenylylated glutamine synthetase from salmonella typhimurium (see paper)
36% identity, 14% coverage: 275:377/730 of query aligns to 195:297/445 of 1lgrA

query
sites
1lgrA

R

Q

L

M

G

G

V

L

P

V

V

V

K
x
E

T

A

R

H

H

H

N

H

E
|
E

V

V

A

A

-

T

P

A

N

G

Q

Q

F

N

E
|
E

V

V

A

A

P
x
T

I

R

F
|
F

E

N

E

T

A

M

N

T

L

K

A

K

N

A

D

D

H

E

N

I

Q

Q

M

I

V

Y

M

K

D

Y

L

V

M

V

K

H

R

N

V

V

A

A

R

H

R

R

H

F

K

G

F

K

R

T

V

A

L

T

F

F

H

M

E

P

K

K

P

P

F

M

K

F

G

G

I

D

N

N

G

G

S

S

G

G

K

M

H
|
H

S

C

N
x
H

W

M

S
|
S

L

L

S

A

T

K

N

N

T

-

G

G

V

T

N

N

L

L

L

F

S

S

P

G

G

D

K

K

N

Y

P

A

K

G

T

L

N

S

L

E

Q

Q

F

A

L

L

T

Y

F

Y

L

I

V

G

N

G

V

V

L

I

K

K

binding adenosine monophosphate: E201 (≠ K281), T217 (≠ P296), F219 (= F298), H265 (≠ N344), S267 (= S346)
binding manganese (ii) ion: E206 (= E286), E214 (= E293), H263 (= H342)

Sites not aligning to the query:

8s59O Glutamine synthetase
27% identity, 23% coverage: 211:379/730 of query aligns to 130:284/446 of 8s59O

query
sites
8s59O

N

N

L

V

G

G

W

P

E

E

Q

L

E

E

Y

F

F

F

L

L

V

F

D

-

E

K

A

L

L

D

F

A

N

N

A

G

R

N

P

P

D

T

L

T

V

E

L

L

T

T

G

-

R

-

T

-

L

-

M

-

G

-

H

-

S

-

A

-

K

-

D

D

Q

Q

Q

-

L

-

D

-

D

G

H

G

Y

Y

F

F

G

D

S

F

I

A

P

P

-

L

E

D

R

R

V

A

I
x
Q

A

D

F

V

M
x
R

E
x
R

D

D

F

I

E

D

K

Y

E

A

A

L

Y

E

R

H

L

M

G

G

V

F

P

Q

V

I

K

E

T

A

R
x
S

H

H

N

H

E

E

V

V

A

A

P

P

N

S

Q

Q

F

H

E

E

V

I

A

D

P

F

I

R

F

F

E

G

E

D

A

V

N

L

L

C

A

T

N

A

D

D

H

N

N

V

Q

V

M

T

V

F

M

K

D

Y

L

V

M

V

K

K

R

S

V

I

A

A

R

Y

R

H

H

K

K

G

F

Y

R

Y

V

A

L

S

F

F

H

M

E

P

K

K

P

P

F

L

K

F

G

G

I

V

N

N

G

G

S

S

G

G

K

M

H

H

S

S

N

N

W

Q

S

S

L

L

S

F

T

K

N

D

T

G

G

K

V

N

N

V

L

F

L

Y

S

D

P

P

G

D

K

T

N

P

P

T

K

K

T

L

N

S

L

Q

Q

D

F

A

L

M

T

Y

F

Y

L

I

V

G

N

G

V

L

L

L

K

K

A

H

V

I

binding 2-oxoglutaric acid: Q168 (≠ I263), R171 (≠ M266), R172 (≠ E267), S188 (≠ R283)

Sites not aligning to the query:

binding 2-oxoglutaric acid: 23, 25, 39, 86, 92

Query Sequence

>WP_010527758.1 NCBI__GCF_000220155.1:WP_010527758.1
MAKLRFSALEELLNRETKPSKEPRIPTSEYFGELVFDRPKMKKYLSKEAFDHVIEAIEKG
TRIDRRMADQIALGMKAWAMEKGATHYTHWFHPLTDGTAEKHDAFLTFGEFGSMVESFSG
SLLVQQEPDASSFPSGGIRNTFEARGYTAWDVSSPAFIVGSTLCIPTIFVSYTGHALDYK
FPLLKALNAVDKAATAVCQYFDKNVTRVISNLGWEQEYFLVDEALFNARPDLVLTGRTLM
GHSSAKDQQLDDHYFGSIPERVIAFMEDFEKEAYRLGVPVKTRHNEVAPNQFEVAPIFEE
ANLANDHNQMVMDLMKRVARRHKFRVLFHEKPFKGINGSGKHSNWSLSTNTGVNLLSPGK
NPKTNLQFLTFLVNVLKAVYDNQDILLASIMTASNSHRLGANEAPPSILSVFLGSQISAM
LDDLETRVPDKKMTPDEKTALKLDIGKIPEILLDNTDRNRTSPFAFTGNRFEYRAVGSSA
NCASALIVLNTAVANQLKVFKKEVDALIEKGVKKDEAIFQIIKEYIKASKKIRFDGDGYS
QEWVEEARRRGLVNVSNVPDALKAYTTDKAKKLFTENGVFTEVELEARTEVELEKFVKKI
QIEARVLGDLALNHIVPTGVRYMNTLIDNVQGLKDVFGEKDDFHELAADRIDLIKKISYH
IQNIKNKTHDMVEARKVANKIEDMKEKAEAYDQKVRPYLDDIRYHIDKLELTVDNSIWPL
PKYRELLFAR

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