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)
25% identity, 32% coverage: 281:511/726 of query aligns to 174:362/443 of 4lnkA

query
sites
4lnkA

E

E

L

L

Y

E

K

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

S

G

Q

Q

Y

H

E
|
E

I

I

A

D

P
x
F

I

K

Y
|
Y

E

A

T

G

G

A

N

V

L

R

A

S

T

C

D

D

H

D

N

I

Q

Q

I

T

I

F

M

K

T

L

T

V

L

V

R

K

S

T

V

I

A

A

K

R

R

K

Y

H

G

G

M

L

L

H

C

A

L

T

L

F

H

M

E

P

K

K

P

P

F

L

A

F

G

G

I

V

N
|
N

G
|
G

S

S

G
|
G

K

M

H
|
H

L

C

N
|
N

Y

L

S
|
S

I

L

G

F

N

K

A

N

E

G

L

V

G

N

S

A

L

F

F

F

D

D

P

-

G

-

D

-

T

-

P

-

H

-

E

E

N

N

A

A

K

D

F

L

L

Q

V

L

-

S

-

E

-

T

-

A

-

K

-

H

F

F

C

I

A

A

A

G

A

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I

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R

K

A

H

L

A

H

T

K

S

F

F

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A

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V

L

T

R

N

A

P

T

T

V

V

A

N

S

S

A

Y

S

K

N

-

D

-

H

-

R

R

L

L

G

-

A

-

N

-

E

-

A

-

P

-

A

-

I

-

M

-

S

-

M

-

Y

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L

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D

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V

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F

-

E

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Q

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K

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Q

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G

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K

-

V

V

N

P

G

G

C

Y

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x
E

Q

A

K

P

C

C

V

Y

M

V

N

A

V

W

G

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A

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N

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x
R

P

S

P

P

L

L

P

I

R

R

D

I

P

P

G

A

D
x
S

R

R

N

G

R

I

T
x
S

S

T

P

-

F

-

A

-

F

-

T

-

G

-

N

-

R
|
R

F

V

E
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E

F

V

R
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R

A

S

V

V

G

D

S

P

S

A

M

-

S

-

I

-

A

A

G

N

S

P

Q

Y

V

L

A

A

L

L

N

S

T

V

M

L

A

A

D

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E

active site: E188 (= E295), E195 (= E302), H244 (= H351), R315 (≠ L454), E332 (= E478), R334 (= R480)
binding adenosine-5'-diphosphate: F198 (≠ P305), Y200 (= Y307), N246 (= N353), S248 (= S355), S324 (≠ D463), S328 (≠ T467), R330 (= R476)
binding glutamic acid: E188 (= E295), V189 (= V296), N239 (= N346), G240 (= G347), G242 (= G349), E303 (≠ K442)
binding magnesium ion: E188 (= E295), E195 (= E302), H244 (= H351), E332 (= E478)

Sites not aligning to the query:

active site: 52, 131, 133
binding adenosine-5'-diphosphate: 43, 50
binding glutamic acid: 133
binding magnesium ion: 131

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)
25% identity, 32% coverage: 281:511/726 of query aligns to 174:362/443 of 4lniA

query
sites
4lniA

E

E

L

L

Y

E

K

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

S

G

Q

Q

Y

H

E
|
E

I

I

A
x
D

P

F

I

K

Y
|
Y

E

A

T

G

G

A

N

V

L

R

A

S

T

C

D

D

H

D

N

I

Q

Q

I

T

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F

M

K

T

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T

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I

A

A

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R

R

K

Y

H

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G

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C

A

L

T

L

F

H

M

E

P

K

K

P

P

F

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A

F

G

G

I

V

N

N

G

G

S

S

G

G

K

M

H
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H

L

C

N
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N

Y

L

S
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S

I

L

G

F

N

K

A

N

E

G

L

V

G

N

S

A

L

F

F

F

D

D

P

-

G

-

D

-

T

-

P

-

H

-

E

E

N

N

A

A

K

D

F

L

L

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V

L

-

S

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E

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A

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F

F

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A

A

A

G

A

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I

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A

H

L

A

H

T

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F

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A

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P

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T

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V

A

N

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S

A

Y

S

K

N

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D

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H

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R
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R

L

L

G

-

A

-

N

-

E

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A

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P

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A

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I

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M

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M

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N

P

G

G

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x
E

Q

A

K

P

C

C

V

Y

M

V

N

A

V

W

G

S

V

A

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N

L
x
R

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S

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P

L

L

P

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R
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R

D

I

P

P

G

A

D

S

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R

N

G

R

I

T

S

S

T

P

-

F

-

A

-

F

-

T

-

G

-

N

-

R
|
R

F

V

E
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E

F

V

R
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R

A

S

V

V

G

D

S

P

S

A

M

-

S

-

I

-

A

A

G

N

S

P

Q

Y

V

L

A

A

L

L

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T

V

M

L

A

A

D

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Y

G

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A

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N

E

K

L

L

E

E

active site: E188 (= E295), E195 (= E302), H244 (= H351), R315 (≠ L454), E332 (= E478), R334 (= R480)
binding adenosine-5'-diphosphate: E183 (≠ K290), D197 (≠ A304), Y200 (= Y307), N246 (= N353), S248 (= S355), R320 (= R459), R330 (= R476)
binding magnesium ion: E188 (= E295), E195 (= E302), E195 (= E302), H244 (= H351), E332 (= E478)
binding l-methionine-s-sulfoximine phosphate: E188 (= E295), H244 (= H351), R297 (= R407), E303 (≠ K442), R315 (≠ L454), R334 (= R480)

Sites not aligning to the query:

active site: 52, 131, 133
binding adenosine-5'-diphosphate: 131
binding magnesium ion: 131, 131, 133
binding l-methionine-s-sulfoximine phosphate: 133

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)
25% identity, 32% coverage: 281:511/726 of query aligns to 175:363/444 of P12425

query
sites
P12425

E

E

L

L

Y

E

K

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

S

G

Q

Q

Y

H

E
|
E

I

I

A

D

P

F

I

K

Y

Y

E

A

T

G

G

A

N

V

L

R

A

S

T

C

D

D

H

D

N

I

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Q

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F

M

K

T

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T

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L

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A

A

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R

R

K

Y

H

G

G

M

L

L

H

C

A

L

T

L

F

H

M

E

P

K

K

P

P

F

L

A

F

G

G

I

V

N

N

G
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G

S

S

G

G

K

M

H
|
H

L

C

N

N

Y

L

S

S

I

L

G

F

N

K

A

N

E

G

L

V

G

N

S

A

L

F

F

F

D

D

P

-

G

-

D

-

T

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P

-

H

-

E

E

N

N

A

A

K

D

F

L

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L

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S

-

E

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T

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A

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K

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H

F

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C

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A

A

A

G

A

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A

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L

A

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F

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V

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R

N

A

P

T

T

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V

A

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S

S

A

Y

S

K

N

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D

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H

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R

R

L

L

G

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A

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N

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E

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A

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A

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M

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F

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E

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Q

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F

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Q

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G

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K

-

V

V

N

P

G
|
G

C

Y

K
x
E

Q

A

K
x
P

C

C

V

Y

M

V

N

A

V

W

G

S

V

A

D

Q

T

N

L

R

P

S

P

P

L

L

P

I

R

R

D

I

P

P

G

A

D

S

R

R

N

G

R

I

T

S

S

T

P

-

F

-

A

-

F

-

T

-

G

-

N

-

R

R

F

V

E
|
E

F

V

R

R

A

S

V

V

G

D

S

P

S

A

M

-

S

-

I

-

A

A

G

N

S

P

Q

Y

V

L

A

A

L

L

N

S

T

V

M

L

A

A

D

A

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G

L

L

D

D

Y

G

I

I

A

K

S

N

E

K

L

L

E

E

E189 (= E295) binding
V190 (= V296) 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 (= E302) binding
G241 (= G347) binding
H245 (= H351) binding
G302 (= G440) 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 (≠ K442) 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 (≠ K444) 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 (= E478) binding

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
134 binding
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.

4s0rD Structure of gs-tnra complex (see paper)
25% identity, 32% coverage: 281:511/726 of query aligns to 178:366/447 of 4s0rD

query
sites
4s0rD

E

E

L

L

Y

E

K

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

S

G

Q

Q

Y

H

E
|
E

I

I

A

D

P

F

I

K

Y

Y

E

A

T

G

G

A

N

V

L

R

A

S

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C

D

D

H

D

N

I

Q

Q

I

T

I

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M

K

T

L

T

V

L

V

R

K

S

T

V

I

A

A

K

R

R

K

Y

H

G

G

M

L

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H

C

A

L

T

L

F

H

M

E

P

K

K

P

P

F

L

A

F

G
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G

I
x
V

N
|
N

G

G

S

S

G

G

K

M

H
|
H

L

C

N

N

Y

L

S

S

I

L

G

F

N

K

A

N

E

G

L

V

G

N

S

A

L

F

F

F

D

D

P

-

G

-

D

-

T

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P

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H

-

E

E

N

N

A

A

K

D

F

L

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Q

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L

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S

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E

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T

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A

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K

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F

F

C

I

A

A

A

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A

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R

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A

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L

A

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A

P

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T

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V

A

N

S

S

A

Y

S

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N

-

D

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H

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R
|
R

L

L

G

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A

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N

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G

C
x
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K
x
E

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C

C

V

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M

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N

A

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W

G

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x
R

P

S

P

P

L

L

P

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R

R

D

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P

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G

A

D

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R

R

N

G

R

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T

S

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T

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-

F

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A

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F

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T

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G

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N

-

R

R

F

V

E
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E

F

V

R
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R

A

S

V

V

G

D

S

P

S

A

M

-

S

-

I

-

A

A

G

N

S

P

Q

Y

V

L

A

A

L

L

N

S

T

V

M

L

A

A

D

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L

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D

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Y

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A

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S

N

E

K

L

L

E

E

active site: E192 (= E295), E199 (= E302), H248 (= H351), R319 (≠ L454), E336 (= E478), R338 (= R480)
binding glutamine: E192 (= E295), R301 (= R407), E307 (≠ K442)
binding magnesium ion: E199 (= E302), H248 (= H351), H248 (= H351), E336 (= E478)
binding : G241 (= G344), V242 (≠ I345), N243 (= N346), G305 (= G440), Y306 (≠ C441)

Sites not aligning to the query:

active site: 56, 135, 137
binding glutamine: 137
binding magnesium ion: 66, 135, 135, 419
binding : 63, 64, 65, 66, 161, 376, 426, 430

7tf6A Glutamine synthetase (see paper)
33% identity, 12% coverage: 281:367/726 of query aligns to 169:255/438 of 7tf6A

query
sites
7tf6A

E

E

L

L

Y

E

K

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

S

G

Q

Q

Y

H

E
|
E

I

I

A

D

P

F

I

K

Y

Y

E

A

T

D

G

A

N

V

L

T

A

A

T

C

D

D

H

N

N

I

Q

Q

I

T

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F

M

K

T

L

T

V

L

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R

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S

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V

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A

A

K

R

R

K

Y

H

G

N

M

L

L

H

C

A

L

T

L

F

H

M

E

P

K

K

P

P

F

L

A

F

G
|
G

I

V

N
|
N

G
|
G

S

S

G

G

K

M

H
|
H

L

F

N

N

Y

V

S

S

I

L

G

F

N

K

A

G

E

K

L

E

G

N

S

A

L

F

F

F

D

D

P

P

binding glutamine: E183 (= E295), G235 (= G347), H239 (= H351)
binding magnesium ion: E183 (= E295), E190 (= E302), H239 (= H351)
binding : G232 (= G344), N234 (= N346)

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

7tdvC Glutamine synthetase (see paper)
33% identity, 12% coverage: 281:367/726 of query aligns to 174:260/443 of 7tdvC

query
sites
7tdvC

E

E

L

L

Y

E

K

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

S

G

Q

Q

Y

H

E
|
E

I

I

A
x
D

P
x
F

I
x
K

Y
|
Y

E

A

T

D

G

A

N

V

L

T

A

A

T

C

D

D

H

N

N

I

Q

Q

I

T

I

F

M

K

T

L

T

V

L

V

R

K

S

T

V

I

A

A

K

R

R

K

Y

H

G

N

M

L

L

H

C

A

L

T

L

F

H

M

E

P

K

K

P

P

F

L

A

F

G

G

I

V

N

N

G
|
G

S

S

G

G

K

M

H
|
H

L

F

N
|
N

Y
x
V

S
|
S

I

L

G

F

N

K

A

G

E

K

L

E

G

N

S

A

L

F

F

F

D

D

P

P

binding adenosine-5'-diphosphate: E183 (≠ K290), D197 (≠ A304), F198 (≠ P305), K199 (≠ I306), Y200 (= Y307), N246 (= N353), V247 (≠ Y354), S248 (= S355)
binding magnesium ion: E188 (= E295), E195 (= E302), E195 (= E302), H244 (= H351)
binding l-methionine-s-sulfoximine phosphate: E188 (= E295), E195 (= E302), G240 (= G347), H244 (= H351)

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

8oooA Glutamine synthetase from methanothermococcus thermolithotrophicus in complex with 2-oxoglutarate and mgatp at 2.15 a resolution (see paper)
30% identity, 19% coverage: 220:356/726 of query aligns to 132:254/447 of 8oooA

query
sites
8oooA

F

F

A

V

G

G

P

P

E
|
E

Q

P

E

E

Y

F

F

F

L

L

I

L

D

K

R

K

N

D

F

P

A

-

F

-

S

H

R

N

P

P

D

H

L

K

L

Y

I

I

A

P

G

A

R

D

S

D

L

-

F

-

G

-

A

-

R

-

P

-

K

-

G

G

Q

G

E

Y

F

F

E

D

D

L

Q

E

Y

P

F

M

G

D

V

E

I

A

P
|
P

-

D

-

I

R
|
R

V

D

L

I

A

V

F

F

M

A

M

L

E

E

V

-

E

-

R

-

E

-

L

-

Y

-

K

N

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

S

G

Q

Q

Y

H

E

E

I

V

A

D

P
x
F

I
x
K

Y
x
F

E

D

T

D

G

A

N

L

L

K

A

T

T

A

D

D

H

S

N

V

Q

I

I

T

I

F

M

K

T

T

L

I

R

K

S

T

V

I

A

A

K

E

R

Q

Y

H

G

G

M

L

L

K

C

A

L

T

L

F

H

M

E

P

K

K

P

P

F

F

A

F

G

G

I

M

N

N

G

G

S

S

G

G

K

M

H

H

L

C

N
x
H

Y

Q

S
|
S

I

I

binding 2-oxoglutaric acid: P170 (= P268), R173 (= R269), R174 (= R270), S190 (≠ R292)
binding adenosine-5'-triphosphate: E136 (= E224), E188 (≠ K290), F203 (≠ P305), K204 (≠ I306), F205 (≠ Y307), H251 (≠ N353), S253 (= S355)

Sites not aligning to the query:

8ooqB Glutamine synthetase from Methanothermococcus thermolithotrophicus (see paper)
30% identity, 19% coverage: 220:356/726 of query aligns to 131:253/446 of 8ooqB

query
sites
8ooqB

F

F

A

V

G

G

P

P

E

E

Q

P

E
|
E

Y

F

F

F

L

L

I

L

D

K

R

K

N

D

F

P

A

-

F

-

S

H

R

N

P

P

D

H

L

K

L

Y

I

I

A

P

G

A

R

D

S

D

L

-

F

-

G

-

A

-

R

-

P

-

K

-

G

G

Q

G

E

Y

F

F

E

D

D

L

Q

E

Y

P

F

M

G

D

V

E

I

A

P
|
P

-

D

-

I

R
|
R

V

D

L

I

A

V

F

F

M

A

M

L

E

E

V

-

E

-

R

-

E

-

L

-

Y

-

K

N

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

S

G

Q

Q

Y

H

E
|
E

I

V

A

D

P

F

I

K

Y

F

E

D

T

D

G

A

N

L

L

K

A

T

T

A

D

D

H

S

N

V

Q

I

I

T

I

F

M

K

T

T

L

I

R

K

S

T

V

I

A

A

K

E

R

Q

Y

H

G

G

M

L

L

K

C

A

L

T

L

F

H

M

E

P

K

K

P

P

F

F

A

F

G

G

I

M

N

N

G

G

S

S

G

G

K

M

H

H

L

C

N

H

Y

Q

S

S

I

I

binding 2-oxoglutaric acid: P169 (= P268), R172 (= R269), R173 (= R270), S189 (≠ R292)
binding magnesium ion: E137 (= E226), E192 (= E295), E199 (= E302)

Sites not aligning to the query:

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

7tfaB Glutamine synthetase (see paper)
31% identity, 13% coverage: 277:369/726 of query aligns to 168:260/441 of 7tfaB

query
sites
7tfaB

E

E

V

I

E

V

R

L

E

K

L

L

Y

E

K

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

S

G

Q

Q

Y

H

E
|
E

I

I

A

D

P

F

I

K

Y

Y

E

A

T

D

G

A

N

V

L

K

A

A

T

A

D

D

H

Q

N

I

Q

Q

I

T

I

F

M

K

T

L

T

V

L

V

R

K

S

T

V

I

A

A

K

R

R

Q

Y

H

G

G

M

L

L

H

C

A

L

T

L

F

H

M

E

P

K

K

P

P

F

L

A

F

G

G

I

V

N
|
N

G
|
G

S

S

G

G

K

M

H
|
H

L

C

N

N

Y

Q

S

S

I

L

G

F

N

K

A

D

E

N

L

E

G

N

S

V

L

F

F

Y

D

D

P

E

G

T

D

D

binding glutamine: E186 (= E295), G238 (= G347), H242 (= H351)
binding magnesium ion: E186 (= E295), E193 (= E302), H242 (= H351)
binding : V187 (= V296), N237 (= N346)

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)
31% identity, 13% coverage: 277:369/726 of query aligns to 166:258/439 of 7tdpA

query
sites
7tdpA

E

E

V

I

E

V

R

L

E

K

L

L

Y

E

K

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

S

G

Q

Q

Y

H

E
|
E

I

I

A
x
D

P

F

I

K

Y
|
Y

E

A

T

D

G

A

N

V

L

K

A

A

T

A

D

D

H

Q

N

I

Q

Q

I

T

I

F

M

K

T

L

T

V

L

V

R

K

S

T

V

I

A

A

K

R

R

Q

Y

H

G

G

M

L

L

H

C

A

L

T

L

F

H

M

E

P

K

K

P

P

F

L

A

F

G

G

I

V

N

N

G
|
G

S

S

G

G

K

M

H
|
H

L

C

N
|
N

Y

Q

S
|
S

I

L

G

F

N

K

A

D

E

N

L

E

G

N

S

V

L

F

F

Y

D

D

P

E

G

T

D

D

binding adenosine-5'-diphosphate: E179 (≠ K290), D193 (≠ A304), Y196 (= Y307), N242 (= N353), S244 (= S355)
binding magnesium ion: E184 (= E295), E191 (= E302), E191 (= E302), H240 (= H351)
binding l-methionine-s-sulfoximine phosphate: E184 (= E295), E191 (= E302), G236 (= G347), H240 (= H351)

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

8ooxB Glutamine synthetase (see paper)
29% identity, 24% coverage: 214:385/726 of query aligns to 117:272/438 of 8ooxB

query
sites
8ooxB

K

K

L

L

P

G

V

Y

I

V

A

M

F

N

A

T

G

G

P

P

E

E

Q

M

E
|
E

Y

F

F

F

L

L

I

-

D

-

R

-

N

-

F

-

A

-

F

F

S

K

R

R

P

Q

D

D

L

-

I

-

A

-

G

-

R

-

S

-

L

-

F

-

G

-

A

G

R

M

P

P

P

T

K

N

G

I

Q

P

E

Q

F

D

E

R

D

G

Q

G

Y

Y

F

F

G

D

V

L

I

A

P

P

R

-

V

-

L

I

A

D

F

L

M

A

M

E

E

E

V

I

E

K

R

R

E

E

-

I

-

V

-

L

-

V

L

L

Y

E

K

E

L

M

G

G

V

F

P

E

V

V

K

E

T

A

R

A

H

H

N

H

E
|
E

V

V

A

A

P

F

S

G

Q

Q

Y

H

E
|
E

I

I

A

D

P

F

I

K

Y

Y

E

D

T

N

G

A

N

-

L

L

A

A

T

T

D

A

H

D

N

N

Q

V

I

I

I

T

M

L

T

K

T

Y

L

V

-

A

R

K

S

T

V

L

A

A

K

L

R

Q

Y

H

G

G

M

L

L

H

C

A

L

T

L

F

H

M

E

P

K

K

P

P

F

I

A

F

G

G

I

V

N

N

G

G

S

S

G

G

K

M

H

H

L

T

N

N

Y

T

S

S

I

L

G

F

N

K

A

D

E

G

L

K

G

N

S

A

L

F

F

Y

D

D

P

P

G

-

D

D

T

A

P

P

H

D

E

Q

N

I

A

S

K

D

F

T

L

L

V

R

F

Y

C

F

A

V

A

G

I

V

binding magnesium ion: E129 (= E226), E183 (= E295), E190 (= E302)

8oozA Glutamine synthetase (see paper)
29% identity, 24% coverage: 214:385/726 of query aligns to 109:264/430 of 8oozA

query
sites
8oozA

K

K

L

L

P

G

V

Y

I

V

A

M

F

N

A

T

G
|
G

P

P

E
|
E

Q

M

E

E

Y

F

F

F

L

L

I

-

D

-

R

-

N

-

F

-

A

-

F

F

S

K

R

R

P

Q

D

D

L

-

I

-

A

-

G

-

R

-

S

-

L

-

F

-

G

-

A

G

R

M

P

P

P

T

K

N

G

I

Q

P

E

Q

F

D

E

R

D

G

Q

G

Y

Y

F

F

G

D

V

L

I

A

P

P

R

-

V

-

L

I

A

D

F

L

M

A

M

E

E

E

V

I

E

K

R

R

E

E

-

I

-

V

-

L

-

V

L

L

Y

E

K

E

L

M

G

G

V

F

P

E

V

V

K
x
E

T

A

R

A

H

H

N

H

E

E

V

V

A

A

P

F

S

G

Q

Q

Y

H

E

E

I

I

A

D

P
x
F

I
x
K

Y
|
Y

E

D

T

N

G

A

N

-

L

L

A

A

T

T

D

A

H

D

N

N

Q

V

I

I

I

T

M

L

T

K

T

Y

L

V

-

A

R

K

S

T

V

L

A

A

K

L

R

Q

Y

H

G

G

M

L

L

H

C

A

L

T

L

F

H

M

E

P

K

K

P

P

F

I

A

F

G

G

I

V

N

N

G

G

S

S

G

G

K

M

H
|
H

L

T

N
|
N

Y

T

S
|
S

I

L

G

F

N

K

A

D

E

G

L

K

G

N

S

A

L

F

F

Y

D

D

P

P

G

-

D

D

T

A

P

P

H

D

E

Q

N

I

A

S

K

D

F

T

L

L

V

R

F

Y

C

F

A

V

A

G

I

V

binding adenosine-5'-triphosphate: G117 (= G222), E170 (≠ K290), F185 (≠ P305), K186 (≠ I306), Y187 (= Y307), N233 (= N353), S235 (= S355)
binding magnesium ion: E119 (= E224), H231 (= H351)

Sites not aligning to the query:

8tfkA Glutamine synthetase (see paper)
27% identity, 20% coverage: 258:401/726 of query aligns to 145:291/440 of 8tfkA

query
sites
8tfkA

E

E

F

L

E

T

D

D

Q

Q

-

G

Y

Y

F

F

G

D

V

F

I

A

P

P

-

L

R

D

R

R

V

A

L

Q

A

D

F

V

M

R

E

D

V

I

E

D

R

Y

E

A

L

L

Y

E

K

H

L

M

G

G

V

F

P

Q

V

I

K

E

T

A

R

S

H

H

N

H

E
|
E

V

V

A

A

P

P

S

S

Q

Q

Y

H

E
|
E

I

I

A
x
D

P

-

I

-

Y
x
F

E

R

T
x
F

G

G

N

D

L

V

A

L

T

C

D

T

H

A

N

D

Q

N

I

V

M

T

-

F

-

K

T

Y

T

V

L

V

R

K

S

S

V

I

A

A

K

Y

R

H

Y

K

G

G

M

Y

L

Y

C

A

L

S

L

F

H

M

E

P

K

K

P

P

F

L

A

F

G

G

I

V

N

N

G
|
G

S

S

G

G

K

M

H
|
H

L

S

N
|
N

Y

Q

S

S

I

L

G

F

N

K

A

D

E

G

L

K

G

N

S

V

L

F

F

Y

D

D

P

P

G

-

D

D

T

T

P

P

H

T

E

K

-

L

N

S

A

Q

K

D

F

A

L

M

V

Y

F

Y

C

I

A

G

A

L

I

L

R

K

A

H

L

I

H

R

K

E

F

F

G

T

P

A

M

V

L

T

R

N

A

P

T

V

V

V

A

N

S

S

binding adenosine-5'-diphosphate: D194 (≠ A304), F195 (≠ Y307), F197 (≠ T309), N243 (= N353)
binding magnesium ion: E185 (= E295), E192 (= E302), E192 (= E302), H241 (= H351)
binding l-methionine-s-sulfoximine phosphate: E185 (= E295), E192 (= E302), G237 (= G347), H241 (= H351)

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

8ufjB Glutamine synthetase (see paper)
27% identity, 20% coverage: 258:401/726 of query aligns to 149:295/444 of 8ufjB

query
sites
8ufjB

E

E

F

L

E

T

D

D

Q

Q

-

G

Y

Y

F

F

G

D

V

F

I

A

P

P

R

-

V

-

L

L

A

D

F

L

M

G

M

Q

E

D

V

V

E

R

R

R

E

D

-

I

-

D

-

Y

-

A

L

L

Y

E

K

H

L

M

G

G

V

F

P

Q

V

I

K

E

T

A

R

S

H

H

N

H

E
|
E

V

V

A

A

P

P

S

S

Q

Q

Y

H

E
|
E

I

I

A

D

P

-

I

-

Y

F

E

R

T

F

G

G

N

D

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V

A

L

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C

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A

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D

Q

N

I

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M

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-

F

-

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S

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I

A

A

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Y

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L

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H

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P

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G

G

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N

G

G

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S

G

G

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S

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F

Y

D

D

P

P

G

-

D

D

T

T

P

P

H

T

E

K

-

L

N

S

A

Q

K

D

F

A

L

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Y

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Y

C

I

A

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A

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I

L

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A

H

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A

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S

binding magnesium ion: E189 (= E295), E196 (= E302), H245 (= H351)

Sites not aligning to the query:

binding magnesium ion: 132, 134, 333

3ng0A Crystal structure of glutamine synthetase from synechocystis sp. Pcc 6803
27% identity, 23% coverage: 193:356/726 of query aligns to 103:275/465 of 3ng0A

query
sites
3ng0A

R

R

S

D

M

P

Q

R

A

T

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I

N

A

T

A

Q

K

A

A

K

A

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Y

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G

G

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I

E

A

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-

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-

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x
Y

A

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E

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E
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E

Y

F

F

F

L

L

I

F

D

D

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D

-

I

-

R

-

F

-

G

-

Q

-

T

-

E

-

N

-

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-

Y

N

Y

F

F

A

A

F

D

S

S

R

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E

D

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L

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I

N

A

T

G

G

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R

S

E

L

E

F

E

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G

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N

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L

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E

G

F

Y

E

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D

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Y

Y

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V

I

A

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P

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E

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Y

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A

L

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G

G

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V

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P

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x
K

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H

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N

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E
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E

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V

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S

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G

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Y

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E
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E

I

L

A

G

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x
I

I

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Y
x
F

E

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T

K

G

L

N

V

L

N

A

S

T

A

D

D

H

N

N

L

Q

M

I

I

I

Y

M

K

T

Y

T

V

L

I

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S

N

V

V

A

A

K

K

R

K

Y

Y

G

G

M

K

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C

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L

T

L

F

H

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E

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K

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P

F

I

A

F

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N

I

D

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N

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S

G

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H
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H

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x
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S

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L

active site: E130 (= E224), E132 (= E226), E213 (= E295), E221 (= E302), H270 (= H351)
binding phosphoaminophosphonic acid-adenylate ester: Y126 (≠ F220), E130 (= E224), K209 (≠ T291), I224 (≠ P305), F226 (≠ Y307), H272 (≠ N353), S274 (= S355)
binding manganese (ii) ion: E130 (= E224), E132 (= E226), E213 (= E295), E221 (= E302), H270 (= H351)

Sites not aligning to the query:

active site: 51, 340, 359, 361
binding phosphoaminophosphonic acid-adenylate ester: 340, 345, 357
binding manganese (ii) ion: 359, 361

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)
28% identity, 23% coverage: 193:356/726 of query aligns to 103:275/469 of P0A9C5

query
sites
P0A9C5

R

R

S

D

M

P

Q

R

A

S

L

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N

A

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-

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A

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P

E

E

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P

E

E

Y

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D

-

I

N

R

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F

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A

A

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G

Y

Y

F

F

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I

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D

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-

A

-

Q

-

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-

I

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H

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E

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V

A

A

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A

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G

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Y

N

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E

I

V

A

A

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T

I

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Y

F

E

N

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Q

I

I

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T

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V

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A

L

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L

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A

F

G

G

I

D

N

N

G

G

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S

G

G

K

M

H

H

L

C

N

H

Y

M

S

S

I

L

Sites not aligning to the query:

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

1fpyA Crystal structure of glutamine synthetase from salmonella typhimurium with inhibitor phosphinothricin (see paper)
28% identity, 23% coverage: 193:356/726 of query aligns to 102:274/468 of 1fpyA

query
sites
1fpyA

R

R

S

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R

A

A

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L

A

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G

I

I

E

A

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K

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G

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E

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E

Y

F

F

F

L

L

I

F

D

D

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D

-

I

N

R

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F

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F

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S

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S

L

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A

A

G

I

R

D

S

D

L

I

F

E

G

G

A

A

R

W

P

N

P

S

-

S

-

T

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K

-

Y

-

E

-

G

-

N

K

K

G

G

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E

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-

G

F

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E

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D

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G

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Y

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x
E

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E

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-

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E
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E

I

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A

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x
T

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Y
x
F

E

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T

G

M

N

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A

K

T

A

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D

H

E

N

I

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Q

I

I

I

Y

M

K

T

Y

T

V

L

V

R

H

S

N

V

V

A

A

K

H

R

R

Y

F

G

G

M

K

L

T

C

A

L

T

L

F

H

M

E

P

K

K

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P

F

M

A

F

G

G

I

D

N

N

G
|
G

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S

G

G

K

M

H
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H

L

C

N
x
H

Y

M

S
|
S

I

L

binding adenosine-5'-diphosphate: G127 (= G222), E129 (= E224), E207 (≠ K290), T223 (≠ P305), F225 (≠ Y307), H271 (≠ N353), S273 (= S355)
binding manganese (ii) ion: E129 (= E224), E131 (= E226), E212 (= E295), E220 (= E302), H269 (= H351)
binding phosphinothricin: E131 (= E226), E212 (= E295), G265 (= G347), H269 (= H351)

Sites not aligning to the query:

Query Sequence

>206697 MicrobesOnline__882:206697
MSGIQARLNAISAVTNYKPSTAPMNFSETKLTEFFGCNVFNEKVMRERLPKDVFKSLQKT
IELGEKLDPSIADIVANTMKDWAIEKGATHFTHVFYPLTGLTAEKHDSFLTPDGKGGALA
EFSGKMLIQGEPDASSFPSGGLRSTFEARGYTAWDVTSPAYILENPNGTFLCIPTAFLSW
TGEALDKKTPLLRSMQALNTQAKRVLKLFGIETKLPVIAFAGPEQEYFLIDRNFAFSRPD
LLIAGRSLFGARPPKGQEFEDQYFGVIPRRVLAFMMEVERELYKLGVPVKTRHNEVAPSQ
YEIAPIYETGNLATDHNQIIMTTLRSVAKRYGMLCLLHEKPFAGINGSGKHLNYSIGNAE
LGSLFDPGDTPHENAKFLVFCAAAIRALHKFGPMLRATVASASNDHRLGANEAPPAIMSM
YLGEQLTDVFEQFKQGKVNGCKQKCVMNVGVDTLPPLPRDPGDRNRTSPFAFTGNRFEFR
AVGSSMSIAGSQVALNTMMADSLDYIASELEKAIGGDASKLNEAVQSLLQKIMVEHEAII
FNGDGYSEAWHKEAERRGLPNLRTTPDALPMLTKPEVIELFTKYGVFSEAELRSREEIYL
EQYCKTVKTEANLVIRMARTIIFPAAMRYQGELATTCANLKAAGHDYQMVTLEDVTAKLR
SMQKAANELEKLLDHEAASVLEEARHMCDAILPAMNDVRKWADSLETIVADDLWSLPSYQ
EMLFIK

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