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)
32% identity, 13% coverage: 254:347/729 of query aligns to 155:249/443 of 4lnkA

query
sites
4lnkA

Y

Y

F

F

G

D

A

L

I

A

P

P

T

T

R

D

V

L

A

G

A

E

-

N

F

C

M

R

K

R

D

D

L

I

E

V

I

L

E

E

A

L

L

E

K

E

L

M

G

G

I

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

-

H

-
x
E

-

I

-

D

F
|
F

E

K

L
x
Y

A

A

P

G

I

A

F

V

E

R

E

S

C

C

N

D

L

D

A

I

N

Q

D

T

H

F

N

K

L

L

L

V

I

V

M

-

S

-

L

-

M

-

R

K

K

T

V

I

S

A

R

R

R

K

H

H

G

G

F

L

R

H

V

A

L

T

L

F

H

M

E

P

K

K

P

P

F

L

K

F

G

G

V

V

N
|
N

G
|
G

S

S

G
|
G

K

M

H
|
H

N

C

N
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N

W

L

S
|
S

L

L

active site: E188 (= E286), E195 (vs. gap), H244 (= H342)
binding adenosine-5'-diphosphate: F198 (= F292), Y200 (≠ L294), N246 (= N344), S248 (= S346)
binding glutamic acid: E188 (= E286), V189 (= V287), N239 (= N337), G240 (= G338), G242 (= G340)
binding magnesium ion: E188 (= E286), E195 (vs. gap), 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)
32% identity, 13% coverage: 254:347/729 of query aligns to 155:249/443 of 4lniA

query
sites
4lniA

Y

Y

F

F

G

D

A

L

I

A

P

P

T

T

R

D

V

L

A

G

A

E

-

N

F

C

M

R

K

R

D

D

L

I

E

V

I

L

E

E

A

L

L

E

K

E

L

M

G

G

I

F

P

E

V

I

K
x
E

T

A

R

S

H

H

N

H

E
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E

V

V

A

A

P

P

N

G

Q

Q

-

H

-
x
E

-

I

-
x
D

F

F

E

K

L
x
Y

A

A

P

G

I

A

F

V

E

R

E

S

C

C

N

D

L

D

A

I

N

Q

D

T

H

F

N

K

L

L

L

V

I

V

M

-

S

-

L

-

M

-

R

K

K

T

V

I

S

A

R

R

R

K

H

H

G

G

F

L

R

H

V

A

L

T

L

F

H

M

E

P

K

K

P

P

F

L

K

F

G

G

V

V

N

N

G

G

S

S

G

G

K

M

H
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H

N

C

N
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N

W

L

S
|
S

L

L

active site: E188 (= E286), E195 (vs. gap), H244 (= H342)
binding adenosine-5'-diphosphate: E183 (≠ K281), D197 (vs. gap), Y200 (≠ L294), N246 (= N344), S248 (= S346)
binding magnesium ion: E188 (= E286), E195 (vs. gap), E195 (vs. gap), 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)
32% identity, 13% coverage: 254:347/729 of query aligns to 156:250/444 of P12425

query
sites
P12425

Y

Y

F

F

G

D

A

L

I

A

P

P

T

T

R

D

V

L

A

G

A

E

-

N

F

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M

R

K

R

D

D

L

I

E

V

I

L

E

E

A

L

L

E

K

E

L

M

G

G

I

F

P

E

V

I

K

E

T

A

R

S

H

H

N

H

E
|
E

V
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V

A

A

P

P

N

G

Q

Q

-

H

-
x
E

-

I

-

D

F

F

E

K

L

Y

A

A

P

G

I

A

F

V

E

R

E

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C

C

N

D

L

D

A

I

N

Q

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F

N

K

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L

L

V

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V

M

-

S

-

L

-

M

-

R

K

K

T

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A

R

R

R

K

H

H

G

G

F

L

R

H

V

A

L

T

L

F

H

M

E

P

K

K

P

P

F

L

K

F

G

G

V

V

N

N

G
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G

S

S

G

G

K

M

H
|
H

N

C

N

N

W

L

S

S

L

L

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 (vs. gap) 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.

4s0rD Structure of gs-tnra complex (see paper)
32% identity, 13% coverage: 254:347/729 of query aligns to 159:253/447 of 4s0rD

query
sites
4s0rD

Y

Y

F

F

G
x
D

A

L

I

A

P

P

T

T

R

D

V

L

A

G

A

E

-

N

F

C

M

R

K

R

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D

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V

I

L

E

E

A

L

L

E

K

E

L

M

G

G

I

F

P

E

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I

K

E

T

A

R

S

H

H

N

H

E
|
E

V

V

A

A

P

P

N

G

Q

Q

-

H

-
x
E

-

I

-

D

F

F

E

K

L

Y

A

A

P

G

I

A

F

V

E

R

E

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C

C

N

D

L

D

A

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N

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K

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L

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-

S

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L

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M

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R

K

K

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R

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H

H

G

G

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A

L

T

L

F

H

M

E

P

K

K

P

P

F

L

K

F

G
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G

V
|
V

N
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N

G

G

S

S

G

G

K

M

H
|
H

N

C

N

N

W

L

S

S

L

L

active site: E192 (= E286), E199 (vs. gap), H248 (= H342)
binding glutamine: E192 (= E286)
binding magnesium ion: E199 (vs. gap), H248 (= H342), H248 (= H342)
binding : D161 (≠ G256), G241 (= G335), V242 (= V336), N243 (= N337)

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, 305, 306, 376, 426, 430

3ng0A Crystal structure of glutamine synthetase from synechocystis sp. Pcc 6803
25% identity, 26% coverage: 209:398/729 of query aligns to 124:321/465 of 3ng0A

query
sites
3ng0A

V

T

A

V

Y
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Y

L

F

G

G

W

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E
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E

Q

A

E
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E

Y

F

F

F

L

L

V

F

D

D

E

D

G

I

L

R

Y

F

A

G

A

Q

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P

E

D

N

-

S

-

Y

-

F

-

A

-

D

-

S

-

V

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E

-

G

L

R

L

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N

T

T

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G

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Y

Y

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A

A

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M

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K

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E

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L

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L

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A

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T
x
K

R

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H

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N

H

E
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E

V

V

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A

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N

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G

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E

L

L

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x
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F
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F

E

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E

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N

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L

N

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N

A

D

D

H

N

N

L

L

M

L

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I

Y

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Y

L

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K

N

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Y

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G

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V

L

T

L

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K

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P

F

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G

N

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D

N

N

G

G

S

S

G

G

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H
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H

N

V

N
x
H

W

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S
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S

L

L

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K

D

D

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G

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G

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D

D

K

N

Y

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A

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N

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R

K

active site: E130 (= E215), E132 (= E217), E213 (= E286), E221 (= E293), H270 (= H342)
binding phosphoaminophosphonic acid-adenylate ester: Y126 (= Y211), E130 (= E215), K209 (≠ T282), I224 (≠ P296), F226 (= F298), H272 (≠ N344), S274 (= S346)
binding manganese (ii) ion: E130 (= E215), E132 (= E217), E213 (= E286), E221 (= E293), H270 (= H342)

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

7tdvC Glutamine synthetase (see paper)
32% identity, 13% coverage: 254:347/729 of query aligns to 155:249/443 of 7tdvC

query
sites
7tdvC

Y

Y

F

F

G

D

A

L

I

A

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P

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T

R

D

V

L

A

G

A

E

-

N

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K

R

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D

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E

A

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L

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G

G

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x
E

T

A

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H

H

N

H

E
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E

V

V

A

A

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E

L

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A
x
D

P
x
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x
K

F
x
Y

E

A

E

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C

A

N

V

L

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A

A

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N

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N

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E

P

K

K

P

P

F

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K

F

G

G

V

V

N

N

G
|
G

S

S

G

G

K

M

H
|
H

N

F

N
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N

W
x
V

S
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S

L

L

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

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)
32% identity, 13% coverage: 254:347/729 of query aligns to 150:244/438 of 7tf6A

query
sites
7tf6A

Y

Y

F

F

G

D

A

L

I

A

P

P

T

T

R

D

V

L

A

G

A

E

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N

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K

R

D

D

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H

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E

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Y

E

A

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N

V

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A

A

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D

H

N

N

I

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L

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K

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L

L

V

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V

R

K

K

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A

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R

R

K

H

H

G

N

F

L

R

H

V

A

L

T

L

F

H

M

E

P

K

K

P

P

F

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K

F

G
|
G

V

V

N
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N

G
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G

S

S

G

G

K

M

H
|
H

N

F

N

N

W

V

S

S

L

L

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

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

7tfaB Glutamine synthetase (see paper)
34% identity, 10% coverage: 275:350/729 of query aligns to 175:250/441 of 7tfaB

query
sites
7tfaB

K

E

L

M

G

G

I

F

P

E

V

I

K

E

T

A

R

S

H

H

N

H

E
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E

V
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V

A

A

P

P

N

G

Q

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F

H

E
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E

L

I

A

D

P

F

I

K

F

Y

E

A

E

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C

A

N

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A

A

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A

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D

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A

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F

H

M

E

P

K

K

P

P

F

L

K

F

G

G

V

V

N
|
N

G
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G

S

S

G

G

K

M

H
|
H

N

C

N

N

W

Q

S

S

L

L

G

F

T

K

D

D

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)
34% identity, 10% coverage: 275:350/729 of query aligns to 173:248/439 of 7tdpA

query
sites
7tdpA

K

E

L

M

G

G

I

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E

V

I

K
x
E

T

A

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H

H

N

H

E
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E

V

V

A

A

P

P

N

G

Q

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F

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E
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E

L

I

A
x
D

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x
Y

E

A

E

D

C

A

N

V

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K

A

A

N

A

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D

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N

I

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K

K

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P

F

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K

F

G

G

V

V

N

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G
|
G

S

S

G

G

K

M

H
|
H

N

C

N
|
N

W

Q

S
|
S

L

L

G

F

T

K

D

D

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

P77961 Glutamine synthetase; GS; Glutamate--ammonia ligase; Glutamine synthetase I beta; GSI beta; EC 6.3.1.2 from Synechocystis sp. (strain PCC 6803 / Kazusa)
25% identity, 26% coverage: 209:398/729 of query aligns to 126:323/473 of P77961

query
sites
P77961

V

T

A

V

Y

Y

L

F

G

G

W

P

E

E

Q

A

E
|
E

Y

F

F

F

L

L

V

F

D

D

E

D

G

I

L

R

Y

F

A

G

A

Q

R

T

P

E

D

N

-

S

-

Y

-

F

-

A

-

D

-

S

-

V

-

E

-

G

L

R

L

W

M

N

T

T

G

G

R

R

T

E

L

E

M

E

G

G

H

G

D

N

S

L

A

G

K

Y

N

K

Q

P

Q

G

L

Y

E

K

D

Q

H

G

Y

Y

F

F

G

P

A

V

I

A

P

P

T

T

R

D

V

T

A

A

A

-

F

-

M

-

K

Q

D

D

L

I

E

R

I

T

E

E

A

M

L

L

-

L

-

T

-

M

-

A

K

G

L

L

G

C

I

V

P

P

V

I

K

E

T

K

R

H

H

H

N

H

E
|
E

V

V

A

A

P

S

N

G

-

G

Q

Q

F

N

E
|
E

L

L

A

G

P

I

I

K

F

F

E

D

E

K

C

L

N

V

L

N

A

S

N

A

D

D

H

N

N

L

L

M

L

I

I

Y

M

K

S

Y

L

V

M

I

R

K

K

N

V

V

S

A

R

K

H

Y

G

G

F

K

R

T

V

V

L

T

L

F

H

M

E

P

K

K

P

P

F

I

K

F

G

N

V

D

N

N

G

G

S

S

G

G

K

M

H

H

N

V

N

H

W

Q

S

S

L

L

G

W

T

K

D

D

T

G

G

Q

I

P

L

L

L

F

M

A

G

G

P

-

G

-

K

-

T

-

P

-

E

D

D

K

N

Y

L

A

R

G

F

F

V

S

T

Q

F

M

V

G

V

L

N

W

T

Y

L

I

M

G

A

G

V

I

Y

L

R

K

H

H

N

A

G

P

L

A

L

L

K

L

A

A

S

F

I

T

S

N

S

P

A

T

T

T

N

N

A

S

H

Y

R

K

E134 (= E217) binding Mg(2+)
E215 (= E286) binding Mg(2+)
E223 (= E293) binding Mg(2+)

Sites not aligning to the query:

361 binding Mn(2+)

8tfkA Glutamine synthetase (see paper)
26% identity, 22% coverage: 254:410/729 of query aligns to 152:306/440 of 8tfkA

query
sites
8tfkA

Y

Y

F

F

G

D

A

F

I

A

P

P

-

L

T

D

R

R

V

A

A

Q

A

D

F

V

M

R

K

R

D

D

L

I

E

D

I

Y

E

A

A

L

L

E

K

H

L

M

G

G

I

F

P

Q

V

I

K

E

T

A

R

S

H

H

N

H

E
|
E

V

V

A

A

P

P

N

S

Q

Q

F

H

E
|
E

L

I

A
x
D

P
x
F

I

R

F
|
F

E

G

E

D

C

V

N

L

L

C

A

T

N

A

D

D

H

N

N

V

L

V

L

T

I

F

M

K

S

Y

L

V

M

V

R

K

K

S

V

I

S

A

R

Y

R

H

H

K

G

G

F

Y

R

Y

V

A

L

S

L

F

H

M

E

P

K

K

P

P

F

L

K

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

G

F

T

K

D

D

T

G

G

K

I

N

L

V

L

F

M

Y

G

D

P

P

G

-

K

D

T

T

P

P

E

T

D

K

N

L

L

S

R

Q

F

D

V

A

T

M

F

Y

V

Y

V

I

N

G

T

G

L

L

M

L

A

-

V

-

Y

-

R

K

H

H

N

I

G

R

L

E

L

F

K

T

A

A

S

V

I

T

S

N

S

P

A

V

T

V

N

N

A

S

H

Y

-

K

R
|
R

L

L

G

V

A

P

N

G

E

Y

A
x
E

P

A

P

P

A

V

I

Y

I

I

S

S

binding adenosine-5'-diphosphate: D194 (≠ A295), F195 (≠ P296), F197 (= F298), N243 (= N344)
binding magnesium ion: E185 (= E286), E192 (= E293), E192 (= E293), H241 (= H342)
binding l-methionine-s-sulfoximine phosphate: E185 (= E286), E192 (= E293), G237 (= G338), H241 (= H342), R294 (= R398), E300 (≠ A404)

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, 312, 331

8oooA Glutamine synthetase from methanothermococcus thermolithotrophicus in complex with 2-oxoglutarate and mgatp at 2.15 a resolution (see paper)
31% identity, 11% coverage: 267:347/729 of query aligns to 174:254/447 of 8oooA

query
sites
8oooA

K
x
R

D

D

L

I

E

V

I

F

E

A

A

L

L

E

K

N

L

L

G

G

I

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

L

V

A

D

P
x
F

I
x
K

F
|
F

E

D

C

A

N

L

L

K

A

T

N

A

D

D

H

S

N

V

L

I

L

T

I

F

M

K

S

T

L

T

M

I

R

K

K

T

V

I

S

A

R

E

R

Q

H

H

G

G

F

L

R

K

V

A

L

T

L

F

H

M

E

P

K

K

P

P

F

F

K

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: R174 (≠ K267), S190 (≠ R283)
binding adenosine-5'-triphosphate: E188 (≠ K281), F203 (≠ P296), K204 (≠ I297), F205 (= F298), H251 (≠ N344), S253 (= S346)

Sites not aligning to the query:

binding 2-oxoglutaric acid: 17, 19, 33, 87, 93, 170, 173
binding adenosine-5'-triphosphate: 136, 325, 335

8ooqB Glutamine synthetase from Methanothermococcus thermolithotrophicus (see paper)
31% identity, 11% coverage: 267:347/729 of query aligns to 173:253/446 of 8ooqB

query
sites
8ooqB

K
x
R

D

D

L

I

E

V

I

F

E

A

A

L

L

E

K

N

L

L

G

G

I

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

L

V

A

D

P

F

I

K

F

F

E

D

C

A

N

L

L

K

A

T

N

A

D

D

H

S

N

V

L

I

L

T

I

F

M

K

S

T

L

T

M

I

R

K

K

T

V

I

S

A

R

E

R

Q

H

H

G

G

F

L

R

K

V

A

L

T

L

F

H

M

E

P

K

K

P

P

F

F

K

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: R173 (≠ K267), 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
binding magnesium ion: 137

8ufjB Glutamine synthetase (see paper)
26% identity, 20% coverage: 267:410/729 of query aligns to 170:310/444 of 8ufjB

query
sites
8ufjB

K

R

D

D

L

I

E

D

I

Y

E

A

A

L

L

E

K

H

L

M

G

G

I

F

P

Q

V

I

K

E

T

A

R

S

H

H

N

H

E
|
E

V

V

A

A

P

P

N

S

Q

Q

F

H

E
|
E

L

I

A

D

P

F

I

R

F

F

E

G

E

D

C

V

N

L

L

C

A

T

N

A

D

D

H

N

N

V

L

V

L

T

I

F

M

K

S

Y

L

V

M

V

R

K

K

S

V

I

S

A

R

Y

R

H

H

K

G

G

F

Y

R

Y

V

A

L

S

L

F

H

M

E

P

K

K

P

P

F

L

K

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

G

F

T

K

D

D

T

G

G

K

I

N

L

V

L

F

M

Y

G

D

P

P

G

-

K

D

T

T

P

P

E

T

D

K

N

L

L

S

R

Q

F

D

V

A

T

M

F

Y

V

Y

V

I

N

G

T

G

L

L

M

L

A

-

V

-

Y

-

R

K

H

H

N

I

G

R

L

E

L

F

K

T

A

A

S

V

I

T

S

N

S

P

A

V

T

V

N

N

A

S

H

Y

-

K

R

R

L

L

G

V

A

P

N

G

E

Y

A

E

P

A

P

P

A

V

I

Y

I

I

S

S

binding magnesium ion: E189 (= E286), E196 (= E293), H245 (= H342)

Sites not aligning to the query:

binding magnesium ion: 132, 134, 333

8oozA Glutamine synthetase (see paper)
27% identity, 18% coverage: 254:381/729 of query aligns to 142:283/430 of 8oozA

query
sites
8oozA

Y

Y

F

F

G

D

A

L

I

A

P

P

T

I

R

D

V

L

A

A

A

E

F

E

M

I

K

K

D

R

L

E

E

I

I

V

E

L

A

V

L

L

K

E

-

E

L

M

G

G

I

F

P

E

V

V

K
x
E

T

A

R

A

H

H

N

H

E

E

V

V

A

A

P

F

N

G

Q

Q

F

H

E

E

L

I

A

D

P
x
F

I
x
K

F
x
Y

E

D

E

N

C

A

N

L

L

A

A

T

N

A

D

D

H

N

N

V

L

I

L

T

I

L

M

K

S

Y

L

V

M

A

R

K

K

T

V

L

S

A

R

L

R

Q

H

H

G

G

F

L

R

H

V

A

L

T

L

F

H

M

E

P

K

K

P

P

F

I

K

F

G

G

V

V

N

N

G

G

S

S

G

G

K

M

H
|
H

N

T

N
|
N

W

T

S
|
S

L

L

G

F

T

K

D

D

T

G

G

K

I

N

L

A

L

F

M

Y

G

D

P

P

G

D

K

A

T

P

P

D

E

Q

-

I

-

S

D

D

N

T

L

L

R

R

F

Y

-

F

-

V

-

G

-

V

-

L

-

K

-

H

-

I

-

R

-

A

V

I

T

T

F

A

V

I

V

T

N

N

T

P

L

L

M

V

A

N

V

S

Y

Y

R

K

binding adenosine-5'-triphosphate: E170 (≠ K281), F185 (≠ P296), K186 (≠ I297), Y187 (≠ F298), N233 (= N344), S235 (= S346)
binding magnesium ion: H231 (= H342)

Sites not aligning to the query:

5zlpL Crystal structure of glutamine synthetase from helicobacter pylori (see paper)
25% identity, 28% coverage: 209:410/729 of query aligns to 128:338/476 of 5zlpL

query
sites
5zlpL

V

V

A

A

Y

Y

L

F

G
|
G

W

A

E
|
E

Q

N

E
|
E

Y

F

F

F

L

I

V

F

D

D

-

S

-

I

-

K

-

I

-

K

-

D

-

A

-

S

-

N

-

S

-

Q

-

Y

-

E

-

V

-

D

-

S

-

E

E

E

G

G

L

E

Y

W

A

-

R

N

P

R

D

D

L

R

L

S

M

F

T

E

G

N

R

G

T

V

L

N

M

F

G

G

H

H

D

R

S

P

A

G

K

K

N

Q

Q

G

Q

-

L

-

E

-

D

-

H

-

Y

-

F

-

G

G

A

Y

I

M

P

P

T

V

R

P

V

P

A

T

A

D

F

T

M

M

K

M

D

D

L

I

E

R

I

T

E

E

A

I

L

V

K

K

L

V

-

L

-

N

-

Q

-

V

G

G

I

L

P

E

V

T

K
x
F

T

V

R

V

H

H

N

H

E
|
E

V

V

A

A

P

Q

N

A

Q

Q

F

G

E
|
E

L

V

A

G

P

V

I

K

F
|
F

E

G

E

D

C

L

N

V

L

E

A

A

N

A

D

D

H

N

N

V

L

Q

L

K

I

L

M

K

S

Y

L

V

M

V

R

K

K

M

V

V

S

A

R

H

R

L

H

N

G

G

F

K

R

T

V

A

L

T

L

F

H

M

E

P

K

K

P

P

F

L

K

Y

G

G

V

D

N

N

G
|
G

S

S

G

G

K

M

H
|
H

N

T

N
x
H

W

V

S
|
S

L

V

G

W

T

K

D

N

T

N

G

E

I

N

L

L

L

F

M

S

G

G

P

-

G

-

K

-

T

-

P

-

E

E

D

T

N

Y

L

K

R

G

F

L

V

S

T

E

F

F

V

A

V

L

N

H

T

F

L

L

M

G

A

G

V

V

Y

L

R

R

H

H

N

A

G

R

L

G

L

L

K

A

A

A

S

F

I

T

S

N

S

A

A

S

T

T

N

N

A

S

H

Y

-

K

R

R

L

L

G

I

A

P

N

G

E

Y

A
x
E

P

A

P

P

A

S

I

I

I

L

S

T

binding adenosine-5'-diphosphate: G132 (= G213), E134 (= E215), F213 (≠ K281), F230 (= F298), H276 (≠ N344), S278 (= S346)
binding magnesium ion: E136 (= E217), E218 (= E286), E225 (= E293)
binding (2s)-2-amino-4-[methyl(phosphonooxy)phosphoryl]butanoic acid: E136 (= E217), E218 (= E286), G270 (= G338), H274 (= H342), E332 (≠ A404)

Sites not aligning to the query:

5zlpA Crystal structure of glutamine synthetase from helicobacter pylori (see paper)
25% identity, 28% coverage: 209:410/729 of query aligns to 128:338/476 of 5zlpA

query
sites
5zlpA

V

V

A

A

Y

Y

L

F

G

G

W

A

E
|
E

Q

N

E

E

Y

F

F

F

L

I

V

F

D

D

-

S

-

I

-

K

-

I

-

K

-

D

-

A

-

S

-

N

-

S

-

Q

-

Y

-

E

-

V

-

D

-

S

-

E

E

E

G

G

L

E

Y

W

A

-

R

N

P

R

D

D

L

R

L

S

M

F

T

E

G

N

R

G

T

V

L

N

M

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A

G

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K

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Q

Q

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Q

-

L

-

E

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D

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Y

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F

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G

G

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I

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A

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x
V

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|
F

E

G

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D

C

L

N

V

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A

N

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D

D

H

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N

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G

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N

N

G

G

S

S

G

G

K

M

H

H

N

T

N
x
H

W

V

S

S

L

V

G

W

T

K

D

N

T

N

G

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I

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L

L

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A

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R

L

G

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L

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A

A

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F

I

T

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N

S

A

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T

T

N

N

A

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R

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N

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binding adenosine-5'-triphosphate: E134 (= E215), V228 (≠ P296), F230 (= F298), H276 (≠ N344)

Sites not aligning to the query:

binding adenosine-5'-triphosphate: 358, 360

Query Sequence

>350071 FitnessBrowser__Btheta:350071
MSKLRFRVVETAFKKKAVEVATPAERPSEYFGKYVFNKEKMFKYLPSKVYNALIDAIDNG
APLDRSIADEVAAGMKKWAVEMGVTHYTHWFAPLTEGTAEKHDAFVEHDGKGGMMEEFTG
KLLVQQEPDASSFPNGGIRNTFEARGYSAWDPSSPAFIVDDTLCIPTVFIAYTGEALDYK
APLLKALRAVDKAATAVCHYFNPEVKKVVAYLGWEQEYFLVDEGLYAARPDLLMTGRTLM
GHDSAKNQQLEDHYFGAIPTRVAAFMKDLEIEALKLGIPVKTRHNEVAPNQFELAPIFEE
CNLANDHNLLIMSLMRKVSRRHGFRVLLHEKPFKGVNGSGKHNNWSLGTDTGILLMGPGK
TPEDNLRFVTFVVNTLMAVYRHNGLLKASISSATNAHRLGANEAPPAIISSFLGKQLSQV
LDHIENSTKDDLINLSGKQGMKLDIPQIPELLIDNTDRNRTSPFAFTGNRFEFRAVGSEA
NCASAMIALNAAVAEQLMKFKKDVDALIEKGEPKVSAILEVIRGYIKECKAIHFDGNGYS
DEWKVEAARRGLDCETSVPVIFDNYLKPETIAMFEAIGVMTKKELEARNEVKWETYTKKI
QIEARVLGDLAMNHIIPVATQYQTDLINNVYKMQSLFPADKAARLSAKNLELIEEIADRT
AFIKEHVDAMIEARKVANKIESEREKAIAYHDTIVPALEEIRYHIDKLELIVDNQMWTLP
KYRELLFVR

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