SitesBLAST

E189 (= E263) binding Mg(2+)
V190 (= V264) 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 (= E270) binding Mg(2+)
G241 (= G315) binding L-glutamate
H245 (= H319) binding Mg(2+)

Sites not aligning to the query:

1 modified: Initiator methionine, Removed
59 G→R: Unable to form stable complex with TnrA. In the presence of glutamine, this mutant derepresses amtB-lacZ fusion and glnRA-lacZ fusion.
62 Important for inhibition by glutamine; R→A: Highly resistant to inhibition by glutamine and AMP. Regulation by TnrA and GlnR is abolished. Only small differences (less than 2-fold) in its steady-state kinetic constants compared with the wild-type. Similar sensitivity to Met-Sox that compared to the wild-ytpe.
132 binding Mg(2+)
134 binding Mg(2+)
302 G→E: Unable to form stable complex with TnrA. In the presence of glutamine, amtB-lacZ fusion is only 4-fold regulated by TnrA, whereas glnRA-lacZ fusion is derepressed. This mutant retains enzymatic specific activity with a 2-fold decrease of the affinity for glutamate and glutamine compared to the wild-type. Slightly less sensitive to inhibition by glutamine.
304 E→A: Highly resistant to Met-Sox inhibition. 8- and 2-fold increase of the affinity for glutamate and ATP, respectively. Strong decrease of the affinity for ammonium.
306 P→H: Unable to form stable complex with TnrA. In the presence of glutamine, this mutant completely derepresses glnRA-lacZ fusion, whereas amtB-lacZ fusion expression is only partially derepresses.
333 binding Mg(2+)
424 E→K: Unable to form stable complex with TnrA. In the presence of glutamine, this mutant derepresses amtB-lacZ fusion and glnRA-lacZ fusion. Although it is defective in regulation, this mutant retains enzymatic specific activity and similar affinity for ATP, glutamate and glutamine compared to the wild-type. Slightly less sensitive to inhibition by glutamine.

4lnkA B. Subtilis glutamine synthetase structures reveal large active site conformational changes and basis for isoenzyme specific regulation: structure of gs-glutamate-amppcp complex (see paper)
35% identity, 12% coverage: 244:324/695 of query aligns to 169:249/443 of 4lnkA

query
sites
4lnkA

K

R

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N

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V
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V

A

A

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G

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E

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x
F

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N

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H

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S

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L

active site: E188 (= E263), E195 (= E270), H244 (= H319)
binding adenosine-5'-diphosphate: F198 (≠ P273), Y200 (≠ F275), N246 (= N321), S248 (= S323)
binding glutamic acid: E188 (= E263), V189 (= V264), N239 (= N314), G240 (= G315), G242 (= G317)
binding magnesium ion: E188 (= E263), E195 (= E270), H244 (= H319)

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)
35% identity, 12% coverage: 244:324/695 of query aligns to 169:249/443 of 4lniA

query
sites
4lniA

K

R

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E

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S

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L

active site: E188 (= E263), E195 (= E270), H244 (= H319)
binding adenosine-5'-diphosphate: E183 (≠ K258), D197 (≠ A272), Y200 (≠ F275), N246 (= N321), S248 (= S323)
binding magnesium ion: E188 (= E263), E195 (= E270), E195 (= E270), H244 (= H319)
binding l-methionine-s-sulfoximine phosphate: E188 (= E263), H244 (= H319)

Sites not aligning to the query:

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

4s0rD Structure of gs-tnra complex (see paper)
35% identity, 12% coverage: 244:324/695 of query aligns to 173:253/447 of 4s0rD

query
sites
4s0rD

K

R

E

D

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N

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E

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E

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G

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V

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N

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H

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N

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L

active site: E192 (= E263), E199 (= E270), H248 (= H319)
binding glutamine: E192 (= E263)
binding magnesium ion: E199 (= E270), H248 (= H319), H248 (= H319)
binding : G241 (= G312), V242 (= V313), N243 (= N314)

Sites not aligning to the query:

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

8tfkA Glutamine synthetase (see paper)
27% identity, 18% coverage: 237:362/695 of query aligns to 159:284/440 of 8tfkA

query
sites
8tfkA

E

D

R

R

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x
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F

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N

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binding adenosine-5'-diphosphate: D194 (≠ A272), F195 (≠ P273), F197 (= F275), N243 (= N321)
binding magnesium ion: E185 (= E263), E192 (= E270), E192 (= E270), H241 (= H319)
binding l-methionine-s-sulfoximine phosphate: E185 (= E263), E192 (= E270), G237 (= G315), H241 (= H319)

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)
28% identity, 17% coverage: 244:362/695 of query aligns to 170:288/444 of 8ufjB

query
sites
8ufjB

K

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N

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H

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N

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binding magnesium ion: E189 (= E263), E196 (= E270), H245 (= H319)

Sites not aligning to the query:

binding magnesium ion: 132, 134, 333

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)
28% identity, 25% coverage: 182:354/695 of query aligns to 118:304/469 of P0A1P6

query
sites
P0A1P6

A

A

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x
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E

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D

N
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N

G
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G

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H

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N
x
H

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x
M

S
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S

M

L

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S

A

S

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G

G

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N

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K

E130 (= E192) binding Mn(2+)
E132 (= E194) binding Mn(2+)
E208 (≠ K258) binding ATP
E213 (= E263) binding Mn(2+)
E221 (= E270) binding Mn(2+)
NG 265:266 (= NG 314:315) binding L-glutamate
H270 (= H319) binding Mn(2+)
HMS 272:274 (≠ NWS 321:323) binding ATP

Sites not aligning to the query:

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)
28% identity, 25% coverage: 182:354/695 of query aligns to 117:303/468 of 1fpyA

query
sites
1fpyA

A

A

T

T

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L

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G

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Y

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A

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x
E

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E

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E

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x
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F

E

N

T

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D

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N

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Q

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Y

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N

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G

G

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N

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G

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S

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H
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H

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x
H

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S

M

L

S

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S

A

S

K

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N

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G

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N

N

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L

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K

binding adenosine-5'-diphosphate: G127 (= G190), E129 (= E192), E207 (≠ K258), T223 (≠ P273), F225 (= F275), H271 (≠ N321), S273 (= S323)
binding manganese (ii) ion: E129 (= E192), E131 (= E194), E212 (= E263), E220 (= E270), H269 (= H319)
binding phosphinothricin: E131 (= E194), E212 (= E263), G265 (= G315), H269 (= H319)

Sites not aligning to the query:

1f1hA Crystal structure of glutamine synthetase from salmonella typhimurium with thallium ions (see paper)
28% identity, 25% coverage: 182:354/695 of query aligns to 117:303/468 of 1f1hA

query
sites
1f1hA

A

A

T

T

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E

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E

Y

F

F

F

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D

K

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F

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C

-

L

-

V

-

M

-

E

K

Q

L

M

G

G

V

L

T

V

A

V

K
x
E

T

A

Q

H

H
|
H

N

H

E
|
E

V

V

A

A

-

T

P

A

G

G

Q

Q

F

N

E
|
E

V

V

A

A

P
x
T

I

R

F
|
F

E

N

T

T

T

M

N

T

I

K

A

K

T

A

D

D

H

E

N

I

Q

Q

L

I

V

Y

M

K

D

Y

V

V

L

V

K

H

R

N

V

V

A

A

I

H

R

R

H

F

D

G

M

K

I

T

C

A

L

T

M

F

H

M

E

P

K

K

P

P

F

M

A

F

G

G

V

D

N

N

G

G

S

S

G

G

K

M

H
|
H

N

C

N
x
H

W

M

S
|
S

M

L

S

-

S

A

S

K

D

N

G

G

Q

T

N

N

L

L

L

F

D

S

P

G

G

D

K

K

T

Y

P

A

H

G

E

L

N

S

A

E

Q

Q

F

A

L

L

T

Y

F

Y

L

I

M

G

A

G

T

V

I

I

K

K

binding adenosine-5'-diphosphate: E129 (= E192), E207 (≠ K258), H210 (= H261), E220 (= E270), T223 (≠ P273), F225 (= F275), H271 (≠ N321), S273 (= S323)
binding manganese (ii) ion: E129 (= E192), E131 (= E194), E212 (= E263), E220 (= E270), H269 (= H319)

Sites not aligning to the query:

2lgsA Feedback inhibition of fully unadenylylated glutamine synthetase from salmonella typhimurium by glycine, alanine, and serine (see paper)
28% identity, 25% coverage: 182:354/695 of query aligns to 111:297/445 of 2lgsA

query
sites
2lgsA

A

A

T

T

R

G

V

I

T

A

S

D

T

T

V

V

-

L

-

F

G

G

P

P

E
|
E

Q

P

E
|
E

Y

F

F

F

L

L

V

F

D

D

K

D

S

I

Y

R

F

F

-

G

-

A

-

S

-

I

-

S

-

G

-

S

-

H

-

V

-

A

L

I

D

D

R

D

L

I

D

E

L

G

V

A

M

W

A

N

G

S

R

S

T

T

L

K

F

Y

-

E

G

G

A

G

M

N

P

K

P

G

K

H

G

R

Q

P

E

G

M

V

E

K

D

G

H

G

Y

Y

F

F

G

P

S

V

I

P

K

P

E

-

R

-

V

-

V

V

S

D

Y

S

M

A

K

Q

E

D

V

I

N

R

T

S

E

E

L

M

W

C

-

L

-

V

-

M

-

E

K

Q

L

M

G

G

V

L

T

V

A

V

K

E

T

A

Q

H

H

H

N

H

E
|
E

V

V

A

A

-

T

P

A

G

G

Q

Q

F

N

E
|
E

V

V

A

A

P

T

I

R

F

F

E

N

T

T

T

M

N

T

I

K

A

K

T

A

D

D

H

E

N

I

Q

Q

L

I

V

Y

M

K

D

Y

V

V

L

V

K

H

R

N

V

V

A

A

I

H

R

R

H

F

D

G

M

K

I

T

C

A

L

T

M

F

H

M

E

P

K

K

P

P

F

M

A

F

G

G

V

D

N
|
N

G
|
G

S

S

G
|
G

K

M

H
|
H

N

C

N

H

W

M

S

S

M

L

S

-

S

A

S

K

D

N

G

G

Q

T

N

N

L

L

L

F

D

S

P

G

G

D

K

K

T

Y

P

A

H

G

E

L

N

S

A

E

Q

Q

F

A

L

L

T

Y

F

Y

L

I

M

G

A

G

T

V

I

I

K

K

binding glutamic acid: E125 (= E194), N258 (= N314), G259 (= G315), G261 (= G317), H263 (= H319)
binding manganese (ii) ion: E123 (= E192), E125 (= E194), E206 (= E263), E214 (= E270), H263 (= H319)

Sites not aligning to the query:

1lgrA Interactions of nucleotides with fully unadenylylated glutamine synthetase from salmonella typhimurium (see paper)
28% identity, 25% coverage: 182:354/695 of query aligns to 111:297/445 of 1lgrA

query
sites
1lgrA

A

A

T

T

R

G

V

I

T

A

S

D

T

T

V

V

-

L

-

F

G

G

P

P

E
|
E

Q

P

E
|
E

Y

F

F

F

L

L

V

F

D

D

K

D

S

I

Y

R

F

F

-

G

-

A

-

S

-

I

-

S

-

G

-

S

-

H

-

V

-

A

L

I

D

D

R

D

L

I

D

E

L

G

V

A

M

W

A

N

G

S

R

S

T

T

L

K

F

Y

-

E

G

G

A

G

M

N

P

K

P

G

K

H

G

R

Q

P

E

G

M

V

E

K

D

G

H

G

Y

Y

F

F

G

P

S

V

I

P

K

P

E

-

R

-

V

-

V

V

S

D

Y

S

M

A

K

Q

E

D

V

I

N

R

T

S

E

E

L

M

W

C

-

L

-

V

-

M

-

E

K

Q

L

M

G

G

V

L

T

V

A

V

K
x
E

T

A

Q

H

H

H

N

H

E
|
E

V

V

A

A

-

T

P

A

G

G

Q

Q

F

N

E
|
E

V

V

A

A

P
x
T

I

R

F
|
F

E

N

T

T

T

M

N

T

I

K

A

K

T

A

D

D

H

E

N

I

Q

Q

L

I

V

Y

M

K

D

Y

V

V

L

V

K

H

R

N

V

V

A

A

I

H

R

R

H

F

D

G

M

K

I

T

C

A

L

T

M

F

H

M

E

P

K

K

P

P

F

M

A

F

G

G

V

D

N

N

G

G

S

S

G

G

K

M

H
|
H

N

C

N
x
H

W

M

S
|
S

M

L

S

-

S

A

S

K

D

N

G

G

Q

T

N

N

L

L

L

F

D

S

P

G

G

D

K

K

T

Y

P

A

H

G

E

L

N

S

A

E

Q

Q

F

A

L

L

T

Y

F

Y

L

I

M

G

A

G

T

V

I

I

K

K

binding adenosine monophosphate: E201 (≠ K258), T217 (≠ P273), F219 (= F275), H265 (≠ N321), S267 (= S323)
binding manganese (ii) ion: E123 (= E192), E125 (= E194), E206 (= E263), E214 (= E270), H263 (= H319)

Sites not aligning to the query:

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)
27% identity, 28% coverage: 161:354/695 of query aligns to 103:304/469 of P0A9C5

query
sites
P0A9C5

R

R

S

D

M

P

E

R

A

S

L

I

S

A

T

K

Q

R

A

A

L

E

R

D

I

Y

L

L

R

R

L

-

F

-

G

-

N

-

Q

S

T

T

A

G

T

I

R

A

V

D

T

T

S

V

T

L

V

F

G

G

P

P

E

E

Q

P

E

E

Y

F

F

F

L

L

V

F

D

D

K

D

S

I

Y

R

F

F

-

G

-

S

-

I

-

S

-

G

-

S

-

H

-

V

-

A

L

I

D

D

R

D

L

I

D

E

L

G

V

A

M

W

A

N

G

S

R

S

T

T

L

Q

F

Y

-

E

G

G

A

G

M

N

P

K

P

G

K

H

G

R

Q

P

E

A

M

V

E

K

D

G

H

G

Y

Y

F

F

G

P

S

V

I

P

K

P

E

-

R

-

V

-

V

V

S

D

Y

S

M

A

K

Q

E

D

V

I

N

R

T

S

E

E

L

M

W

C

-

L

-

V

-

M

-

E

K

Q

L

M

G

G

V

L

T

V

A

V

K

E

T

A

Q

H

H

H

N

H

E

E

V

V

A

A

-

T

P

A

G

G

Q

Q

F

N

E

E

V

V

A

A

P

T

I

R

F

F

E

N

T

T

T

M

N

T

I

K

A

K

T

A

D

D

H

E

N

I

Q

Q

L

I

V

Y

M

K

D

Y

V

V

L

V

K

H

R

N

V

V

A

A

I

H

R

R

H

F

D

G

M

K

I

T

C

A

L

T

M

F

H

M

E

P

K

K

P

P

F

M

A

F

G

G

V

D

N

N

G

G

S

S

G

G

K

M

H

H

N

C

N

H

W

M

S

S

M

L

S

-

S

S

S

K

D

N

G

G

Q

V

N

N

L

L

L

F

D

A

P

G

G

D

K

K

T

Y

P

A

H

G

E

L

N

S

A

E

Q

Q

F

A

L

L

T

Y

F

Y

L

I

M

G

A

G

T

V

I

I

K

K

Sites not aligning to the query:

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

8oozA Glutamine synthetase (see paper)
28% identity, 24% coverage: 190:353/695 of query aligns to 117:264/430 of 8oozA

query
sites
8oozA

G
|
G

P

P

E
|
E

Q

M

E

E

Y

F

F

F

L

L

V

F

D

K

K

R

S

Q

Y

-

F

-

L

-

D

-

R

-

L

-

D

-

L

-

V

-

M

-

A

-

G

-

R

-

T

-

L

-

F

-

G

D

A

G

M

M

P

P

P

T

K

N

G

I

Q

P

E

Q

M

D

E

R

D

G

H

G

Y

Y

F

F

G

D

S

L

I

A

K

P

E

I

R

D

V

L

V

A

S

E

Y

E

M

I

K

K

-

R

E

E

V

I

N

V

T

L

E

V

L

L

W

E

K

E

L

M

G

G

V

F

T

E

A

V

K
x
E

T

A

Q

A

H

H

N

H

E

E

V

V

A

A

P

F

G

G

Q

Q

F

H

E

E

V

I

A

D

P

-

I

-

F
|
F

E
x
K

T
x
Y

T

D

N

N

-

A

I

L

A

A

T

T

D

A

H

D

N

N

Q

V

L

I

V

T

M

L

D

K

-

Y

V

V

L

A

K

K

R

T

V

L

A

A

I

L

R

Q

H

H

D

G

M

L

I

H

C

A

L

T

M

F

H

M

E

P

K

K

P

P

F

I

A

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

M

L

S

-

S

F

S

K

D

D

G

G

Q

K

N

N

L

A

L

F

D

Y

P

D

G

P

K

D

T

A

P

P

H

D

E

Q

N

I

A

S

Q

D

F

T

L

L

T

R

F

Y

L

F

M

V

A

G

T

G

I

V

binding adenosine-5'-triphosphate: G117 (= G190), E170 (≠ K258), F185 (= F275), K186 (≠ E276), Y187 (≠ T277), N233 (= N321), S235 (= S323)
binding magnesium ion: E119 (= E192), H231 (= H319)

Sites not aligning to the query:

Query Sequence

>WP_011735573.1 NCBI__GCF_000015045.1:WP_011735573.1
MEIFGQNVFNQDVMRERLPKAVYKNLKKTIDEGLPLDPSIADVVATAMKEWAVERGATHF
THWFQPMTGVTAEKQDSFITPTDNGIVMDFSGKELVKGEPDASSFPSGGLRATFEARGYT
AWDCTSPAFLKEEADAITLCIPTAFCSYTGEALDKKTPLLRSMEALSTQALRILRLFGNQ
TATRVTSTVGPEQEYFLVDKSYFLDRLDLVMAGRTLFGAMPPKGQEMEDHYFGSIKERVV
SYMKEVNTELWKLGVTAKTQHNEVAPGQFEVAPIFETTNIATDHNQLVMDVLKRVAIRHD
MICLMHEKPFAGVNGSGKHNNWSMSSSDGQNLLDPGKTPHENAQFLTFLMATIKAVDEYA
GLLRSSCASAGNDHRLGANEAPPAIISMFLGEQLAEILEQIEKGATKSSKSGSEIKIGVT
TLPALPKDTTDRNRTSPFAFTGNRFEFRMLGSTFSISGPNIVINTIIAEALKQFADTLEG
SKDFTADLEKLLQETAKKHKRVVFNGNNYSDEWVEEAKKRGLLNIPNTPEALKELVTKEA
VDLFVAHKVFTEKELHSRYEIMVEQYVKTLNIEALTMIDMAKHSIMPAATSFATEVAQSI
SAVAAVSSKIDVSAQTELLEELSNNLSSMNKNVKALEKVLEDALNITDIDTQAAAFRENV
FAKMLELRADGDALEKIISADYWPLPTYAEMLFNL

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