SitesBLAST

A0R083 Glutamine synthetase; GS; Glutamate--ammonia ligase; Glutamine synthetase I alpha; GSI alpha; EC 6.3.1.2 from Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis) (see paper)
53% identity, 97% coverage: 14:446/447 of query aligns to 8:446/446 of A0R083

query
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A0R083

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K363 (≠ E363) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)

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)
51% identity, 97% coverage: 12:444/447 of query aligns to 7:441/444 of P12425

query
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P12425

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G59 (= G64) mutation to R: Unable to form stable complex with TnrA. In the presence of glutamine, this mutant derepresses amtB-lacZ fusion and glnRA-lacZ fusion.
R62 (= R67) Important for inhibition by glutamine; mutation to 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.
E132 (= E136) binding Mg(2+)
E134 (= E138) binding Mg(2+)
E189 (= E189) binding Mg(2+)
V190 (= V190) 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 (= E196) binding Mg(2+)
G241 (= G241) binding L-glutamate
H245 (= H245) binding Mg(2+)
G302 (= G302) 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 (= E304) 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 (= P306) 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 (= E336) binding Mg(2+)
E424 (= E427) mutation to 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.

Sites not aligning to the query:

1 modified: Initiator methionine, Removed

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)
51% identity, 97% coverage: 12:444/447 of query aligns to 6:440/443 of 4lnkA

query
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S

P

V

D

D

P

P

A

A

N

N

P

P

Y

Y

L

L

S

A

F

L

A

S

V

V

M

L

L

L

A

A

G

G

L

L

K

D

G

G

I

I

E

K

E

N

G

K

Y

L

E

E

L

A

P

P

D

A

P

P

V

I

E

D

E

R

N

N

I

I

F

Y

A

V

M

M

D

S

A

K

P

E

T

E

L

R

S

M

E

E

H

N

G

G

I

I

T

V

A

D

L

L

P

P

G

A

S

T

L

L

Y

A

E

E

A

A

A

L

I

E

E

E

M

F

R

K

N

S

S

N

E

E

M

V

V

M

R

V

E

K

C

A

L

L

G

G

D

E

H

H

I

L

H

F

T

E

N

H

F

F

Y

I

N

E

N

A

K

K

I

E

K

I

E

E

W

W

D

D

Q

M

Y

F

R

R

T

T

Q

Q

V

V

T

H

E

P

Y

W

E

E

I

R

E

E

N

Q

Y

Y

L

M

active site: D52 (= D58), E131 (= E136), E133 (= E138), E188 (= E189), E195 (= E196), H244 (= H245), R315 (= R316), E332 (= E336), R334 (= R338)
binding adenosine-5'-diphosphate: K43 (≠ G49), M50 (≠ G56), F198 (≠ L199), Y200 (= Y201), N246 (≠ H247), S248 (= S249), S324 (≠ G328), S328 (≠ A332), R330 (= R334)
binding glutamic acid: E133 (= E138), E188 (= E189), V189 (= V190), N239 (= N240), G240 (= G241), G242 (= G243), E303 (= E304)
binding magnesium ion: E131 (= E136), E188 (= E189), E195 (= E196), H244 (= H245), E332 (= E336)

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)
51% identity, 97% coverage: 12:444/447 of query aligns to 6:440/443 of 4lniA

query
sites
4lniA

D

E

D

D

V

I

L

E

K

K

A

L

V

V

R

K

D

E

Y

E

N

N

I

V

S

K

F

Y

V

I

Q

R

F

L

W

Q

F

F

V

T

D

D

I

I

L

L

G

G

T

T

L

I

K

K

S

N

F

V

Q

E

I

I

T

P

P

V

K

S

E

Q

L

L

E

G

G

K

A

A

F

L

E

D

E

N

G

K

M

V

G

M

F

F

D
|
D

G

G

S

S

I

I

L

E

G

G

F

F

T

V

R

R

I

I

E

E

S

S

D

D

M

M

I

Y

A

L

Y

Y

P

P

D

D

P

L

T

N

T

T

F

F

Q

V

L

I

C

F

S

P

W

W

R

T

P

A

T

E

D

K

R

G

P

K

V

V

A

A

R

R

M

F

F

I

C

C

D

D

I

I

Q

Y

K

N

P

P

D

D

G

G

S

T

A

P

Y

F

E

E

G

G

D

D

S

P

R

R

W

N

V

N

L

L

K

K

R

R

A

I

L

L

E

K

K

E

A

M

A

E

E

D

R

L

G

G

Y

F

T

S

-

D

Y

F

Y

N

V

L

G

G

P

P

E
|
E

L

P

E
|
E

F

F

L

L

F

F

E

K

-

L

D

D

E

E

K

K

G

G

T

E

K

P

I

T

I

L

-

E

-

L

-

N

D

D

R

K

G

G

Y

Y

F

F

D

D

A

L

P

A

P

P

L

T

D

D

L

L

G

G

N

E

D

N

V

C

R

R

D

D

I

I

I

V

F

L

S

E

L

L

E

E

Q

E

M

M

G

G

Y

F

P

E

I

I

E
|
E

Y

A

S

S

H

H

E
|
E

V

V

A

A

P

P

S

G

Q

Q

H

H

E
|
E

I

I

D
|
D

L

F

R

K

Y
|
Y

A

A

E

G

G

A

M

V

K

R

M

S

A

C

D

D

T

D

A

I

M

Q

T

T

Y

F

R

K

V

L

V

V

K

K

E

T

I

I

A

A

R

R

K

K

H

H

G

G

I

L

Y

H

A

A

T

T

F

F

M

M

P

P

K

K

P

P

I

L

F

F

G

G

E

V

N

N

G

G

S

S

G

G

M

M

H
|
H

V

C

H
x
N

Q

L

S
|
S

L

L

F

F

K

K

N

N

G

G

K

V

N

N

V

A

F

F

D

D

A

E

N

N

D

A

E

D

Y

L

H

Q

L

L

T

S

A

E

E

T

G

A

K

K

S

H

Y

F

I

I

A

A

G

G

I

I

L

V

K

K

H

H

A

A

P

T

E

S

F

F

T

T

C

A

I

V

T

T

N

N

Q

P

W

T

V

V

N

N

S

S

Y

Y

K

K

R
|
R

L

L

V

V

P

P

G

G

Y

Y

E
|
E

A

A

P

P

V

C

Y

Y

V

V

A

A

W

W

A

S

R

A

R

Q

N

N

R
|
R

S

S

A

P

L

L

V

I

R
|
R

V

I

P

P

M

A

Y

-

K

-

P

-

G

S

K

R

E

G

A

I

A

S

T

T

R
|
R

M

V

E
|
E

L

V

R
|
R

S

S

P

V

D

D

P

P

A

A

N

N

P

P

Y

Y

L

L

S

A

F

L

A

S

V

V

M

L

L

L

A

A

G

G

L

L

K

D

G

G

I

I

E

K

E

N

G

K

Y

L

E

E

L

A

P

P

D

A

P

P

V

I

E

D

E

R

N

N

I

I

F

Y

A

V

M

M

D

S

A

K

P

E

T

E

L

R

S

M

E

E

H

N

G

G

I

I

T

V

A

D

L

L

P

P

G

A

S

T

L

L

Y

A

E

E

A

A

A

L

I

E

E

E

M

F

R

K

N

S

S

N

E

E

M

V

V

M

R

V

E

K

C

A

L

L

G

G

D

E

H

H

I

L

H

F

T

E

N

H

F

F

Y

I

N

E

N

A

K

K

I

E

K

I

E

E

W

W

D

D

Q

M

Y

F

R

R

T

T

Q

Q

V

V

T

H

E

P

Y

W

E

E

I

R

E

E

N

Q

Y

Y

L

M

active site: D52 (= D58), E131 (= E136), E133 (= E138), E188 (= E189), E195 (= E196), H244 (= H245), R315 (= R316), E332 (= E336), R334 (= R338)
binding adenosine-5'-diphosphate: E131 (= E136), E183 (= E184), D197 (= D198), Y200 (= Y201), N246 (≠ H247), S248 (= S249), R320 (= R321), R330 (= R334)
binding magnesium ion: E131 (= E136), E131 (= E136), E133 (= E138), E188 (= E189), E195 (= E196), E195 (= E196), H244 (= H245), E332 (= E336)
binding l-methionine-s-sulfoximine phosphate: E133 (= E138), E188 (= E189), H244 (= H245), R297 (= R298), E303 (= E304), R315 (= R316), R334 (= R338)

4s0rD Structure of gs-tnra complex (see paper)
51% identity, 97% coverage: 12:444/447 of query aligns to 10:444/447 of 4s0rD

query
sites
4s0rD

D

E

D

D

V

I

L

E

K

K

A

L

V

V

R

K

D

E

Y

E

N

N

I

V

S

K

F

Y

V

I

Q

R

F

L

W

Q

F

F

V

T

D

D

I

I

L

L

G

G

T

T

L

I

K

K

S

N

F

V

Q

E

I

I

T

P

P

V

K

S

E

Q

L

L

E

G

G

K

A

A

F

L

E

D

E

N

G

K

M

V

G

M

F

F

D
|
D

G

G

S

S

I

I

L

E

G

G

F
|
F

T
x
V

R
|
R

I
|
I

E

E

S

S

D

D

M

M

I

Y

A

L

Y

Y

P

P

D

D

P

L

T

N

T

T

F

F

Q

V

L

I

C

F

S

P

W

W

R

T

P

A

T

E

D

K

R

G

P

K

V

V

A

A

R

R

M

F

F

I

C

C

D

D

I

I

Q

Y

K

N

P

P

D

D

G

G

S

T

A

P

Y

F

E

E

G

G

D

D

S

P

R

R

W

N

V

N

L

L

K

K

R

R

A

I

L

L

E

K

K

E

A

M

A

E

E

D

R

L

G

G

Y

F

T

S

-

D

Y

F

Y

N

V

L

G

G

P

P

E
|
E

L

P

E
|
E

F

F

L

L

F

F

E

K

-

L

D

D

E

E

K

K

G

G

T

E

K

P

I

T

I

L

-

E

-

L

-

N

D

D

R

K

G

G

Y

Y

F

F

D
|
D

A

L

P

A

P

P

L

T

D

D

L

L

G

G

N

E

D

N

V

C

R

R

D

D

I

I

I

V

F

L

S

E

L

L

E

E

Q

E

M

M

G

G

Y

F

P

E

I

I

E

E

Y

A

S

S

H

H

E
|
E

V

V

A

A

P

P

S

G

Q

Q

H

H

E
|
E

I

I

D

D

L

F

R

K

Y

Y

A

A

E

G

G

A

M

V

K

R

M

S

A

C

D

D

T

D

A

I

M

Q

T

T

Y

F

R

K

V

L

V

V

K

K

E

T

I

I

A

A

R

R

K

K

H

H

G

G

I

L

Y

H

A

A

T

T

F

F

M

M

P

P

K

K

P

P

I

L

F

F

G
|
G

E
x
V

N
|
N

G

G

S

S

G

G

M

M

H
|
H

V

C

H

N

Q

L

S

S

L

L

F

F

K

K

N

N

G

G

K

V

N

N

V

A

F

F

D

D

A

E

N

N

D

A

E

D

Y

L

H

Q

L

L

T

S

A

E

E

T

G

A

K

K

S

H

Y

F

I

I

A

A

G

G

I

I

L

V

K

K

H

H

A

A

P

T

E

S

F

F

T

T

C

A

I

V

T

T

N

N

Q

P

W

T

V

V

N

N

S

S

Y

Y

K

K

R
|
R

L

L

V

V

P

P

G
|
G

Y
|
Y

E
|
E

A

A

P

P

V

C

Y

Y

V

V

A

A

W

W

A

S

R

A

R

Q

N

N

R
|
R

S

S

A

P

L

L

V

I

R

R

V

I

P

P

M

A

Y

-

K

-

P

-

G

S

K

R

E

G

A

I

A

S

T

T

R

R

M

V

E
|
E

L

V

R
|
R

S

S

P

V

D

D

P

P

A

A

N

N

P

P

Y

Y

L

L

S

A

F

L

A

S

V

V

M

L

L

L

A

A

G

G

L

L

K

D

G

G

I

I

E

K

E

N

G

K

Y

L

E

E

L

A

P

P

D

A

P

P

V

I

E

D

E

R

N

N

I

I

F
x
Y

A

V

M

M

D

S

A

K

P

E

T

E

L

R

S

M

E

E

H

N

G

G

I

I

T

V

A

D

L

L

P

P

G

A

S

T

L

L

Y

A

E

E

A

A

A

L

I

E

E

E

M

F

R

K

N

S

S

N

E

E

M

V

V

M

R

V

E

K

C

A

L

L

G

G

D

E

H

H

I

L

H

F

T

E

N
x
H

F

F

Y

I

N

E

N

A

K

K

I

E

K
x
I

E

E

W

W

D

D

Q
x
M

Y

F

R

R

T

T

Q

Q

V

V

T

H

E

P

Y

W

E

E

I

R

E

E

N

Q

Y

Y

L

M

active site: D56 (= D58), E135 (= E136), E137 (= E138), E192 (= E189), E199 (= E196), H248 (= H245), R319 (= R316), E336 (= E336), R338 (= R338)
binding glutamine: E137 (= E138), E192 (= E189), R301 (= R298), E307 (= E304)
binding magnesium ion: I66 (= I68), E135 (= E136), E135 (= E136), E199 (= E196), H248 (= H245), H248 (= H245), E336 (= E336), H419 (≠ N419)
binding : F63 (= F65), V64 (≠ T66), R65 (= R67), I66 (= I68), D161 (= D158), G241 (= G238), V242 (≠ E239), N243 (= N240), G305 (= G302), Y306 (= Y303), Y376 (≠ F376), I426 (≠ K426), M430 (≠ Q430)

P9WN37 Glutamine synthetase; GS; Glutamate--ammonia ligase; Glutamine synthetase I alpha; GSI alpha; EC 6.3.1.2 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see paper)
52% identity, 97% coverage: 14:446/447 of query aligns to 8:446/446 of P9WN37

query
sites
P9WN37

V

V

L

L

K

R

A

T

V

L

R

E

D

E

Y

R

N

D

I

I

S

R

F

F

V

V

Q

R

F

L

W

W

F

F

V

T

D

D

I

V

L

L

G

G

T

F

L

L

K

K

S

S

F

V

Q

A

I

I

T

A

P

P

K

A

E

E

L

L

E

E

G

G

A

A

F

F

E

E

G

G

M

I

G

G

F

F

D

D

G

G

S

S

I

I

L

E

G

G

F

F

T

A

R

R

I

V

E

S

E

E

S

S

D

D

M

T

I

V

A

A

Y

H

P

P

D

D

P

P

T

S

T

T

F

F

Q

Q

L

V

C

L

S

P

W

W

R

A

P

T

T

S

D

S

-

G

-

H

R

H

P

H

V

S

A

A

R

R

M

M

F

F

C

C

D

D

I

I

Q

T

K

M

P

P

D

D

G

G

S

S

A

P

Y

S

E

W

G

A

D

D

S

P

R

R

W

H

V

V

L

L

K

R

R

R

A

Q

L

L

E

T

K

K

A

A

A

G

E

E

R

L

G

G

Y

F

T

S

Y

C

Y

Y

V

V

G

H

P

P

E

E

L

I

E

E

F

F

L

L

F

L

-

K

-

P

-

G

-

P

E

E

D

D

E

G

K

S

G

V

T

P

K

V

I

P

I

V

D

D

R

N

G

A

G

G

Y

Y

F

F

D

D

A

Q

P

A

P

V

L

H

D

D

L

S

G

A

N

L

D

N

V

F

R

R

D

H

I

A

I

I

F

D

S

A

L

L

E

E

Q

F

M

M

G

G

Y

I

P

S

I

V

E

E

Y

F

S

S

H

H

E

E

V

G

A

A

P

P

S

G

Q

Q

H

Q

E

E

I

I

D

D

L

L

R

R

Y

F

A

A

E

D

G

A

M

L

K

S

M

M

A

A

D

D

T

N

A

V

M

M

T

T

Y

F

R

R

V

Y

V

V

V

I

K

K

E

E

I

V

A

A

R

L

K

E

H

E

G

G

I

A

Y

R

A

A

T

S

F

F

M

M

P

P

K

K

P

P

I

F

F

G

G

Q

E

H

N

P

G

G

S

S

G

A

M

M

H

H

V

T

H

H

Q

M

S

S

L

L

F

F

K

E

N

G

G

D

K

V

N

N

V

A

F

F

F

H

D

S

A

A

N

D

D

D

E

P

Y

L

H

Q

L

L

T

S

A

E

E

V

G

G

K

K

S

S

Y

F

I

I

A

A

G

G

I

I

L

L

K

E

H

H

A

A

P

C

E

E

F

I

T

S

C

A

I

V

T

T

N

N

Q

Q

W

W

V

V

N

N

S

S

Y

Y

K

K

R

R

L

L

V

V

P

Q

G

G

Y

G

E

E

A

A

P

P

V

T

Y

A

V

A

A

S

W

W

A

G

R

A

N

N

R

R

S

S

A

A

L

L

V

V

R

R

V

V

P

P

M

M

Y

Y

K

T

P

P

G

H

K

K

E

T

A

S

T

R

R

R

M

V

E

E

L

V

R

R

S

S

P

P

D

D

P

S

A

A

A

C

N

N

P

P

Y

Y

L

L

S

T

F

F

A

A

V

V

M

L

L

L

A

A

G

G

L

L

K

R

G

G

I

V

E

E

E
x
K

G

G

Y

Y

E

V

L

L

P

G

D

P

P

Q

V

A

E

E

E

D

N

N

I

V

F

W

A

D

M

L

D

T

A

P

P

E

T

E

L

R

S

R

E

A

H

M

G

G

I

Y

T

R

A

E

L

L

P

P

G

S

S

S

L

L

Y

D

E

S

A

A

A

L

I

R

E

A

M

M

R

E

N

A

S

S

E

E

M

L

V

V

R

A

E

E

C

A

L

L

G

G

D

E

H

H

I

V

H

F

T

D

N

F

F

F

Y

L

N

R

N

N

K

K

I

R

K

T

E

E

W

W

D

A

Q

N

Y

Y

R

R

T

S

Q

H

V

V

T

T

E

P

Y

Y

E

E

I

L

E

R

N

T

Y

Y

L

L

P

S

V

L

K363 (≠ E363) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)

7tdvC Glutamine synthetase (see paper)
50% identity, 97% coverage: 12:444/447 of query aligns to 6:440/443 of 7tdvC

query
sites
7tdvC