SitesBLAST

E132 (= E224) binding Mg(2+)
E134 (= E226) binding Mg(2+)
E189 (= E295) binding Mg(2+)
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 Mg(2+)
G241 (= G347) binding L-glutamate
H245 (= H351) binding Mg(2+)
G302 (≠ A410) 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 (= E412) 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 (= P414) 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 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.
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)
26% identity, 40% coverage: 220:512/728 of query aligns to 127:363/443 of 4lnkA

query
sites
4lnkA

N

N

A

L

G

G

P

P

E
|
E

Q

P

E
|
E

Y

F

F

F

L

L

-

F

-

K

I

L

D

D

R

E

N

K

F

-

A

G

R

E

P

P

D

T

L

L

Q

E

M

L

A

N

G

D

R

K

T

G

-

G

L

Y

F

F

G

D

A

L

K

A

P

P

A

T

K

D

G

-

Q

-

E

-

L

-

D

-

H

-

Y

-

F

L

G

G

A

E

I

N

P

C

R

R

V

-

L

-

S

-

F

-

M

-

D

D

V

I

E

V

H

L

Q

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

G

G

Q

Q

F

H

E
|
E

I

I

A

D

P
x
F

V

K

Y
|
Y

E

A

Q

G

S

A

N

V

I

R

A

S

T

C

D

D

H

D

N

I

Q

Q

M

T

V

F

M

K

T

L

T

V

L

V

K

K

S

T

V

I

A

A

K

R

K

K

H

H

G

G

M

L

A

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

L

L

S

F

C

K

S

N

G

G

H

V

G

N

S

A

L

F

F

F

D

D

P

-

G

-

E

-

N

-

P

-

T

-

E

E

N

N

A

A

Q

D

F

L

L

Q

I

L

F

S

C

E

A

T

A

A

-

K

-

H

V

F

I

I

R

A

S

G

V

I

H

V

K

K

Y

H

S

A

K

T

L

S

L

F

R

T

A

A

V

V

V

T

A

N

T

P

A

T

S

V

N

N

D

S

H

Y

R

K

-

R

-

L

L

V

G

P

A

G

N

Y

E
|
E

A

A

P

P

P

-

A

-

I

-

L

-

S

-

I

-

F

-

L

-

G

-

D

-

H

-

L

-

S

-

E

-

I

-

F

-

S

-

K

-

I

-

Q

-

E

-

G

-

N

-

S

-

P

-

T

-

P

-

T

-

S

-

T

-

G

C

F

Y

L

V

K

A

A

W

G

S

V

A

D

Q

T

N

L
x
R

P

S

P

P

L

L

P

I

R

R

D

I

A

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
|
E

F

V

R
|
R

A

S

V

V

G

-

S

-

N

-

S

D

S

P

I

A

A

A

G

N

P

P

Q

Y

V

L

A

A

I

L

N

S

T

V

M

L

I

L

A

A

D

A

S

G

L

L

D

D

Y

G

I

I

A

K

D

N

E

K

L

L

E

E

A

A

active site: E131 (= E224), E133 (= E226), 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: E133 (= E226), E188 (= E295), V189 (= V296), N239 (= N346), G240 (= G347), G242 (= G349), E303 (= E412)
binding magnesium ion: E131 (= E224), E188 (= E295), E195 (= E302), H244 (= H351), E332 (= E478)

Sites not aligning to the query:

active site: 52
binding adenosine-5'-diphosphate: 43, 50

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)
26% identity, 40% coverage: 220:512/728 of query aligns to 127:363/443 of 4lniA

query
sites
4lniA

N

N

A

L

G

G

P

P

E
|
E

Q

P

E
|
E

Y

F

F

F

L

L

-

F

-

K

I

L

D

D

R

E

N

K

F

-

A

G

R

E

P

P

D

T

L

L

Q

E

M

L

A

N

G

D

R

K

T

G

-

G

L

Y

F

F

G

D

A

L

K

A

P

P

A

T

K

D

G

-

Q

-

E

-

L

-

D

-

H

-

Y

-

F

L

G

G

A

E

I

N

P

C

R

R

V

-

L

-

S

-

F

-

M

-

D

D

V

I

E

V

H

L

Q

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

G

G

Q

Q

F

H

E
|
E

I

I

A
x
D

P

F

V

K

Y
|
Y

E

A

Q

G

S

A

N

V

I

R

A

S

T

C

D

D

H

D

N

I

Q

Q

M

T

V

F

M

K

T

L

T

V

L

V

K

K

S

T

V

I

A

A

K

R

K

K

H

H

G

G

M

L

A

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

L

L

S

F

C

K

S

N

G

G

H

V

G

N

S

A

L

F

F

F

D

D

P

-

G

-

E

-

N

-

P

-

T

-

E

E

N

N

A

A

Q

D

F

L

L

Q

I

L

F

S

C

E

A

T

A

A

-

K

-

H

V

F

I

I

R

A

S

G

V

I

H

V

K

K

Y

H

S

A

K

T

L

S

L

F

R

T

A

A

V

V

V

T

A

N

T

P

A

T

S

V

N

N

D

S

H

Y

R

K

-
x
R

-

L

L

V

G

P

A

G

N

Y

E
|
E

A

A

P

P

P

-

A

-

I

-

L

-

S

-

I

-

F

-

L

-

G

-

D

-

H

-

L

-

S

-

E

-

I

-

F

-

S

-

K

-

I

-

Q

-

E

-

G

-

N

-

S

-

P

-

T

-

P

-

T

-

S

-

T

-

G

C

F

Y

L

V

K

A

A

W

G

S

V

A

D

Q

T

N

L
x
R

P

S

P

P

L

L

P

I

R
|
R

D

I

A

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

-

S

-

N

-

S

D

S

P

I

A

A

A

G

N

P

P

Q

Y

V

L

A

A

I

L

N

S

T

V

M

L

I

L

A

A

D

A

S

G

L

L

D

D

Y

G

I

I

A

K

D

N

E

K

L

L

E

E

A

A

active site: E131 (= E224), E133 (= E226), E188 (= E295), E195 (= E302), H244 (= H351), R315 (≠ L454), E332 (= E478), R334 (= R480)
binding adenosine-5'-diphosphate: E131 (= E224), E183 (≠ K290), D197 (≠ A304), Y200 (= Y307), N246 (= N353), S248 (= S355), R320 (= R459), R330 (= R476)
binding magnesium ion: E131 (= E224), E131 (= E224), E133 (= E226), E188 (= E295), E195 (= E302), E195 (= E302), H244 (= H351), E332 (= E478)
binding l-methionine-s-sulfoximine phosphate: E133 (= E226), E188 (= E295), H244 (= H351), R297 (vs. gap), E303 (= E412), R315 (≠ L454), R334 (= R480)

Sites not aligning to the query:

active site: 52

4s0rD Structure of gs-tnra complex (see paper)
26% identity, 40% coverage: 220:512/728 of query aligns to 131:367/447 of 4s0rD

query
sites
4s0rD

N

N

A

L

G

G

P

P

E
|
E

Q

P

E
|
E

Y

F

F

F

L

L

-

F

-

K

I

L

D

D

R

E

N

K

F

-

A

G

R

E

P

P

D

T

L

L

Q

E

M

L

A

N

G

D

R

K

T

G

-

G

L

Y

F

F

G
x
D

A

L

K

A

P

P

A

T

K

D

G

-

Q

-

E

-

L

-

D

-

H

-

Y

-

F

L

G

G

A

E

I

N

P

C

R

R

V

-

L

-

S

-

F

-

M

-

D

D

V

I

E

V

H

L

Q

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

G

G

Q

Q

F

H

E
|
E

I

I

A

D

P

F

V

K

Y

Y

E

A

Q

G

S

A

N

V

I

R

A

S

T

C

D

D

H

D

N

I

Q

Q

M

T

V

F

M

K

T

L

T

V

L

V

K

K

S

T

V

I

A

A

K

R

K

K

H

H

G

G

M

L

A

H

C

A

L

T

L

F

H

M

E

P

K

K

P

P

F

L

A

F

G
|
G

I
x
V

N
|
N

G

G

S

S

G

G

K

M

H
|
H

L

C

N

N

Y

L

S

S

L

L

S

F

C

K

S

N

G

G

H

V

G

N

S

A

L

F

F

F

D

D

P

-

G

-

E

-

N

-

P

-

T

-

E

E

N

N

A

A

Q

D

F

L

L

Q

I

L

F

S

C

E

A

T

A

A

-

K

-

H

V

F

I

I

R

A

S

G

V

I

H

V

K

K

Y

H

S

A

K

T

L

S

L

F

R

T

A

A

V

V

V

T

A

N

T

P

A

T

S

V

N

N

D

S

H

Y

R

K

-
x
R

-

L

L

V

G

P

A
x
G

N
x
Y

E
|
E

A

A

P

P

P

-

A

-

I

-

L

-

S

-

I

-

F

-

L

-

G

-

D

-

H

-

L

-

S

-

E

-

I

-

F

-

S

-

K

-

I

-

Q

-

E

-

G

-

N

-

S

-

P

-

T

-

P

-

T

-

S

-

T

-

G

C

F

Y

L

V

K

A

A

W

G

S

V

A

D

Q

T

N

L
x
R

P

S

P

P

L

L

P

I

R

R

D

I

A

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

-

S

-

N

-

S

D

S

P

I

A

A

A

G

N

P

P

Q

Y

V

L

A

A

I

L

N

S

T

V

M

L

I

L

A

A

D

A

S

G

L

L

D

D

Y

G

I

I

A

K

D

N

E

K

L

L

E

E

A

A

active site: E135 (= E224), E137 (= E226), E192 (= E295), E199 (= E302), H248 (= H351), R319 (≠ L454), E336 (= E478), R338 (= R480)
binding glutamine: E137 (= E226), E192 (= E295), R301 (vs. gap), E307 (= E412)
binding magnesium ion: E135 (= E224), E135 (= E224), E199 (= E302), H248 (= H351), H248 (= H351), E336 (= E478)
binding : D161 (≠ G250), G241 (= G344), V242 (≠ I345), N243 (= N346), G305 (≠ A410), Y306 (≠ N411)

Sites not aligning to the query:

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

7tfaB Glutamine synthetase (see paper)
30% identity, 20% coverage: 220:366/728 of query aligns to 125:257/441 of 7tfaB

query
sites
7tfaB

N

N

A

V

G

G

P

P

E
|
E

Q

P

E
|
E

Y

F

F

F

L

L

I

F

D

K

R

T

N

D

F

-

A

-

R

-

P

-

D

-

L

-

Q

-

M

-

A

-

G

-

R

-

T

-

L

-

F

-

G

-

A

E

K

K

P

G

A

D

K

P

G

T

Q

T

E

E

L

L

D

N

D

D

H

Q

-

G

Y
|
Y

F

F

G

D

A

L

I

A

P

P

R

M

R

D

V

L

-

G

L

E

S

N

F

C

M

R

D

E

V

I

E

V

H

L

Q

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

G

G

Q

Q

F

H

E
|
E

I

I

A

D

P

F

V

K

Y

Y

E

A

Q

D

S

A

N

V

I

K

A

A

T

A

D

D

H

Q

N

I

Q

Q

M

T

V

F

M

K

T

L

T

V

L

V

K

K

S

T

V

I

A

A

K

R

K

Q

H

H

G

G

M

L

A

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

L

L

S

F

C

K

S

D

G

N

H

E

G

N

S

V

L

F

F

Y

D

D

binding glutamine: E131 (= E226), Y153 (= Y263), E186 (= E295), G238 (= G347), H242 (= H351)
binding magnesium ion: E129 (= E224), E131 (= E226), 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)
30% identity, 20% coverage: 220:366/728 of query aligns to 123:255/439 of 7tdpA

query
sites
7tdpA

N
|
N

A

V

G
|
G

P

P

E
|
E

Q

P

E
|
E

Y

F

F

F

L

L

I

F

D

K

R

T

N

D

F

-

A

-

R

-

P

-

D

-

L

-

Q

-

M

-

A

-

G

-

R

-

T

-

L

-

F

-

G

-

A

E

K

K

P

G

A

D

K

P

G

T

Q

T

E

E

L

L

D

N

D

D

H

Q

-

G

Y

Y

F

F

G

D

A

L

I

A

P

P

R

M

R

D

V

L

-

G

L

E

S

N

F

C

M

R

D

E

V

I

E

V

H

L

Q

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

G

G

Q

Q

F

H

E
|
E

I

I

A
x
D

P

F

V

K

Y
|
Y

E

A

Q

D

S

A

N

V

I

K

A

A

T

A

D

D

H

Q

N

I

Q

Q

M

T

V

F

M

K

T

L

T

V

L

V

K

K

S

T

V

I

A

A

K

R

K

Q

H

H

G

G

M

L

A

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

L

L

S

F

C

K

S

D

G

N

H

E

G

N

S

V

L

F

F

Y

D

D

binding adenosine-5'-diphosphate: N123 (= N220), G125 (= G222), E127 (= E224), E179 (≠ K290), D193 (≠ A304), Y196 (= Y307), N242 (= N353), S244 (= S355)
binding magnesium ion: E127 (= E224), E127 (= E224), E129 (= E226), E184 (= E295), E191 (= E302), E191 (= E302), H240 (= H351)
binding l-methionine-s-sulfoximine phosphate: E127 (= E224), E129 (= E226), E184 (= E295), E191 (= E302), G236 (= G347), H240 (= H351)

Sites not aligning to the query:

8tfkA Glutamine synthetase (see paper)
27% identity, 25% coverage: 220:399/728 of query aligns to 124:289/440 of 8tfkA

query
sites
8tfkA

N

N

A

V

G

G

P

P

E
|
E

Q

L

E
|
E

Y

F

F

F

L

L

I

F

D

K

R

L

N

D

F

-

A

-

R

-

P

-

D

-

L

-

Q

-

M

-

A

-

G

-

R

-

T

-

L

-

F

-

G

-

A

A

K

N

P

G

A

N

K

P

G

T

Q

T

E

E

L

L

D

T

D

D

H

Q

-

G

Y

Y

F

F

G

D

A

F

I

A

P

P

-

L

R

D

R

R

V

A

L

Q

S

D

F

V

M

R

D

D

V

I

E

D

H

Y

Q

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

G

S

Q

Q

F

H

E
|
E

I

I

A
x
D

P
x
F

V

R

Y
x
F

E

G

Q

D

S

V

N

L

I

C

A

T

T

A

D

D

H

N

N

V

Q

V

M

T

V

F

M

K

T

Y

T

V

L

V

K

K

S

S

V

I

A

A

K

Y

K

H

H

K

G

G

M

Y

A

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

L

L

S

F

C

K

S

D

G

G

H

K

G

N

S

V

L

F

F

Y

D

D

P

P

G

-

E

D

N

T

P

P

T

T

E

K

N

L

A

S

Q

Q

-

D

F

A

L

M

I

Y

F

Y

C

I

A

G

V

L

I

L

R

K

S

H

V

I

H

R

K

E

Y

F

S

T

K

A

L

V

L

T

R

N

A

P

V

V

binding adenosine-5'-diphosphate: E128 (= E224), D194 (≠ A304), F195 (≠ P305), F197 (≠ Y307), N243 (= N353)
binding magnesium ion: E128 (= E224), E128 (= E224), E130 (= E226), E185 (= E295), E192 (= E302), E192 (= E302), H241 (= H351)
binding l-methionine-s-sulfoximine phosphate: E128 (= E224), E130 (= E226), E185 (= E295), E192 (= E302), G237 (= G347), H241 (= H351)

Sites not aligning to the query:

8ooxB Glutamine synthetase (see paper)
27% identity, 25% coverage: 218:399/728 of query aligns to 121:287/438 of 8ooxB

query
sites
8ooxB

V

V

S

M

N

N

A

T

G

G

P

P

E

E

Q

M

E
|
E

Y

F

F

F

L

L

I

-

D

-

R

-

N

-

F

-

F

F

A

K

R

R

P

Q

D

D

L

-

Q

-

M

-

A

-

G

-

R

-

T

-

L

-

F

-

G

-

A

G

K

M

P

P

A

T

K

N

G

I

Q

P

E

Q

L

D

D

R

D

G

H

G

Y

Y

F

F

G

D

A

L

I

A

P

P

R

I

R

D

V

L

L

A

S

E

-

E

F

I

M

K

M

R

D

E

V

I

E

V

H

L

Q

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

G

G

Q

Q

F

H

E
|
E

I

I

A

D

P

F

V

K

Y

Y

E

D

Q

N

S

A

N

L

I

A

A

T

T

A

D

D

H

N

N

V

Q

I

M

T

V

L

M

K

T

Y

T

V

L

A

K

K

S

T

V

L

A

A

K

L

K

Q

H

H

G

G

M

L

A

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

L

L

S

F

C

K

S

D

G

G

H

K

G

N

S

A

L

F

F

Y

D

D

P

P

G

D

E

A

N

P

P

D

T

Q

E

I

N

S

A

D

Q

T

F

L

L

R

I

Y

F

F

C

V

A

G

V

V

I

L

R

K

S

H

V

I

H

R

K

A

Y

I

S

T

K

A

L

I

L

T

R

N

A

P

V

L

V

V

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

8oozA Glutamine synthetase (see paper)
27% identity, 25% coverage: 218:399/728 of query aligns to 113:279/430 of 8oozA

query
sites
8oozA

V

V

S

M

N

N

A

T

G
|
G

P

P

E
|
E

Q

M

E

E

Y

F

F

F

L

L

I

-

D

-

R

-

N

-

F

-

F

F

A

K

R

R

P

Q

D

D

L

-

Q

-

M

-

A

-

G

-

R

-

T

-

L

-

F

-

G

-

A

G

K

M

P

P

A

T

K

N

G

I

Q

P

E

Q

L

D

D

R

D

G

H

G

Y

Y

F

F

G

D

A

L

I

A

P

P

R

I

R

D

V

L

L

A

S

E

-

E

F

I

M

K

M

R

D

E

V

I

E

V

H

L

Q

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

G

G

Q

Q

F

H

E

E

I

I

A

D

P
x
F

V
x
K

Y
|
Y

E

D

Q

N

S

A

N

L

I

A

A

T

T

A

D

D

H

N

N

V

Q

I

M

T

V

L

M

K

T

Y

T

V

L

A

K

K

S

T

V

L

A

A

K

L

K

Q

H

H

G

G

M

L

A

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

L

L

S

F

C

K

S

D

G

G

H

K

G

N

S

A

L

F

F

Y

D

D

P

P

G

D

E

A

N

P

P

D

T

Q

E

I

N

S

A

D

Q

T

F

L

L

R

I

Y

F

F

C

V

A

G

V

V

I

L

R

K

S

H

V

I

H

R

K

A

Y

I

S

T

K

A

L

I

L

T

R

N

A

P

V

L

V

V

binding adenosine-5'-triphosphate: G117 (= G222), E170 (≠ K290), F185 (≠ P305), K186 (≠ V306), Y187 (= Y307), N233 (= N353), S235 (= S355)
binding magnesium ion: E119 (= E224), H231 (= H351)

Sites not aligning to the query:

8ufjB Glutamine synthetase (see paper)
28% identity, 25% coverage: 220:399/728 of query aligns to 128:293/444 of 8ufjB

query
sites
8ufjB

N

N

A

V

G

G

P

P

E
|
E

Q

L

E
|
E

Y

F

F

F

L

L

-

F

-

K

I

L

D

D

R

A

N

N

F

-

A

G

R

N

P

P

D

T

L

T

Q

E

M

L

A

T

G

D

R

Q

T

G

-

G

L

Y

F

F

G

D

A

F

K

A

P

P

A

L

K

D

-

L

G

G

Q

Q

E

D

L

V

D

-

H

-

Y

-

F

-

G

-

A

-

I

-

P

-

R

R

V

-

L

-

S

-

F

-

M

-

D

D

V

I

E

D

H

Y

Q

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

G

S

Q

Q

F

H

E
|
E

I

I

A

D

P

F

V

R

Y

F

E

G

Q

D

S

V

N

L

I

C

A

T

T

A

D

D

H

N

N

V

Q

V

M

T

V

F

M

K

T

Y

T

V

L

V

K

K

S

S

V

I

A

A

K

Y

K

H

H

K

G

G

M

Y

A

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

L

L

S

F

C

K

S

D

G

G

H

K

G

N

S

V

L

F

F

Y

D

D

P

P

G

-

E

D

N

T

P

P

T

T

E

K

N

L

A

S

Q

Q

-

D

F

A

L

M

I

Y

F

Y

C

I

A

G

V

L

I

L

R

K

S

H

V

I

H

R

K

E

Y

F

S

T

K

A

L

V

L

T

R

N

A

P

V

V

binding magnesium ion: E132 (= E224), E134 (= E226), E189 (= E295), E196 (= E302), H245 (= H351)

Sites not aligning to the query:

binding magnesium ion: 333

7cquA Gmas/adp/metsox-p complex (see paper)
26% identity, 35% coverage: 150:407/728 of query aligns to 48:286/429 of 7cquA

query
sites
7cquA

G

G

Y

F

T

A

A

A

W

W

D

L

V

D

T

M

S

S

P

P

A

A

Y

-

I

-

L

-

E

-

N

-

P

-

N

D

G

A

T

D

F

I

L

L

C

A

I

I

P

P

T

D

A

P

-

E

-

S

-

L

-

I

F

Q

I

L

S

P

W

W

K

K

G

P

E

S

A

V

L

G

D

W

K

L

K

A

T

A

P

D

L

V

L

H

R

F

A

E

N

G

Q

R

A

P

V

F

N

P

K

K

S

A

A

P

Q

R

R

V

I

A

L

L

K

K

-

S

I

V

F

L

G

A

D

R

D

A