SitesBLAST

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)
26% identity, 30% coverage: 171:385/714 of query aligns to 105:323/473 of P77961

query
sites
P77961

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E134 (= E204) binding Mg(2+)
E215 (= E273) binding Mg(2+)
E223 (= E280) binding Mg(2+)

Sites not aligning to the query:

361 binding Mn(2+)

7tfaB Glutamine synthetase (see paper)
25% identity, 28% coverage: 182:379/714 of query aligns to 111:292/441 of 7tfaB

query
sites
7tfaB

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binding glutamine: E131 (= E204), Y153 (= Y241), E186 (= E273), G238 (= G325), H242 (= H329)
binding magnesium ion: E129 (= E202), E131 (= E204), E186 (= E273), E193 (= E280), H242 (= H329)
binding : V187 (= V274), N237 (= N324)

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)
25% identity, 28% coverage: 182:379/714 of query aligns to 109:290/439 of 7tdpA

query
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7tdpA

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binding adenosine-5'-diphosphate: N123 (= N196), G125 (= G200), E127 (= E202), E179 (≠ K268), D193 (≠ A282), Y196 (≠ F285), N242 (= N331), S244 (= S333)
binding magnesium ion: E127 (= E202), E127 (= E202), E129 (= E204), E184 (= E273), E191 (= E280), E191 (= E280), H240 (= H329)
binding l-methionine-s-sulfoximine phosphate: E127 (= E202), E129 (= E204), E184 (= E273), E191 (= E280), G236 (= G325), H240 (= H329)

Sites not aligning to the query:

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)
27% identity, 28% coverage: 182:379/714 of query aligns to 113:294/443 of 4lnkA

query
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4lnkA

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active site: E131 (= E202), E133 (= E204), E188 (= E273), E195 (= E280), H244 (= H329)
binding adenosine-5'-diphosphate: F198 (≠ P283), Y200 (≠ F285), N246 (= N331), S248 (= S333)
binding glutamic acid: E133 (= E204), E188 (= E273), V189 (= V274), N239 (= N324), G240 (= G325), G242 (= G327)
binding magnesium ion: E131 (= E202), E188 (= E273), E195 (= E280), H244 (= H329)

Sites not aligning to the query:

active site: 52, 315, 332, 334
binding adenosine-5'-diphosphate: 43, 50, 324, 328, 330
binding glutamic acid: 303
binding magnesium ion: 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)
27% identity, 28% coverage: 182:379/714 of query aligns to 113:294/443 of 4lniA

query
sites
4lniA

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active site: E131 (= E202), E133 (= E204), E188 (= E273), E195 (= E280), H244 (= H329)
binding adenosine-5'-diphosphate: E131 (= E202), E183 (≠ K268), D197 (≠ A282), Y200 (≠ F285), N246 (= N331), S248 (= S333)
binding magnesium ion: E131 (= E202), E131 (= E202), E133 (= E204), E188 (= E273), E195 (= E280), E195 (= E280), H244 (= H329)
binding l-methionine-s-sulfoximine phosphate: E133 (= E204), E188 (= E273), H244 (= H329)

Sites not aligning to the query:

active site: 52, 315, 332, 334
binding adenosine-5'-diphosphate: 320, 330
binding magnesium ion: 332
binding l-methionine-s-sulfoximine phosphate: 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)
27% identity, 28% coverage: 182:379/714 of query aligns to 114:295/444 of P12425

query
sites
P12425

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V

A

A

P

P

H

G

Q

Q

F

H

E
|
E

I

I

A

D

P

F

I

K

F

Y

E

A

Q

G

V

A

N

V

L

R

A

S

S

C

D

D

H

D

N

I

L

Q

L

T

V

F

M

K

E

L

V

V

M

V

R

K

K

T

V

I

A

A

D

R

K

K

K

H

G

G

F

L

A

H

L

A

L

T

L

F

F

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

N

C

N

N

W

L

S

S

I

L

G

F

I

K

D

N

G

G

G

V

M

N

N

A

L

F

D

D

P

E

G

N

D

A

T

D

P

L

E

Q

S

L

N

S

I

E

S

T

F

A

L

K

V

H

F

F

L

I

V

A

A

G

V

I

L

V

K

K

G

H

V

A

L

T

K

S

R

F

S

T

A

A

I

V

L

T

R

N

A

P

S

T

V

V

A

N

S

S

E132 (= E202) binding Mg(2+)
E134 (= E204) binding Mg(2+)
E189 (= E273) binding Mg(2+)
V190 (= V274) 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 (= E280) binding Mg(2+)
G241 (= G325) binding L-glutamate
H245 (= H329) 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.
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)
27% identity, 28% coverage: 182:379/714 of query aligns to 117:298/447 of 4s0rD

query
sites
4s0rD

R

R

L

I

L

L

D

K

T

E

I

M

G

E

I

D

T

L

G

G

V

F

T

S

K

D

V

F

N

N

T

L

Y

-

A

-

G

G

P

P

E
|
E

Q

P

E
|
E

Y

F

F

F

L

L

-

F

-

K

I

L

D

D

K

E

K

K

F

-

Y

-

A

-

Q

G

R

E

P

P

D

T

L

L

I

-

M

-

T

-

G

-

R

-

T

-

L

-

G

-

A

E

L

L

P

N

P

D

K

K

G

G

Q

G

Q

-

L

-

E

-

D

-

H

-

Y

Y

F

F

G
x
D

S

L

I

A

P

P

D

T

R

D

V

L

L

G

E

E

-

N

F

C

M

R

Q

R

E

D

V

I

E

V

E

L

E

E

L

L

F

E

L

E

L

M

G

G

I

F

P

E

A

I

K

E

T

A

R

S

H

H

N

H

E
|
E

V

V

A

A

P

P

H

G

Q

Q

F

H

E
|
E

I

I

A

D

P

F

I

K

F

Y

E

A

Q

G

V

A

N

V

L

R

A

S

S

C

D

D

H

D

N

I

L

Q

L

T

V

F

M

K

E

L

V

V

M

V

R

K

K

T

V

I

A

A

D

R

K

K

K

H

G

G

F

L

A

H

L

A

L

T

L

F

F

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

N

C

N

N

W

L

S

S

I

L

G

F

I

K

D

N

G

G

G

V

M

N

N

A

L

F

D

D

P

E

G

N

D

A

T

D

P

L

E

Q

S

L

N

S

I

E

S

T

F

A

L

K

V

H

F

F

L

I

V

A

A

G

V

I

L

V

K

K

G

H

V

A

L

T

K

S

R

F

S

T

A

A

I

V

L

T

R

N

A

P

S

T

V

V

A

N

S

S

active site: E135 (= E202), E137 (= E204), E192 (= E273), E199 (= E280), H248 (= H329)
binding glutamine: E137 (= E204), E192 (= E273)
binding magnesium ion: E135 (= E202), E135 (= E202), E199 (= E280), H248 (= H329), H248 (= H329)
binding : D161 (≠ G243), G241 (= G322), V242 (≠ I323), N243 (= N324)

Sites not aligning to the query:

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

7tf6A Glutamine synthetase (see paper)
27% identity, 28% coverage: 182:379/714 of query aligns to 108:289/438 of 7tf6A

query
sites
7tf6A

R

R

L

V

L

L

D

K

T

E

I

M

G

E

I

D

T

L

G

G

V

F

T

T

K

D

V

F

N

N

T

L

Y

-

A

-

G

G

P

P

E
|
E

Q

P

E
|
E

Y

F

F

F

L

L

I

F

D

-

K

-

F

-

Y

-

A

-

Q

-

R

-

P

-

D

-

L

-

I

-

M

-

T

-

G

-

R

-

T

-

L

-

G

-

A

K

L

L

P

D

P

E

K

K

G

G

Q

E

-

P

-

T

-

L

Q

E

L

L

E

N

D

D

H

D

-

G

Y

Y

F

F

G

D

S

L

I

A

P

P

D

T

R

D

V

L

L

G

E

E

-

N

F

C

M

R

Q

R

E

D

V

I

E

V

E

L

E

E

L

L

F

E

L

D

L

M

G

G

I

F

P

D

A

I

K

E

T

A

R

S

H

H

N

H

E
|
E

V

V

A

A

P

P

H

G

Q

Q

F

H

E
|
E

I

I

A

D

P

F

I

K

F

Y

E

A

Q

D

V

A

N

V

L

T

A

A

S

C

D

D

H

N

N

I

L

Q

L

T

V

F

M

K

E

L

V

V

M

V

R

K

K

T

V

I

A

A

D

R

K

K

K

H

G

N

F

L

A

H

L

A

L

T

L

F

F

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

N

F

N

N

W

V

S

S

I

L

G

F

I

K

D

G

G

K

G

E

M

N

N

A

L

F

D

D

P

P

G

N

D

T

T

E

P

M

E

G

S

L

N

T

I

E

S

T

F

A

L

Y

V

Q

F

F

L

T

V

A

A

G

V

V

L

L

K

K

G

N

V

A

L

R

K

G

R

F

S

T

A

A

I

V

L

C

R

N

A

P

S

L

V

V

A

N

S

S

binding glutamine: E128 (= E204), E183 (= E273), G235 (= G325), H239 (= H329)
binding magnesium ion: E126 (= E202), E128 (= E204), E183 (= E273), E190 (= E280), H239 (= H329)
binding : G232 (= G322), N234 (= N324)

Sites not aligning to the query:

binding glutamine: 292, 298
binding magnesium ion: 327
binding : 58, 60, 296, 297, 310, 367, 421, 433, 437

7tdvC Glutamine synthetase (see paper)
27% identity, 28% coverage: 182:379/714 of query aligns to 113:294/443 of 7tdvC

query
sites
7tdvC

R

R

L

V

L

L

D

K

T

E

I

M

G

E

I

D

T

L

G

G

V

F

T

T

K

D

V

F

N

N

T

L

Y

-

A

-

G
|
G

P

P

E
|
E

Q

P

E
|
E

Y

F

F

F

L

L

I

F

D

-

K

-

F

-

Y

-

A

-

Q

-

R

-

P

-

D

-

L

-

I

-

M

-

T

-

G

-

R

-

T

-

L

-

G

-

A

K

L

L

P

D

P

E

K

K

G

G

Q

E

-

P

-

T

-

L

Q

E

L

L

E

N

D

D

H

D

-

G

Y

Y

F

F

G

D

S

L

I

A

P

P

D

T

R

D

V

L

L

G

E

E

-

N

F

C

M

R

Q

R

E

D

V

I

E

V

E

L

E

E

L

L

F

E

L

D

L

M

G

G

I

F

P

D

A

I

K
x
E

T

A

R

S

H

H

N

H

E
|
E

V

V

A

A

P

P

H

G

Q

Q

F

H

E
|
E

I

I

A
x
D

P
x
F

I
x
K

F
x
Y

E

A

Q

D

V

A

N

V

L

T

A

A

S

C

D

D

H

N

N

I

L

Q

L

T

V

F

M

K

E

L

V

V

M

V

R

K

K

T

V

I

A

A

D

R

K

K

K

H

G

N

F

L

A

H

L

A

L

T

L

F

F

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

N

F

N
|
N

W
x
V

S
|
S

I

L

G

F

I

K

D

G

G

K

G

E

M

N

N

A

L

F

D

D

P

P

G

N

D

T

T

E

P

M

E

G

S

L

N

T

I

E

S

T

F

A

L

Y

V

Q

F

F

L

T

V

A

A

G

V

V

L

L

K

K

G

N

V

A

L

R

K

G

R

F

S

T

A

A

I

V

L

C

R

N

A

P

S

L

V

V

A

N

S

S

binding adenosine-5'-diphosphate: G129 (= G200), E131 (= E202), E183 (≠ K268), D197 (≠ A282), F198 (≠ P283), K199 (≠ I284),