SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing PfGW456L13_926 FitnessBrowser__pseudo13_GW456_L13:PfGW456L13_926 to proteins with known functional sites using BLASTp with E ≤ 0.001.

Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures

Found 20 (the maximum) hits to proteins with known functional sites (download)

P78061 Gamma-glutamylputrescine synthetase PuuA; Gamma-Glu-Put synthetase; Glutamate--putrescine ligase; EC 6.3.1.11 from Escherichia coli (strain K12) (see paper)
37% identity, 95% coverage: 20:449/452 of query aligns to 40:469/472 of P78061

query
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P78061

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H282 (= H261) mutation to N: Activity is impaired to 9% of wild-type.
R357 (= R337) mutation to Q: Activity is impaired to 3% of wild-type.

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)
31% identity, 82% coverage: 78:446/452 of query aligns to 67:438/444 of P12425

query
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P12425

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E132 (= E140) binding
E134 (= E142) binding
E189 (= E205) binding
V190 (≠ D206) 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 (= E212) binding
G241 (= G257) binding
H245 (= H261) binding
G302 (≠ D318) 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 (≠ S320) 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 (= P322) 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 (= E349) binding
E424 (= E432) 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
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.

4s0rD Structure of gs-tnra complex (see paper)
31% identity, 82% coverage: 78:446/452 of query aligns to 70:441/447 of 4s0rD

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K

R

E

A
x
I

E

E

H

W

E

D

N
x
M

F

F

K

R

R

T

V

Q

I

V

S

H

S

P

W

W

E

E

R

R

E

E

active site: E135 (= E140), E137 (= E142), E192 (= E205), E199 (= E212), H248 (= H261), R319 (= R332), E336 (= E349), R338 (= R351)
binding glutamine: E137 (= E142), E192 (= E205), R301 (= R314), E307 (≠ S320)
binding magnesium ion: E135 (= E140), E135 (= E140), E199 (= E212), H248 (= H261), H248 (= H261), E336 (= E349), H419 (≠ G424)
binding : D161 (≠ S174), G241 (= G254), V242 (≠ E255), N243 (≠ P256), G305 (≠ D318), Y306 (≠ T319), Y376 (= Y389), I426 (≠ A431), M430 (≠ N435)

Sites not aligning to the query:

active site: 56
binding magnesium ion: 66
binding : 63, 64, 65, 66

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)
31% identity, 82% coverage: 78:446/452 of query aligns to 66:437/443 of 4lnkA

query
sites
4lnkA

D

D

M

M

I

Y

C

L

R

Y

P

P

D

D

Q

L

S

N

A

T

V

F

Y

V

L

I

V

F

P

P

W

W

A

T

I

A

E

E

P

K

T

G

A

K

I

V

V

A

-

R

-

F

I

I

H

C

D

D

T

I

Y

Y

D

N

K

P

Q

D

G

G

N

T

P

P

I

F

E

E

L

G

S

D

P

P

R

R

N

N

V

N

L

L

K

K

K

R

V

I

L

L

K

K

L

E

Y

M

T

E

D

D

K

L

G

G

W

F

Q

S

P

D

I

F

-

N

V

L

A

G

P

P

E
|
E

M

P

E
|
E

F

F

Y

F

L

L

T

F

K

K

R

-

S

-

D

-

P

-

D

-

Y

-

P

-

L

-

Q

-

P

-

I

L

G

D

R

E

S

K

G

G

R

E

P

P

E

T

I

L

G

E

R

L

Q

N

S

-

F

-

S

-

I

-

E

D

A

K

A

G

N

G

E

Y

F

F

D

D

P

L

L

A

F

P

E

T

D

D

V

L

Y

G

D

E

W

N

C

C

-

R

-

D

-

I

-

V

-

L

E

E

L

L

Q

E

D

E

L

M

-

G

-

F

D

E

L

I

D

E

T

A

L

S

I

H

H

H

E
|
E

D
x
V

G

A

T

P

A

G

Q

Q

M

H

E
|
E

I

I

N

D

F
|
F

R

K

H
x
Y

G

A

D

G

A

A

L

V

S

R

L

S

A

C

D

D

Q

D

I

I

L

Q

V

T

F

F

K

K

R

L

T

V

M

V

R

K

E

T

A

I

A

A

L

R

K

K

H

H

D

G

V

L

A

H

A

A

T

T

F

F

M

M

A

P

K

K

P

P

M

L

T

F

G

G

E

V

P
x
N

G
|
G

S

S

A
x
G

M

M

H
|
H

L

C

H
x
N

Q

L

S
|
S

V

L

I

F

D

-

I

-

E

K

T

N

G

G

K

V

N

N

I

A

F

F

-

F

-

D

S

E

N

N

E

A

D

D

G

L

T

Q

M

L

S

S

Q

E

L

T

F

A

L

K

H

H

H

F

I

I

G

A

G

G

L

I

Q

V

K

K

L

H

I

A

P

T

E

S

L

F

L

T

P

A

L

V

F

T

A

N

P

P

N

T

V

V

N

N

S

S

F

Y

R

K

R

R

F

L

L

V

P

P

D

G

T

Y

S
x
E

A

A

P

P

V

C

N

Y

V

V

E

A

W

W

G

S

E

A

E

Q

N

N

R
|
R

T

S

V

P

G

L

L

I

R

R

V

I

P

P

D

A

A
x
S

G

R

P

G

Q

I

N
x
S

R

T

R
|
R

V

V

E
|
E

N

V

R
|
R

L

S

P

V

G

D

A

P

D

A

A

A

N

N

P

P

Y

Y

L

L

A

A

I

L

A

S

A

V

S

L

L

L

L

A

C

A

G

G

Y

L

I

D

G

G

M

I

V

K

E

N

G

K

L

L

N

E

P

A

S

P

A

A

P

P

V

I

V

D

G

R

R

N

G

I

Y

Y

-

V

-

M

-

S

-

K

-

E

-

R

-

M

E

E

R

N

R

G

N

I

L

V

R

D

L

L

P

P

L

A

T

T

I

L

E

A

D

E

A

A

L

L

E

E

R

E

M

F

E

K

H

S

S

N

S

E

T

V

I

M

E

V

K

K

Y

A

L

L

G

G

K

E

N

H

F

L

I

F

T

E

G

H

Y

F

V

I

A

E

V

A

K

K

R

E

A

I

E

E

H

W

E

D

N

M

F

F

K

R

R

T

V

Q

I

V

S

H

S

P

W

W

E

E

R

R

E

E

active site: E131 (= E140), E133 (= E142), E188 (= E205), E195 (= E212), H244 (= H261), R315 (= R332), E332 (= E349), R334 (= R351)
binding adenosine-5'-diphosphate: F198 (= F215), Y200 (≠ H217), N246 (≠ H263), S248 (= S265), S324 (≠ A341), S328 (≠ N345), R330 (= R347)
binding glutamic acid: E133 (= E142), E188 (= E205), V189 (≠ D206), N239 (≠ P256), G240 (= G257), G242 (≠ A259), E303 (≠ S320)
binding magnesium ion: E131 (= E140), E188 (= E205), E195 (= E212), H244 (= H261), E332 (= E349)

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)
31% identity, 82% coverage: 78:446/452 of query aligns to 66:437/443 of 4lniA

query
sites
4lniA

D

D

M

M

I

Y

C

L

R

Y

P

P

D

D

Q

L

S

N

A

T

V

F

Y

V

L

I

V

F

P

P

W

W

A

T

I

A

E

E

P

K

T

G

A

K

I

V

V

A

-

R

-

F

I

I

H

C

D

D

T

I

Y

Y

D

N

K

P

Q

D

G

G

N

T

P

P

I

F

E

E

L

G

S

D

P

P

R

R

N

N

V

N

L

L

K

K

K

R

V

I

L

L

K

K

L

E

Y

M

T

E

D

D

K

L

G

G

W

F

Q

S

P

D

I

F

-

N

V

L

A

G

P

P

E
|
E

M

P

E
|
E

F

F

Y

F

L

L

T

F

K

K

R

-

S

-

D

-

P

-

D

-

Y

-

P

-

L

-

Q

-

P

-

I

L

G

D

R

E

S

K

G

G

R

E

P

P

E

T

I

L

G

E

R

L

Q

N

S

-

F

-

S

-

I

-

E

D

A

K

A

G

N

G

E

Y

F

F

D

D

P

L

L

A

F

P

E

T

D

D

V

L

Y

G

D

E

W

N

C

C

-

R

-

D

-

I

-

V

-

L

E

E

L

L

Q

E

D

E

L

M

-

G

-

F

D

E

L

I

D
x
E

T

A

L

S

I

H

H

H

E
|
E

D

V

G

A

T

P

A

G

Q

Q

M

H

E
|
E

I

I

N
x
D

F

F

R

K

H
x
Y

G

A

D

G

A

A

L

V

S

R

L

S

A

C

D

D

Q

D

I

I

L

Q

V

T

F

F

K

K

R

L

T

V

M

V

R

K

E

T

A

I

A

A

L

R

K

K

H

H

D

G

V

L

A

H

A

A

T

T

F

F

M

M

A

P

K

K

P

P

M

L

T

F

G

G

E

V

P

N

G

G

S

S

A

G

M

M

H
|
H

L

C

H
x
N

Q

L

S
|
S

V

L

I

F

D

-

I

-

E

K

T

N

G

G

K

V

N

N

I

A

F

F

-

F

-

D

S

E

N

N

E

A

D

D

G

L

T

Q

M

L

S

S

Q

E

L

T

F

A

L

K

H

H

H

F

I

I

G

A

G

G

L

I

Q

V

K

K

L

H

I

A

P

T

E

S

L

F

L

T

P

A

L

V

F

T

A

N

P

P

N

T

V

V

N

N

S

S

F

Y

R

K

R
|
R

F

L

L

V

P

P

D

G

T

Y

S
x
E

A

A

P

P

V

C

N

Y

V

V

E

A

W

W

G

S

E

A

E

Q

N

N

R
|
R

T

S

V

P

G

L

L

I

R
|
R

V

I

P

P

D

A

A

S

G

R

P

G

Q

I

N

S

R

T

R
|
R

V

V

E
|
E

N

V

R
|
R

L

S

P

V

G

D

A

P

D

A

A

A

N

N

P

P

Y

Y

L

L

A

A

I

L

A

S

A

V

S

L

L

L

L

A

C

A

G

G

Y

L

I

D

G

G

M

I

V

K

E

N

G

K

L

L

N

E

P

A

S

P

A

A

P

P

V

I

V

D

G

R

R

N

G

I

Y

Y

-

V

-

M

-

S

-

K

-

E

-

R

-

M

E

E

R

N

R

G

N

I

L

V

R

D

L

L

P

P

L

A

T

T

I

L

E

A

D

E

A

A

L

L

E

E

R

E

M

F

E

K

H

S

S

N

S

E

T

V

I

M

E

V

K

K

Y

A

L

L

G

G

K

E

N

H

F

L

I

F

T

E

G

H

Y

F

V

I

A

E

V

A

K

K

R

E

A

I

E

E

H

W

E

D

N

M

F

F

K

R

R

T

V

Q

I

V

S

H

S

P

W

W

E

E

R

R

E

E

active site: E131 (= E140), E133 (= E142), E188 (= E205), E195 (= E212), H244 (= H261), R315 (= R332), E332 (= E349), R334 (= R351)
binding adenosine-5'-diphosphate: E131 (= E140), E183 (≠ D200), D197 (≠ N214), Y200 (≠ H217), N246 (≠ H263), S248 (= S265), R320 (= R337), R330 (= R347)
binding magnesium ion: E131 (= E140), E131 (= E140), E133 (= E142), E188 (= E205), E195 (= E212), E195 (= E212), H244 (= H261), E332 (= E349)
binding l-methionine-s-sulfoximine phosphate: E133 (= E142), E188 (= E205), H244 (= H261), R297 (= R314), E303 (≠ S320), R315 (= R332), R334 (= R351)

Sites not aligning to the query:

active site: 52

7tdpA Structure of paenibacillus polymyxa gs bound to met-sox-p-adp (transition state complex) to 1.98 angstom (see paper)
30% identity, 84% coverage: 71:449/452 of query aligns to 49:436/439 of 7tdpA

query
sites
7tdpA

L

M

L

F

D

D

P

G

A

S

D

S

I

I

D

E

M

G

I

Y

C

V

R

R

P

I

D

E

Q

E

S

S

A

D

V

M

Y

Y

L

L

V

Y

P

P

-

D

-

L

-

D

-

T

W

W

A

V

I

V

E

F

P

P

-

W

-

S

-

D

-

R

T

V

A

A

I

R

V

L

I

I

H

C

D

D

T

I

Y

Y

D

K

K

P

Q

D

G

G

N

S

P

P

I

F

E

A

L

G

S

D

P

P

R

R

N

G

V

I

L

L

K

K

K

R

V

V

L

L

K

K

L

E

Y

A

T

E

D

E

K

L

G

G

W

Y

Q

T

P

S

I

M

-
x
N

V

V

A
x
G

P

P

E
|
E

M

P

E
|
E

F

F

Y

F

L

L

T

F

K

K

R

-

S

T

D

D

D

E

P

K

D

G

Y

D

P

P

L

T

Q

T

P

E

P

L

I

N

G

D

R

Q

S

G

G

G

R

Y

P

F

E

D

I

L

G

A

R

P

Q

M

S

D

F

L

S

G

I

E

E

N

A

C

A

R

N

R

E

E

F

I

D

V

P

L

L

K

F

L

E

E

D

E

V

M

Y

-

D

-

W

-

C

-

E

-

L

-

Q

-

D

G

L

F

D

E

L

I

D
x
E

T

A

L

S

I

H

H

H

E
|
E

D

V

G

A

T

P

A

G

Q

Q

M

H

E
|
E

I

I

N
x
D

F

F

R

K

H
x
Y

G

A

D

D

A

A

L

V

S

K

L

A

A

A

D

D

Q

Q

I

I

L

Q

V

T

F

F

K

K

R

L

T

V

M

V

R

K

E

T

A

I

A

A

L

R

K

Q

H

H

D

G

V

L

A

H

A

A

T

T

F

F

M

M

A

P

K

K

P

P

M

L

T

F

G

G

E

V

P

N

G
|
G

S

S

A

G

M

M

H
|
H

L

C

H
x
N

Q

Q

S
|
S

V

L

I

F

D

-

I

-

E

K

T

D

G

N

K

E

N

N

I

V

F

F

S

Y

N

D

E

E

D

T

G

D

T

E

M

L

-

G

-

L

S

S

Q

Q

L

T

F

A

L

R

H

H

H

Y

I

M

G

A

G

G

L

I

Q

L

K

K

L

H

I

A

P

R

E

A

L

M

L

A

P

A

L

I

F

T

A

N

P

P

N

T

V

V

N

N

S

S

F

Y

R

K

R
|
R

F

L

L

V

P

P

D

G

T

Y

S
x
E

A

A

P

P

V

C

N

Y

V

V

E

A

W

W

G

S

E

A

E

S

N

N

R
|
R

T

S

V

P

G

M

L

I

R
|
R

V

I

P

P

D

A

A

S

G

R

P

G

Q

L

N

S

R

T

R
|
R

V

V

E
|
E

N

V

R
|
R

L

N

P

P

G

D

A

P

D

A

A

A

N

N

P

P

Y

Y

L

L

A

A

I

L

A

A

A

V

S

M

L

L

L

R

C

A

G

G

Y

L

I

D

G

G

M

I

V

K

E

R

G

Q

L

M

N

A

P

L

S

P

A

A

P

P

V

I

V

D

G

R

R

N

G

I

Y

Y

-

V

-

M

-

S

-

E

-

R

-

I

E

E

R

E

R

G

N

I

L

P

R

S

L

L

P

P

L

A

T

D

I

L

E

K

D

E

A

A

L

L

E

S

R

E

M

L

E

I

H

R

S

S

S

E

T

V

I

I

E

S

K

D

Y

A

L

L

G

G

K

D

N

H

F

A

I

L

T

A

G

Y

Y

F

V

Y

A

E

V

L

K

K

R

E

A

I

E

E

H

W

E

D

N

M

F

Y

K

R

R

T

V

Q

I

V

S

H

S

Q

W

W

E

E

R

R

E

D

F

Q

L

Y

L

L

binding adenosine-5'-diphosphate: N123 (vs. gap), G125 (≠ A138), E127 (= E140), E179 (≠ D200), D193 (≠ N214), Y196 (≠ H217), N242 (≠ H263), S244 (= S265), R316 (= R337), R326 (= R347)
binding magnesium ion: E127 (= E140), E127 (= E140), E129 (= E142), E184 (= E205), E191 (= E212), E191 (= E212), H240 (= H261), E328 (= E349)
binding l-methionine-s-sulfoximine phosphate: E127 (= E140), E129 (= E142), E184 (= E205), E191 (= E212), G236 (= G257), H240 (= H261), R293 (= R314), E299 (≠ S320), R311 (= R332), R330 (= R351)

7tfaB Glutamine synthetase (see paper)
30% identity, 84% coverage: 71:449/452 of query aligns to 49:438/441 of 7tfaB

query
sites
7tfaB

L

M

L

F

D

D

P

G

A

S

D

S

I

I

D

E

M

G

I
x
Y

C

V

R
|
R

P

I

D

E

Q

E

S

S

A

D

V

M

Y

Y

L

L

V

Y

P

P

-

D

-

L

-

D

-

T

W

W

A

V

I

V

E

F

P

P

-

W

-

V

-

T

-

S

-

D

-

R

T

V

A

A

I

R

V

L

I

I

H

C

D

D

T

I

Y

Y

D

K

K

P

Q

D

G

G

N

S

P

P

I

F

E

A

L

G

S

D

P

P

R

R

N

G

V

I

L

L

K

K

K

R

V

V

L

L

K

K

L

E

Y

A

T

E

D

E

K

L

G

G

W

Y

Q

T

P

S

I

M

-

N

V

V

A

G

P

P

E
|
E

M

P

E
|
E

F

F

Y

F

L

L

T

F

K

K

R

-

S

T

D

D

D

E

P

K

D

G

Y

D

P

P

L

T

Q

T

P

E

P

L

I

N

G

D

R

Q

S

G

G

G

R
x
Y

P

F

E

D

I

L

G

A

R

P

Q

M

S

D

F

L

S

G

I

E

E

N

A

C

A

R

N

R

E

E

F

I

D

V

P

L

L

K

F

L

E

E

D

E

V

M

Y

-

D

-

W

-

C

-

E

-

L

-

Q

-

D

G

L

F

D

E

L

I

D

E

T

A

L

S

I

H

H

H

E
|
E

D
x
V

G

A

T

P

A

G

Q

Q

M

H

E
|
E

I

I

N

D

F

F

R

K

H

Y

G

A

D

D

A

A

L

V

S

K

L

A

A

A

D

D

Q

Q

I

I

L

Q

V

T

F

F

K

K

R

L

T

V

M

V

R

K

E

T

A

I

A

A

L

R

K

Q

H

H

D

G

V

L

A

H

A

A

T

T

F

F

M

M

A

P

K

K

P

P

M

L

T

F

G

G

E

V

P
x
N

G
|
G

S

S

A

G

M

M

H
|
H

L

C

H

N

Q

Q

S

S

V

L

I

F

D

-

I

-

E

K

T

D

G

N

K

E

N

N

I

V

F

F

S

Y

N

D

E

E

D

T

G

D

T

E

M

L

-

G

-

L

S

S

Q

Q

L

T

F

A

L

R

H

H

H

Y

I

M

G

A

G

G

L

I

Q

L

K

K

L

H

I

A

P

R

E

A

L

M

L

A

P

A

L

I

F

T

A

N

P

P

N

T

V

V

N

N

S

S

F

Y

R

K

R
|
R

F

L

L

V

P

P

D
x
G

T
x
Y

S
x
E

A

A

P

P

V

C

N

Y

V

V

E

A

W

W

G

S

E

A

E

S

N

N

R
|
R

T

S

V

P

G

M

L

I

R

R

V

I

P

P

D

A

A

S

G

R

P

G

Q

L

N

S

R

T

R

R

V

V

E
|
E

N

V

R

R

L

N

P

P

G

D

A

P

D

A

A

A

N

N

P

P

Y

Y

L

L

A

A

I

L

A

A

A

V

S

M

L

L

L

R

C

A

G

G

Y

L

I

D

G

G

M

I

V

K

E

R

G

Q

L

M

N

A

P

L

S

P

A

A

P

P

V

I

V

D

G

R

R

N

G

I

Y

Y

-

V

-

M

-

S

-

E

-

R

-

I

E

E

R

E

R

G

N

I

L

P

R

S

L

L

P

P

L

A

T

D

I

L

E

K

D

E

A

A

L

L

E

S

R

E

M

L

E

I

H

R

S

S

S

E

T

V

I

I

E

S

K

D

Y

A

L

L

G

G

K

D

N

H

F

A

I

L

T

A

G

Y

Y

F

V

Y

A

E

V

L

K

K

R

E

A

I

E

E

H

W

E

D

N
x
M

F

Y

K

R

R

T

V

Q

I

V

S

H

S

Q

W

W

E

E

R

R

E

D

F

Q

L

Y

L

L

binding glutamine: E131 (= E142), Y153 (≠ R165), E186 (= E205), G238 (= G257), H242 (= H261), R295 (= R314), E301 (≠ S320)
binding magnesium ion: E129 (= E140), E131 (= E142), E186 (= E205), E193 (= E212), H242 (= H261), E330 (= E349)
binding : Y58 (≠ I80), R60 (= R82), V187 (≠ D206), N237 (≠ P256), G299 (≠ D318), Y300 (≠ T319), R313 (= R332), M424 (≠ N435)

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)
31% identity, 81% coverage: 78:444/452 of query aligns to 66:439/446 of A0R083

query
sites
A0R083

D

D

M

T

I

V

C

A

R

R

P

P

D

D

Q

P

S

S

A

T

V

F

Y

Q

L

V

V

L

P

P

W

W

A

K

I

T

E

S

P

D

-

G

-

N

-

H

-

Y

T

S

A

A

I

R

V

M

I

F

H

C

D

D

T

I

Y

T

D

M

K

P

Q

D

G

G

N

S

P

P

I

S

E

W

L

A

S

D

P

S

R

R

N

H

V

V

L

L

K

R

V

Q

L

L

K

A

L

K

Y

A

T

S

D

D

K

L

G

G

W

F

Q

T

P

C

I

Y

V

V

A

H

P

P

E

E

M

I

E

E

F

F

Y

F

L

L

T

L

K

K

R

P

S

G

D

P

D

N

P

D

D

G

Y

T

P

P

L

P

Q

E

P

P

P

-

I

-

G

-

R

-

S

-

G

-

R

-

P

-

E

-

I

A

G

D

R

N

Q

G

S

G

F

Y

S

F

I

D

E

Q

A

A

A

V

N

H

E

D

F

A

D

A

P

P

L

N

F

F

E

R

-

R

D

H

V

A

Y

I

D

E

W

A

C

L

E

E

L

Q

Q

M

D

G

L

I

D

S

L

V

D

E

T

F

L

S

I

H

H

H

E

E

D

G

G

A

T

P

A

G

Q

Q

M

Q

E

E

I

I

N

D

F

L

R

R

H

Y

G

A

D

D

A

A

L

L

S

S

L

M

A

A

D

D

Q

N

I

V

L

M

V

T

F

F

K

R

R

Y

T

L

M

V

R

K

E

E

A

V

A

A

L

L

K

A

H

D

D

G

V

V

A

R

A

A

T

S

F

F

M

M

A

P

K

K

P

P

M

F

T

A

G

E

E

H

P

P

G

G

S

S

A

A

M

M

H

H

L

T

H

H

Q

M

S

S

V

L

I

F

D

E

I

G

E

D

T

T

G

-

K

-

N

N

I

A

F

F

S

H

N

S

E

P

D

D

G

D

-

P

-

L

T

Q

M

L

S

S

Q

D

L

V

F

A

L

K

H

S

H

F

I

I

G

A

G

G

L

I

Q

L

K

E

L

H

I

A

P

N

E

E

L

I

L

S

P

A

L

V

F

T

A

N

P

Q

N

W

V

V

N

N

S

S

F

Y

R

K

R

R

F

L

L

V

P

H

D

G

T

G

S

E

A

A

P

P

V

T

N

A

V

A

E

S

W

W

G

G

E

A

N

N

R

R

T

S

V

A

G

L

L

V

R

R

V

V

P

P

D

M

A

Y

G

T

P

P

Q

H

-

K

-

V

-

S

N

S

R

R

V

V

E

E

N

V

R

R

L

S

P

P

G

D

A

S

D

A

A

C

N

N

P

P

Y

Y

L

L

A

T

I

F

A

A

A

V

S

L

L

L

L

A

C

A

G

G

Y

L

I

R

G

G

M

V

V

E

E
x
K

G

G

-

Y

-

V

L

L

N

G

P

P

S

Q

A

A

P

E

-

D

-

N

V

V

V

W

G

S

R

L

G

T

Y

Q

E

E

R

E

R

R

N

R

L

A

-

M

-

G

-

Y

-

R

R

E

L

L

P

P

L

T

T

S

I

L

E

G

D

N

A

A

L

L

E

E

R

S

M

M

E

E

H

N

S

S

S

E

T

L

I

V

E

A

K

E

Y

A

L

L

G

G

K

E

N

H

F

V

I

F

T

D

G

Y

Y

F

V

L

A

R

V

N

K

K

R

R

A

S

E

E

H

W

E

E

N

N

F

Y

K

R

R

S

V

H

I

V

S

T

S

P

W

Y

E

E

K363 (≠ E376) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)

7tenA Glutamine synthetase (see paper)
31% identity, 83% coverage: 71:446/452 of query aligns to 49:436/442 of 7tenA

query
sites
7tenA

L

M

L

F

D

D

P

G

A

S

D

S

I

I

D

E

M

G

I

F

C

V

R

R

P

I

D

E

Q

E

S

S

A

D

V

M

Y

Y

L

L

V

F

P

P

-

D

-

L

-

D

-

T

W

W

A

V

I

V

E

F

P

P

-

W

-

T

-

A

-

E

-

K

-

G

-

K

T

V

A

A

I

R

V

M

I

I

H

C

D

D

T

I

Y

Y

D

N

K

P

Q

D

G

M

N

T

P

P

I

F

E

A

L

G

S

D

P

P

R

R

N

A

V

N

L

L

K

K

K

R

V

V

L

L

K

K

L

E

Y

M

T

E

D

E

K

L

G

G

W

F

Q

T

P

E

I

F

-

N

V

L

A
x
G

P

P

E
|
E

M

P

E
|
E

F

F

Y

F

L

L

T

F

K

K

R

L

S

D

D

E

D

N

P

R

D

R

Y

P

P

T

L

L

Q

E

P

-

I

L

G

N

R

D

S

S

G

G

R

-

P

-

E

-

I

-

G

-

R

-

Q

G

S

Y

F

F

S

D

I

L

E

A

A

P

A

T

N

D

E

L

F

G

D

E

P

N

L

C

F

R

E

R

D

D

V

I

Y

V

D

L

W

E

C

L

E

E

L

E

Q

M

D

G

L

F

D

E

L

I

D
x
E

T

A

L

S

I

H

H

H

E
|
E

D

V

G

A

T

P

A

G

Q

Q

M

H

E
|
E

I

I

N
x
D

F
|
F

R
x
K

H
x
Y

G

E

D

D

A

A

L

I

S

T

L

A

A

C

D

D

Q

S

I

I

L

Q

V

T

F

F

K

K

R

L

T

V

M

V

R

K

E

T

A

I

A

A

L

R

K

K

H

H

D

G

V

L

A

H

A

A

T

T

F

F

M

M

A

P

K

K

P

P

M

L

T

F

G

G

E

V

P
x
N

G
|
G

S

S

A

G

M

M

H
|
H

L

F

H
x
N

Q

M

S
|
S

V

L

I

F

D

N

I

-

E

E

T

K

G

G

K

-

N

N

I

A

F

F

S

F

N

D

E

E

D

S

G

G

T

E

M

L

-

E

-

L

S

S

Q

Q

L

T

F

A

L

Y

H

H

H

F

I

L

G

A

G

G

L

M

Q

L

K

K

L

H

I

A

P

R

E

G

L

Y

L

T

P

A

L

V

F

T

A

N

P

P

N

T

V

I

N

N

S

S

F

F

R

K

R
|
R

F

L

L

V

P

P

D

G

T

Y

S
x
E

A

A

P

P

V

C

N

Y

V

I

E

A

W

W

G

S

E

G

E

K

N

N

R
|
R

T

S

V

P

G

L

L

V

R
|
R

V

V

P

P

D

S

A

S

G

R

P

G

Q

L

N
x
S

R

T

R
|
R

V

L

E

E

N

L

R
|
R

L

S

P

V

G

D

A

P

D

S

A

A

N

N

P

P

Y

Y

L

L

A

A

I

M

A

A

A

V

S

L

L

L

L

K

C

A

G

G

Y

L

I

S

G

G

M

I

V

K

E

D

G

E

L

L

N

T

P

P

S

P

A

A

P

P

V

V

-

D

-

R

-

N

-

I

V

Y

G

G

R

M

G

N

Y

E

E

E

R

E

R

R

N

E

L

A

R

T

-

G

-

I

-

Y

-

D

L

L

P

P

L

E

T

S

I

L

E

G

D

H

A

A

L

L

E

I

R

E

M

L

E

E

H

K

S

N

S

E

T

I

I

I

E

K

K

D

Y

G

L

L

G

G

K

E

N

H

F

I

I

F

T

E

G

H

Y

F

V

I

A

E

V

A

K

K

R

T

A

I

E

E

H

C

E

D

N

M

F

F

K

R

R

T

V

A

I

V

S

H

S

P

W

W

E

E

R

R

E

E

binding adenosine-5'-diphosphate: G128 (≠ A138), E130 (= E140), E182 (≠ D200), D196 (≠ N214), F197 (= F215), K198 (≠ R216), Y199 (≠ H217), N245 (≠ H263), S247 (= S265), R319 (= R337), S327 (≠ N345), R329 (= R347)
binding l-methionine-s-sulfoximine phosphate: E130 (= E140), E132 (= E142), E187 (= E205), E194 (= E212), N238 (≠ P256), G239 (= G257), H243 (= H261), R296 (= R314), E302 (≠ S320), R314 (= R332), R333 (= R351)

7tf9S L. Monocytogenes gs(14)-q-glnr peptide (see paper)
31% identity, 83% coverage: 71:446/452 of query aligns to 50:437/443 of 7tf9S

query
sites
7tf9S

L

M

L

F

D

D

P

G

A

S

D

S

I

I

D

E

M

G

I
x
F

C
x
V

R

R

P

I

D

E

Q

E

S

S

A

D

V

M

Y

Y

L

L

V

F

P

P

-

D

-

L

-

D

-

T

W

W

A

V

I

V

E

F

P

P

-

W

-

T

-

A

-

E

-

K

-

G

-

K

T

V

A

A

I

R

V

M

I

I

H

C

D

D

T

I

Y

Y

D

N

K

P

Q

D

G

M

N

T

P

P

I

F

E

A

L

G

S

D

P

P

R

R

N

A

V

N

L

L

K

K

K

R

V

V

L

L

K

K

L

E

Y

M

T

E

D

E

K

L

G

G

W

F

Q

T

P

E

I

F

-

N

V

L

A

G

P

P

E
|
E

M

P

E
|
E

F

F

Y

F

L

L

T

F

K

K

R

L

S

D

D

E

D

N

P

R

D

R

Y

P

P

T

L

L

Q

E

P

-

I

L

G

N

R

D

S

S

G

G

R

-

P

-

E

-

I

-

G

-

R

-

Q

G

S
x
Y

F

F

S

D

I

L

E

A

A

P

A

T

N

D

E

L

F

G

D

E

P

N

L

C

F

R

E

R

D

D

V

I

Y

V

D

L

W

E

C

L

E

E

L

E

Q

M

D

G

L

F

D

E

L

I

D

E

T

A

L

S

I

H

H

H

E
|
E

D

V

G

A

T

P

A

G

Q

Q

M

H

E
|
E

I

I

N

D

F

F

R

K

H

Y

G

E

D

D

A

A

L

I

S

T

L

A

A

C

D

D

Q

S

I

I

L

Q

V

T

F

F

K

K

R

L

T

V

M

V

R

K

E

T

A

I

A

A

L

R

K

K

H

H

D

G

V

L

A

H

A

A

T

T

F

F

M

M

A

P

K

K

P

P

M

L

T

F

G

G

E

V

P

N

G
|
G

S

S

A
x
G

M

M

H
|
H

L

F

H

N

Q

M

S

S

V

L

I

F

D

N

I

-

E

E

T

K

G

G

K

-

N

N

I

A

F

F

S

F

N

D

E

E

D

S

G

G

T

E

M

L

-

E

-

L

S

S

Q

Q

L

T

F

A

L

Y

H

H

H

F

I

L

G

A

G

G

L

M

Q

L

K

K

L

H

I

A

P

R

E

G

L

Y

L

T

P

A

L

V

F

T

A

N

P

P

N

T

V

I

N

N

S

S

F

F

R

K

R
|
R

F

L

L

V

P

P

D

G

T

Y

S
x
E

A

A

P

P

V

C

N

Y

V

I

E

A

W

W

G

S

E

G

E

K

N

N

R

R

T

S

V

P

G

L

L

V

R

R

V

V

P

P

D

S

A

S

G

R

P

G

Q

L

N

S

R

T

R

R

V

L

E
|
E

N

L

R

R

L

S

P

V

G

D

A

P

D

S

A

A

N

N

P

P

Y

Y

L

L

A

A

I

M

A

A

A

V

S

L

L

L

L

K

C

A

G

G

Y

L

I

S

G

G

M

I

V

K

E

D

G

E

L

L

N

T

P

P

S

P

A

A

P

P

V

V

-

D

-

R

-

N

-

I

V

Y

G

G

R

M

G

N

Y

E

E

E

R

E

R

R

N

E

L

A

R

T

-

G

-

I

-

Y

-

D

L

L

P

P

L

E

T

S

I

L

E

G

D

H

A

A

L

L

E

I

R

E

M

L

E

E

H

K

S

N

S

E

T

I

I

I

E

K

K

D

Y

G

L

L

G

G

K

E

N

H

F

I

I

F

T

E

G

H

Y

F

V

I

A
x
E

V

A

K

K

R

T

A
x
I

E

E

H

C

E

D

N
x
M

F

F

K

R

R

T

V

A

I

V

S

H

S

P

W

W

E

E

R

R

E

E

binding glutamine: E133 (= E142), Y155 (≠ S172), E188 (= E205), G240 (= G257), G242 (≠ A259), R297 (= R314), E303 (≠ S320)
binding magnesium ion: E131 (= E140), E133 (= E142), E188 (= E205), E195 (= E212), H244 (= H261), E332 (= E349)
binding : F59 (≠ I80), V60 (≠ C81), E418 (≠ A427), I422 (≠ A431), M426 (≠ N435)

7tf6A Glutamine synthetase (see paper)
31% identity, 83% coverage: 71:446/452 of query aligns to 49:432/438 of 7tf6A

query
sites
7tf6A

L

M

L

F

D

D

P

G

A

S

D

S

I

I

D

E

M

G

I
x
F

C

V

R
|
R

P

I

D

E

Q

E

S

S

A

D

V

M

Y

Y

L

L

V

H

P

P

-

D

-

L

-

D

-

T

W

W

A

V

I

I

E

F

P

P

-

W

-

G

-

K

T

V

A

A

I

R

V

L

I

I

H

C

D

D

T

V

Y

Y

D

K

K

T

Q

D

G

G

N

T

P

P

I

F

E

E

L

G

S

D

P

P

R

R

N

A

V

N

L

L

K

K

K

R

V

V

L

L

K

K

L

E

Y

M

T

E

D

D

K

L

G

G

W

F

Q

T

P

D

I

F

-

N

V

L

A

G

P

P

E
|
E

M

P

E
|
E

F

F

Y

F

L

L

T

F

K

K

R

-

S

-

D

-

P

-

D

-

Y

-

P

-

L

-

Q

-

P

-

I

L

G

D

R

E

S

K

G

G

R

E

P

P

E

T

I

L

G

E

R

L

Q

N

S

-

F

-

S

-

I

-

E

D

A

D

A

G

N

G

E

Y

F

F

D

D

P

L

L

A

F

P

E

T

D

D

V

L

Y

G

D

E

W

N

C

C

-

R

-

D

-

I

-

V

-

L

E

E

L

L

Q

E

D

D

L

M

-

G

-

F

D

D

L

I

D

E

T

A

L

S

I

H

H

H

E
|
E

D

V

G

A

T

P

A

G

Q

Q

M

H

E
|
E

I

I

N

D

F

F

R

K

H

Y

G

A

D

D

A

A

L

V

S

T

L

A

A

C

D

D

Q

N

I

I

L

Q

V

T

F

F

K

K

R

L

T

V

M

V

R

K

E

T

A

I

A

A

L

R

K

K

H

H

D

N

V

L

A

H

A

A

T

T

F

F

M

M

A

P

K

K

P

P

M

L

T

F

G
|
G

E

V

P
x
N

G
|
G

S

S

A

G

M

M

H
|
H

L

F

H

N

Q

V

S

S

V

L

I

F

D

K

I

G

E

K

T

E

G

N

K

A

N

F

I

F

F

D

S

P

N

N

E

T

D

E

G

M

T

G

M

L

S

T

Q

E

L

T

F

A

L

Y

H

Q

H

F

I

T

G

A

G

G

L

V

Q

L

K

K

L

N

I

A

P

R

E

G

L

F

L

T

P

A

L

V

F

C

A

N

P

P

N

L

V

V

N

N

S

S

F

Y

R

K

R
|
R

F

L

L

V

P

P

D
x
G

T
x
Y

S
x
E

A

A

P

P

V

C

N

Y

V

I

E

A

W

W

G

S

E

G

E

K

N

N

R
|
R

T

S

V

P

G

L

L

I

R

R

V

V

P

P

D

S

A

S

G

R

P

G

Q

L

N

S

R

T

R

R

V

I

E
|
E

N

V

R

R

L

S

P

V

G

D

A

P

D

A

A

A

N

N

P

P

Y

Y

L

M

A

A

I

L

A

A

S

I

L

L

L

E

C

A

G

G

Y

L

I

D

G

G

M

I

V

K

E

N

G

K

L

L

N

K

P

V

S

P

A

E

P

P

V

V

V

N

G

Q

R

N

G

I

Y
|
Y

E

E

-

M

R

N

R

R

N

E

L

E

R

R

-

E

-

A

-

V

-

G

-

I

-

Q

-

D

L

L

P

P

L

S

T

T

I

L

E

Y

D

T

A

A

L

L

E

K

R

A

M

M

E

R

H

E

S

N

S

E

T

V

I

I

E

K

K

K

Y

A

L

L

G

G

K

N

N

H

F

I

I

Y

T

N

G

Q

Y

F

V

I

A

N

V

S

K

K

R

S

A

I

E

E

H

W

E

D

N
x
Y

F

Y

K

R

R

T

V

Q

I

V

S

S

S

E

W

W

E

E

R

R

E

D

binding glutamine: E128 (= E142), E183 (= E205), G235 (= G257), H239 (= H261), R292 (= R314), E298 (≠ S320)
binding magnesium ion: E126 (= E140), E128 (= E142), E183 (= E205), E190 (= E212), H239 (= H261), E327 (= E349)
binding : F58 (≠ I80), R60 (= R82), G232 (= G254), N234 (≠ P256), G296 (≠ D318), Y297 (≠ T319), R310 (= R332), Y367 (= Y389), Y421 (≠ N435)

Sites not aligning to the query:

binding : 433, 437

5dm3C Crystal structure of glutamine synthetase from chromohalobacter salexigens dsm 3043(csal_0679, target efi-550015) with bound adp
31% identity, 81% coverage: 80:444/452 of query aligns to 55:390/396 of 5dm3C

query
sites
5dm3C

I

I

C

M

R

K

P

P

D

D

Q

L

S

A

A

T

V

L

Y

R

L

C

V

V

P

P

W

W

A

-

I

L

E

E

P

G

T

T

A

A

I

M

V

V

I

L

H

C

D

D

T

L

Y

L

D

D

K

H