SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing GFF5300 FitnessBrowser__WCS417:GFF5300 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.

8ooqB Glutamine synthetase from Methanothermococcus thermolithotrophicus (see paper)
29% identity, 97% coverage: 5:444/452 of query aligns to 2:439/446 of 8ooqB

query
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8ooqB

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binding 2-oxoglutaric acid: F16 (≠ E19), R18 (≠ E21), A32 (≠ I35), R86 (vs. gap), V92 (≠ T98), P169 (≠ D182), R172 (≠ F185), R173 (≠ E186), S189 (≠ L202)
binding magnesium ion: E137 (= E142), E192 (= E205), E199 (= E212)

8oooA Glutamine synthetase from methanothermococcus thermolithotrophicus in complex with 2-oxoglutarate and mgatp at 2.15 a resolution (see paper)
29% identity, 98% coverage: 3:444/452 of query aligns to 1:440/447 of 8oooA

query
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8oooA

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K

H

L

N

D

P

A

S

P

A

E

P

P

V

V

V

E

G

R

R

N

G

I

Y

F

-

A

-

M

-

S

-

E

-

A

E

E

R

K

N

E

L

L

-

G

-

I

-

E

R

S

L

V

P

P

L

A

T

N

I

L

E

K

D

A

A

A

L

L

E

D

R

E

M

L

E

E

N

N

S

N

K

D

T

V

I

L

E

K

K

N

Y

A

L

L

G

G

Q

K

K

H

F

I

I

F

T

E

G

S

Y

F

V

L

A

E

V

I

K

K

R

N

A

A

E

E

H

W

E

D

N

S

F

F

K

R

R

T

V

S

I

V

S

T

S

D

W

W

E

E

binding 2-oxoglutaric acid: F17 (≠ E19), R19 (≠ E21), A33 (≠ I35), R87 (vs. gap), V93 (≠ T98), P170 (≠ D182), R173 (≠ F185), R174 (≠ E186), S190 (≠ L202)
binding adenosine-5'-triphosphate: E136 (= E140), E188 (≠ D200), F203 (= F215), K204 (≠ R216), F205 (≠ H217), H251 (= H263), S253 (= S265), R325 (= R337), R335 (= R347)

8tfkA Glutamine synthetase (see paper)
32% identity, 81% coverage: 78:444/452 of query aligns to 64:432/440 of 8tfkA

query
sites
8tfkA

D

D

M

M

I

K

C

L

R

A

P

L

D

D

Q

P

N

S

A

T

V

F

F

R

L

I

V

L

P

P

W

W

-

R

-

P

A

A

I

T

E

G

P

A

T

V

A

A

Q

R

V

I

I

L

H

G

D

D

T

V

Y

Y

D

L

K

P

Q

D

G

G

N

N

P

P

I

F

E

K

L

G

S

D

P

P

R

R

N

Y

V

V

L

L

K

K

K

T

V

A

L

I

K

K

L

E

Y

A

A

E

D

K

K

M

G

G

W

F

Q

S

P

M

I

N

V

V

A

G

P

P

E
|
E

M

L

E
|
E

F

F

Y

F

L

L

T

F

K

K

R

-

C

-

E

-

D

-

P

-

D

-

F

-

P

-

L

-

Q

-

P

-

I

L

G

D

R

A

S

N

G

G

R

N

P

P

E

T

T

T

G

E

R

L

Q

T

S

D

-

Q

-

G

-

Y

F

F

S

D

I

F

E

A

A

P

A

L

N

D

E

R

F

A

D

Q

P

D

L

V

F

R

E

R

D

D

V

I

Y

D

D

Y

W

A

C

L

E

E

L

H

Q

M

E

G

L

F

D

Q

L

I

D

E

T

A

L

S

I

H

H

H

E
|
E

D

V

G

A

T

P

A

S

Q

Q

M

H

E
|
E

I

I

N
x
D

F
|
F

R

R

H
x
F

G

G

D

D

A

V

L

L

S

C

L

T

A

A

D

D

Q

N

I

V

L

V

V

T

F

F

K

K

R

Y

T

V

M

V

R

K

E

S

A

I

A

A

L

Y

K

H

H

K

D

G

V

Y

A

Y

A

A

T

S

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

S

H
x
N

Q

Q

S

S

I

L

I

F

D

-

I

-

A

K

T

D

G

G

K

K

N

N

V

V

F

F

S

Y

N

D

E

P

D

D

G

T

-

P

-

T

T

K

M

L

S

S

Q

Q

L

D

F

A

L

M

N

Y

H

Y

I

I

G

G

L

L

Q

L

K

K

F

H

I

I

P

R

E

E

L

F

L

T

P

A

L

V

F

T

A

N

P

P

N

V

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

V

N

Y

V

I

E

S

W

W

G

S

E

A

E

Q

N

N

R
|
R

T

S

V

S

G

L

L

I

R
|
R

V

I

P

P

D

A

A

T

G

R

P

G

Q

N

N
x
G

R

T

R
|
R

V

I

E
|
E

N

L

R
|
R

L

C

P

P

G

D

A

P

D

A

A

C

N

N

P

P

Y

Y

L

L

A

A

I

F

A

A

A

L

S

M

L

L

L

R

C

A

G

G

Y

L

I

E

G

G

M

I

V

K

E

N

G

K

H

I

N

D

P

P

S

G

A

E

P

P

-

T

-

N

-

V

-

N

-

I

-

F

-

H

V

L

V

S

G

D

R

K

G

E

Y

R

E

E

R

E

R

R

N

G

L

I

R

R

-

S

L

L

P

P

L

A

T

D

I

L

E

K

D

E

A

A

L

I

E

D

R

E

M

M

E

K

N

G

S

S

K

K

T

F

I

V

E

K

K

E

Y

A

L

L

G

G

Q

E

K

H

F

V

I

F

T

S

G

H

Y

Y

V

L

A

C

V

A

K

K

R

E

A

M

E

E

H

W

E

D

N

E

F

Y

K

K

R

A

V

V

I

V

S

H

S

P

W

W

E

E

binding adenosine-5'-diphosphate: E128 (= E140), D194 (≠ N214), F195 (= F215), F197 (≠ H217), N243 (≠ H263), R312 (= R332), R317 (= R337), G325 (≠ N345), R327 (= R347)
binding magnesium ion: E128 (= E140), E128 (= E140), E130 (= E142), E185 (= E205), E192 (= E212), E192 (= E212), H241 (= H261), E329 (= E349)
binding l-methionine-s-sulfoximine phosphate: E128 (= E140), E130 (= E142), E185 (= E205), E192 (= E212), G237 (= G257), H241 (= H261), R294 (= R314), E300 (≠ S320), R312 (= R332), R331 (= R351)

8ufjB Glutamine synthetase (see paper)
32% identity, 81% coverage: 78:444/452 of query aligns to 68:436/444 of 8ufjB

query
sites
8ufjB

D

D

M

M

I

K

C

L

R

A

P

L

D

D

Q

P

N

S

A

T

V

F

F

R

L

I

V

L

P

P

W

W

-

R

-

P

A

A

I

T

E

G

P

A

T

V

A

A

Q

R

V

I

I

L

H

G

D

D

T

V

Y

Y

D

L

K

P

Q

D

G

G

N

N

P

P

I

F

E

K

L

G

S

D

P

P

R

R

N

Y

V

V

L

L

K

K

K

T

V

A

L

I

K

K

L

E

Y

A

A

E

D

K

K

M

G

G

W

F

Q

S

P

M

I

N

V

V

A

G

P

P

E
|
E

M

L

E
|
E

F

F

Y

F

L

L

T

F

K

K

R

-

C

-

E

-

D

-

P

-

D

-

F

-

P

-

L

-

Q

-

P

-

I

L

G

D

R

A

S

N

G

G

R

N

P

P

E

T

T

T

G

E

R

L

Q

T

S

D

-

Q

-

G

-

Y

F

F

S

D

I

F

E

A

A

P

A

L

N

D

E

L

F

G

D

Q

P

D

L

V

F

R

E

R

D

D

V

I

Y

D

D

Y

W

A

C

L

E

E

L

H

Q

M

E

G

L

F

D

Q

L

I

D

E

T

A

L

S

I

H

H

H

E
|
E

D

V

G

A

T

P

A

S

Q

Q

M

H

E
|
E

I

I

N

D

F

F

R

R

H

F

G

G

D

D

A

V

L

L

S

C

L

T

A

A

D

D

Q

N

I

V

L

V

V

T

F

F

K

K

R

Y

T

V

M

V

R

K

E

S

A

I

A

A

L

Y

K

H

H

K

D

G

V

Y

A

Y

A

A

T

S

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

S

H

N

Q

Q

S

S

I

L

I

F

D

-

I

-

A

K

T

D

G

G

K

K

N

N

V

V

F

F

S

Y

N

D

E

P

D

D

G

T

-

P

-

T

T

K

M

L

S

S

Q

Q

L

D

F

A

L

M

N

Y

H

Y

I

I

G

G

L

L

Q

L

K

K

F

H

I

I

P

R

E

E

L

F

L

T

P

A

L

V

F

T

A

N

P

P

N

V

V

V

N

N

S

S

F

Y

R

K

R

R

F

L

L

V

P

P

D

G

T

Y

S

E

A

A

P

P

V

V

N

Y

V

I

E

S

W

W

G

S

E

A

E

Q

N

N

R

R

T

S

V

S

G

L

L

I

R

R

V

I

P

P

D

A

A

T

G

R

P

G

Q

N

N

G

R

T

R

R

V

I

E
|
E

N

L

R

R

L

C

P

P

G

D

A

P

D

A

A

C

N

N

P

P

Y

Y

L

L

A

A

I

F

A

A

A

L

S

M

L

L

L

R

C

A

G

G

Y

L

I

E

G

G

M

I

V

K

E

N

G

K

H

I

N

D

P

P

S

G

A

E

P

P

-

T

-

N

-

V

-

N

-

I

-

F

-

H

V

L

V

S

G

D

R

K

G

E

Y

R

E

E

R

E

R

R

N

G

L

I

R

R

-

S

L

L

P

P

L

A

T

D

I

L

E

K

D

E

A

A

L

I

E

D

R

E

M

M

E

K

N

G

S

S

K

K

T

F

I

V

E

K

K

E

Y

A

L

L

G

G

Q

E

K

H

F

V

I

F

T

S

G

H

Y

Y

V

L

A

C

V

A

K

K

R

E

A

M

E

E

H

W

E

D

N

E

F

Y

K

K

R

A

V

V

I

V

S

H

S

P

W

W

E

E

binding magnesium ion: E132 (= E140), E134 (= E142), E189 (= E205), E196 (= E212), H245 (= H261), E333 (= E349)

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

query
sites
4s0rD

D

D

M

M

I

Y

C

L

R

Y

P

P

D

D

Q

L

N

N

A

T

V

F

F

V

L

I

V

F

P

P

W

W

A

T

I

A

E

E

P

K

-

G

-

K

T

V

A

A

Q

R

V

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

A

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

L

C

D

E

E

-

K

-

G

D

E

P

P

D

T

F

L

P

E

L

L

Q

N

P

D

P

K

I

G

G

G

R

Y

S

-

G

-

R

-

P

-

E

-

T

-

G

-

R

-

Q

-

S

-

F

F

S
x
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

E

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

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
x
V

P
x
N

G

G

S

S

A

G

M

M

H
|
H

L

C

H

N

Q

L

S

S

I

L

I

F

D

-

I

-

A

K

T

N

G

G

K

V

N

N

V

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

N

H

H

F

I

I

G

A

G

G

L

I

Q

V

K

K

F

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
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

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

H

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

N

S

S

N

K

E

T

V

I

M

E

V

K

K

Y

A

L

L

G

G

Q

E

K

H

F

L

I

F

T

E

G
x
H

Y

F

V

I

A

E

V

A

K

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

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
sites
P12425

D

D

M

M

I

Y

C

L

R

Y

P

P

D

D

Q

L

N

N

A

T

V

F

F

V

L

I

V

F

P

P

W

W

A

T

I

A

E

E

P

K

-

G

-

K

T

V

A

A

Q

R

V

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

A

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

L

C

D

E

E

-

K

-

G

D

E

P

P

D

T

F

L

P

E

L

L

Q

N

P

D

P

K

I

G

G

G

R

Y

S

-

G

-

R

-

P

-

E

-

T

-

G

-

R

-

Q

-

S

-

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

E

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

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

N

Q

L

S

S

I

L

I

F

D

-

I

-

A

K

T

N

G

G

K

V

N

N

V

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

N

H

H

F

I

I

G

A

G

G

L

I

Q

V

K

K

F

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
x
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

H

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

N

S

S

N

K

E

T

V

I

M

E

V

K

K

Y

A

L

L

G

G

Q

E

K

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

E132 (= E140) binding Mg(2+)
E134 (= E142) binding Mg(2+)
E189 (= E205) binding Mg(2+)
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 Mg(2+)
G241 (= G257) binding L-glutamate
H245 (= H261) binding Mg(2+)
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 Mg(2+)
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.

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

N

N

A

T

V

F

F

V

L

I

V

F

P

P

W

W

A

T

I

A

E

E

P

K

-

G

-

K

T

V

A

A

Q

R

V

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

A

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

L

C

D

E

E

-

K

-

G

D

E

P

P

D

T

F

L

P

E

L

L

Q

N

P

D

P

K

I

G

G

G

R

Y

S

-

G

-

R

-

P

-

E

-

T

-

G

-

R

-

Q

-

S

-

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

E

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
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

I

L

I

F

D

-

I

-

A

K

T

N

G

G

K

V

N

N

V

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

N

H

H

F

I

I

G

A

G

G

L

I

Q

V

K

K

F

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

H

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

N

S

S

N

K

E

T

V

I

M

E

V

K

K

Y

A

L

L

G

G

Q

E

K

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

N

N

A

T

V

F

F

V

L

I

V

F

P

P

W

W

A

T

I

A

E

E

P

K

-

G

-

K

T

V

A

A

Q

R

V

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

A

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

L

C

D

E

E

-

K

-

G

D

E

P

P

D

T

F

L

P

E

L

L

Q

N

P

D

P

K

I

G

G

G

R

Y

S

-

G

-

R

-

P

-

E

-

T

-

G

-

R

-

Q

-

S

-

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

E

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

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

I

L

I

F

D

-

I

-

A

K

T

N

G

G

K

V

N

N

V

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

N

H

H

F

I

I

G

A

G

G

L

I

Q

V

K

K

F

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

H

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

N

S

S

N

K

E

T

V

I

M

E

V

K

K

Y

A

L

L

G

G

Q

E

K

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

8oozA Glutamine synthetase (see paper)
31% identity, 81% coverage: 78:444/452 of query aligns to 58:422/430 of 8oozA

query
sites
8oozA

D

D

M

M

I

V

C

L

R

R

P

P

D

D

Q

P

N

D

A

T

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F

F

R

L

V

V

L

P

P

W

W

A

S

I

T

E

A

P

-

T

E

A

A

Q

R

V

L

I

I

H

C

D

D

T

I

Y

E

D

L

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P

Q

D

G

G

N

K

P

P

I

F

E

M

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G

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C

P

P

R

R

N

Q

V

V

L

L

K

K

V

N

L

M

K

E

L

E

Y

A

A

A

D

K

K

L

G

G

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Y

Q

V

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M

I

N

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A
x
G

P

P

E
|
E

M

M

E

E

F

F

Y

F

L

L

T

F

K

K

R

R

C

Q

E

D

D

G

P

-

D

-

F

M

P

P

L

T

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N

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I

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I

Q

G

D

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R

S

G

G

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Y

P

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E

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T

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G

A

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Q

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F

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S

A

I

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I

A

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E

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I

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L

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-

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-

W

-

C

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-

L

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E

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D
x
E

T

A

L

A

I

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H

H

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G

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|
F

R
x
K

H
x
Y

G

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A

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A

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A

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|
H

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|
S

I

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I

F

D

K

I

-

A

-

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D

G

G

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K

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N

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A

-

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-

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Q

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L

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G

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L

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K

F

H

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I

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R

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A

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P

A

L

I

F

T

A

N

P

P

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S

S

F

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F

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A

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Y

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W

G

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E

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N

N

R

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V

S

G

L

L

I

R

R

V

V

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P

D

A

A

P

G

R

P

G

Q

N

N
x
S

R

T

R
|
R

V

I

E
|
E

N

I

R

R

L

S

P

P

G

D

A

P

D

S

A

C

N

N

P

P

Y

Y

L

L

A

A

I

F

A

A

S

I

L

L

L

A

C

A

G

G

Y

L

I

D

G

G

M

V

V

K

E

N

G

K

H

I

N

E

P

P

S

P

A

E

P

R

V

V

V

E

G

K

R

N

G

I

Y

Y

-

K

-

L

-

T

-

E

E

E

R

R

R

E

N

K

L

L

-

G

-

I

-

G

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A

A

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F

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K

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A

L

L

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G

Q

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K

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F

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G

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I

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E

binding adenosine-5'-triphosphate: G117 (≠ A138), E170 (≠ D200), F185 (= F215), K186 (≠ R216), Y187 (≠ H217), N233 (≠ H263), S235 (= S265), S315 (≠ N345), R317 (= R347)
binding magnesium ion: E119 (= E140), H231 (= H261), E319 (= E349)

8ooxB Glutamine synthetase (see paper)
31% identity, 81% coverage: 78:444/452 of query aligns to 64:430/438 of 8ooxB

query
sites
8ooxB

D

D

M

M

I

V

C

L

R

R

P

P

D

D

Q

P

N

D

A

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F

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V

L

P

P

W

W

A

S

I

G

E

N

P

T

T

A

-

E

A

A

Q

R

V

L

I

I

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C

D

D

T

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Y

E

D

L

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Q

D

G

G

N

K

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P

I

F

E

M

L

G

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C

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P

R

R

N

Q

V

V

L

L

K

K

V

N

L

M

K

E

L

E

Y

A

A

A

D

K

K

L

G

G

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Y

Q

V

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M

I

N

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T

A

G

P

P

E

E

M

M

E
|
E

F

F

Y

F

L

L

T

F

K

K

R

R

C

Q

E

D

D

G

P

-

D

-

F

M

P

P

L

T

Q

N

P

I

P

P

I

Q

G

D

R

R

S

G

G

G

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Y

P

F

E

D

T

L

G

A

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P

Q

I

S

D

F

L

S

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I

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E

E

A

I

A

K

N

R

E

E

F

I

D

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P

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L

V

F

L

E

E

D

E

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M

Y

-

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-

W

-

C

-

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-

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-

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-

E

G

L

F

D

E

L

V

D

E

T

A

L

A

I

H

H

H

E
|
E

D

V

G

A

T

F

A

G

Q

Q

M

H

E
|
E

I

I

N

D

F

F

R

K

H

Y

G

D

D

N

A

A

L

L

S

A

L

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A

A

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Q

N

I

V

L

I

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F

L

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K

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A

R

K

E

T

A

L

A

A

L

L

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

I

T

F

G

G

E

V

P

N

G

G

S

S

A

G

M

M

H

H

L

T

H

N

Q

T

S

S

I

L

I

F

D

K

I

-

A

-

T

D

G

G

K

K

N

N

V

A

F

F

S

Y

N

D

E

P

D

D

G

A

-

P

-

D

T

Q

M

I

S

S

Q

D

L

T

F

L

L

R

N

Y

H

F

I

V

G

G

L

V

Q

L

K

K

F

H

I

I

P

R

E

A

L

I

L

T

P

A

L

I

F

T

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

G

T

Y

S

E

A

A

P

P

V

V

N

Y

V

I

E

T

W

W

G

S

E

G

E

P

N

N

R

R

T

S

V

S

G

L

L

I

R

R

V

V

P

P

D

A

A

P

G

R

P

G

Q

N

N

S

R

T

R

R

V

I

E

E

N

I

R

R

L

S

P

P

G

D

A

P

D

S

A

C

N

N

P

P

Y

Y

L

L

A

A

I

F

A

A

S

I

L

L

L

A

C

A

G

G

Y

L

I

D

G

G

M

V

V

K

E

N

G

K

H

I

N

E

P

P

S

P

A

E

P

R

V

V

V

E

G

K

R

N

G

I

Y

Y

-

K

-

L

-

T

-

E

E

E

R

R

R

E

N

K

L

L

-

G

-

I

-

G

R

M

L

L

P

P

L

G

T

T

I

L

E

K

D

E

A

A

L

I

E

E

R

C

M

F

E

K

N

E

S

D

K

E

T

L

I

L

E

V

K

S

Y

A

L

L

G

G

Q

E

K

H

F

V

I

S

T

Q

G

S

Y

I

V

I

A

N

V

V

K

A

R

M

A

A

E

D

H

W

E

D

N

S

F

Y

K

R

R

T

V

Q

I

V

S

H

S

Q

W

W

E

E

binding magnesium ion: E129 (= E142), E183 (= E205), E190 (= E212)

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

N

S

A

T

V

F

F

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

Q

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

A

S

D

D