SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing 5208460 FitnessBrowser__PV4:5208460 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)
33% identity, 96% coverage: 16:446/449 of query aligns to 40:469/472 of P78061

query
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P78061

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H282 (= H257) mutation to N: Activity is impaired to 9% of wild-type.
R357 (= R333) mutation to Q: Activity is impaired to 3% of wild-type.

8oooA Glutamine synthetase from methanothermococcus thermolithotrophicus in complex with 2-oxoglutarate and mgatp at 2.15 a resolution (see paper)
28% identity, 98% coverage: 1:441/449 of query aligns to 3:440/447 of 8oooA

query
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binding 2-oxoglutaric acid: F17 (≠ E15), R19 (≠ E17), A33 (≠ I31), R87 (vs. gap), V93 (≠ T94), P170 (≠ D178), R173 (≠ F181), R174 (≠ E182), S190 (≠ L198)
binding adenosine-5'-triphosphate: E136 (= E136), E188 (≠ D196), F203 (= F211), K204 (≠ S212), F205 (≠ H213), H251 (= H259), S253 (= S261), R325 (= R333), R335 (= R343)

8ooqB Glutamine synthetase from Methanothermococcus thermolithotrophicus (see paper)
28% identity, 98% coverage: 1:441/449 of query aligns to 2:439/446 of 8ooqB

query
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8ooqB

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V

K

E

N

D

K

V

L

K

D

P

A

S

P

T

E

P

P

V

V

Q

E

-

R

-

N

-

I

-

F

-

A

-

M

G

S

R

E

A

A

N

E

E

K

N

K

R

E

Q

L

G

G

I

I

-

E

S

S

L

V

P

P

L

A

T

N

L

L

E

K

E

A

A

A

L

L

A

D

V

E

M

L

S

E

E

N

S

N

S

D

A

V

V

L

R

K

E

N

Y

A

L

L

G

G

D

K

T

H

F

I

T

F

S

E

G

S

Y

F

I

L

A

E

V

I

K

K

Q

N

A

A

D

E

L

W

E

D

N

S

F

F

R

R

R

T

V

S

I

V

S

T

S

D

W

W

E

E

binding 2-oxoglutaric acid: F16 (≠ E15), R18 (≠ E17), A32 (≠ I31), R86 (vs. gap), V92 (≠ T94), P169 (≠ D178), R172 (≠ F181), R173 (≠ E182), S189 (≠ L198)
binding magnesium ion: E137 (= E138), E192 (= E201), E199 (= E208)

8ufjB Glutamine synthetase (see paper)
33% identity, 81% coverage: 80:441/449 of query aligns to 74:436/444 of 8ufjB

query
sites
8ufjB

D

D

E

P

N

S

A

T

V

F

F

R

M

I

L

L

P

P

W

W

-

R

-

P

T

A

V

T

E

G

A

A

T

V

A

A

Q

R

V

I

I

L

H

G

D

D

T

V

F

Y

D

L

K

P

M

D

G

G

N

N

P

P

I

F

E

K

L

G

S

D

P

P

R

R

N

Y

L

V

L

L

K

K

K

T

V

A

L

I

K

K

L

E

Y

A

E

E

D

K

K

M

G

G

W

F

K

S

P

M

V

N

I

V

A

G

P

P

E
|
E

M

L

E
|
E

F

F

Y

F

L

L

T

F

H

K

R

L

N

D

S

A

D

N

P

G

D

N

M

-

P

P

L

T

I

T

P

E

P

L

V

T

G

D

R

Q

S

G

G

G

R

Y

K

F

E

D

S

F

G

A

R

P

Q

L

S

D

F

L

S

G

I

Q

D

D

A

V

A

R

N

R

E

D

Y

I

D

D

P

Y

L

A

F

L

E

E

D

H

M

M

Y

-

D

-

W

-

C

-

E

-

A

-

Q

-

G

G

L

F

D

Q

I

I

D

E

T

A

L

S

I

H

H

H

E
|
E

E

V

G

A

T

P

A

S

Q

Q

M

H

E
|
E

I

I

N

D

F

F

S

R

H

F

G

G

D

D

A

V

L

L

S

C

L

T

A

A

D

D

Q

N

V

V

F

V

V

T

F

F

K

K

R

Y

T

V

L

V

R

K

E

S

A

I

A

A

L

Y

K

H

H

K

D

G

V

Y

C

Y

A

A

T

S

F

F

M

M

A

P

K

K

P

P

V

L

T

F

D

G

E

V

P

N

G

G

S

S

A

G

M

M

H
|
H

I

S

H

N

Q

Q

S

S

V

L

V

-

D

-

I

F

K

K

T

D

G

G

K

K

N

N

I

V

F

F

T

Y

N

D

E

P

D

D

G

T

-

P

T

T

K

K

-

L

S

S

A

Q

K

D

F

A

L

M

C

Y

Y

Y

I

I

G

G

L

L

Q

L

K

K

Y

H

I

I

P

R

E

E

L

F

L

T

P

A

L

V

M

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

G

G

T

Y

S

E

A

A

P

P

V

V

N

Y

L

I

E

S

W

W

G

S

D

A

E

Q

N

N

R

R

T

S

C

S

G

L

L

I

R

R

I

I

P

P

E

A

S

T

S

R

P

G

Q

N

N

G

R

T

R

R

I

I

E
|
E

N

L

R

R

I

C

A

P

G

D

A

P

D

A

A

C

N

N

S

P

Y

Y

L

L

A

A

I

F

A

A

A

L

T

M

L

L

L

R

C

A

G

G

Y

L

M

E

G

G

M

I

V

K

E

N

D

K

V

I

K

D

P

P

S

G

T

E

P

P

-

T

-

N

-

V

-

N

-

I

-

F

-

H

V

L

Q

S

G

D

R

K

A

E

N

R

E

E

N

E

R

R

Q

G

G

I

I

R

S

S

L

L

P

P

L

A

T

D

L

L

E

K

E

E

A

A

L

I

A

D

V

E

M

M

S

K

E

G

S

S

S

K

A

F

V

V

R

K

E

E

Y

A

L

L

G

G

D

E

T

H

F

V

T

F

S

S

G

H

Y

Y

I

L

A

C

V

A

K

K

Q

E

A

M

D

E

L

W

E

D

N

E

F

Y

R

K

R

A

V

V

I

V

S

H

S

P

W

W

E

E

binding magnesium ion: E132 (= E136), E134 (= E138), E189 (= E201), E196 (= E208), H245 (= H257), E333 (= E345)

8tfkA Glutamine synthetase (see paper)
33% identity, 81% coverage: 80:441/449 of query aligns to 70:432/440 of 8tfkA

query
sites
8tfkA

D

D

E

P

N

S

A

T

V

F

F

R

M

I

L

L

P

P

W

W

-

R

-

P

T

A

V

T

E

G

A

A

T

V

A

A

Q

R

V

I

I

L

H

G

D

D

T

V

F

Y

D

L

K

P

M

D

G

G

N

N

P

P

I

F

E

K

L

G

S

D

P

P

R

R

N

Y

L

V

L

L

K

K

K

T

V

A

L

I

K

K

L

E

Y

A

E

E

D

K

K

M

G

G

W

F

K

S

P

M

V

N

I

V

A

G

P

P

E
|
E

M

L

E
|
E

F

F

Y

F

L

L

T

F

H

K

R

L

N

D

S

A

D

N

P

G

D

N

M

-

P

P

L

T

I

T

P

E

P

L

V

T

G

D

R

Q

S

G

G

G

R

Y

K

F

E

D

S

F

G

A

R

P

Q

L

S

D

F

R

S

A

I

Q

D

D

A

V

A

R

N

R

E

D

Y

I

D

D

P

Y

L

A

F

L

E

E

D

H

M

M

Y

-

D

-

W

-

C

-

E

-

A

-

Q

-

G

G

L

F

D

Q

I

I

D

E

T

A

L

S

I

H

H

H

E
|
E

E

V

G

A

T

P

A

S

Q

Q

M

H

E
|
E

I

I

N
x
D

F
|
F

S

R

H
x
F

G

G

D

D

A

V

L

L

S

C

L

T

A

A

D

D

Q

N

V

V

F

V

V

T

F

F

K

K

R

Y

T

V

L

V

R

K

E

S

A

I

A

A

L

Y

K

H

H

K

D

G

V

Y

C

Y

A

A

T

S

F

F

M

M

A

P

K

K

P

P

V

L

T

F

D

G

E

V

P

N

G
|
G

S

S

A

G

M

M

H
|
H

I

S

H
x
N

Q

Q

S

S

V

L

V

-

D

-

I

F

K

K

T

D

G

G

K

K

N

N

I

V

F

F

T

Y

N

D

E

P

D

D

G

T

-

P

T

T

K

K

-

L

S

S

A

Q

K

D

F

A

L

M

C

Y

Y

Y

I

I

G

G

L

L

Q

L

K

K

Y

H

I

I

P

R

E

E

L

F

L

T

P

A

L

V

M

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

G

G

T

Y

S
x
E

A

A

P

P

V

V

N

Y

L

I

E

S

W

W

G

S

D

A

E

Q

N

N

R
|
R

T

S

C

S

G

L

L

I

R
|
R

I

I

P

P

E

A

S

T

S

R

P

G

Q

N

N
x
G

R

T

R
|
R

I

I

E
|
E

N

L

R
|
R

I

C

A

P

G

D

A

P

D

A

A

C

N

N

S

P

Y

Y

L

L

A

A

I

F

A

A

A

L

T

M

L

L

L

R

C

A

G

G

Y

L

M

E

G

G

M

I

V

K

E

N

D

K

V

I

K

D

P

P

S

G

T

E

P

P

-

T

-

N

-

V

-

N

-

I

-

F

-

H

V

L

Q

S

G

D

R

K

A

E

N

R

E

E

N

E

R

R

Q

G

G

I

I

R

S

S

L

L

P

P

L

A

T

D

L

L

E

K

E

E

A

A

L

I

A

D

V

E

M

M

S

K

E

G

S

S

S

K

A

F

V

V

R

K

E

E

Y

A

L

L

G

G

D

E

T

H

F

V

T

F

S

S

G

H

Y

Y

I

L

A

C

V

A

K

K

Q

E

A

M

D

E

L

W

E

D

N

E

F

Y

R

K

R

A

V

V

I

V

S

H

S

P

W

W

E

E

binding adenosine-5'-diphosphate: E128 (= E136), D194 (≠ N210), F195 (= F211), F197 (≠ H213), N243 (≠ H259), R312 (= R328), R317 (= R333), G325 (≠ N341), R327 (= R343)
binding magnesium ion: E128 (= E136), E128 (= E136), E130 (= E138), E185 (= E201), E192 (= E208), E192 (= E208), H241 (= H257), E329 (= E345)
binding l-methionine-s-sulfoximine phosphate: E128 (= E136), E130 (= E138), E185 (= E201), E192 (= E208), G237 (= G253), H241 (= H257), R294 (= R310), E300 (≠ S316), R312 (= R328), R331 (= R347)

8oozA Glutamine synthetase (see paper)
32% identity, 84% coverage: 74:448/449 of query aligns to 58:429/430 of 8oozA

query
sites
8oozA

D

D

F

M

V

V

C

L

V

R

P

P

D

D

E

P

N

D

A

T

V

F

F

R

M

V

L

L

P

P

W

W

T

S

V

T

E

-

A

A

T

E

A

A

Q

R

V

L

I

I

H

C

D

D

T

I

F

E

D

L

K

P

M

D

G

G

N

K

P

P

I

F

E

M

L

G

S

C

P

P

R

R

N

Q

L

V

L

L

K

K

V

N

L

M

K

E

L

E

Y

A

E

A

D

K

K

L

G

G

W

Y

K

V

P

M

V

N

I

T

A
x
G

P

P

E
|
E

M

M

E

E

F

F

Y

F

L

L

T

F

H

K

R

R

N

Q

S

D

D

G

P

-

D

-

M

M

P

P

L

T

I

N

P

I

P

P

V

Q

G

D

R

R

S

G

G

G

R

Y

K

F

E

D

S

L

G

A

R

-

Q

-

S

-

F

-

S

P

I

I

D

D

A

L

A

A

N

E

E

E

Y

-

D

-

P

-

L

I

F

K

E

R

D

E

M

I

Y

V

D

L

W

V

C

L

E

E

A

E

Q

M

G

G

L

F

D

E

I

V

D
x
E

T

A

L

A

I

H

H

H

E

E

E

V

G

A

T

F

A

G

Q

Q

M

H

E

E

I

I

N

D

F
|
F

S
x
K

H
x
Y

G

D

D

N

A

A

L

L

S

A

L

T

A

A

D

D

Q

N

V

V

F

I

V

T

F

L

K

K

R

Y

T

V

L

A

R

K

E

T

A

L

A

A

L

L

K

Q

H

H

D

G

V

L

C

H

A

A

T

T

F

F

M

M

A

P

K

K

P

P

V

I

T

F

D

G

E

V

P

N

G

G

S

S

A

G

M

M

H
|
H

I

T

H
x
N

Q

T

S
|
S

V

L

V

-

D

-

I

F

K

K

T

D

G

G

K

K

N

N

I

A

F

F

T

Y

N

D

E

P

D

D

G

A

T

P

K

D

-

Q

-

I

S

S

A

D

K

T

F

L

L

R

C

Y

Y

F

I

V

G

G

L

V

Q

L

K

K

Y

H

I

I

P

R

E

A

L

I

L

T

P

A

L

I

M

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

G

G

T

Y

S

E

A

A

P

P

V

V

N

Y

L

I

E

T

W

W

G

S

D

G

E

P

N

N

R

R

T

S

C

S

G

L

L

I

R

R

I

V

P

P

E

A

S

P

S

R

P

G

Q

N

N
x
S

R

T

R
|
R

I

I

E
|
E

N

I

R

R

I

S

A

P

G

D

A

P

D

S

A

C

N

N

S

P

Y

Y

L

L

A

A

I

F

A

A

T

I

L

L

L

A

C

A

G

G

Y

L

M

D

G

G

M

V

V

K

E

N

D

K

V

I

K

E

P

P

S

P

T

E

P

R

V

V

Q

E

G

K

R

N

-

I

-

Y

-

K

-

L

A

T

N

E

E

E

N

E

R

R

Q

E

G

K

I

L

S

G

-

I

-

G

-

M

L

L

P

P

L

G

T

T

L

L

E

K

E

E

A

A

L

I

A

E

V

C

M

F

S

K

E

E

S

D

S

E

A

L

V

L

R

V

E

S

Y

A

L

L

G

G

D

E

T

H

F

V

T

S

S

Q

G

S

Y

I

I

I

A

N

V

V

K

A

Q

M

A

A

D

D

L

W

E

D

N

S

F

Y

R

R

R

T

V

Q

I

V

S

H

S

Q

W

W

E

E

R

L

E

D

F

R

L

Y

L

L

L

Q

T

T

binding adenosine-5'-triphosphate: G117 (≠ A134), E170 (≠ D196), F185 (= F211), K186 (≠ S212), Y187 (≠ H213), N233 (≠ H259), S235 (= S261), S315 (≠ N341), R317 (= R343)
binding magnesium ion: E119 (= E136), H231 (= H257), E319 (= E345)

8ooxB Glutamine synthetase (see paper)
31% identity, 92% coverage: 36:448/449 of query aligns to 21:437/438 of 8ooxB

query
sites
8ooxB

K

Q

F

F

I

V

D

D

E

V

K

Q

G

G

M

I

-

P

-

K

-

N

-

V

R

A

L

I

P

P

E

V

S

G

V

Q

L

L

L

E

Q

K

T

A

V

L

-

G

T

P

G

G

D

I

Y

H

V

F

D

D

D

G

D

S

L

S

Y

I

D

E

S

G

L

F

L

V

D

R

K

I

A

E

D

E

I

S

D

D

F

M

V

V

C

L

V

R

P

P

D

D

E

P

N

D

A

T

V

F

F

R

M

V

L

L

P

P

W

W

T

S

V

G

E

N

-

T

A

A

T

E

A

A

Q

R

V

L

I

I

H

C

D

D

T

I

F

E

D

L

K

P

M

D

G

G

N

K

P

P

I

F

E

M

L

G

S

C

P

P

R

R

N

Q

L

V

L

L

K

K

V

N

L

M

K

E

L

E

Y

A

E

A

D

K

K

L

G

G

W

Y

K

V

P

M

V

N

I

T

A

G

P

P

E

E

M

M

E
|
E

F

F

Y

F

L

L

T

F

H

K

R

R

N

Q

S

D

D

G

P

-

D

-

M

M

P

P

L

T

I

N

P

I

P

P

V

Q

G

D

R

R

S

G

G

G

R

Y

K

F

E

D

S

L

G

A

R

-

Q

-

S

-

F

-

S

P

I

I

D

D

A

L

A

A

N

E

E

E

Y

-

D

-

P

-

L

I

F

K

E

R

D

E

M

I

Y

V

D

L

W

V

C

L

E

E

A

E

Q

M

G

G

L

F

D

E

I

V

D

E

T

A

L

A

I

H

H

H

E
|
E

E

V

G

A

T

F

A

G

Q

Q

M

H

E
|
E

I

I

N

D

F

F

S

K

H

Y

G

D

D

N

A

A

L

L

S

A

L

T

A

A

D

D

Q

N

V

V

F

I

V

T

F

L

K

K

R

Y

T

V

L

A

R

K

E

T

A

L

A

A

L

L

K

Q

H

H

D

G

V

L

C

H

A

A

T

T

F

F

M

M

A

P

K

K

P

P

V

I

T

F

D

G

E

V

P

N

G

G

S

S

A

G

M

M

H

H

I

T

H

N

Q

T

S

S

V

L

V

-

D

-

I

F

K

K

T

D

G

G

K

K

N

N

I

A

F

F

T

Y

N

D

E

P

D

D

G

A

T

P

K

D

-

Q

-

I

S

S

A

D

K

T

F

L

L

R

C

Y

Y

F

I

V

G

G

L

V

Q

L

K

K

Y

H

I

I

P

R

E

A

L

I

L

T

P

A

L

I

M

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

G

G

T

Y

S

E

A

A

P

P

V

V

N

Y

L

I

E

T

W

W

G

S

D

G

E

P

N

N

R

R

T

S

C

S

G

L

L

I

R

R

I

V

P

P

E

A

S

P

S

R

P

G

Q

N

N

S

R

T

R

R

I

I

E

E

N

I

R

R

I

S

A

P

G

D

A

P

D

S

A

C

N

N

S

P

Y

Y

L

L

A

A

I

F

A

A

T

I

L

L

L

A

C

A

G

G

Y

L

M

D

G

G

M

V

V

K

E

N

D

K

V

I

K

E

P

P

S

P

T

E

P

R

V

V

Q

E

G

K

R

N

-

I

-

Y

-

K

-

L

A

T

N

E

E

E

N

E

R

R

Q

E

G

K

I

L

S

G

-

I

-

G

-

M

L

L

P

P

L

G

T

T

L

L

E

K

E

E

A

A

L

I

A

E

V

C

M

F

S

K

E

E

S

D

S

E

A

L

V

L

R

V

E

S

Y

A

L

L

G

G

D

E

T

H

F

V

T

S

S

Q

G

S

Y

I

I

I

A

N

V

V

K

A

Q

M

A

A

D

D

L

W

E

D

N

S

F

Y

R

R

R

T

V

Q

I

V

S

H

S

Q

W

W

E

E

R

L

E

D

F

R

L

Y

L

L

L

Q

T

T

binding magnesium ion: E129 (= E138), E183 (= E201), E190 (= E208)

7tfaB Glutamine synthetase (see paper)
31% identity, 83% coverage: 74:446/449 of query aligns to 65:438/441 of 7tfaB

query
sites
7tfaB

D

D

F

M

V

Y

C

L

V

Y

P

P

D

D

E

L

N

D

A

T

V

W

F

V

M

V

L

F

P

P

W

W

-

V

T

T

V

S

E

D

A

R

T

V

A

A

Q

R

V

L

I

I

H

C

D

D

T

I

F

Y

D

K

K

P

M

D

G

G

N

S

P

P

I

F

E

A

L

G

S

D

P

P

R

R

N

G

L

I

L

L

K

K

K

R

V

V

L

L

K

K

L

E

Y

A

E

E

D

E

K

L

G

G

W

Y

K

T

P

S

V

M

-

N

I

V

A

G

P

P

E
|
E

M

P

E
|
E

F

F

Y

F

L

L

-

F

-

K

T

T

H

D

R

E

N

K

S

G

D

D

P

P

D

T

M

T

P

E

L

L

I

N

P

-

V

-

G

-

R

-

S

-

G

-

R

-

K

-

E

-

S

-

G

-

R

-

Q

-

S

-

F

-

S

-

I

-

D

D

A

Q

A

G

N

G

E
x
Y

Y

F

D

D

P

L

L

A

F

P

E

M

D

D

M

L

Y

G

D

E

W

N

C

C

-

R

-

E

-

I

-

V

-

L

-

K

-

L

E

E

A

E

Q

M

G

G

L

F

D

E

I

I

D

E

T

A

L

S

I

H

H

H

E
|
E

E
x
V

G

A

T

P

A

G

Q

Q

M

H

E
|
E

I

I

N

D

F

F

S

K

H

Y

G

A

D

D

A

A

L

V

S

K

L

A

A

A

D

D

Q

Q

V

I

F

Q

V

T

F

F

K

K

R

L

T

V

L

V

R

K

E

T

A

I

A

A

L

R

K

Q

H

H

D

G

V

L

C

H

A

A

T

T

F

F

M

M

A

P

K

K

P

P

V

L

T

F

D

G

E

V

P
x
N

G
|
G

S

S

A

G

M

M

H
|
H

I

C

H

N

Q

Q

S

S

V

L

V

-

D

-

I

F

K

K

T

D

G

N

K

E

N

N

I

V

F

F

-

Y

-

D

-

E

T

T

N

D

E

E

D

L

G

G

-

L

T

S

K

Q

S

T

A

A

K

R

F

H

L

-

C

-

Y

Y

I

M

G

A

G

G

L

I

Q

L

K

K

Y

H

I

A

P

R

E

A

L

M

L

A

P

A

L

I

M

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

G
|
G

T
x
Y

S
x
E

A

A

P

P

V

C

N

Y

L

V

E

A

W

W

G

S

D

A

E

S

N

N

R
|
R

T

S

C

P

G

M

L

I

R

R

I

I

P

P

E

A

S

S

S

R

P

G

Q

L

N

S

R

T

R

R

I

V

E
|
E

N

V

R

R

I

N

A

P

G

D

A

P

D

A

A

A

N

N

S

P

Y

Y

L

L

A

A

I

L

A

A

A

V

T

M

L

L

L

R

C

A

G

G

Y

L

M

D

G

G

M

I

V

K

E

R

D

Q

V

M

K

A

P

L

S

P

T

A

P

P

V

I

Q

D

G

R

R

N

-

I

-

Y

-

V

-

M

A

S

N

E

E

E

N

E

R

R

-

I

-

E

Q

E

G

G

I

I

-

P

S

S

L

L

P

P

L

A

T

D

L

L

E

K

E

E

A

A

L

L

A

S

V

E

M

L

S

I

E

R

S

S

S

E

A

V

V

I

R

S

E

D

Y

A

L

L

G

G

D

D

T

H

F

A

T

L

S

A

G

Y

Y

F

I

Y

A

E

V

L

K

K

Q

E

A

I

D

E

L

W

E

D

N
x
M

F

Y

R

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 (= E138), Y153 (≠ E176), E186 (= E201), G238 (= G253), H242 (= H257), R295 (= R310), E301 (≠ S316)
binding magnesium ion: E129 (= E136), E131 (= E138), E186 (= E201), E193 (= E208), H242 (= H257), E330 (= E345)
binding : V187 (≠ E202), N237 (≠ P252), G299 (= G314), Y300 (≠ T315), R313 (= R328), M424 (≠ N432)

Sites not aligning to the query:

binding : 58, 60

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: 74:443/449 of query aligns to 66:437/443 of 4lnkA

query
sites
4lnkA

D

D

F

M

V

Y

C

L

V

Y

P

P

D

D

E

L

N

N

A

T

V

F

F

V

M

I

L

F

P

P

W

W

T

T

V

A

E

E

A

K

-

G

-

K

T

V

A

A

Q

R

V

F

I

I

H

C

D

D

T

I

F

Y

D

N

K

P

M

D

G

G

N

T

P

P

I

F

E

E

L

G

S

D

P

P

R

R

N

N

L

N

L

L

K

K

K

R

V

I

L

L

K

K

L

E

Y

M

E

E

D

D

K

L

G

G

W

F

K

S

P

D

V

F

-

N

I

L

A

G

P

P

E
|
E

M

P

E
|
E

F

F

Y

F

L

L

T

F

H

K

R

L

N

D

S

-

D

-

P

-

D

-

M

-

P

-

L

-

I

-

P

-

V

-

G

-

R

-

S

-

G

-

R

-

K

-

E

E

S

K

G

G

R

E

Q

P

S

T

F

L

S

E

I

L

-

N

D

D

A

K

A

G

N

G

E

Y

Y

F

D

D

P

L

L

A

F

P

E

T

D

D

M

L

Y

G

D

E

W

N

C

C

-

R

-

D

-

I

-

V

-

L

-

E

-

L

E

E

A

E

Q

M

G

G

L

F

D

E

I

I

D

E

T

A

L

S

I

H

H

H

E
|
E

E
x
V

G

A

T

P

A

G

Q

Q

M

H

E
|
E

I

I

N

D

F
|
F

S

K

H
x
Y

G

A

D

G

A

A

L

V

S

R

L

S

A

C

D

D

Q

D

V

I

F

Q

V

T

F

F

K

K

R

L

T

V

L

V

R

K

E

T

A

I

A

A

L

R

K

K

H

H

D

G

V

L

C

H

A

A

T

T

F

F

M

M

A

P

K

K

P

P

V

L

T

F

D

G

E

V

P
x
N

G
|
G

S

S

A
x
G

M

M

H
|
H

I

C

H
x
N

Q

L

S
|
S

V

L

V

-

D

-

I

F

K

K

T

N

G

G

K

V

N

N

I

A

F

F

T

F

N

D

E

E

D

N

G

A

-

D

-

L

-

Q

-

L

T

S

K

E

S

T

A

A

K

K

F

H

L

-

C

-

Y

F

I

I

G

A

G

G

L

I

Q

V

K

K

Y

H

I

A

P

T

E

S

L

F

L

T

P

A

L

V

M

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

G

G

T

Y

S
x
E

A

A

P

P

V

C

N

Y

L

V

E

A

W

W

G

S

D

A

E

Q

N

N

R
|
R

T

S

C

P

G

L

L

I

R

R

I

I

P

P

E

A

S
|
S

S

R

P

G

Q

I

N
x
S

R

T

R
|
R

I

V

E
|
E

N

V

R
|
R

I

S

A

V

G

D

A

P

D

A

A

A

N

N

S

P

Y

Y

L

L

A

A

I

L

A

S

A

V

T

L

L

L

L

A

C

A

G

G

Y

L

M

D

G

G

M

I

V

K

E

N

D

K

V

L

K

E

P

A

S

P

T

A

P

P

-

I

-

D

-

R

-

N

-

I

-

Y

V

V

Q

M

G

S

R

K

A

E

N

E

E

R

N

M

R

E

Q

N

G

G

I

I

-

V

S

D

L

L

P

P

L

A

T

T

L

L

E

A

E

E

A

A

L

L

A

E

V

E

M

F

S

K

E

S

S

N

S

E

A

V

V

M

R

V

E

K

Y

A

L

L

G

G

D

E

T

H

F

L

T

F

S

E

G

H

Y

F

I

I

A

E

V

A

K

K

Q

E

A

I

D

E

L

W

E

D

N

M

F

F

R

R

R

T

V

Q

I

V

S

H

S

P

W

W

E

E

R

R

E

E

active site: E131 (= E136), E133 (= E138), E188 (= E201), E195 (= E208), H244 (= H257), R315 (= R328), E332 (= E345), R334 (= R347)
binding adenosine-5'-diphosphate: F198 (= F211), Y200 (≠ H213), N246 (≠ H259), S248 (= S261), S324 (= S337), S328 (≠ N341), R330 (= R343)
binding glutamic acid: E133 (= E138), E188 (= E201), V189 (≠ E202), N239 (≠ P252), G240 (= G253), G242 (≠ A255), E303 (≠ S316)
binding magnesium ion: E131 (= E136), E188 (= E201), E195 (= E208), H244 (= H257), E332 (= E345)

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: 74:443/449 of query aligns to 66:437/443 of 4lniA

query
sites
4lniA

D

D

F

M

V

Y

C

L

V

Y

P

P

D

D

E

L

N

N

A

T

V

F

F

V

M

I

L

F

P

P

W

W

T

T

V

A

E

E

A

K

-

G

-

K

T

V

A

A

Q

R

V

F

I

I

H

C

D

D

T

I

F

Y

D

N

K

P

M

D

G

G

N

T

P

P

I

F

E

E

L

G

S

D

P

P

R

R

N

N

L

N

L

L

K

K

K

R

V

I

L

L

K

K

L

E

Y

M

E

E

D

D

K

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K

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-

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E

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E

F

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x
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S

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R

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E

active site: E131 (= E136), E133 (= E138), E188 (= E201), E195 (= E208), H244 (= H257), R315 (= R328), E332 (= E345), R334 (= R347)
binding adenosine-5'-diphosphate: E131 (= E136), E183 (≠ D196), D197 (≠ N210), Y200 (≠ H213), N246 (≠ H259), S248 (= S261), R320 (= R333), R330 (= R343)
binding magnesium ion: E131 (= E136), E131 (= E136), E133 (= E138), E188 (= E201), E195 (= E208), E195 (= E208), H244 (= H257), E332 (= E345)
binding l-methionine-s-sulfoximine phosphate: E133 (= E138), E188 (= E201), H244 (= H257), R297 (= R310), E303 (≠ S316), R315 (= R328), R334 (= R347)

Sites not aligning to the query:

active site: 52

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: 74:443/449 of query aligns to 67:438/444 of P12425

query
sites
P12425

D

D

F

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N

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P

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I

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L

L

L

L

A

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A

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A

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P

-

I

-

D

-

R

-

N

-

I

-

Y

V

V

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M

G

S

R

K

A

E

N

E

E

R

N

M

R

E

Q

N

G

G

I

I

-

V

S

D

L

L

P

P

L

A

T

T

L

L

E

A

E

E

A

A

L

L

A

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V

E

M

F

S

K

E

S

S

N

S

E

A

V

V

M

R

V

E

K

Y

A

L

L

G

G

D

E

T

H

F

L

T

F

S

E

G

H

Y

F

I

I

A

E

V

A

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K

Q

E

A

I

D
x
E

L

W

E

D

N

M

F

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R

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W

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E

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R

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E

E132 (= E136) binding Mg(2+)
E134 (= E138) binding Mg(2+)
E189 (= E201) binding Mg(2+)
V190 (≠ E202) 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 (= E208) binding Mg(2+)
G241 (= G253) binding L-glutamate
H245 (= H257) binding Mg(2+)
G302 (= G314) 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 (≠ S316) 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 (= P318) 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 (= E345) binding Mg(2+)
E424 (≠ D429) 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: 74:443/449 of query aligns to 70:441/447 of 4s0rD

query
sites
4s0rD

D

D

F

M

V

Y

C

L

V

Y

P

P

D

D

E

L

N

N

A

T

V

F

F

V

M

I

L

F

P

P

W

W

T

T

V

A

E

E

A

K

-

G

-

K