SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing WP_011840249.1 NCBI__GCF_000015985.1:WP_011840249.1 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)
38% identity, 97% coverage: 13:463/464 of query aligns to 25:471/472 of P78061

query
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P78061

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H282 (= H271) mutation to N: Activity is impaired to 9% of wild-type.
R357 (= R347) mutation to Q: Activity is impaired to 3% of wild-type.

8tfkA Glutamine synthetase (see paper)
30% identity, 81% coverage: 71:445/464 of query aligns to 40:421/440 of 8tfkA

query
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8tfkA

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binding adenosine-5'-diphosphate: E128 (= E148), D194 (≠ T223), F195 (≠ L224), F197 (≠ Y226), N243 (≠ H273), R312 (= R342), R317 (= R347), G325 (≠ A355), R327 (= R357)
binding magnesium ion: E128 (= E148), E128 (= E148), E130 (= E150), E185 (= E214), E192 (= E221), E192 (= E221), H241 (= H271), E329 (= E359)
binding l-methionine-s-sulfoximine phosphate: E128 (= E148), E130 (= E150), E185 (= E214), E192 (= E221), G237 (= G267), H241 (= H271), R294 (= R324), E300 (≠ Y330), R312 (= R342), R331 (= R361)

8ufjB Glutamine synthetase (see paper)
30% identity, 81% coverage: 71:445/464 of query aligns to 44:425/444 of 8ufjB

query
sites
8ufjB

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binding magnesium ion: E132 (= E148), E134 (= E150), E189 (= E214), E196 (= E221), H245 (= H271), E333 (= E359)

8ooqB Glutamine synthetase from Methanothermococcus thermolithotrophicus (see paper)
26% identity, 84% coverage: 72:461/464 of query aligns to 47:444/446 of 8ooqB

query
sites
8ooqB

D

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T

N

G

G

L

L

I

Y

W

F

D

D

Q

G

-

S

-

I

-

E

-

G

-

F

-

V

-

G

-

I

G

N

D

E

G

S

D

D

L

M

R

M

A

L

W

K

P

P

I

D

P

L

G

S

T

T

L

F

-

S

-

V

V

L

P

P

L

W

H
x
R

G

P

T

S

T

E

P

K

P

S

R
x
V

G

A

E

R

V

V

F

I

M

C

C

D

M

V

Y

Y

D

T

L

T

D

K

G

G

R

K

P

P

M

F

S

E

S

G

D

D

P

P

R

R

H

G

A

C

L

L

A

K

R

R

Q

V

V

M

E

E

A

E

L

F

A

K

-

K

E

E

L

F

G

N

L

G

H

E

P

Y

S

F

A

V

A

G

F

P

E

E

L

P

E
|
E

F

F

L

L

A

K

N

K

E

D

R

P

G

H

P

N

D

P

G

H

R

K

V

Y

Q

I

P

P

A

A

A

D

D

D

V

-

L

-

D

-

G

-

R

-

S

-

A

-

K

-

T

G

E

G

V

Y

Y

F

S

D

V

L

D

E

H

P

L

M

H

D

G

E

M

A

M
x
P

P

D

L

I

F
x
R

S
x
R

D

D

I

I

Y

V

A

F

G

A

A

L

E

E

A

N

A

L

G

G

I

F

K

H

A

V

E

E

T

A

M
x
S

I

H

S

H

E
|
E

Y

V

A

A

P

P

G

G

Q

Q

Y

H

E
|
E

L

V

T

D

L

F

H

K

Y

F

R

-

T

D

D

D

V

A

L

L

Q

K

A

T

A

A

D

D

D

S

L

V

M

I

R

T

L

F

K

K

R

T

I

T

V

I

R

K

A

T

Q

I

A

A

R

E

R

Q

H

H

G

G

V

L

T

K

A

A

C

T

F

F

M

M

A

P

K

K

P

P

V

F

E

F

S

G

Y

M

A

N

G

G

S

S

G

G

M

M

H

H

L

C

H

H

V

Q

S

S

L

I

C

W

D

L

A

N

E

G

G

E

R

P

N

S

I

F

F

Y

V

D

E

E

E

N

T

A

E

P

G

Y

Q

Q

W

L

S

S

R

E

P

T

I

C

L

M

H

N

A

Y

L

V

G

A

G

G

L

I

R

L

E

K

T

H

M

A

G

K

E

A

S

I

M

V

L

A

V

I

F

T

A

N

P

P

H

T

A

V

N

N

S

S

W

Y

R

K

R

R

F

L

A

V

S

P

Q

G

S

Y

Y

E

A

A

P

P

V

V

S

N

P

I

S

A

W

W

G

A

V

N

N

S

N

N

R

R

S

S

V

A

A

I

L

I

R

R

I

V

P

P

A

A

G

A

D

R

I

G

R

K

A

G

R

T

R

R

I

I

E

E

H

F

R

R

P

A

A

P

G

D

V

P

D

S

A

C

N

N

P

P

Y

Y

L

L

V

A

A

F

A

T

T

V

V

M

L

L

A

A

G

A

I

G

R

L

R

D

G

G

L

V

E

K

Q

N

Q

K

I

L

D

D

P

A

G

P

P

E

E

P

T

V

T

E

G

R

N

N

G

I

Y

F

-

A

-

M

-

S

-

E

-

A

-

E

E

K

D

K

P

E

G

L

D

G

T

I

Q

E

P

S

I

V

P

P

T

A

C

N

W

L

R

K

S

A

A

A

I

L

A

D

A

E

A

L

Q

E

H

N

S

N

A

D

F

V

L

L

R

K

E

N

A

A

L

L

G

G

P

K

D

H

M

I

H

F

R

E

T

S

F

F

T

L

A

E

I

I

K

K

A

N

A

A

E

E

Y

W

A

D

R

S

V

F

A

R

R

T

T

S

I

V

P

T

D

D

V

W

D

E

Y

T

D

T

L

A

Y

Y

L

L

binding 2-oxoglutaric acid: R86 (≠ H100), V92 (≠ R106), P169 (≠ M191), R172 (≠ F194), R173 (≠ S195), S189 (≠ M211)
binding magnesium ion: E137 (= E150), E192 (= E214), E199 (= E221)

Sites not aligning to the query:

binding 2-oxoglutaric acid: 16, 18, 32

8oooA Glutamine synthetase from methanothermococcus thermolithotrophicus in complex with 2-oxoglutarate and mgatp at 2.15 a resolution (see paper)
26% identity, 84% coverage: 72:461/464 of query aligns to 48:445/447 of 8oooA

query
sites
8oooA

D

D

V

V

H

L

E

E

T

N

G

G

L

L

I

Y

W

F

D

D

Q

G

-

S

-

I

-

E

-

G

-

F

-

V

-

G

-

I

G

N

D

E

G

S

D

D

L

M

R

M

A

L

W

K

P

P

I

D

P

L

G

S

T

T

L

F

-

S

-

V

V

L

P

P

L

W

H
x
R

G

P

T

S

T

E

P

K

P

S

R
x
V

G

A

E

R

V

V

F

I

M

C

C

D

M

V

Y

Y

D

T

L

T

D

K

G

G

R

K

P

P

M

F

S

E

S

G

D

D

P

P

R

R

H

G

A

C

L

L

A

K

R

R

Q

V

V

M

E

E

A

E

L

F

A

K

-

K

E

E

L

F

G

N

L

G

H

E

P

Y

S

F

A

V

A

G

F

P

E
|
E

L

P

E

E

F

F

L

L

A

K

N

K

E

D

R

P

G

H

P

N

D

P

G

H

R

K

V

Y

Q

I

P

P

A

A

A

D

D

D

V

-

L

-

D

-

G

-

R

-

S

-

A

-

K

-

T

G

E

G

V

Y

Y

F

S

D

V

L

D

E

H

P

L

M

H

D

G

E

M

A

M
x
P

P

D

L

I

F
x
R

S
x
R

D

D

I

I

Y

V

A

F

G

A

A

L

E

E

A

N

A

L

G

G

I

F

K

H

A

V

E
|
E

T

A

M
x
S

I

H

S

H

E

E

Y

V

A

A

P

P

G

G

Q

Q

Y

H

E

E

L

V

T

D

L
x
F

H
x
K

Y
x
F

R

-

T

D

D

D

V

A

L

L

Q

K

A

T

A

A

D

D

D

S

L

V

M

I

R

T

L

F

K

K

R

T

I

T

V

I

R

K

A

T

Q

I

A

A

R

E

R

Q

H

H

G

G

V

L

T

K

A

A

C

T

F

F

M

M

A

P

K

K

P

P

V

F

E

F

S

G

Y

M

A

N

G

G

S

S

G

G

M

M

H

H

L

C

H
|
H

V

Q

S
|
S

L

I

C

W

D

L

A

N

E

G

G

E

R

P

N

S

I

F

F

Y

V

D

E

E

E

N

T

A

E

P

G

Y

Q

Q

W

L

S

S

R

E

P

T

I

C

L

M

H

N

A

Y

L

V

G

A

G

G

L

I

R

L

E

K

T

H

M

A

G

K

E

A

S

I

M

V

L

A

V

I

F

T

A

N

P

P

H

T

A

V

N

N

S

S

W

Y

R

K

R

R

F

L

A

V

S

P

Q

G

S

Y

Y

E

A

A

P

P

V

V

S

N

P

I

S

A

W

W

G

A

V

N

N

S

N

N

R

R

S

S

V

A

A

I

L

I

R
|
R

I

V

P

P

A

A

G

A

D

R

I

G

R

K

A

G

R

T

R
|
R

I

I

E

E

H

F

R

R

P

A

A

P

G

D

V

P

D

S

A

C

N

N

P

P

Y

Y

L

L

V

A

A

F

A

T

T

V

V

M

L

L

A

A

G

A

I

G

R

L

R

D

G

G

L

V

E

K

Q

N

Q

K

I

L

D

D

P

A

G

P

P

E

E

P

T

V

T

E

G

R

N

N

G

I

Y

F

-

A

-

M

-

S

-

E

-

A

-

E

E

K

D

K

P

E

G

L

D

G

T

I

Q

E

P

S

I

V

P

P

T

A

C

N

W

L

R

K

S

A

A

A

I

L

A

D

A

E

A

L

Q

E

H

N

S

N

A

D

F

V

L

L

R

K

E

N

A

A

L

L

G

G

P

K

D

H

M

I

H

F

R

E

T

S

F

F

T

L

A

E

I

I

K

K

A

N

A

A

E

E

Y

W

A

D

R

S

V

F

A

R

R

T

T

S

I

V

P

T

D

D

V

W

D

E

Y

T

D

T

L

A

Y

Y

L

L

binding 2-oxoglutaric acid: R87 (≠ H100), V93 (≠ R106), P170 (≠ M191), R173 (≠ F194), R174 (≠ S195), S190 (≠ M211)
binding adenosine-5'-triphosphate: E136 (= E148), E188 (= E209), F203 (≠ L224), K204 (≠ H225), F205 (≠ Y226), H251 (= H273), S253 (= S275), R325 (= R347), R335 (= R357)

Sites not aligning to the query:

binding 2-oxoglutaric acid: 17, 19, 33

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)
30% identity, 74% coverage: 117:461/464 of query aligns to 101:444/446 of A0R083

query
sites
A0R083

D

D

G

G

R

S

P

P

M

S

S

W

S

A

D

D

P

S

R

R

H

H

A

V

L

L

A

R

R

R

Q

Q

V

L

E

A

A

K

L

A

A

S

E

D

L

L

G

G

L

F

H

T

P

C

S

Y

A

V

A

H

F

P

E

E

L

I

E

E

F

F

L

L

A

-

N

-

E

K

R

P

G

G

P

P

D

N

G

D

R

G

V

T

Q

P

P

P

A

-

D

-

V

-

L

-

D

-

G

-

R

-

R

E

S

P

A

A

K

D

T

N

E

G

V

G

Y

Y

S

F

V

D

D

Q

H

A

L

V

H

H

G

D

M

A

P

P

L

N

F

F

S

R

-

R

D

H

I

A

Y

I

A

E

G

A

A

L

E

E

A

Q

A

M

G

G

I

I

K

S

A

V

E

E

T

F

M

S

I

H

S

H

E

E

Y

G

A

A

P

P

G

G

Q

Q

Y

Q

E

E

L

I

T

D

L

L

H

R

Y

Y

R

-

T

A

D

D

V

A

L

L

Q

S

A

M

A

A

D

D

D

N

L

V

M

M

R

T

L

F

K

R

R

Y

I

L

V

V

R

K

A

E

Q

V

A

A

R

L

R

A

H

D

G

G

V

V

T

R

A

A

C

S

F

F

M

M

A

P

K

K

P

P

V

F

E

A

S

E

Y

H

A

P

G

G

S

S

G

A

M

M

H

H

L

T

H

H

V

M

S

S

L

L

C

F

D

E

A

G

E

D

G

T

R

N

N

A

I

F

F

H

V

S

E

P

E

D

T

D

E

P

G

L

Q

Q

W

L

S

S

R

D

P

V

I

A

L

K

H

S

A

F

L

I

G

A

G

G

L

I

R

L

E

E

T

H

M

A

G

N

E

E

S

I

M

S

L

A

V

V

F

T

A

N

P

Q

H

W

A

V

N

N

S

S

W

Y

R

K

R

R

F

L

A

V

S

H

Q

G

S

G

Y

E

A

A

P

P

V

T

S

A

P

A

S

S

W

W

G

G

V

A

N

A

N

N

R

R

S

S

V

A

A

L

L

V

R

R

I

V

P

P

A

M

-

Y

-

T

-

P

G

H

D

K

I

V

R

S

A

S

R

R

I

V

E

E

H

V

R

R

P

S

A

P

G

D

V

S

D

A

A

C

N

N

P

P

Y

Y

L

L

V

T

A

F

A

A

T

V

V

L

L

L

A

A

G

A

I

G

R

L

R

R

G

G

L

V

E

E

Q
x
K

Q

G

I

Y

D

V

P

L

G

G

P

P

E

Q

T

A

T

E

G

D

N

N

G

V

Y

W

E

S

D

L

P

T

G

Q

D

E

T

E

-

R

-

A

-

M

-

G

-

Y

Q

R

P

E

I

L

P

P

T

T

C

S

W

L

R

G

S

N

A

A

I

L

A

E

A

S

A

M

Q

E

H

N

S

S

A

E

F

L

L

V

R

A

E

E

A

A

L

L

G

G

P

E

D

H

M

V

H

F

R

D

T

Y

F

F

T

L

A

R

I

N

K

K

A

R

A

S

E

E

Y

W

A

E

R

N

V

Y

A

R

R

S

T

H

I

V

P

T

D

P

V

Y

D

E

Y

L

D

K

L

N

Y

Y

L

L

K363 (≠ Q386) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)

8ooxB Glutamine synthetase (see paper)
28% identity, 83% coverage: 81:463/464 of query aligns to 61:437/438 of 8ooxB

query
sites
8ooxB

D

E

Q

E

G

S

D

D

G

M

D

V

L

L

R

R

A

P

W

D

P

P

I

D

P

T

G

F

T

R

L

V

V

L

P

P

L

W

H

S

G

G

T

N

T

T

P

A

P

E

R

A

G

R

E

-

V

-

F

L

M

I

C

C

M

D

Y

I

D

E

L

L

-

P

D

D

G

G

R

K

P

P

M

F

S

M

S

G

D

C

P

P

R

R

H

Q

A

V

L

L

A

K

R

K

Q

N

V

M

E

E

A

E

L

A

A

A

E

K

L

L

G

G

L

Y

H

V

P

M

S

N

A

T

A

G

F

P

E

E

L

M

E
|
E

F

F

L

L

L

F

A

K

N

R

E

Q

R

D

G

G

P

-

D

-

G

-

R

-

V

-

Q

M

P

P

A

T

A

N

D

I

V

P

L

Q

D

D

G

-

R

-

R

R

S

G

A

G

K

Y

T

F

E

D

V

L

Y

A

S

P

V

I

D

D

H

L

L

A

H

E

G

E

M

I

M

K

P

-

L

-

F

-

S

R

D

E

I

I

Y

V

A

L

G

V

A

L

E

E

A

E

A

M

G

G

I

F

K

E

A

V

E

E

T

A

M

A

I

H

S

H

E
|
E

Y

V

A

A

P

F

G

G

Q

Q

Y

H

E
|
E

L

I

T

D

L

F

H

K

Y

Y

R

-

T

D

D

N

V

A

L

L

Q

A

A

T

A

A

D

D

D

N

L

V

M

I

R

T

L

L

K

K

R

Y

I

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V

A

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K

A

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Q

L

A

A

R

L

R

Q

H

H

G

G

V

L

T

H

A

A

C

T

F

F

M

M

A

P

K

K

P

P

V

I

E

F

S

G

Y

V

A

N

G

G

S

S

G

G

M

M

H

H

L

T

H

N

V

T

S

S

L

L

C

F

D

-

A

K

E

D

G

G

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K

N

N

I

A

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Y

E

D

-

P

E

D

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A

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D

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Q

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T

I

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L

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A

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K

T

H

M

I

G

R

E

A

S

I

M

T

L

A

V

I

F

T

A

N

P

P

H

L

A

V

N

N

S

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W

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R

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R

R

F

L

A

V

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Q

G

S

Y

Y

E

A

A

P

P

V

V

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Y

P

I

S

T

W

W

G

S

V

G

N

P

N

N

R

R

S

S

V

S

A

L

L

I

R

R

I

V

P

P

A

A

G

P

D

R

I

G

R

N

A

S

R

T

R

R

I

I

E

E

H

I

R

R

P

S

A

P

G

D

V

P

D

S

A

C

N

N

P

P

Y

Y

L

L

V

A

A

F

A

A

T

A

V

I

L

L

A

A

G

A

I

G

R

L

R

D

G

G

L

V

E

K

Q

N

Q

K

I

I

D

E

P

P

G

P

P

E

E

R

T

V

T

E

G

K

N

N

G

I

Y

Y

E

K

D

L

P

T

G

E

D

E

T

E

Q

R

P

E

-

K

-

L

-

G

-

I

-

G

-

M

I

L

P

P

T

G

C

T

W

L

R

K

S

E

A

A

I

I

A

E

A

C

A

F

Q

K

H

E

S

D

A

E

F

L

L

L

R

V

E

S

A

A

L

L

G

G

P

E

D

H

M

V

H

S

R

Q

T

S

F

I

T

I

A

N

I

V

K

A

A

M

A

A

E

D

Y

W

A

D

R

S

V

Y

A

R

R

T

T

Q

I

V

P

H

D

Q

V

W

D

E

Y

L

D

D

L

R

Y

Y

L

L

H

Q

T

T

binding magnesium ion: E129 (= E150), E183 (= E214), E190 (= E221)

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)
28% identity, 78% coverage: 84:445/464 of query aligns to 65:425/444 of P12425

query
sites
P12425

D

E

G

S

D

D

L

M

R

Y

A

L

W

Y

P

P

I

D

P

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-

L

I

H

F

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P

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W

T

T

P

A

P

E

R

K

G

G

E

K

V

V

-

A

-

R

F

F

M

I

C

C

-

D

M

I

Y

Y

D

N

L

P

D

D

G

G

R

T

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P

M

F

S

E

S

G

D

D

P

P

R

R

H

N

A

N

L

L

A

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R

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Q

I

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L

E

K

A

E

L

M

A

E

E

D

L

L

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G

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D

-

F

S

N

A

L

A

G

F

P

E
|
E

L

P

E
|
E

F

F

L

L

L

F

A

K

-

L

N

D

E

E

R

K

G

G

P

-

D

-

G

-

R

-

V

-

Q

E

P

P

A

T

A

L

D

E

V

L

L

N

D

D

G

-

R

-

R

K

S

G

A

G

K

Y

T

F

E

D

V

L

Y

A

S

P

V

T

D

D

H

L

L

G

H

E

G

N

M

C

M

R

P

-

L

-

F

-

S

R

D

D

I

I

Y

V

A

L

G

E

A

L

E

E

A

E

A

M

G

G

I

F

K

E

A

I

E

E

T

A

M

S

I

H

S

H

E
|
E

Y
x
V

A

A

P

P

G

G

Q

Q

Y

H

E
|
E

L

I

T

D

L

F

H

K

Y

Y

R

-

T

A

D

G

V

A

L

V

Q

R

A

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A

C

D

D

L

I

M

Q

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T

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F

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K

R

L

I

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V

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A

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Q

I

A

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R

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R

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H

H

G

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V

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T

H

A

A

C

T

F

F

M

M

A

P

K

K

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P

V

L

E

F

S

G

Y

V

A

N

G
|
G

S

S

G

G

M

M

H
|
H

L

C

H

N

V

L

S

S

L

L

C

F

D

K

A

N

E

G

G

V

R

N

N

A

I

F

F

F

V

D

E

E

E

N

T

A

E

D

G

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Q

Q

W

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T

I

A

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K

H

H

A

F

L

I

G

A

G

G

L

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V

E

K

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M

A

G

T

E

S

S

F

M

T

L

A

V

V

F

T

A

N

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P

H

T

A

V

N

N

S

S

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K

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R

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L

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x
G

S

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Y
x
E

A

A

P
|
P

V

C

S

Y

P

V

S

A

W

W

G

S

V

A

N

Q

N

N

R

R

S

S

V

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A

L

L

I

R

R

I

I

P

P

A

A

G

S

D

R

I

G

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I

A

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T

R

R

I

V

E
|
E

H

V

R

R

P

S

A

V

G

D

V

P

D

A

A

A

N

N

P

P

Y

Y

L

L

V

A

A

L

A

S

T

V

V

L

L

L

A

A

G

A

I

G

R

L

R

D

G

G

L

I

E

K

Q

N

Q

K

I

L

D

E

-

A

P

P

G

A

P

P

-

I

-

D

-

R

-

N

-

I

-

Y

-

V

-

M

-

S

-

K

-

E

E

E

T

R

T

M

G

E

N

N

G

G

Y

I

E

V

D

D

P

-

G

-

D

-

T

-

Q

-

P

-

I

L

P

P

T

A

C

T

W

L

R

A

S

E

A

A

I

L

A

E

A

F

Q

K

H

S

S

N

A

E

F

V

L

M

R

V

E

K

A

A

L

L

G

G

P

E

D

H

M

L

H

F

R

E

T

H

F

F

T

I

A

E

I

A

K

K

A

E

A

I

E
|
E

Y

W

E132 (= E148) binding Mg(2+)
E134 (= E150) binding Mg(2+)
E189 (= E214) binding Mg(2+)
V190 (≠ Y215) 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 (= E221) binding Mg(2+)
G241 (= G267) binding L-glutamate
H245 (= H271) binding Mg(2+)
G302 (≠ Q328) 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 (≠ Y330) 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 (= P332) 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 (= E359) binding Mg(2+)
E424 (= E444) 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)
29% identity, 78% coverage: 84:445/464 of query aligns to 68:428/447 of 4s0rD

query
sites
4s0rD

D

E

G

S

D

D

L

M

R

Y

A

L

W

Y

P

P

I

D

P

L

G

N

T

T

L

F

V

V

P

-

L

I

H

F

G

P

T

W

T

T

P

A

P

E

R

K

G

G

E

K

V

V

-

A

-

R

F

F

M

I

C

C

-

D

M

I

Y

Y

D

N

L

P

D

D

G

G

R

T

P

P

M

F

S

E

S

G

D

D

P

P

R

R

H

N

A

N

L

L

A

K

R

R

Q

I

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L

E

K

A

E

L

M

A

E

E

D

L

L

G

G

L

F

H

-

P

-

S

-

A

S

A

D

F

F

E

N

L

L

-

G

-

P

-
x
E

-

P

E
|
E

F

F

L

L

L

F

A

K

-

L

N

D

E

E

R

K

G

G

P

-

D

-

G

-

R

-

V

-

Q

E

P

P

A

T

A

L

D

E

V

L

L

N

D

D

G

-

R

-

R

K

S

G

A

G

K

Y

T

F

E
x
D

V

L

Y

A

S

P

V

T

D

D

H

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L

G

H

E

G

N

M

C

M

R

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-

L

-

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-

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R

D

D

I

I

Y

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A

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G

E

A

L

E

E

A

E

A

M

G

G

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F

K

E

A

I

E

E

T

A

M

S

I

H

S

H

E
|
E

Y

V

A

A

P

P

G

G

Q

Q

Y

H

E
|
E

L

I

T

D

L

F

H

K

Y

Y

R

-

T

A

D

G

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A

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D

L

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Q

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K

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K

A

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A

A

R

R

R

K

H

H

G

G

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H

A

A

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T

F

F

M

M

A

P

K

K

P

P

V

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E

F

S
x
G

Y
x
V

A
x
N

G

G

S

S

G

G

M

M

H
|
H

L

C

H

N

V

L

S

S

L

L

C

F

D

K

A

N

E

G

G

V

R

N

N

A

I

F

F

F

V

D

E

E

E

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T

A

E

D

G

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Q

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I

A

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K

H

H

A

F

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A

G

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E

K

T

H

M

A

G

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M

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L

A

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V

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T

A

N

P

P

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T

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N

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S

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R
|
R

F

L

A

V

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x
G

S
x
Y

Y
x
E

A

A

P

P

V

C

S

Y

P

V

S

A

W

W

G

S

V

A

N

Q

N

N

R
|
R

S

S

V

P

A

L

L

I

R

R

I

I

P

P

A

A

G

S

D

R

I

G

R

I

A

S

R

T

R

R

I

V

E
|
E

H

V

R
|
R

P

S

A

V

G

D

V

P

D

A

A

A

N

N

P

P

Y

Y

L

L

V

A

A

L

A

S

T

V

V

L

L

L

A

A

G

A

I

G

R

L

R

D

G

G

L

I

E

K

Q

N

Q

K

I

L

D

E

-

A

P

P

G

A

P

P

-

I

-

D

-

R

-

N

-

I

-
x
Y

-

V

-

M

-

S

-

K

-

E

E

E

T

R

T

M

G

E

N

N

G

G

Y

I

E

V

D

D

P

-

G

-

D

-

T

-

Q

-

P

-

I

L

P

P

T

A

C

T

W

L

R

A

S

E

A

A

I

L

A

E

A

F

Q

K

H

S

S

N

A

E

F

V

L

M

R

V

E

K

A

A

L

L

G

G

P

E

D

H

M

L

H

F

R

E

T
x
H

F

F

T

I

A

E

I

A

K

K

A

E

A
x
I

E

E

Y

W

active site: E135 (vs. gap), E137 (= E150), E192 (= E214), E199 (= E221), H248 (= H271), R319 (= R342), E336 (= E359), R338 (= R361)
binding glutamine: E137 (= E150), E192 (= E214), R301 (= R324), E307 (≠ Y330)
binding magnesium ion: E135 (vs. gap), E135 (vs. gap), E199 (= E221), H248 (= H271), H248 (= H271), E336 (= E359), H419 (≠ T436)
binding : D161 (≠ E180), G241 (≠ S264), V242 (≠ Y265), N243 (≠ A266), G305 (≠ Q328), Y306 (≠ S329), Y376 (vs. gap), I426 (≠ A443)

Sites not aligning to the query:

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

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)
29% identity, 78% coverage: 84:445/464 of query aligns to 64:424/443 of 4lnkA

query
sites
4lnkA

D

E

G

S

D

D

L

M

R

Y

A

L

W

Y

P

P

I

D

P

L

G

N

T

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L

F

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P

-

L

I

H

F

G

P

T

W

T

T

P

A

P

E

R

K

G

G

E

K

V

V

-

A

-

R

F

F

M

I

C

C

-

D

M

I

Y

Y

D

N

L

P

D

D

G

G

R

T

P

P

M

F

S

E

S

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D

D

P

P

R

R

H

N

A

N

L

L

A

K

R

R

Q

I

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L

E

K

A

E

L

M

A

E

E

D

L

L

G

G

L

F

H

-

P

-

S

-

A

S

A

D

F

F

E

N

L

L

-

G

-

P

-
x
E

-

P

E
|
E

F

F

L

L

L

F

A

K

-

L

N

D

E

E

R

K

G

G

P

-

D

-

G

-

R

-

V

-

Q

E

P

P

A

T

A

L

D

E

V

L

L

N

D

D

G

-

R

-

R

K

S

G

A

G

K

Y

T

F

E

D

V

L

Y

A

S

P

V

T

D

D

H

L

L

G

H

E

G

N

M

C

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R

P

-

L

-

F

-

S

R

D

D

I

I

Y

V

A

L

G

E

A

L

E

E

A

E

A

M

G

G

I

F

K

E

A

I

E

E

T

A

M

S

I

H

S

H

E
|
E

Y
x
V

A

A

P

P

G

G

Q

Q

Y

H

E
|
E

L

I

T

D

L
x
F

H

K

Y
|
Y

R

-

T

A

D

G

V

A

L

V

Q

R

A

S

A

C

D

D

L

I

M

Q

R

T

L

F

K

K

R

L

I

V

V

V

R

K

A

T

Q

I

A

A

R

R

R

K

H

H

G

G

V

L

T

H

A

A

C

T

F

F

M

M

A

P

K

K

P

P

V

L

E

F

S

G

Y

V

A
x
N

G
|
G

S

S

G
|
G

M

M

H
|
H

L

C

H
x
N

V

L

S
|
S

L

L

C

F

D

K

A

N

E

G

G

V

R

N

N

A

I

F

F

F

V

D

E

E

E

N

T

A

E

D

G

L

Q

Q

W

L

S

S

R

E

P

T

I

A

L

K

H

H

A

F

L

I

G

A

G

G

L

I

R

V

E

K

T

H

M

A

G

T

E

S

S

F

M

T

L

A

V

V

F

T

A

N

P

P

H

T

A

V

N

N

S

S

W

Y

R

K

R

R

F

L

A

V

S

P

Q

G

S

Y

Y
x
E

A

A

P

P

V

C

S

Y

P

V

S

A

W

W

G

S

V

A

N

Q

N

N

R
|
R

S

S

V

P

A

L

L

I

R

R

I

I

P

P

A

A

G
x
S

D

R

I

G

R

I

A
x
S

R

T

R
|
R

I

V

E
|
E

H

V

R
|
R

P

S

A

V

G

D

V

P

D

A

A

A

N

N

P

P

Y

Y

L

L

V

A

A

L

A

S

T

V

V

L

L

L

A

A

G

A

I

G

R

L

R

D

G

G

L

I

E

K

Q

N

Q

K

I

L

D

E

-

A

P

P

G

A

P

P

-

I

-

D

-

R

-

N

-

I

-

Y

-

V

-

M

-

S

-

K

-

E

E

E

T

R

T

M

G

E

N

N

G

G

Y

I

E

V

D

D

P

-

G

-

D

-

T

-

Q

-

P

-

I

L

P

P

T

A

C

T

W

L

R

A

S

E

A

A

I

L

A

E

A

F

Q

K

H

S

S

N

A

E

F

V

L

M

R

V

E

K

A

A

L

L

G

G

P

E

D

H

M

L

H

F

R

E

T

H

F

F

T

I

A

E

I

A

K

K

A

E

A

I

E

E

Y

W

active site: E131 (vs. gap), E133 (= E150), E188 (= E214), E195 (= E221), H244 (= H271), R315 (= R342), E332 (= E359), R334 (= R361)
binding adenosine-5'-diphosphate: F198 (≠ L224), Y200 (= Y226), N246 (≠ H273), S248 (= S275), S324 (≠ G351), S328 (≠ A355), R330 (= R357)
binding glutamic acid: E133 (= E150), E188 (= E214), V189 (≠ Y215), N239 (≠ A266), G240 (= G267), G242 (= G269), E303 (≠ Y330)
binding magnesium ion: E131 (vs. gap), E188 (= E214), E195 (= E221), H244 (= H271), E332 (= E359)

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)
29% identity, 78% coverage: 84:445/464 of query aligns to 64:424/443 of 4lniA

query
sites
4lniA

D

E

G

S

D

D

L

M

R

Y

A

L

W

Y

P

P

I

D

P

L

G

N

T

T

L

F

V

V

P

-

L

I

H

F

G

P

T

W

T

T

P

A

P

E

R

K

G

G

E

K

V

V

-

A

-

R

F

F

M

I

C

C

-

D

M

I

Y

Y

D

N

L

P

D

D

G

G

R

T

P

P

M

F

S

E

S

G

D

D

P

P

R

R

H

N

A

N

L

L

A

K

R

R

Q

I

V

L

E

K

A

E

L

M

A

E

E

D

L

L

G

G

L

F

H

-

P

-

S

-

A

S

A

D

F

F

E

N

L

L

-

G

-

P

-
x
E

-

P

E
|
E

F

F

L

L

L

F

A

K

-

L

N

D

E

E

R

K

G

G

P

-

D

-

G

-

R

-

V

-

Q

E

P

P

A

T

A

L

D

E

V

L

L

N

D

D

G

-

R

-

R

K

S

G

A

G

K

Y

T

F

E

D

V

L

Y

A

S

P

V

T

D

D

H

L

L

G

H

E

G

N

M

C

M

R

P

-

L

-

F

-

S

R

D

D

I

I

Y

V

A

L

G

E

A

L

E

E

A

E

A

M

G

G

I

F

K

E

A

I

E
|
E

T

A

M

S

I

H

S

H

E
|
E

Y

V

A

A

P

P

G

G

Q

Q

Y

H

E
|
E

L

I

T
x
D

L

F

H

K

Y
|
Y

R

-

T

A

D

G

V

A

L

V

Q

R

A

S

A

C

D

D

L

I

M

Q

R

T

L

F

K

K

R

L

I

V

V

V

R

K

A

T

Q

I

A

A

R

R

R

K

H

H

G

G

V

L

T

H

A

A

C

T

F

F

M

M

A

P

K

K

P

P

V

L

E

F

S

G

Y

V

A

N

G

G

S

S

G

G

M

M

H
|
H

L

C

H
x
N

V

L

S
|
S

L

L

C

F

D

K

A

N

E

G

G

V

R

N

N

A

I

F

F

F

V

D

E

E

E

N

T

A

E

D

G

L

Q

Q

W

L

S

S

R

E

P

T

I

A

L

K

H

H

A

F

L

I

G

A

G

G

L

I

R

V

E

K

T

H

M

A

G

T

E

S

S

F

M

T

L

A

V

V

F

T

A

N

P

P

H

T

A

V

N

N

S

S

W

Y

R

K

R
|
R

F

L

A

V

S

P

Q

G

S

Y

Y
x
E

A

A

P

P

V

C

S

Y

P

V

S

A

W

W

G

S

V

A

N

Q

N

N

R
|
R

S

S

V

P

A

L

L

I

R
|
R

I

I

P

P

A

A

G

S

D

R

I

G

R

I

A

S

R

T

R
|
R

I

V

E
|
E

H

V

R
|
R

P

S

A

V

G

D

V

P

D

A

A

A

N

N

P

P

Y

Y

L

L

V

A

A

L

A

S

T

V

V

L

L

L

A

A

G

A

I

G

R

L

R

D

G

G

L

I

E

K

Q

N

Q

K

I

L

D

E

-

A

P

P

G

A

P

P

-

I

-

D

-

R

-

N

-

I

-

Y

-

V

-

M

-

S

-

K

-

E

E

E

T

R

T

M

G

E

N

N

G

G

Y

I

E

V

D

D

P

-

G

-

D

-

T

-

Q

-

P

-

I

L

P

P

T

A

C

T

W

L

R

A

S

E

A

A

I

L

A

E

A

F

Q

K

H

S

S

N

A

E

F

V

L

M

R

V

E

K

A

A

L

L

G

G

P

E

D

H

M

L

H

F

R

E

T

H

F

F

T

I

A

E

I

A

K

K

A

E

A

I

E

E

Y

W

active site: E131 (vs. gap), E133 (= E150), E188 (= E214), E195 (= E221), H244 (= H271), R315 (= R342), E332 (= E359), R334 (= R361)
binding adenosine-5'-diphosphate: E131 (vs. gap), E183 (= E209), D197 (≠ T223), Y200 (= Y226), N246 (≠ H273), S248 (= S275), R320 (= R347), R330 (= R357)
binding magnesium ion: E131 (vs. gap), E131 (vs. gap), E133 (= E150), E188 (= E214), E195 (= E221), E195 (= E221), H244 (= H271), E332 (= E359)
binding l-methionine-s-sulfoximine phosphate: E133 (= E150), E188 (= E214), H244 (= H271), R297 (= R324), E303 (≠ Y330), R315 (= R342), R334 (= R361)

Sites not aligning to the query:

active site: 52

P9WN37 Glutamine synthetase; GS; Glutamate--ammonia ligase; Glutamine synthetase I alpha; GSI alpha; EC 6.3.1.2 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see paper)
31% identity, 74% coverage: 117:461/464 of query aligns to 101:444/446 of P9WN37

query
sites
P9WN37

D

D

G

G

R

S

P

P

M

S

S

W

S

A

D

D

P

P

R

R

H

H

A

V

L

L

A

R

R

R

Q

Q

V

L

E

T

A

K

L

A

A

G

E

E

L

L

G

G

L

F

H

S

P

C

S

Y

A

V

A

H

F

P

E

E

L

I

E

E

F

F

L

L

A

-

N

-

E

K

R

P

G

G

P

P

-

E

D

D

G

G

R

S

V

V

Q

P

P

V

A

P

A

V

D

D

-

N

-

A

-

G

-

Y

-

F

-

D

-

Q

-

A

-

V

-

H

-

D

-

S

V

A

L

L

D

N

G

F

R

R

S

H

A

A

K

-

T

-

E

-

V

-

Y

-

S

-

V

I

D

D

H

A

L

L

H

E

G

F

M

M

M

-

P

-

L

-

F

-

S

-

D

-

I

-

Y

-

A

-

G

-

A

-

E

-

A

-

G

G

I

I

K

S

A

V

E

E

T

F

M

S

I

H

S

H

E

E

Y

G

A

A

P

P

G

G

Q

Q

Y

Q

E

E

L

I

T

D

L

L

H

R

Y

F

R

-

T

A

D

D

V

A

L

L

Q

S

A

M

A

A

D

D

D

N

L

V

M

M

R

T

L

F

K

R

R

Y

I

V

V

I

R

K

A

E

Q

V

A

A

R

L

R

E

H

E

G

G

V

A

T

R

A

A

C

S

F

F

M

M

A

P

K

K

P

P

V

F

E

G

S

Q

Y

H

A

P

G

G

S

S

G

A

M

M

H

H

L

T

H

H

V

M

S

S

L

L

C

F

D

E

A

G

E

D

G

V

R

N

N

A

I

F

F

H