SitesBLAST

Q8IJR9 GMP synthase [glutamine-hydrolyzing]; PfGMPS; Glutamine amidotransferase; Guanosine monophosphate synthetase; EC 6.3.5.2 from Plasmodium falciparum (isolate 3D7) (see 3 papers)
42% identity, 99% coverage: 6:515/515 of query aligns to 8:555/555 of Q8IJR9

query
sites
Q8IJR9

K

K

V

I

I

L

I

V

I

L

D

N

Y

F

G

G

S

S

Q

Q

V
x
Y

T

F

Q
x
H

L

L

I

I

A

V

R
x
K

R
|
R

V

L

R

N

E

N

A

I

G

K

V

I

Y

F

S

S

E

E

I

T

H

K

P

D

C

Y

I

G

V

V

T

E

A

L

E

K

Q

D

V

I

R

K

A

D

M

M

K

N

P

I

A

K

A

G

I

V

I

I

L

L

S

S

G

G

P

P

A

Y

S

S

V

V

G

T

E

E

K

A

D

G

A

S

P

P

A

H

L

L

E

K

K

K

G

E

-

V

-

F

-

E

-

Y

L

F

L

L

D

E

L

K

G

K

V

I

P

P

V

I

L

F

G

G

I

I

C
|
C

Y

Y

G

G

M

M

Q
|
Q

L

E

L

I

G

A

Q

V

D

Q

L

M

G

N

G

G

E

E

L

V

A

K

T

K

S

S

E

K

T

T

R

S

E

E

Y

Y

G

G

P
x
C

A

T

D

D

L

V

T

N

-

I

-

L

-

R

-

N

-

D

-

N

-

I

-

N

-

I

-

T

-

Y

-

C

-

R

-

N

-

F

-

G

-

D

-

S

-

A

-

M

-

D

-

L

-

Y

-

S

-

N

-

Y

-

K

-

L

L

M

T

N

A

E

P

T

C

C

P

C

L

L

W

F

D

E

G

N

L

I

D
x
K

L

S

G

D

T

I

T

T

S

T

R

-

V

V

W
|
W

M

M

S
x
N

H

H

G

N

D
|
D

K

E

V

V

K

T

T

K

P

I

P

P

P

E

G

N

F

F

K

Y

V

L

V

V

G

S

R

S

T

S

A

E

T

N

L

C

E

L

V

I

A

C

A

S

M

I

A

Y

D

N

E

K

A

E

R

Y

R

N

I

I

Y

Y

A

G

V

V

Q

Q

F

Y

H
|
H

P

P

E

E

V

V

H
x
Y

H
x
E

S

S

E

L

D

D

G

G

A

E

R

L

I

M

I

F

N

Y

N

N

F

F

L

A

F

Y

H

N

V

I

A

C

K

K

L

C

K

K

A

K

D

Q

W

F

T

D

M

P

S

I

S

R

F

Y

V

H

E

E

R

L

A

E

V

L

K

K

E

N

M

I

A

E

E

K

V

Y

V

K

G

H

D

D

R

H

H

Y

V

V

V

I

C

A

A

A

L

M

S

S

G

G

I

I

D

D

S

S

T

T

V

V

V

A

A

A

V

A

L

Y

L

T

H

H

K

K

A

I

I

F

G

K

K

E

Q

R

L

F

H

F

C

G

I

I

F

F

V

I

D

D

N

N

G

G

V

L

L

L

R

R

L

K

N

N

E

E

G

A

Q

E

E

N

V

V

V

Y

D

T

Y

F

L

L

R

K

E

S

H

T

F

F

-

P

D

D

L

M

N

N

L

I

K

T

Y

K

V

I

Q

D

A

A

Q

S

E

E

R

N

F

F

L

L

S

S

K

N

L

L

H

Q

G

G

V

V

D

T

D

D

P

P

E

E

Q

Q

K

K

R
|
R

K

K

I

I

G

G

Y

K

T

L

F

F

I

I

E

E

V

E

F

F

D

E

E

-

A

-

K

K

A

A

L

V

G

N

H

N

V

I

D

D

-

I

-

D

-

I

-

N

-

K

-

T

F

F

L

L

A

L

Q

Q

G

G

T

T

L

L

Y

Y

P

P

D
|
D

V

I

I

I

E
|
E

S

S

V
x
K

S

C

H

S

K

K

G

N

P

L

S

S

A

D

V

T

I

I

K
|
K

S
x
T

H
|
H

N
|
N

V

V

G

G

L

L

P

P

E

K

K

N

M

L

N

K

L

F

K

K

L

L

I

F

E

E

P

P

L

F

R

K

E

Y

L

L

F

F

K
|
K

D
|
D

E
x
D

V

V

R
x
K

K

T

V

L

A

S

A

R

E

E

L

L

G

N

L

L

P

P

D

E

F

E

I

I

I

T

W

N

R

R

H

H

P

P

F

F

P

P

G

G

P

P

G

G

L

L

A

A

I

I

R

R

V

V

I

I

G

G

E

E

I

I

T

N

E

K

E

H

R

K

L

L

D

N

I

I

L

L

R

R

R

E

A

V

D

D

K

D

V

I

V

F

Q

I

Q

N

E

D

L

L

M

K

S

Q

S

Y

G

G

W

L

Y

Y

R

N

K

Q

V

I

W

S

Q
|
Q

G

A

F

F

A

A

V

V

L

L

P

S

L

S

K

K

T

S

V

V

G

G

V

V

M

R

G

G

D

D

G

A

R

R

T

S

Y

Y

E

D

H

Y

V

V

I

C

A

V

L

L

R

R

I

A

V

V

D

K

S

T

V

S

D

S

A

F

M

M

T

T

A

A

D

N

W

W

A

Y

R

Q

L

I

P

P

S

Y

E

D

L

I

L

L

E

D

R

K

I

I

S

T

R

R

I

I

I

L

N

S

E

E

V

V

K

K

G

G

V

V

N

N

R
|
R

V

I

V

L

Y

Y

D

D

I

V

S

S

K
|
K

P

P

S

A

T

T

I
|
I

E
|
E

W

F

E
|
E

Y18 (≠ V16) mutation to F: Slight increase in affinity for glutamine. No defect in glutaminase activity.
H20 (≠ Q18) mutation to A: Slight decrease in affinity for glutamine. 1.8-fold increase in affinity for ATP. Slight increase in affinity for XMP. Moderate reduction in glutaminase activity.
K24 (≠ R22) mutation to L: 50 percent decrease in glutaminase activity. 5.3-fold decrease in affinity for glutamine. 1.7-fold increase in affinity for ATP. 2.8-fold decrease in affinity for XMP.
R25 (= R23) mutation to L: No effect on glutaminase activity. 1.4-fold decrease in affinity for glutamine.
C89 (= C83) mutation to A: Loss of glutaminase activity, however, glutamine binding is not affected. In presence of exogenous ammonia, the amination of XMP to produce GMP is normal. 2.3-fold decrease in affinity for ATP and 1.8-fold decrease in affinity for XMP. 2.9-fold decrease in affinity for ATP and 1.9-fold decrease in affinity for XMP; when associated with A-113.
Q93 (= Q87) binding
C113 (≠ P107) mutation to A: 2.9-fold decrease in affinity for ATP and 1.9-fold decrease in affinity for XMP; when associated with A-89.
K160 (≠ D123) mutation to L: No effect on glutaminase activity. 1.2-fold decrease in affinity for ATP. 1.8-fold decrease in affinity for XMP.
W167 (= W131) mutation to F: Slight decrease in affinity for glutamine. Slight increase in glutaminase activity.
N169 (≠ S133) binding ; mutation to S: Slight increase in affinity for glutamine. No defect in glutaminase activity.
D172 (= D136) binding ; mutation to A: 172-fold decrease in affinity for glutamine. Severe loss of glutaminase activity.
H208 (= H172) binding
Y212 (≠ H176) mutation to W: 2.7-fold decrease in affinity for glutamine. No defect in glutaminase activity.
E213 (≠ H177) mutation to A: 40 percent decrease in glutaminase activity. 1.4-fold decrease in affinity for glutamine. 1.3-fold decrease in affinity for ATP. 1.8-fold decrease in affinity for XMP.
R336 (= R299) binding
D371 (= D331) Important for ATPPase activity; mutation to A: Impaired formation of adenyl-XMP intermediate. Slight increase in glutaminase activity.
E374 (= E334) mutation to L: 8.9-fold decrease in affinity for ammonia. Severe loss of glutaminase activity.
K376 (≠ V336) mutation to L: 20 percent decrease in glutaminase activity. 4.4-fold decrease in affinity for glutamine. 1.8-fold decrease in affinity for XMP.
K386 (= K346) mutation to L: Severe loss of ATP pyrophosphatase (ATPPase) activity. 80 percent decrease in glutaminase activity. Impaired GMP formation.
T387 (≠ S347) mutation to A: No effect on ATP pyrophosphatase (ATPPase) activity. 20 percent decrease in glutaminase activity. No effect on GMP formation.
H388 (= H348) Important for ATPPase activity; mutation to A: Moderate decrease in ATP pyrophosphatase (ATPPase) activity. Reduces 49 percent decrease in glutaminase activity. Impaired GMP formation.
H389 (= H349) Important for ATPPase activity; mutation to A: Loss of ATP pyrophosphatase (ATPPase) activity. 67 percent decrease in glutaminase activity. Impaired GMP formation.
N390 (= N350) mutation to A: No effect on ATP pyrophosphatase (ATPPase) activity. Increases glutaminase activity. Loss of GMP formation.
K411 (= K371) mutation to L: 70 percent decrease in glutaminase activity. Loss of GMP formation.
D412 (= D372) mutation to A: 30 percent decrease in glutaminase activity. 7.9-fold decrease in affinity for glutamine.
D413 (≠ E373) mutation to A: 35 percent decrease in glutaminase activity. 3.6-fold decrease in affinity for glutamine.
K415 (≠ R375) mutation to L: Increases glutaminase activity. 4.2-fold decrease in affinity for ATP.
Q476 (= Q436) binding
R539 (= R499) mutation to L: 85 percent decrease in glutaminase activity.
K547 (= K507) binding ; mutation to L: 85 percent decrease in glutaminase activity.
I552 (= I512) binding
E553 (= E513) binding ; mutation to L: 85 percent decrease in glutaminase activity.
E555 (= E515) mutation to L: 20 percent decrease in glutaminase activity. No effect on GMP formation.

2ywcA Crystal structure of gmp synthetase from thermus thermophilus in complex with xmp
50% identity, 99% coverage: 7:515/515 of query aligns to 2:475/475 of 2ywcA

query
sites
2ywcA

V

V

I

L

I

V

I

L

D

D

Y

F

G

G

S

S

Q

Q

V

Y

T

T

Q

R

L

L

I

I

A

A

R

R

V

L

R

R

E

E

A

L

G

R

V

A

Y

F

S

S

E

L

I

I

H

L

P

P

C

G

I

D

V

A

T

P

A

L

E

E

Q

E

V

V

R

L

A

K

M

H

K

R

P

P

A

Q

A

A

I

L

I

I

L

L

S

S

G

G

G
|
G

P

P

A
x
R

S

S

V

V

G

F

E

D

K

P

D

D

A

A

P

P

A

R

L

P

E

D

K

P

G

R

L

L

L

F

D

S

L

S

G

G

V

L

P

P

V

L

L

L

G

G

I

I

C
|
C

Y
|
Y

G

G

M

M

Q

Q

L

L

G

A

Q

Q

D

E

L

L

G

G

E

R

L

V

A

E

T

R

S

A

E

G

T

R

R

A

E

E

Y

Y

G

G

P

K

A

A

D

L

L

L

T

T

L

-

T

R

A

H

P

E

C

G

P

P

L

L

W

F

D

R

G

G

L

L

D

E

L

-

G

-

T

G

T

E

S

V

R

Q

V

V

W

W

M

M

S

S

H

H

G

Q

D

D

K

A

V

V

K

T

T

A

P

P

G

G

F

W

K

R

V

V

G

A

R

E

T

T

A

E

T

E

L

N

E

P

V

V

A

A

M

I

A

A

D

S

E

P

A

D

R

G

R

R

I

A

Y

Y

A

G

V

V

Q

Q

F

F

H
|
H

P

P

E
|
E

V

V

H

A

H

H

S

T

E

P

D

K

G

G

A

M

R

Q

I

I

I

L

N

E

N

N

F

F

L

L

F

-

H

E

V

L

A

A

K

G

L

V

K

K

A

R

D

D

W

W

T

T

M

P

S

E

S

H

F

V

V

L

E

E

R

E

A

L

V

L

K

R

E

E

M

V

A

R

E

E

V

R

V

A

G

G

D

K

R

D

H

R

V

V

V

L

C

L

A

A

L

V

S

S

G

G

I

V

D
|
D

S

S

T

S

V

T

V

L

A

A

V

L

L

L

H

A

K

K

A

A

I

-

G

G

K

V

Q

D

L

H

H

L

C

A

I

V

F

F

V

V

D

D

N

H

G

G

V

L

L

L

R

R

L

L

N

G

E

E

G

R

Q

E

E

E

V

V

V

E

D

G

Y

A

L

L

R

R

E

-

H

A

F

L

D

G

L

V

N

N

L

L

K

L

Y

V

V

V

Q

D

A

A

Q

K

E

E

R

R

F

F

L

L

S

K

K

A

L

L

H

K

G

G

V

V

D

E

D

D

P

P

E

E

Q

E

K

K

R
|
R

K

K

I

I

G

G

Y

R

T

E

F

F

I

V

E

A

V

A

F

F

D

S

E

Q

E

V

A

A

K

R

A

E

L

R

G

G

H

P

V

F

D

R

F

F

L

L

A

A

Q

Q

G

G

T

T

L

L

Y

Y

P

P

D

D

V

V

I

I

E

E

S

-

V

-

S

-

H

-

K

-

G

-

P

-

S

-

A

-

V

-

I

-

K

-

S

-

H

-

N

-

V

-

G

G

L

L

P

P

E

E

K

D

M

L

N

E

L

F

K

E

L

L

I

L

E

E

P

P

L

F

R

R

E

L

L

L

F

F

K
|
K

D

D

E

E

V

V

R

R

K

E

V

L

A

A

A

L

E

L

L

L

G

G

L

L

P

P

D

D

F

T

I

L

I

R

W

L

R

R

H

H

P

P

F

F

P
|
P

G
|
G

P
|
P

G

G

L

L

A

A

I

V

R

R

V

V

I

L

G

G

E

E

I

V

T

T

E

E

R

R

L

L

D

E

I

I

L

L

R

R

A

A

D

D

K

D

V

I

V

F

Q

T

Q

S

E

L

L

L

M

R

S

E

S

W

G

G

W

L

Y

Y

R

E

K

K

V

V

W

A

Q
|
Q

G

A

F

L

A

A

V

V

L

L

L

T

P

P

L

V

K

G

T

-

V

-

G

-

V

-

M

-

G

-

D

-

G

-

R

-

T

-

Y

-

E

-

H

Y

V

V

I

L

A

A

L

L

R

R

I

A

V

V

D

T

S

T

V

E

D

D

A

F

M

M

T

T

A

A

D

D

W

W

A

A

R

R

L

L

P

P

S

L

E

E

L

F

L

L

E

D

R

E

I

A

S

A

S

R

R

R

I

I

I

T

N

R

E

R

V

V

K

P

G

E

V

I

N

G

R

R

V

V

Y

Y

D

D

I

L

S

T

S

S

K
|
K

P

P

S

A

T
|
T

I
|
I

E
|
E

W

W

E

E

active site: G51 (= G56), R53 (≠ A58), C78 (= C83), Y79 (= Y84), H164 (= H172), E166 (= E174), D221 (= D230), K343 (= K371)
binding xanthosine-5'-monophosphate: R288 (= R299), P366 (= P394), G367 (= G395), P368 (= P396), Q408 (= Q436), K467 (= K507), T471 (= T511), I472 (= I512), E473 (= E513)

4wioA Crystal structure of the c89a gmp synthetase inactive mutant from plasmodium falciparum in complex with glutamine (see paper)
40% identity, 99% coverage: 6:515/515 of query aligns to 2:525/525 of 4wioA

query
sites
4wioA

K

K

V

I

I

L

I

V

I

L

D

N

Y

F

G

G

S

S

Q

Q

V

Y

T

F

Q

H

L

L

I

I

A

V

R

K

R

R

V

L

R

N

E

N

A

I

G

K

V

I

Y

F

S

S

E

E

I

T

H

K

P

D

C

Y

I

G

V

V

T

E

A

L

E

K

Q

D

V

I

R

K

A

D

M

M

K

N

P

I

A

K

A

G

I

V

I

I

L

L

S

S

G

G

G
|
G

P

P

A

Y

S

S

V

V

G

T

E

E

K

A

D

G

A

S

P

P

A

H

L

L

E

K

K

K

G

E

-

V

-

F

-

E

-

Y

L

F

L

L

D

E

L

K

G

K

V

I

P

P

V

I

L

F

G

G

I

I

C
x
A

Y
|
Y

G

G

M

M

Q
|
Q

L

E

L

I

G

A

Q

V

D

Q

L

M

G

N

G

G

E

E

L

V

A

K

T

K

S

S

E

K

T

T

R

S

E

E

Y

Y

G

G

P

C

A

T

D

D

L

V

T

N

L

I

-

L

-

R

-

N

-

D

-

N

-

I

-

N

-

I

T

T

A

Y

P

C

C

R

P

N

L

F

W

S

D

S

G

A

L

M

D

D

L

L

G

Y

T

S

T

N

S

Y

R

K

-

L

-

M

-

N

-

E

-

C

-

L

-

F

-

E

-

N

-

I

-

K

-

S

-

D

-

I

-

T

V

V

W

W

M

M

S
x
N

H
|
H

G
x
N

D
|
D

K

E

V

V

K

T

T

K

P

I

P

P

P

E

G

N

F

F

K

Y

V

L

V

V

G

S

R

S

T

S

A

E

T

N

L

C

E

L

V

I

A

C

A

S

M

I

A

Y

D

N

E

K

A

E

R

Y

R

N

I

I

Y

Y

A

G

V

V

Q

Q

F

Y

H
|
H

P

P

E
|
E

V

V

H

Y

H

E

S

S

E

L

D

D

G

G

A

E

R

L

I

M

I

F

N

Y

N

N

F

F

L

A

F

Y

H

N

V

I

A

C

K

K

L

C

K

K

A

K

D

Q

W

F

T

D

M

P

S

I

S

R

F

Y

V

H

E

E

R

L

A

E

V

L

K

K

E

N

M

I

A

E

E

K

V

Y

V

K

G

H

D

D

R

H

H

Y

V

V

V

I

C

A

A

A

L

M

S

S

G

G

I

I

D
|
D

S

S

T

T

V

V

V

A

A

A

V

A

L

Y

L

T

H

H

K

K

A

I

I

F

G

K

K

E

Q

R

L

F

H

F

C

G

I

I

F

F

V

I

D

D

N

N

G

G

V

L

L

L

R

R

L

K

N

N

E

E

G

A

Q

E

E

N

V

V

V

Y

D

T

Y

F

L

L

R

K

E

S

H

T

F

F

-

P

D

D

L

M

N

N

L

I

K

T

Y

K

V

I

Q

D

A

A

Q

S

E

E

R

N

F

F

L

L

S

S

K

N

L

L

H

Q

G

G

V

V

D

T

D

D

P

P

E

E

Q

Q

K

K

R

R

K

K

I

I

G

G

Y

K

T

L

F

F

I

I

E

E

V

E

F

F

D

E

E

-

A

-

K

K

A

A

L

V

G

N

H

N

V

I

D

D

-

I

-

D

-

I

-

N

-

K

-

T

F

F

L

L

A

L

Q

Q

G

G

T

T

L

L

Y

Y

P

P

D

D

V

I

I

I

E

E

S

S

V

K

S

C

H

S

K

K

G

N

P

L

S

S

A

D

V

T

I

I

K

K

S

T

H

H

N

N

V

-

G

-

L

-

P

-

E

-

K

-

M

L

N

K

L

F

K

K

L

L

I

F

E

E

P

P

L

F

R

K

E

Y

L

L

F

F

K
|
K

D

D

E

D

V

V

R

K

K

T

V

L

A

S

A

R

E

E

L

L

G

N

L

L

P

P

D

E

F

E

I

I

I

T

W

N

R

R

H

H

P

P

F

F

P

P

G

G

P

P

G

G

L

L

A

A

I

I

R

R

V

V

I

I

G

G

E

E

I

I

T

N

E

K

E

H

R

K

L

L

D

N

I

I

L

L

R

R

R

E

A

V

D

D

K

D

V

I

V

F

Q

I

Q

N

E

D

L

L

M

K

S

Q

S

Y

G

G

W

L

Y

Y

R

N

K

Q

V

I

W

S

Q

Q

G

A

F

F

A

A

V

V

L

L

P

-

L

-

K

-

T

-

V

-

G

-

V

-

M

-

G

-

D

-

G

-

R

-

T

S

Y

Y

E

D

H

Y

V

V

I

C

A

V

L

L

R

R

I

A

V

V

D

K

S

T

V

S

D

S

A

F

M

M

T

T

A

A

D

N

W

W

A

Y

R

Q

L

I

P

P

S

Y

E

D

L

I

L

L

E

D

R

K

I

I

S

T

R

R

I

I

I

L

N

S

E

E

V

V

K

K

G

G

V

V

N

N

R

R

V

I

V

L

Y

Y

D

D

I

V

S

S

K

K

P

P

S

A

T

T

I

I

E

E

W

F

E

E

active site: G52 (= G56), A83 (≠ C83), Y84 (= Y84), H197 (= H172), E199 (= E174), D255 (= D230), K393 (= K371)
binding glutamine: Q87 (= Q87), N158 (≠ S133), H159 (= H134), N160 (≠ G135), D161 (= D136), H197 (= H172)

3uowA Crystal structure of pf10_0123, a gmp synthetase from plasmodium falciparum
39% identity, 99% coverage: 6:515/515 of query aligns to 3:517/517 of 3uowA

query
sites
3uowA

K

K

V

I

I

L

I

V

I

L

D

N

Y

F

G

G

S

S

Q

Q

V

Y

T

F

Q

H

L

L

I

I

A

V

R

K

R

R

V

L

R

N

E

N

A

I

G

K

V

I

Y

F

S

S

E

E

I

T

H

K

P

D

C

Y

I

G

V

V

T

E

A

L

E

K

Q

D

V

I

R

K

A

D

M

M

K

N

P

I

A

K

A

G

I

V

I

I

L

L

S

S

G

G

G
|
G

P

P

A

Y

S

S

V

V

G

T

E

E

K

A

D

G

A

S

P

P

A

H

L

L

E

K

K

K

G

E

-

V

-

F

-

E

-

Y

L

F

L

L

D

E

L

K

G

K

V

I

P

P

V

I

L

F

G

G

I

I

C
|
C

Y
|
Y

G

G

M

M

Q

Q

L

E

L

I

G

A

Q

V

D

Q

L

M

G

N

G

G

E

E

L

V

A

K

T

K

S

S

E

K

T

T

R

S

E

E

Y

Y

G

G

P

C

A

T

D

D

L

V

T

N

L

I

T

L

-

R

-

N

-

D

-

N

-

I

-

N

-

I

-

T

-

Y

-

C

-

R

-

N

-

F

-

S

-

A

-

M

-

D

-

L

-

Y

-

S

-

N

-

Y

-

K

-

L

A

M

P

N

C

C

P

C

L

L

W

F

D

E

G

N

L

I

D

K

L

S

G

D

T

I

T

T

S

T

R

-

V

V

W

W

M

M

S

N

H

H

G

N

D

D

K

E

V

V

K

T

T

K

P

I

P

P

P

E

G

N

F

F

K

Y

V

L

V

V

G

S

R

S

T

S

A

E

T

N

L

C

E

L

V

I

A

C

A

S

M

I

A

Y

D

N

E

K

A

E

R

Y

R

N

I

I

Y

Y

A

G

V

V

Q

Q

F

Y

H
|
H

P

P

E
|
E

V

V

H

Y

H

E

S

S

E

L

D

D

G

G

A

E

R

L

I

M

I

F

N

Y

N

N

F

F

L

A

F

Y

H

N

V

I

A

C

K

K

L

C

K

K

A

K

D

-

W

F

T

D

M

P

S

I

S

R

F

Y

V

H

E

E

R

L

A

E

V

L

K

K

E

N

M

I

A

E

E

K

V

Y

V

K

G

H

D

D

R

H

H

Y

V

V

V

I

C

A

A

A

L

M

S

S

G

G

I

I

D
|
D

S

S

T

T

V

V

V

A

A

A

V

A

L

Y

L

T

H

H

K

K

A

I

I

F

G

K

K

E

Q

R

L

F

H

F

C

G

I

I

F

F

V

I

D

D

N

N

G

G

V

L

L

L

R

R

L

K

N

N

E

E

G

A

Q

E

E

N

V

V

V

Y

D

T

Y

F

L

L

R

K

E

S

H

T

F

F

-

P

D

D

L

M

N

N

L

I

K

T

Y

K

V

I

Q

D

A

A

Q

S

E

E

R

N

F

F

L

L

S

S

K

N

L

L

H

Q

G

G

V

V

D

T

D

D

P

P

E

E

Q

Q

K

K

R
|
R

K

K

I

I

G

G

Y

K

T

L

F

F

I

I

E

E

V

E

F

F

D

E

E

-

A

-

K

K

A

A

L

V

G

N

H

N

V

I

D

D

-

I

-

D

-

I

-

N

-

K

-

T

F

F

L

L

A

L

Q

Q

G

G

T

T

L

L

Y

Y

P

P

D

D

V

I

I

I

E

E

S

S

V

K

S

C

H

-

K

-

G

-

P

-

S

-

A

-

V

-

I

-

K

-

S

-

H

-

N

-

V

-

G

-

L

-

P

-

E

-

K

S

M

L

N

K

L

F

K

K

L

L

I

F

E

E

P

P

L

F

R

K

E

Y

L

L

F

F

K
|
K

D

D

E

D

V

V

R

K

K

T

V

L

A

S

A

R

E

E

L

L

G

N

L

L

P

P

D

E

F

E

I

I

I

T

W

N

R

R

H

H

P

P

F

F

P
|
P

G
|
G

P
|
P

G

G

L

L

A

A

I

I

R

R

V

V

I

I

G

G

E

E

I

I

T

N

E

K

E

H

R

K

L

L

D

N

I

I

L

L

R

R

R

E

A

V

D

D

K

D

V

I

V

F

Q

I

Q

N

E

D

L

L

M

K

S

Q

S

Y

G

G

W

L

Y

Y

R

N

K

Q

V

I

W

S

Q
|
Q

G

A

F

F

A

A

V

V

L

L

P

S

L

S

K

K

T

S

V

V

G

-

V

-

M

-

G

-

D

-

G

-

R

-

T

-

Y

Y

E

D

H

Y

V

V

I

C

A

V

L

L

R

R

I

A

V

V

D

K

S

T

V

S

D

S

A

F

M

M

T

T

A

A

D

N

W

W

A

Y

R

Q

L

I

P

P

S

Y

E

D

L

I

L

L

E

D

R

K

I

I

S

T

R

R

I

I

I

L

N

S

E

E

V

V

K

K

G

G

V

V

N

N

R

R

V

I

V

L

Y

Y

D

D

I

V

S

S

K
|
K

P

P

S

A

T
|
T

I
|
I

E
|
E

W

F

E

E

active site: G53 (= G56), C84 (= C83), Y85 (= Y84), H198 (= H172), E200 (= E174), D255 (= D230), K381 (= K371)
binding xanthosine-5'-monophosphate: R325 (= R299), P404 (= P394), G405 (= G395), P406 (= P396), Q446 (= Q436), K509 (= K507), T513 (= T511), I514 (= I512), E515 (= E513)

3uowB Crystal structure of pf10_0123, a gmp synthetase from plasmodium falciparum
38% identity, 99% coverage: 6:515/515 of query aligns to 1:477/477 of 3uowB

query
sites
3uowB

K

K

V

I

I

L

I

V

I

L

D

N

Y

F

G

G

S

S

Q

Q

V

Y

T

F

Q

H

L

L

I

I

A

V

R

K

R

R

V

L

R

N

E

N

A

I

G

K

V

I

Y

F

S

S

E

E

I

T

H

K

P

D

C

-

I

-

V

-

T

-

A

Y

E

K

Q

D

V

I

R

K

A

D

M

M

K

N

P

I

A

K

A

G

I

V

I

I

L

L

S

S

G

G

G
|
G

P

P

A

Y

S

S

V

-

G

-

E

-

K

-

D

-

A

-

P

-

A

E

L

V

E

F

K

E

G

Y

L

F

L

L

D

E

L

K

G

K

V

I

P

P

V

I

L

F

G

G

I

I

C
|
C

Y
|
Y

G

G

M

M

Q

Q

L

E

L

I

G

A

Q

V

D

Q

L

M

G

N

G

-

E

-

L

-

A

-

T

-

S

-

E

-

T

-

R

-

E

-

Y

Y

G

G

P

C

A

T

D

D

L

V

T

N

L

I

T

N

A

I

P

N

C

N

P

I

L

T

W

Y

D

C

G

A

L

M

D

D

L

L

G

Y

T

S

T

N

S

Y

R

K

-

L

-

M

-

N

-

C

-

L

-

F

-

E

-

N

-

I

-

K

-

S

-

D

-

I

-

T

V

V

W

W

M

M

S

N

H

H

G

N

D

D

K

E

V

V

K

T

T

K

P

I

P

P

P

E

G

N

F

F

K

Y

V

L

V

V

G

S

R

S

T

S

A

E

T

N

L

C

E

L

V

I

A

C

A

S

M

I

A

Y

D

N

E

K

A

E

R

Y

R

N

I

I

Y

Y

A

G

V

V

Q

Q

F

Y

H
|
H

P

P

E
|
E

V

V

H

Y

H

E

S

S

E

L

D

D

G

G

A

E

R

L

I

M

I

F

N

Y

N

N

F

F

L

A

F

Y

H

N

V

I

A

C

K

K

L

C

K

K

A

F

D

D

W

P

T

I

M

-

S

-

S

R

F

Y

V

H

E

E

R

L

A

E

V

L

K

K

E

N

M

I

A

E

E

K

V

Y

V

K

G

H

D

D

R

H

H

Y

V

V

V

I

C

A

A

A

L

M

S

S

G

G

I

I

D
|
D

S

S

T

T

V

V

V

A

A

A

V

A

L

Y

L

T

H

H

K

K

A

I

I

F

G

K

K

E

Q

R

L

F

H

F

C

G

I

I

F

F

V

I

D

D

N

N

G

G

V

L

L

L

R

R

L

K

N

N

E

E

G

A

Q

E

E

N

V

V

V

Y

D

T

Y

F

L

L

R

K

E

S

H

T

F

F

-

P

D

D

L

M

N

N

L

I

K

T

Y

K

V

I

Q

D

A

A

Q

S

E

E

R

N

F

F

L

L

S

S

K

N

L

L

H

Q

G

G

V

V

D

T

D

D

P

P

E

E

Q

Q

K

K

R
|
R

K

K

I

I

G

G

Y

K

T

L

F

F

I

I

E

E

V

E

F

F

D

E

E

-

A

-

K

K

A

A

L

V

G

N

H

N

V

I

D

D

-

D

-

I

-

N

-

K

-

T

F

F

L

L

A

L

Q

Q

G

G

T

T

L

L

Y

Y

P

P

D

D

V

I

I

I

E

E

S

S

V

-

S

-

H

-

K

-

G

-

P

-

S

-

A

-

V

-

I

-

K

-

S

-

H

-

N

-

V

-

G

-

L

-

P

-

E

-

K

-

M

K

N

K

L

F

K

K

L

L

I

F

E

E

P

P

L

F

R

K

E

Y

L

L

F

F

K
|
K

D

D

E

D

V

V

R

K

K

T

V

L

A

S

A

R

E

E

L

L

G

N

L

L

P

P

D

E

F

E

I

I

I

T

W

N

R

R

H

H

P

P

F

F

P
|
P

G
|
G

P
|
P

G

G

L

L

A

A

I

I

R

R

V

V

I

I

G

G

E

E

I

I

T

N

E

K

E

H

R

K

L

L

D

N

I

I

L

L

R

R

R

E

A

V

D

D

K

D

V

I

V

F

Q

I

Q

N

E

D

L

L

M

K

S

Q

S

Y

G

G

W

L

Y

Y

R

N

K

Q

V

I

W

S

Q
|
Q

G

A

F

F

A

A

V

V

L

L

P

S

L

S

K

K

T

S

V

V

G

G

V

-

M

-

G

-

D

-

G

-

R

-

T

-

Y

Y

E

D

H

Y

V

V

I

C

A

V

L

L

R

R

I

A

V

V

D

K

S

T

V

S

D

S

A

F

M

M

T

T

A

A

D

N

W

W

A

Y

R

Q

L

I

P

P

S

Y

E

D

L

I

L

L

E

D

R

K

I

I

S

T

R

R

I

I

I

L

N

S

E

E

V

V

K

K

G

G

V

V

N

N

R

R

V

I

V

L

Y

Y

D

D

I

V

S

S

K
|
K

P

P

S

A

T
|
T

I
|
I

E
|
E

W

F

E

E

active site: G47 (= G56), C67 (= C83), Y68 (= Y84), H162 (= H172), E164 (= E174), D218 (= D230), K340 (= K371)
binding xanthosine-5'-monophosphate: R288 (= R299), P363 (= P394), G364 (= G395), P365 (= P396), Q405 (= Q436), K469 (= K507), T473 (= T511), I474 (= I512), E475 (= E513)

P49915 GMP synthase [glutamine-hydrolyzing]; GMP synthetase; Glutamine amidotransferase; EC 6.3.5.2 from Homo sapiens (Human) (see paper)
36% identity, 96% coverage: 7:502/515 of query aligns to 28:562/693 of P49915

query
sites
P49915

V

V

I

V

I

I

I

L

D

D

Y

A

G

G

S

A

Q

Q

V

Y

T

G

Q

K

L

V

I

I

A

D

R

R

V

V

R

R

E

E

A

L

G

F

V

V

Y

Q

S

S

E

E

I

I

H

F

P

P

C

L

I

E

V

T

T

P

A

A

E

F

Q

A

V

I

R

K

A

E

M

Q

K

G

P

F

A

R

A

A

I

I

L

I

S

S

G

G

P

P

A

N

S

S

V

V

G

Y

E

A

K

E

D

D

A

A

P

P

A

W

L

F

E

D

K

P

G

A

L

I

L

F

D

T

L

I

G

G

V

K

P

P

V

V

L

L

G

G

I

I

C
|
C

Y

Y

G

G

M

M

Q

Q

L

M

G

N

Q

K

D

V

L

F

G

G

E

T

L

V

A

H

T

K

S

K

E

S

T

V

R

R

E

E

Y

D

G

G

P

V

A

F

D

N

L

I

T

S

L

V

T

D

A

N

P

T

C

C

P

S

L

L

W

F

D

R

G

G

L

L

D

Q

L

-

G

-

T

K

T

E

S

E

R

V

V

V

W

L

M

L

S

T

H

H

G

G

D

D

K

S

V

V

K

D

T

K

P

V

P

A

P

D

G

G

F

F

K

K

V

V

G

A

R

R

T

S

A

G

T

N

L

I

E

-

V

V

A

A

A

G

M

I

A

A

D

N

E

E

A

S

R

K

I

L

Y

Y

A

G

V

A

Q

Q

F

F

H
|
H

P

P

E
|
E

V

V

H

G

H

L

S

T

E

E

D

N

G

G

A

K

R

V

I

I

I

L

N

K

N

N

F

F

L

L

F

Y

H

D

V

I

A

A

K

G

L

C

K

S

A

G

D

T

W

F

T

T

M

V

S

Q

S

N

F

R

V

E

E

L

R

E

A

C

V

I

K

R

E

E

M

I

A

K

E

E

V

R

V

V

G

G

D

T

R

S

H

K

V

V

V

L

C

V

A

L

L

L

S

S

G

G

I

V

D

D

S

S

T

T

V

V

V

C

A

T

V

A

L

L

H

N

K

R

A

A

I

L

G

N

K

Q

-

E

Q

Q

L

V

H

I

C

A

I

V

F

H

V

I

D

D

N

N

G

G

V

F

L

M

R

R

L

K

N

R

E

E

G

S

Q

Q

E

S

V

V

V

E

D

E

Y

A

L

L

R

K

E

K

H

-

F

L

D

G

L

I

N

Q

L

V

K

K

Y

V

V

I

Q

N

A

A

Q

A

E

H

R

S

F

F

L

Y

S

N

-

G

-

T

-

L

-

P

-

I

-

S

-

D

-

E

-

D

-

R

-

T

-

P

-

R

-

K

-

R

-

I

-

S

-

K

K

T

L

L

H

N

G

M

V

T

D

T

D

S

P

P

E

E

Q

E

K

K

R
|
R

K

K

I

I

G

G

Y

D

T

T

F

F

I

V

E

K

V

I

F

A

D

N

E

E

E

-

A

-

K

-

A

V

L

I

G

G

H

E

V

M

D

N

-

L

-

K

-

P

-

E

-

V

F

F

L

L

A

A

Q

Q

G

G

T

T

L

L

Y

R

P

P

D

D

V

L

I

I

E

E

S

S

V

A

S

S

-

L

-

V

H

A

K

S

G

G

P

K

S

A

A

E

V

L

I

I

K

K

S

T

H

H

N

N

V

D

G

T

G

E

L

L

P

I

E

R

K

K

M

L

N

R

L

E

-

E

-

G

K

K

L

V

I

I

E

E

P

P

L

L

R

K

E

D

L

F

F

H

K

K

D

D

E

E

V

V

R

R

K

I

V

L

A

G

A

R

E

E

L

L

G

G

L

L

P

P

D

E

F

E

I

L

I

V

W

S

R

R

H

H

P

P

F

F

P

P

G

G

P

P

G

G

L

L

A

A

I

I

R

R

V

V

I

I

-

C

-

A

-

E

-

P

-

Y

-

I

-

C

-

K

-

D

-

F

-

P

-

E

-

T

-

N

-

I

-

L

-

K

-

I

-

V

-

A

-

D

-

F

G

S

E

A

I

S

T

V

E

K

R

P

L

H

D

T

I

L

L

L

R

Q

R

R

A

V

D

K

K

A

V

C

V

T

-

T

-

E

-

D

Q

Q

Q

E

E

K

L

L

M

M

S

Q

S

I

G

T

W

S

Y

L

R

H

K

S

V

L

W

N

Q

-

G

-

F

-

A

A

V

F

L

L

P

P

L

I

K

K

T

T

V

V

G

G

V

V

M

Q

G

G

D
|
D

G

C

R

R

T

S

Y

Y

E

S

H

Y

V

V

I

C

A

G

L

I

R

S

I

S

V

K

D

D

S

E

V

-

D

-

A

-

M

-

T

-

A

P

D

D

W

W

A

E

R

S

L

L

P

I

S

-

E

-

L

F

L

L

E

A

R

R

I

L

S

I

S

P

R

R

I

M

I

C

N

H

E

-

V

-

K

-

G

N

V

V

N

N

R

R

V

V

Y

Y

C104 (= C83) active site, For GATase activity
H190 (= H172) active site, For GATase activity
E192 (= E174) active site, For GATase activity
R337 (= R299) binding
D522 (= D452) binding

Sites not aligning to the query:

610 binding
685 binding
691 binding

6jp9A Crsytal structure of a xmp complexed atppase subunit of m. Jannaschii gmp synthetase (see paper)
50% identity, 61% coverage: 202:515/515 of query aligns to 5:298/298 of 6jp9A

query
sites
6jp9A

S

K

F

F

V

I

E

D

R

E

A

A

V

V

K

E

E

E

M

I

A

K

E

Q

V

Q

V

I

G

S

D

D

R

R

H

K

V

A

V

I

C

I

A

A

L

L

S

S

G

G

I

V

D
|
D

S

S

T

S

V

V

V

A

A

A

V

V

L

L

L

T

H

H

K

K

A

A

I

I

G

G

K

D

Q

K

L

L

H

T

C

A

I

V

F

F

V

V

D

D

N

T

G

G

V

L

L

M

R

R

L

K

N

G

E

E

G

R

Q

E

E

E

V

V

V

E

D

K

Y

T

L

F

R

R

E

D

H

K

F

L

D

G

L

L

N

N

L

L

K

I

Y

V

V

V

Q

D

A

A

Q

K

E

D

R

R

F

F

L

L

S

N

K

A

L

L

H

K

G

G

V

V

D

T

D

D

P

P

E

E

Q

E

K

K

R
|
R

K

K

I

I

G

G

Y

K

T

L

F

F

I

I

E

D

V

V

F

F

D

E

E

E

E

I

A

A

K

E

A

D

L

I

G

-

H

K

V

A

D

E

F

V

L

L

A

V

Q

Q

G

G

T

T

L

I

Y

A

P

P

D

D

V

-

I

-

E

-

S

-

V

-

S

-

H

-

K

-

G

-

P

-

S

-

A

-

V

-

I

-

K

-

S

-

H

-

H

H

N

N

V

V

G

A

G

-

L

L

P

P

E

H

K

G

M

M

N

V

L

L

K

E

L

V

I

V

E

E

P

P

L

L

R

R

E

E

L

L

F

Y

K
|
K

D

D

E

E

V

V

R

R

K

L

V

L

A

A

A

K

E

E

L

L

G

G

L

L

P

P

D

D

F

S

I

I

I

V

W

Y

R

R

H

Q

P

P

F

F

P
|
P

G
|
G

P
|
P

G

G

L

L

A

A

I

V

R

R

V

V

I

L

G

G

E

E

I

V

T

T

E

E

R

K

L

L

D

N

I

I

L

C

R

R

R

E

A

A

D

N

K

A

V

I

V

V

Q

E

E

E

L

V

M

K

S

K

S

A

G

N

W

L

Y

D

R

K

K

D

V

L

W

W

Q
|
Q

G

Y

F

F

A

A

V

V

L

V

L

L

P

D

L

C

K

K

T

A

V

T

G

G

V

V

M

K

G

G

D

D

G

-

R

R

T

E

Y

Y

E

N

H

W

V

I

I

V

A

A

L

L

R

R

I

M

V

V

D

K

S

S

V

L

D

D

A

A

M

M

T

T

A

A

D

H

W

V

A

P

R

E

L

I

P

P

S

F

E

D

L

L

E

K

R

R

I

I

S

S

S

K

R

R

I

I

I

T

N

S

E

E

V

I

K

P

G

N

V

V

N

A

R

R

V

V

Y

F

D

D

I

I

S

T

S

D

K
|
K

P

P

S

A

T
|
T

I
|
I

E
|
E

W

F

E

E

active site: D33 (= D230), K155 (= K371)
binding xanthosine-5'-monophosphate: R102 (= R299), P178 (= P394), G179 (= G395), P180 (= P396), Q220 (= Q436), K290 (= K507), T294 (= T511), I295 (= I512), E296 (= E513)

2vxoB Human gmp synthetase in complex with xmp (see paper)
37% identity, 96% coverage: 7:502/515 of query aligns to 6:527/658 of 2vxoB

query
sites
2vxoB

V

V

I

V

I

I

I

L

D

D

Y

A

G

G

S

A

Q

Q

V

Y

T

G

Q

K

L

V

I

I

A

D

R

R

V

V

R

R

E

E

A

L

G

F

V

V

Y

Q

S

S

E

E

I

I

H

F

P

P

C

L

I

E

V

T

T

P

A

A

E

F

Q

A

V

I

R

K

A

E

M

Q

K

G

P

F

A

R

A

A

I

I

L

I

S

S

G

G

G
|
G

P

P

A

N

S

S

V

V

G

Y

E

A

K

E

D

D

A

A

P

P

A

W

L

F

E

D

K

P

G

A

L

I

L

F

D

T

L

I

G

G

V

K

P

P

V

V

L

L

G

G

I

I

C
|
C

Y
|
Y

G

G

M

M

Q

Q

L

M

G

N

Q

K

D

V

L

F

G

G

E

-

L

-

A

-

T

T

S

V

E

H

T

K

R

K

E

S

Y

D

G

G

P

V

A

F

D

N

L

I

T

S

L

V

T

D

A

N

P

T

C

C

P

S

L

L

W

F

D

R

G

G

L

L

D

Q

L

-

G

-

T

K

T

E

S

E

R

V

V

V

W

L

M

L

S

T

H

H

G

G

D

D

K

S

V

V

K

D

T

K

P

V

P

A

P

D

G

G

F

F

K

K

V

V

G

A

R

R

T

S

A

G

T

N

L

I

E

-

V

V

A

A

A

G

M

I

A

A

D

N

E

E

A

S

R

K

I

L

Y

Y

A

G

V

A

Q

Q

F

F

H
|
H

P

P

E
|
E

V

V

H

G

H

L

S

T

E

E

D

N

G

G

A

K

R

V

I

I

I

L

N

K

N

N

F

F

L

L

F

Y

H

D

V

I

A

A

K

G

L

C

K

S

A

G

D

T

W

F

T

T

M

V

S

Q

S

N

F

R

V

E

E

L

R

E

A

C

V

I

K

R

E

E

M

I

A

K

E

E

V

R

V

V

G

G

D

T

R

S

H

K

V

V

V

L

C

V

A

L

L

L

S

S

G

G

I

V

D
|
D

S

S

T

T

V

V

V

C

A

T

V

A

L

L

H

N

K

R

A

A

I

L

G

N

K

Q

-

E

Q

Q

L

V

H

I

C

A

I

V

F

H

V

I

D

D

N

N

G

G

V

F

L

M

R

R

L

K

N

R

E

E

G

S

Q

Q

E

S

V

V

V

E

D

E

Y

A

L

L

R

K

E

K

H

-

F

L

D

G

L

I

N

Q

L

V

K

K

Y

V

V

I

Q

N

A

A

Q

A

E

H

R

S

F

F

L

Y

S

N

-

G

-

T

-

L

-

P

-

R

-

I

-

S

-

K

K

T

L

L

H

N

G

M

V

T

D

T

D

S

P

P

E

E

Q

E

K

K

R
|
R

K

K

I

I

G

G

Y

D

T

T

F

F

I

V

E

K

V

I

F

A

D

N

E

E

E

-

A

-

K

-

A

V

L

I

G

G

H

E

V

M

D

N

-

L

-

K

-

P

-

E

-

V

F

F

L

L

A

A

Q

Q

G

G

T

T

L

L

Y

R

P

P

D

D

V

L

I

I

E

E

S

S

V

A

S

S

-

L

-

V

H

A

K

S

G
|
G

P
x
K

S

A

A

E

V

L

I

I

K

K

S

T

H

H

N

N

V

D

G

T

G

E

L

L

P

I

E

R

K

K

M

L

N

R

L

E

-

E

-

G

K

K

L

V

I

I

E

E

P

P

L

L

R

K

E

D

L

F

F

H

K
|
K

D

D

E

E

V

V

R

R

K

I

V

L

A

G

A

R

E

E

L

L

G

G

L

L

P

P

D

E

F

E

I

L

I

V

W

S

R

R

H

H

P

P

F

F

P
|
P

G
|
G

P
|
P

G

G

L

L

A

A

I

I

R

R

V

V

I

I

-

C

-

A

-

E

-

P

-

Y

-

I

-

C

-

K

-

D

-

F

-

P

-

E

-

T

-

N

-

I

-

L

-

K

-

I

-

V

-

A

-

D

-

F

G

S

E

A

I

S

T

V

E

K

R

P

L

H

D

T

I

L

L

L

R

Q

R

R

A

V

D

K

K

A

V

C

V

T

-

T

-

E

-

D

Q

Q

Q

E

E

K

L

L

M

M

S

Q

S

I

G

T

W

S

Y

L

R

H

K

S

V

L

W

N

Q

-

G

-

F

-

A

A

V

F

L

L

P

P

L

I

K

K

T

T

V

V

G

G

V

V

M

Q

G

G

D

D

G

C

R
|
R

T

S

Y

Y

E

S

H

Y

V

V

I

C

A

G

L

I

R

S

I

S

V

K

D

D

S

E

V

-

D

-

A

-

M

-

T

-

A

P

D

D

W

W

A

E

R

S

L

L

P

I

S

-

E

-

L

F

L

L

E

A

R

R

I

L

S

I

S

P

R

R

I

M

I

C

N

H

E

-

V

-

K

-

G

N

V

V

N

N

R

R

V

V

Y

Y

active site: G55 (= G56), C82 (= C83), Y83 (= Y84), H165 (= H172), E167 (= E174), D223 (= D230), K381 (= K371)
binding xanthosine-5'-monophosphate: R302 (= R299), G348 (= G340), K349 (≠ P341), P404 (= P394), G405 (= G395), P406 (= P396), R489 (= R454)

Sites not aligning to the query:

binding xanthosine-5'-monophosphate: 575, 610, 650, 654, 655, 656

7yc6A Crystal structure of d110p mutant of gatase subunit of methanocaldococcus jannaschii gmp synthetase
35% identity, 36% coverage: 7:189/515 of query aligns to 2:175/183 of 7yc6A

query
sites
7yc6A

V

I

I

V

I

I

I

L

D

D

Y

N

G

G

S

G

Q

Q

V

Y

T

V

Q

H

L

R

I

I

A

H

R

R

R

S

V

L

R

K

E

Y

A

I

G

G

V

V

Y

S

S

S

E

K

I

I

H

V

P

P

C

N

I

T

V

T

T

P

A

L

E

E

Q

E

V

I

R

E

A

S

M

N

K

K

P

E

A

V

-

K

A

G

I

I

L

L

S

S

G

G

P

P

A

D

S

I

V

E

G

K

E

A

K

K

D

N

A

C

P

I

A

D

L

I

E

A

K

-

G

-

L

-

L

L

D

N

L

A

G

K

V

L

P

P

V

I

L

L

G

G

I

I

C
|
C

Y

L

G

G

M

H

Q

Q

L

L

L

I

G

A

Q

L

D

A

L

Y

G

G

E

E

L

V

A

-

T

-

S

-

E

-

T

-

R

-

E

-

Y

-

G

G

P

R

A

A

D

A

L

L

T

T

-

K

-

V

-

Y

L

V

T
x
D

A

K

P

E

C

N

P

P

L

L

W

F

D

K

G

-

L

-

D

N

L

V

G

P

T

R

T

E

S

F

R

N

V

A

W

W

M

A

S

S

H

H

G

K

D

D

K
x
E

V

V

K

K

T

K

P

V

P

P

P

E

G

G

F

F

K

E

V

I

V

L

G

A

R
x
H

T

S

A

D

T

I

L
x
C

E

Q

V

V

A

E

A

A

M

M

A

K

D

H

E

K

A

T

R

K

R

P

I

I

Y

Y

A

G

V

V

Q

Q

F

F

H
|
H

P

P

E

E

V

V

H

A

H

H

S

T

E

E

D

Y

G

G

A

N

R

E

I

I

I

L

N

K

N

N

F

F

L

C

binding zinc ion: C76 (= C83), D101 (≠ T113), E123 (≠ K137), E123 (≠ K137), H136 (≠ R150), C140 (≠ L154), C140 (≠ L154), H158 (= H172)

P00903 Aminodeoxychorismate synthase component 2; ADC synthase; ADCS; 4-amino-4-deoxychorismate synthase component 2; Aminodeoxychorismate synthase, glutamine amidotransferase component; EC 2.6.1.85 from Escherichia coli (strain K12) (see paper)
28% identity, 30% coverage: 38:189/515 of query aligns to 34:185/187 of P00903

query
sites
P00903

V

L

T

T

A

L

E

A

Q

D

V

I

R

D

A

A

M

L

K

K

P

P

A

Q

A

K

I

I

I

V

L

I

S

S

G

P

G

G

P

P

A

C

S

T

V

P

G

D

E

E

K

A

-

G

-

I

-

S

-

L

D

D

A

V

P

I

A

R

L

H

E

Y

K

A

G

G

L

R

L

L

D

-

L

-

G

-

V

-

P

P

V

I

L

L

G

G

I

V

C
|
C

Y

L

G

G

M

H

Q

Q

L

A

L

M

G

A

Q

Q

D

A

L

F

G

G

E

K

L

V

A

V

T

R

S

A

E

A

T

K

R

V

E

M

Y

H

G

G

P

K

A

T

D

S

L

P

T

I

L

T

T

H

A

N

P

G

C

E

P

G

L

V

W

F

D

R

G

G

L

L

D

A

L

N

G

P

T

L

T

T

S

V

R

T

V

R

W

Y

M

H

S

S

H

L

G

V

D

V

K

E

V

P

K

D

T

S

P

L

P

P

P

A

G

C

F

F

K

D

V

V

V

T

G

A

R

W

T

S

A

E

T

T

L

R

E

E

V

I

A

M

A

G

M

I

A

R

D

H

E

R

A

Q

R

W

R

D

I

L

Y

E

A

G

V

V

Q

Q

F

F

H
|
H

P

P

E
|
E

V

S

H

I

H

L

S

S

E

E

D

Q

G

G

A

H

R

Q

I

L

N

A

N

N

F

F

L

L

C79 (= C83) mutation to S: 10000-fold decrease in catalytic efficiency.
H168 (= H172) mutation to Q: Loss of activity.
E170 (= E174) mutation to A: 150-fold decrease in catalytic efficiency.; mutation to D: 4-fold decrease in catalytic efficiency.; mutation E->K,Q: Loss of activity.

Q42565 Anthranilate synthase beta subunit 1, chloroplastic; Anthranilate synthase component 2-1; Anthranilate synthase, glutamine amidotransferase component 2-1; Protein TRYPTOPHAN BIOSYNTHESIS 4; Protein WEAK ETHYLENE INSENSITIVE 7; EC 4.1.3.27 from Arabidopsis thaliana (Mouse-ear cress) (see 2 papers)
26% identity, 37% coverage: 7:198/515 of query aligns to 75:273/276 of Q42565

query
sites
Q42565

V

I

I

I

I

V

I

I

D

D

Y

N

G

Y

S

D

Q

S

V

F

T

T

Q

Y

L

N

I

L

A

C

R

Q

R

Y

V

M

R

G

E

E

A

L

G

G

V

C

Y

H

S

F

E

E

I

V

H

Y

P

R

C

N

I

D

-

E

V

L

T

T

A

V

E

E

Q

E

V

L

R

K

A

K

M

K

K

N

P

P

A

R

A

G

I

V

I

L

L

I

S

S

G

P

G

G

P

P

A

G

S

T

V

-

G

-

E

P

K

Q

D

D

A

S

P

G

A

I

L

S

E

L

K

Q

G

T

L

V

L

L

D

E

L

L

G

G

-

P

-

L

V

V

P

P

V

L

L

F

G
|
G

I

V

C

C

Y

M

G

G

M

L

Q

Q

L

C

L

I

G

G

Q

E

D

A

L

F

G

G

E

K

L

I

A

V

T

R

S

S

E

P

T

F

R

G

E

V

Y

M

G

H

P
x
G

A

K

D

S

L

S

T

M

L

V

T

H

A

Y

P

D

C

E

P

K

L

G

W

E

D

E

G

G

L

L

D

F

L

S

G

G

T

L

T

S

S

N

R

P

-

F

-

I

V

V

W

G

M

R

S

Y

H

H

G

S

-

L

-

V

-

I

D

E

K

K

V

D

K

T

T

F

P

P

P

S

P

D

G

E

F

L

K

E

V

V

V

T

G

A

R

W

T

T

A

E

T

D

-

G

L

L

E

V

V

M

A

A

M

R

A

H

D

R

E

K

A

Y

R

K

R

H

I

I

Y

Q

A

G

V

V

Q

Q

F

F

H

H

P

P

E

E

V

S

H

I

S

T

E

T

D

E

G

G

A

K

R

T

I

I

I

V

N

R

N

N

F

F

L

I

F

K

H

I

V

V

A

E

K

K

L

K

K

E

A

S

D

E

G150 (= G81) mutation to D: In trp4-1; no visible phenotype under normal growth conditions.
G176 (≠ P107) mutation to E: In wei7-2; insensitive to inhibition of root elongation by ethylene.

7d54A Crstal structure msgatase with gln (see paper)
36% identity, 20% coverage: 74:175/515 of query aligns to 92:182/242 of 7d54A

query
sites
7d54A

D

D

L

A

G

G

V

V

P

G

V

I

L

L

G

G

I

V

C
|
C

Y

F

G

G

M

G

Q

Q

L

L

G

A

Q

Q

D

T

L

F

G

G

E

S

L

V

A

A

T

R

S

A

E

E

T

T

R

A

E

E

Y

V

G

G

-

W

-

F

-

E

-

L

-

D

P

T

A

D

D

D

L

A

T

G

L

L

T

I

A

A

P

P

C

G

P

P

L

-

W

-

D

-

G

-

L

-

D

-

L

-

G

-

T

-

S

-

R

-

V

-

W

W

M

F

S

Q

H
x
W

G

H

D

F

K

D

V

R

K

W

T

T

P

V

P

P

G

G

F

A

K

T

V

E

V

I

G

A

R

R

T

T

A

S

T

R

L

-

E

-

V

-

A

S

M

Q

A

A

D

F

E

V

A

L

R

G

R

R

I

A

Y

L

A

A

V

L

Q

Q

F

F

H

H

P

P

E

E

V

V

binding glutamine: C101 (= C83), W144 (≠ H134)

Sites not aligning to the query:

binding glutamine: 66, 190

Q9LVW7 Carbamoyl phosphate synthase small chain, chloroplastic; Carbamoyl phosphate synthetase glutamine chain; Protein VENOSA 6; EC 6.3.5.5 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
41% identity, 18% coverage: 6:96/515 of query aligns to 243:331/430 of Q9LVW7

query
sites
Q9LVW7

K

K

V

V

I

I

I

A

I

Y

D

D

Y

F

G

G

S

-

Q

-

V

I

T

K

Q

Q

L

N

I

I

A

L

R

R

V

L

R

S

E

S

A

Y

G

G

V

C

Y

Q

S

I

E

T

I

V

H

V

P

P

C

S

I

T

V

F

T

P

A

A

E

A

Q

E

V

A

R

L

A

K

M

M

K

N

P

P

A

D

A

G

I

I

I

L

L

F

S

S

G

N

G

G

P

P

A

-

S

-

V

-

G

G

E

D

K

P

D

S

A

A

-

V

-

P

P

Y

A

A

L

V

E

E

K

T

G

V

L

K

L

E

D

L

L

L

G

G

-

K

V

V

P

P

V

V

L

Y

G

G

I

I

C

C

Y

M

G

G

M

H

Q

Q

L

L

G

G

Q

Q

D

A

L

L

G

G

E

K

Sites not aligning to the query:

410 H→Y: In ven6-1; reticulate leaf phenotype.

8hx8A Crystal structure of 4-amino-4-deoxychorismate synthase from streptomyces venezuelae co-crystallized with chorismate (see paper)
28% identity, 27% coverage: 50:188/515 of query aligns to 50:187/673 of 8hx8A

query
sites
8hx8A

A

A

I

I

I

V

L

V

S

S

G

P

G

G

P

P

A

G

S

S

V

P

G

D

-

R

E

E

K

R

D

D

A

F

P

G

A

I

L

S

E

R

K

R

G

A

L

I

L

T

D

D

L

S

G

G

V

L

P

P

V

V

L

L

G

G

I

V

C

C

Y

L

G

G

M

H

Q

Q

L

G

L

I

G

A

Q

Q

D

L

L

F

G

G

E

T

L

V

A

G

T

-

S

-

E

-

T

-

R

-

E

-

Y

-

G

-

P

-

A

-

D

-

L

-

T

-

L

-

T

L

A

A

P

P

C

E

P

P

L

M

W

H

D

-

G

-

L

-

D

-

L

-

G

G

T

R

T

V

S

S

R

E

V

V

W

R

M

H

S

T

H

G

G

E

D

D

K

V

V

F

K

R

T

G

P

L

P

P

P

S

G

P

F

F

K

T

V

A

V

V

G

-

R

R

T

Y

A

H

T

S

L

L

E

A

V

A

A

T

A

D

M

L

A

P

D

D

E

E

-

L

-

E

-

P

-

L

-

A

-

W

-

S

-

D

-

G

-

V

-

M

-

G

-

L

-

R

-

H

-

R

A

E

R

K

R

P

I

L

Y

W

A

G

V

V

Q

Q

F

F

H

H

P

P

E

E

V

S

H
x
I

H

G

S
|
S

E

D

D

F

G

G

A

R

R

E

I

I

I

M

N

A

N

N

F

F

binding magnesium ion: I175 (≠ H176), S177 (= S178)

Sites not aligning to the query:

binding magnesium ion: 521, 655, 658
binding tryptophan: 231, 232, 233, 241, 243, 458, 459, 460, 614

1ce8B Carbamoyl phosphate synthetase from escherichis coli with complexed with the allosteric ligand imp (see paper)
36% identity, 16% coverage: 7:89/515 of query aligns to 193:274/379 of 1ce8B

query
sites
1ce8B

V

V

I

V

I

A

I

Y

D

D

Y

F

G

G

S

A

Q

K

V

-

T

-

Q

R

L

N

I

I

A

L

R

R

R

M

V

L

R

V

E

D

A

R

G

G

V

C

Y

R

S

L

E

T

I

I

H

V

P

P

C

A

I

Q

V

T

T

S

A

A

E

E

Q

D

V

V

R

L

A

K

M

M

K

N

P

P

A

D

A

G

I

I

I

F

L

L

S

S

G

N

G

G

P

P

A

G

S

D

V

P

G

A

E

P

K

C

D

D

A

Y

P

A

-

I

-

T

A

A

L

I

E

Q

K

K

G

-

L

F

L

L

D

E

L

T

G

D

V

I

P

P

V

V

L

F

G

G

I

I

C
|
C

Y

L

G

G

M

H

Q

Q

L

L

active site: C268 (= C83)

Sites not aligning to the query:

active site: 352, 354
binding L-ornithine: 119, 122

P0A6F1 Carbamoyl phosphate synthase small chain; Carbamoyl phosphate synthetase glutamine chain; EC 6.3.5.5 from Escherichia coli (strain K12) (see paper)
36% identity, 16% coverage: 7:89/515 of query aligns to 194:275/382 of P0A6F1

query
sites
P0A6F1

V

V

I

V

I

A

I

Y

D

D

Y

F

G

G

S

A

Q

K

V

-

T

-

Q

R

L

N

I

I

A

L

R

R

R

M

V

L

R

V

E

D

A

R

G

G

V

C

Y

R

S

L

E

T

I

I

H

V

P

P

C

A

I

Q

V

T

T

S

A

A

E

E

Q

D

V

V

R

L

A

K

M

M

K

N

P

P

A

D

A

G

I

I

I

F

L

L

S

S

G

N

G
|
G

P

P

A
x
G

S

D

V

P

G

A

E

P

K

C

D

D

A

Y

P

A

-

I

-

T

A

A

L

I

E

Q

K

K

G

-

L

F

L

L

D

E

L

T

G

D

V

I

P

P

V

V

L

F

G

G

I

I

C

C

Y
x
L

G

G

M

H

Q
|
Q

L

L

G241 (= G56) binding
G243 (≠ A58) binding
L270 (≠ Y84) binding
Q273 (= Q87) binding

Sites not aligning to the query:

47 binding
311 binding
313 binding
314 binding

P00900 Anthranilate synthase component 2; AS; ASII; Anthranilate synthase, GATase component; Anthranilate synthase, glutamine amidotransferase component; EC 4.1.3.27 from Serratia marcescens (see 3 papers)
24% identity, 36% coverage: 7:189/515 of query aligns to 4:187/193 of P00900

query
sites
P00900

V

I

I

L

D

D

Y

N

G

V

S

D

Q

S

V

F

T

T

Q

Y

L

N

I

L

A

V

R

D

R

Q

V

L

R

R

E

A

A

S

G

G

-

H

-

Q

-

V

V

I

Y

Y

S

R

E

N

I

Q

H

I

P

G

C

A

I

E

V

V

T

I

A

I

E

E

Q

R

V

L

R

Q

A

H

M

M

K

E

P

Q

A

P

A

V

I

L

I

M

L

L

S

S

G

P

G

G

P

P

A

G

S

T

V

P

G

S

E

E

K

A

D

G

A

C

-

M

P

P

A

E

L

L

E

L

K

Q

G

R

L

L

L

R

D

G

L

Q

G

-

V

L

P

P

V

I

L

I

G

G

I

I

C
|
C

Y

L

G

G

M

H

Q

Q

L

A

L

I

G

V

Q

E

D

A

L

Y

G

G

E

Q

L

V

A

G

T

Q

S

A

E

G

T

E

R

I

E

L

Y

H

G

G

P

K

A

A

D

S

L

A

T

I

L

A

T

H

A

D

P

G

C

E

P

G

L

M

W

F

D

A

G

G

L

M

D

-

L

-

G

A

T

N

T

P

S

L

R

P

V

V

W

A

M

R

S

Y

H

H

G

S

D

L

K

V

V

G

K

S

T

N

P

I

P

P

P

A

G

D

F

L

K

T

V

V

V

N

G

A

R

R

T

S

A

G

T

E

L

M

E

-

V

V

A

M

A

A

M

V

A

R

D

D

E

D

A

R

R

R

I

V

Y

C

A

G

V

F

Q

Q

F

F

H

H

P

P

E

E

V

S

H

I

H

L

S

T

E

T

D

H

G

G

A

A

R

R

I

L

N

E

N

Q

F

T

L

L

C84 (= C83) active site, Nucleophile; for GATase activity

Sites not aligning to the query:

1 modified: Initiator methionine, Removed

1i7qB Anthranilate synthase from s. Marcescens (see paper)
24% identity, 36% coverage: 7:189/515 of query aligns to 3:186/192 of 1i7qB

query
sites
1i7qB

V

I

I

L

D

D

Y

N

G

V

S

D

Q

S

V

F

T

T

Q

Y

L

N

I

L

A

V

R

D

R

Q

V

L

R

R

E

A

A

S

G

G

-

H

-

Q

-

V

V

I

Y

Y

S

R

E

N

I

Q

H

I

P

G

C

A

I

E

V

V

T

I

A

I

E

E

Q

R

V

L

R

Q

A

H

M

M

K

E

P

Q

A

P

A

V

I

L

I

M

L

L

S

S

G
x
P

G
|
G

P

P

A
x
G

S

T

V

P

G

S

E

E

K

A

D

G

A

C

-

M

P

P

A

E

L

L

E

L

K

Q

G

R

L

L

L

R

D

G

L

Q

G

-

V

L

P

P

V

I

L

I

G

G

I

I

C
|
C

Y
x
L

G

G

M

H

Q
|
Q

L

A

L

I

G

V

Q

E

D

A

L

Y

G

G

E

Q

L

V

A

G

T

Q

S

A

E

G

T

E

R

I

E

L

Y

H

G

G

P

K

A

A

D

S

L

A

T

I

L

A

T

H

A

D

P

G

C

E

P

G

L

M

W

F

D

A

G

G

L

-

D

-

L

M

G

A

T

N

T

P

S

L

R

P

V

V

W

A

M

R

S

Y

H
|
H

G
x
S

D
x
L

K

V

V

G

K

S

T

N

P

I

P

P

P

A

G

D

F

L

K

T

V

V

V

N

G

A

R

R

T

F

A

G

T

E

L

M

E

-

V

V

A

M

A

A

M

V

A

R

D

D

E

D

A

R

R

R

I

V

Y

C

A

G

V

F

Q

Q

F

F

H
|
H

P

P

E
|
E

V

S

H

I

H

L

S

T

E

T

D

H

G

G

A

A

R

R

I

L

N

E

N

Q

F

T

L

L

active site: G58 (≠ A58), C83 (= C83), L84 (≠ Y84), H169 (= H172), E171 (= E174)
binding glutamic acid: P55 (≠ G55), G56 (= G56), G58 (≠ A58), C83 (= C83), L84 (≠ Y84), Q87 (= Q87), H132 (= H134), S133 (≠ G135), L134 (≠ D136)

Query Sequence

>206477 MicrobesOnline__882:206477
MDAQTKVIIIDYGSQVTQLIARRVREAGVYSEIHPCIVTAEQVRAMKPAAIILSGGPASV
GEKDAPALEKGLLDLGVPVLGICYGMQLLGQDLGGELATSETREYGPADLTLTAPCPLWD
GLDLGTTSRVWMSHGDKVKTPPPGFKVVGRTATLEVAAMADEARRIYAVQFHPEVHHSED
GARIINNFLFHVAKLKADWTMSSFVERAVKEMAEVVGDRHVVCALSGGIDSTVVAVLLHK
AIGKQLHCIFVDNGVLRLNEGQEVVDYLREHFDLNLKYVQAQERFLSKLHGVDDPEQKRK
IIGYTFIEVFDEEAKALGHVDFLAQGTLYPDVIESVSHKGPSAVIKSHHNVGGLPEKMNL
KLIEPLRELFKDEVRKVAAELGLPDFIIWRHPFPGPGLAIRVIGEITEERLDILRRADKV
VQQELMSSGWYRKVWQGFAVLLPLKTVGVMGDGRTYEHVIALRIVDSVDAMTADWARLPS
ELLERISSRIINEVKGVNRVVYDISSKPPSTIEWE

Or try a new SitesBLAST search

SitesBLAST's Database

SitesBLAST's database includes (1) SwissProt entries with experimentally-supported functional features; and (2) protein structures with bound ligands, from the BioLip database.

by Morgan Price, Arkin group
Lawrence Berkeley National Laboratory