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)
41% identity, 100% coverage: 3:538/538 of query aligns to 6:555/555 of Q8IJR9

query
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Q8IJR9

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Y18 (≠ V15) mutation to F: Slight increase in affinity for glutamine. No defect in glutaminase activity.
H20 (≠ Q17) 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 (≠ R21) 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 (= R22) mutation to L: No effect on glutaminase activity. 1.4-fold decrease in affinity for glutamine.
C89 (= C85) 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 (= Q89) binding L-glutamine
C113 (≠ Y109) 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 (≠ G132) 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 (= W139) mutation to F: Slight decrease in affinity for glutamine. Slight increase in glutaminase activity.
N169 (≠ S141) binding L-glutamine; mutation to S: Slight increase in affinity for glutamine. No defect in glutaminase activity.
D172 (= D144) binding L-glutamine; mutation to A: 172-fold decrease in affinity for glutamine. Severe loss of glutaminase activity.
H208 (= H180) binding L-glutamine
Y212 (≠ T184) mutation to W: 2.7-fold decrease in affinity for glutamine. No defect in glutaminase activity.
E213 (≠ H185) 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 (= R307) binding XMP
D371 (= D346) Important for ATPPase activity; mutation to A: Impaired formation of adenyl-XMP intermediate. Slight increase in glutaminase activity.
E374 (= E349) mutation to L: 8.9-fold decrease in affinity for ammonia. Severe loss of glutaminase activity.
K376 (≠ G351) 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 (= K362) mutation to L: Severe loss of ATP pyrophosphatase (ATPPase) activity. 80 percent decrease in glutaminase activity. Impaired GMP formation.
T387 (≠ S363) mutation to A: No effect on ATP pyrophosphatase (ATPPase) activity. 20 percent decrease in glutaminase activity. No effect on GMP formation.
H388 (= H364) 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 (= H365) Important for ATPPase activity; mutation to A: Loss of ATP pyrophosphatase (ATPPase) activity. 67 percent decrease in glutaminase activity. Impaired GMP formation.
N390 (= N366) mutation to A: No effect on ATP pyrophosphatase (ATPPase) activity. Increases glutaminase activity. Loss of GMP formation.
K411 (= K387) mutation to L: 70 percent decrease in glutaminase activity. Loss of GMP formation.
D412 (= D388) mutation to A: 30 percent decrease in glutaminase activity. 7.9-fold decrease in affinity for glutamine.
D413 (≠ E389) mutation to A: 35 percent decrease in glutaminase activity. 3.6-fold decrease in affinity for glutamine.
K415 (≠ R391) mutation to L: Increases glutaminase activity. 4.2-fold decrease in affinity for ATP.
Q476 (= Q459) binding XMP
R539 (= R522) mutation to L: 85 percent decrease in glutaminase activity.
K547 (= K530) binding XMP; mutation to L: 85 percent decrease in glutaminase activity.
I552 (= I535) binding XMP
E553 (= E536) binding XMP; mutation to L: 85 percent decrease in glutaminase activity.
E555 (= E538) 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
47% identity, 99% coverage: 6:538/538 of query aligns to 2:475/475 of 2ywcA

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active site: G51 (≠ S59), R53 (≠ A61), C78 (= C85), Y79 (= Y86), H164 (= H180), E166 (= E182), D221 (= D238), K343 (= K387)
binding xanthosine-5'-monophosphate: R288 (= R307), P366 (= P410), G367 (= G411), P368 (= P412), Q408 (= Q459), K467 (= K530), T471 (= T534), I472 (= I535), E473 (= E536)

4wioA Crystal structure of the c89a gmp synthetase inactive mutant from plasmodium falciparum in complex with glutamine (see paper)
39% identity, 99% coverage: 4:538/538 of query aligns to 1:525/525 of 4wioA

query
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4wioA

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I

V

L

L

D

N

F

F

G

G

S

S

Q

Q

V

Y

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F

Q

H

L

L

I

I

A

V

R

K

R

R

V

L

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N

E

N

A

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H

K

V

I

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F

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S

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E

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-

H

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C

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-

T

T

D

K

D

D

W

Y

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D

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I

K

K

D

D

G

M

H

N

L

I

K

K

G

G

V

V

I

I

L

L

S

S

G

G

S
x
G

H

P

A

Y

S

S

V

V

Y

T

E

E

V

A

-

G

D

S

D

P

R

H

A

L

P

K

Q

K

A

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V

V

F

F

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L

Y

-

F

-

L

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-

K

G

K

V

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P

P

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I

L

F

G

G

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x
A

Y
|
Y

G

G

M

M

Q
|
Q

T

E

M

I

A

A

Q

V

Q

Q

L

M

G

N

G

G

K

E

V

V

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K

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K

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S

H

K

Q

T

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Y

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G

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C

A

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V

V

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N

-

I

-

L

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-

D

-

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-

I

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-

I

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Y

A

C

R

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N

H

F

T

S

D

S

-

A

-

M

-

D

-

L

-

Y

-

S

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-

Y

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K

-

L

-

M

-

N

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C

L

L

L

F

K

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D

N

I

I

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K

A

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D

D

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-

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-

H

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G

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M

-

L

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V

W

W

M

M

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x
N

H
|
H

G
x
N

D
|
D

K

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V

V

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T

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K

L

I

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P

P

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F

F

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P

L

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N

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K

A

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H

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F

I

Y

Y

G

G

V

V

Q

Q

F

Y

H
|
H

P

P

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|
E

V

V

T

Y

H

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S

Q

L

Q

D

G

G

R

E

A

L

I

M

L

F

E

Y

R

N

F

F

V

A

L

Y

G

N

I

I

C

C

G

K

A

C

K

K

P

K

D

Q

W

F

V

D

M

P

K

I

D

R

H

Y

I

H

A

E

E

L

A

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V

L

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K

K

N

I

I

R

E

E

K

Q

Y

V

K

G

H

D

D

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H

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Y

V

V

I

I

L

A

G

A

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M

S

S

G

G

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I

D
|
D

S

S

S

T

V

V

A

A

L

Y

I

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H

H

R

K

A

I

I

F

G

K

D

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Q

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T

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C

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I

F

F

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D

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N

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G

L

L

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N

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V

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M

F

F

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F

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K

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L

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I

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K

N

L

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A

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D

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N

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F

F

L

L

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Q

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G

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I

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K

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H

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N

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L

L

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K

L

F

K

K

L

L

L

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E

E

P

P

L

F

R

K

D

Y

L

L

F

F

K
|
K

D

D

E

D

V

V

R

K

E

T

L

L

G

S

V

R

A

E

L

L

G

N

L

L

P

P

P

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E

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M

I

V

T

Y

N

R

R

H

H

P

P

F

F

P

P

G

G

P

P

G

G

L

L

G

A

V

I

R

R

I

V

L

I

G

G

E

E

V

I

K

N

K

K

D

H

Y

K

A

L

D

N

L

I

L

L

R

R

R

E

A

V

D

D

A

D

I

I

F

F

I

I

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N

E

D

L

L

R

K

N

Q

F

Y

R

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D

-

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-

A

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G

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K

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G

W

L

Y

Y

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N

L

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T

I

S

S

Q

Q

A

A

F

F

T

A

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V

F

L

L

L

P

-

V

-

K

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V

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G

-

V

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M

-

G

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-

G

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-

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S

Y

Y

D

D

Y

Y

V

V

V

C

A

V

L

L

R

R

A

A

V

V

Q

K

T

T

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S

D

S

F

F

M

M

T

T

A

A

D

N

W

W

A

Y

E

Q

L

I

P

P

Y

Y

A

D

L

I

L

L

K

D

K

K

V

I

S

T

G

T

R

R

I

I

I

L

N

S

E

E

V

V

R

K

G

G

I

V

N

N

R

R

V

I

T

L

Y

Y

D

D

V

V

S

S

K

K

P

P

A

A

T

T

I

I

E

E

W

F

E

E

active site: G52 (≠ S59), A83 (≠ C85), Y84 (= Y86), H197 (= H180), E199 (= E182), D255 (= D238), K393 (= K387)
binding glutamine: Q87 (= Q89), N158 (≠ S141), H159 (= H142), N160 (≠ G143), D161 (= D144), H197 (= H180)

3uowA Crystal structure of pf10_0123, a gmp synthetase from plasmodium falciparum
39% identity, 100% coverage: 3:538/538 of query aligns to 1:517/517 of 3uowA

query
sites
3uowA

H

Y

D

D

K

K

I

I

L

L

I

V

L

L

D

N

F

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

H

K

V

I

Y

F

S

S

E

E

V

-

H

-

P

-

C

-

D

-

V

-

T

T

D

K

D

D

W

Y

V

G

R

V

E

E

Y

L

A

K

-

D

-

I

K

K

D

D

G

M

H

N

L

I

K

K

G

G

V

V

I

I

L

L

S

S

G

G

S
x
G

H

P

A

Y

S

S

V

V

Y

T

E

E

V

A

-

G

D

S

D

P

R

H

A

L

P

K

Q

K

A

E

V

V

F

F

E

E

L

Y

-

F

-

L

-

E

-

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

T

E

M

I

A

A

Q

V

Q

Q

L

M

G

N

G

G

K

E

V

V

E

K

G

K

S

S

H

K

Q

T

R

S

E

E

F

Y

G

G

Y

C

A

T

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D

V

V

R

N

-

I

-

L

-

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-

N

-

D

-

N

-

I

-

N

-

I

-

T

-

Y

A

C

R

R

G

N

H

F

T

S

D

S

-

A

-

M

-

D

-

L

-

Y

-

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-

N

-

Y

-

K

-

L

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M

-

N

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C

L

L

L

F

K

E

D

N

I

I

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K

A

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D

D

V

I

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T

P

-

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G

-

H

-

G

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M

-

L

-

K

-

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V

W

W

M

M

S

N

H

H

G

N

D

D

K

E

V

V

T

T

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K

L

I

P

P

P

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G

N

F

F

R

Y

L

L

M

V

A

S

S

S

T

S

G

E

S

N

C

C

P

L

I

I

A

C

G

S

M

I

A

Y

D

N

E

K

A

E

R

Y

H

N

F

I

Y

Y

G

G

V

V

Q

Q

F

Y

H
|
H

P

P

E
|
E

V

V

T

Y

H

E

T

S

Q

L

Q

D

G

G

R

E

A

L

I

M

L

F

E

Y

R

N

F

F

V

A

L

Y

G

N

I

I

C

C

G

K

A

C

K

K

P

K

D

F

W

D

V

P

M

I

K

R

D

Y

H

H

I

E

A

L

E

E

A

-

V

L

E

K

K

N

I

I

R

E

E

K

Q

Y

V

K

G

H

D

D

E

H

E

Y

V

V

I

I

L

A

G

A

L

M

S

S

G

G

V

I

D
|
D

S

S

S

T

V

V

A

A

L

Y

I

T

H

H

R

K

A

I

I

F

G

K

D

E

Q

R

L

F

T

F

C

G

V

I

F

F

V

I

D

D

H

N

G

G

L

L

R

R

L

K

D

N

E

E

G

A

K

E

M

N

V

V

M

Y

E

T

M

F

F

L

A

K

G

S

K

T

L

F

-

P

H

D

A

M

R

N

V

I

I

T

H

K

V

I

D

D

A

A

S

S

E

E

Q

N

F

F

L

L

G

S

H

N

L

L

K

Q

G

G

V

V

S

T

D

D

P

P

E

E

Q

Q

K

K

R
|
R

K

K

I

I

G

G

R

K

E

L

F

F

V

I

E

E

V

E

F

F

K

E

A

K

E

A

A

V

A

N

K

N

L

I

K

D

A

I

G

D

G

I

A

-

G

-

H

-

K

-

G

N

A

K

S

T

F

F

L

L

A

L

Q

Q

G

G

T

T

I

L

Y

Y

P

P

D

D

V

I

I

I

E

E

S

S

G

K

G

C

A

S

K

-

S

-

K

-

A

-

V

-

T

-

I

-

K

-

S

-

H

-

N

-

V

-

G

-

L

-

P

-

E

-

Q

-

L

L

G

K

L

F

K

K

L

L

L

F

E

E

P

P

L

F

R

K

D

Y

L

L

F

F

K
|
K

D

D

E

D

V

V

R

K

E

T

L

L

G

S

V

R

A

E

L

L

G

N

L

L

P

P

P

E

E

E

M

I

V

T

Y

N

R

R

H

H

P

P

F

F

P
|
P

G
|
G

P
|
P

G

G

L

L

G

A

V

I

R

R

I

V

L

I

G

G

E

E

V

I

K

N

K

K

D

H

Y

K

A

L

D

N

L

I

L

L

R

R

R

E

A

V

D

D

A

D

I

I

F

F

I

I

E

N

E

D

L

L

R

K

N

Q

F

Y

R

-

D

-

E

-

A

-

T

-

G

-

K

-

T

G

W

L

Y

Y

D

N

L

Q

T

I

S

S

Q
|
Q

A

A

F

F

T

A

V

V

F

L

L

L

P

S

V

S

K

K

S

S

V

V

G

-

V

-

M

-

G

-

D

-

G

-

R

-

T

-

Y

Y

D

D

Y

Y

V

V

V

C

A

V

L

L

R

R

A

A

V

V

Q

K

T

T

S

S

D

S

F

F

M

M

T

T

A

A

D

N

W

W

A

Y

E

Q

L

I

P

P

Y

Y

A

D

L

I

L

L

K

D

K

K

V

I

S

T

G

T

R

R

I

I

I

L

N

S

E

E

V

V

R

K

G

G

I

V

N

N

R

R

V

I

T

L

Y

Y

D

D

V

V

S

S

K
|
K

P

P

A

A

T
|
T

I
|
I

E
|
E

W

F

E

E

active site: G53 (≠ S59), C84 (= C85), Y85 (= Y86), H198 (= H180), E200 (= E182), D255 (= D238), K381 (= K387)
binding xanthosine-5'-monophosphate: R325 (= R307), P404 (= P410), G405 (= G411), P406 (= P412), Q446 (= Q459), K509 (= K530), T513 (= T534), I514 (= I535), E515 (= E536)

3uowB Crystal structure of pf10_0123, a gmp synthetase from plasmodium falciparum
39% identity, 99% coverage: 5:538/538 of query aligns to 1:477/477 of 3uowB

query
sites
3uowB

K

K

I

I

L

L

I

V

L

L

D

N

F

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

H

K

V

I

Y

F

S

S

E

E

V

-

H

-

P

-

C

-

D

-

V

-

T

T

D

K

D

D

W

Y

V

-

R

-

E

K

Y

D

A

I

K

K

D

D

G

M

H

N

L

I

K

K

G

G

V

V

I

I

L

L

S

S

G

G

-
x
G

S

P

H

Y

A

S

S

E

V

V

Y

F

E

E

V

-

D

-

R

-

A

-

P

-

Q

-

A

Y

V

F

F

L

E

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

T

E

M

I

A

A

Q

V

Q

Q

L

M

-

N

-

Y

G

G

G

C

K

T

V

D

E

V

G

N

S

I

H

N

Q

I

R

N

E

N

F

I

G

T

Y

Y

A

C

E

A

V

M

R

D

A

L

R

Y

G

S

H

N

T

Y

D

K

L

L

L

M

K

N

D

C

I

C

-

L

-

F

-

E

-

N

-

I

-

K

A

S

D

D

V

I

T

T

P

-

E

-

G

-

H

-

G

-

M

-

L

-

K

-

V

V

W

W

M

M

S

N

H

H

G

N

D

D

K

E

V

V

T

T

E

K

L

I

P

P

P

E

G

N

F

F

R

Y

L

L

M

V

A

S

S

S

T

S

G

E

S

N

C

C

P

L

I

I

A

C

G

S

M

I

A

Y

D

N

E

K

A

E

R

Y

H

N

F

I

Y

Y

G

G

V

V

Q

Q

F

Y

H
|
H

P

P

E
|
E

V

V

T

Y

H

E

T

S

Q

L

Q

D

G

G

R

E

A

L

I

M

L

F

E

Y

R

N

F

F

V

A

L

Y

G

N

I

I

C

C

G

K

A

C

K

K

P

F

D

D

W

P

V

I

M

-

K

R

D

Y

H

H

I

E

A

L

E

E

A

-

V

L

E

K

K

N

I

I

R

E

E

K

Q

Y

V

K

G

H

D

D

E

H

E

Y

V

V

I

I

L

A

G

A

L

M

S

S

G

G

V

I

D
|
D

S

S

S

T

V

V

A

A

L

Y

I

T

H

H

R

K

A

I

I

F

G

K

D

E

Q

R

L

F

T

F

C

G

V

I

F

F

V

I

D

D

H

N

G

G

L

L

R

R

L

K

D

N

E

E

G

A

K

E

M

N

V

V

M

Y

E

T

M

F

F

L

A

K

G

S

K

T

L

F

-

P

H

D

A

M

R

N

V

I

I

T

H

K

V

I

D

D

A

A

S

S

E

E

Q

N

F

F

L

L

G

S

H

N

L

L

K

Q

G

G

V

V

S

T

D

D

P

P

E

E

Q

Q

K

K

R
|
R

K

K

I

I

G

G

R

K

E

L

F

F

V

I

E

E

V

E

F

F

K

E

A

K

E

-

A

-

K

-

L

-

K

A

A

V

G

N

A

I

G

D

H

D

K

I

G

N

A

K

S

T

F

F

L

L

A

L

Q

Q

G

G

T

T

I

L

Y

Y

P

P

D

D

V

I

I

I

E

E

S

S

G

K

A

-

K

-

S

-

K

-

A

-

V

-

T

-

I

-

K

-

S

-

H

-

N

-

V

-

G

-

L

-

P

-

E

-

Q

-

L

-

G

-

L

F

K

K

L

L

L

F

E

E

P

P

L

F

R

K

D

Y

L

L

F

F

K
|
K

D

D

E

D

V

V

R

K

E

T

L

L

G

S

V

R

A

E

L

L

G

N

L

L

P

P

P

E

E

E

M

I

V

T

Y

N

R

R

H

H

P

P

F

F

P
|
P

G
|
G

P
|
P

G

G

L

L

G

A

V

I

R

R

I

V

L

I

G

G

E

E

V

I

K

N

K

K

D

H

Y

K

A

L

D

N

L

I

L

L

R

R

R

E

A

V

D

D

A

D

I

I

F

F

I

I

E

N

E

D

L

L

R

K

N

Q

F

Y

R

-

D

-

E

-

A

-

T

-

G

-

K

-

T

G

W

L

Y

Y

D

N

L

Q

T

I

S

S

Q
|
Q

A

A

F

F

T

A

V

V

F

L

L

L

P

S

V

S

K

K

S

S

V

V

G

G

V

-

M

-

G

-

D

-

G

-

R

-

T

-

Y

Y

D

D

Y

Y

V

V

V

C

A

V

L

L

R

R

A

A

V

V

Q

K

T

T

S

S

D

S

F

F

M

M

T

T

A

A

D

N

W

W

A

Y

E

Q

L

I

P

P

Y

Y

A

D

L

I

L

L

K

D

K

K

V

I

S

T

G

T

R

R

I

I

I

L

N

S

E

E

V

V

R

K

G

G

I

V

N

N

R

R

V

I

T

L

Y

Y

D

D

V

V

S

S

K
|
K

P

P

A

A

T
|
T

I
|
I

E
|
E

W

F

E

E

active site: G47 (vs. gap), C67 (= C85), Y68 (= Y86), H162 (= H180), E164 (= E182), D218 (= D238), K340 (= K387)
binding xanthosine-5'-monophosphate: R288 (= R307), P363 (= P410), G364 (= G411), P365 (= P412), Q405 (= Q459), K469 (= K530), T473 (= T534), I474 (= I535), E475 (= E536)

2vxoB Human gmp synthetase in complex with xmp (see paper)
36% identity, 97% coverage: 6:525/538 of query aligns to 6:527/658 of 2vxoB

query
sites
2vxoB

I

V

L

V

I

I

L

L

D

D

F

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

H

F

V

V

Y

Q

S

S

E

E

V

I

H

F

P

P

C

L

D

E

V

T

T

P

D

A

D

F

W

A

V

I

R

K

E

E

Y

Q

A

G

K

-

D

-

G

-

H

-

L

F

K

R

G

A

V

I

I

I

L

I

S

S

G

G

S
x
G

H

P

A

N

S

S

V

V

Y

Y

E

A

V

E

D

D

D

-

R

-

A

A

P

P

-

W

-

F

-

D

Q

P

A

A

V

I

F

F

E

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

T

M

M

M

A

N

Q

K

Q

V

L

F

G

G

K

T

V

V

E

-

G

-

S

-

H

H

Q

K

R

K

E

S

F

D

G

G

Y

V

A

F

E

N

V

I

R

S

A

V

R

D

G

N

H

T

T

C

D

S

L

L

L

F

K

R

D

G

I

L

A

Q

D

K

V

E

T

E

T

V

P

-

E

-

G

-

H

-

G

-

M

-

L

-

K

-

V

V

W

L

M

L

S

T

H

H

G

G

D

D

K

S

V

V

T

D

E

K

L

V

P

A

P

D

G

G

F

F

R

K

L

V

M

V

A

A

S

R

T

S

G

G

S

N

C

I

P

-

I

V

A

A

G

G

M

I

A

A

D

N

E

E

A

S

R

K

H

K

F

L

Y

Y

G

G

V

A

Q

Q

F

F

H
|
H

P

P

E
|
E

V

V

T

G

H

L

T

T

Q

E

Q

N

G

G

R

K

A

V

I

I

L

L

E

K

R

N

F

F

V

L

L

Y

G

D

I

I

C

A

G

G

A

C

K

S

P

G

D

T

W

F

V

T

M

V

K

Q

D

N

H

R

I

E

A

L

E

E

A

C

V

I

E

R

K

E

I

I

R

K

E

E

Q

R

V

V

G

G

D

T

E

S

E

K

V

V

I

L

L

V

G

L

L

L

S

S

G

G

V

V

D
|
D

S

S

S

T

V

V

A

C

A

T

A

A

L

L

I

L

H

N

R

R

A

A

I

L

G

N

-

Q

D

E

Q

Q

L

V

T

I

C

A

V

V

F

H

V

I

D

D

H

N

G

G

L

F

L

M

R

R

L

K

D

R

E

E

G

S

K

Q

M

S

V

V

M

E

E

E

M

A

F

L

A

K

G

-

K

K

L

L

H

G

A

I

R

Q

V

V

I

K

H

V

V

I

D

N

A

A

S

A

E

H

Q

S

F

F

L

Y

G

N

-

G

-

T

-

L

-

P

-

R

-

I

-

S

-

K

H

T

L

L

K

N

G

M

V

T

S

T

D

S

P

P

E

E

Q

E

K

K

R
|
R

K

K

I

I

G

G

R

D

E

T

F

F

V

V

E

K

V

I

F

A

K

N

A

E

E

V

A

I

A

G

K

E

L

M

K

N

A

L

G

-

A

-

G

-

H

K

K

P

G

E

A

E

S

V

F

F

L

L

A

A

Q

Q

G

G

T

T

I

L

Y

R

P

P

D

D

V

L

I

I

E

E

S

S

G

A

G

S

-

L

A

V

K

A

S

S

K
x
G

K
|
K

A

A

V

E

T

L

I

I

K

K

S

T

H

H

N

N

V

D

G

T

G

E

L

L

P

I

E

R

Q

K

L

L

G

R

L

E

-

E

-

G

K

K

L

V

L

I

E

E

P

P

L

L

R

K

D

D

L

F

F

H

K
|
K

D

D

E

E

V

V

R

R

E

I

L

L

G

G

V

R

A

E

L

L

G

G

L

L

P

P

P

E

E

E

M

L

V

V

Y

S

R

R

H

H

P

P

F

F

P
|
P

G
|
G

P
|
P

G

G

L

L

G

A

V

I

R

R

I

V

L

I

G

C

E

A

-

E

-

P

-

Y

V

I

K

C

K

K

D

D

Y

F

A

P

D

E

-

T

-

N

-

I

-

L

-

K

-

I

-

V

-

A

-

D

-

F

-

S

-

A

-

S

-

V

-

K

-

P

-

H

-

T

L

L

R

Q

R

R

A

V

D

K

A

A

I

C

F

T

I

T

E

E

L

-

R

-

N

-

F

-

R

-

D

D

E

Q

A

E

T

K

G

L

K

M

T

Q

W

I

Y

T

D

S

L

L

T

H

S

S

-

L

Q

N

A

A

F

F

T

-

V

-

F

L

L

L

P

P

V

I

K

K

S

T

V

V

G

G

V

V

M

Q

G

G

D

D

G

C

R
|
R

T

S

Y

Y

D

S

Y

Y

V

V

V

C

A

G

L

I

R

-

A

-

V

-

Q

-

T

-

S

S

D

S

F

K

M

D

T

E

A

P

D

D

W

W

A

E

E

S

L

L

P

I

Y

F

A

-

L

-

L

L

K

A

K

R

V

L

S

I

G

P

R

R

I

M

I

C

N

H

E

N

V

V

R

-

G

-

I

-

N

N

R

R

V

V

T

V

Y

Y

active site: G55 (≠ S59), C82 (= C85), Y83 (= Y86), H165 (= H180), E167 (= E182), D223 (= D238), K381 (= K387)
binding xanthosine-5'-monophosphate: R302 (= R307), G348 (≠ K356), K349 (= K357), P404 (= P410), G405 (= G411), P406 (= P412), R489 (= R477)

Sites not aligning to the query:

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

P49915 GMP synthase [glutamine-hydrolyzing]; GMP synthetase; Glutamine amidotransferase; EC 6.3.5.2 from Homo sapiens (Human) (see paper)
35% identity, 97% coverage: 6:525/538 of query aligns to 28:562/693 of P49915

query
sites
P49915

I

V

L

V

I

I

L

L

D

D

F

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

H

F

V

V

Y

Q

S

S

E

E

V

I

H

F

P

P

C

L

D

E

V

T

T

P

D

A

D

F

W

A

V

I

R

K

E

E

Y

Q

A

G

K

-

D

-

G

-

H

-

L

F

K

R

G

A

V

I

I

I

L

I

S

S

G

G

S

G

H

P

A

N

S

S

V

V

Y

Y

E

A

V

E

D

D

D

-

R

-

A

A

P

P

-

W

-

F

-

D

Q

P

A

A

V

I

F

F

E

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

T

M

M

M

A

N

Q

K

Q

V

L

F

G

G

K

T

V

V

E

H

G

K

S

K

H

S

Q

V

R

R

E

E

F

D

G

G

Y

V

A

F

E

N

V

I

R

S

A

V

R

D

G

N

H

T

T

C

D

S

L

L

L

F

K

R

D

G

I

L

A

Q

D

K

V

E

T

E

T

V

P

-

E

-

G

-

H

-

G

-

M

-

L

-

K

-

V

V

W

L

M

L

S

T

H

H

G

G

D

D

K

S

V

V

T

D

E

K

L

V

P

A

P

D

G

G

F

F

R

K

L

V

M

V

A

A

S

R

T

S

G

G

S

N

C

I

P

-

I

V

A

A

G

G

M

I

A

A

D

N

E

E

A

S

R

K

H

K

F

L

Y

Y

G

G

V

A

Q

Q

F

F

H
|
H

P

P

E
|
E

V

V

T

G

H

L

T

T

Q

E

Q

N

G

G

R

K

A

V

I

I

L

L

E

K

R

N

F

F

V

L

L

Y

G

D

I

I

C

A

G

G

A

C

K

S

P

G

D

T

W

F

V

T

M

V

K

Q

D

N

H

R

I

E

A

L

E

E

A

C

V

I

E

R

K

E

I

I

R

K

E

E

Q

R

V

V

G

G

D

T

E

S

E

K

V

V

I

L

L

V

G

L

L

L

S

S

G

G

V

V

D

D

S

S

S

T

V

V

A

C

A

T

A

A

L

L

I

L

H

N

R

R

A

A

I

L

G

N

-

Q

D

E

Q

Q

L

V

T

I

C

A

V

V

F

H

V

I

D

D

H

N

G

G

L

F

L

M

R

R

L

K

D

R

E

E

G

S

K

Q

M

S

V

V

M

E

E

E

M

A

F

L

A

K

G

-

K

K

L

L

H

G

A

I

R

Q

V

V

I

K

H

V

V

I

D

N

A

A

S

A

E

H

Q

S

F

F

L

Y

G

N

-

G

-

T

-

L

-

P

-

I

-

S

-

D

-

E

-

D

-

R

-

T

-

P

-

R

-

K

-

R

-

I

-

S

-

K

H

T

L

L

K

N

G

M

V

T

S

T

D

S

P

P

E

E

Q

E

K

K

R
|
R

K

K

I

I

G

G

R

D

E

T

F

F

V

V

E

K

V

I

F

A

K

N

A

E

E

V

A

I

A

G

K

E

L

M

K

N

A

L

G

-

A

-

G

-

H

K

K

P

G

E

A

E

S

V

F

F

L

L

A

A

Q

Q

G

G

T

T

I

L

Y

R

P

P

D

D

V

L

I

I

E

E

S

S

G

A

G

S

-

L

A

V

K

A

S

S

K

G

K

K

A

A

V

E

T

L

I

I

K

K

S

T

H

H

N

N

V

D

G

T

G

E

L

L

P

I

E

R

Q

K

L

L

G

R

L

E

-

E

-

G

K

K

L

V

L

I

E

E

P

P

L

L

R

K

D

D

L

F

F

H

K

K

D

D

E

E

V

V

R

R

E

I

L

L

G

G

V

R

A

E

L

L

G

G

L

L

P

P

P

E

E

E

M

L

V

V

Y

S

R

R

H

H

P

P

F

F

P

P

G

G

P

P

G

G

L

L

G

A

V

I

R

R

I

V

L

I

G

C

E

A

-

E

-

P

-

Y

V

I

K

C

K

K

D

D

Y

F

A

P

D

E

-

T

-

N

-

I

-

L

-

K

-

I

-

V

-

A

-

D

-

F

-

S

-

A

-

S

-

V

-

K

-

P

-

H

-

T

L

L

R

Q

R

R

A

V

D

K

A

A

I

C

F

T

I

T

E

E

L

-

R

-

N

-

F

-

R

-

D

D

E

Q

A

E

T

K

G

L

K

M

T

Q

W

I

Y

T

D

S

L

L

T

H

S

S

-

L

Q

N

A

A

F

F

T

-

V

-

F

L

L

L

P

P

V

I

K

K

S

T

V

V

G

G

V

V

M

Q

G

G

D
|
D

G

C

R

R

T

S

Y

Y

D

S

Y

Y

V

V

V

C

A

G

L

I

R

-

A

-

V

-

Q

-

T

-

S

S

D

S

F

K

M

D

T

E

A

P

D

D

W

W

A

E

E

S

L

L

P

I

Y

F

A

-

L

-

L

L

K

A

K

R

V

L

S

I

G

P

R

R

I

M

I

C

N

H

E

N

V

V

R

-

G

-

I

-

N

N

R

R

V

V

T

V

Y

Y

C104 (= C85) active site, For GATase activity
H190 (= H180) active site, For GATase activity
E192 (= E182) active site, For GATase activity
R337 (= R307) binding XMP
D522 (= D475) binding XMP

Sites not aligning to the query:

610 binding XMP
685 binding XMP
691 binding XMP

6jp9A Crsytal structure of a xmp complexed atppase subunit of m. Jannaschii gmp synthetase (see paper)
48% identity, 61% coverage: 210:538/538 of query aligns to 5:298/298 of 6jp9A

query
sites
6jp9A

K

K

D

K

H

F

I

I

A

D

E

E

A

A

V

V

E

E

K

E

I

I

R

K

E

Q

Q

Q

V

I

G

S

D

D

E

R

E

K

V

A

I

I

L

I

G

A

L

L

S

S

G

G

V

V

D
|
D

S

S

V

V

A

A

A

V

L

L

I

T

H

H

R

K

A

A

I

I

G

G

D

D

Q

K

L

L

T

T

C

A

V

V

F

F

V

V

D

D

H

T

G

G

L

L

L

M

R

R

L

K

D

G

E

E

G

R

K

E

M

E

V

V

M

E

E

K

M

T

F

F

A

R

G

D

K

K

L

L

H

G

A

L

R

N

V

L

I

I

H

V

V

V

D

D

A

A

S

K

E

D

Q

R

F

F

L

L

G

N

H

A

L

L

K

K

G

G

V

V

S

T

D

D

P

P

E

E

Q

E

K

K

R
|
R

K

K

I

I

G

G

R

K

E

L

F

F

V

I

E

D

V

V

F

F

K

E

A

E

E

I

A

A

A

E

K

D

L

I

K

K

A

-

G

-

A

-

G

-

H

-

K

-

G

-

A

A

S

E

F

V

L

L

A

V

Q

Q

G

G

T

T

I

I

Y

A

P

P

D

D

V

-

I

-

E

-

S

-

G

-

A

-

K

-

S

-

K

-

A

-

V

-

T

-

I

-

K

-

S

-

H

-

H

H

N

N

V

V

G

-

G

A

L

L

P

P

E

H

Q

G

L

M

G

V

L

L

K

E

L

V

E

E

P

P

L

L

R

R

D

E

L

L

F

Y

K
|
K

D

D

E

E

V

V

R

R

E

L

L

L

G

A

V

K

A

E

L

L

G

G

L

L

P

P

P

D

E

S

M

I

V

V

Y

Y

R

R

H

Q

P

P

F

F

P
|
P

G
|
G

P
|
P

G

G

L

L

G

A

V

V

R

R

I

V

L

L

G

G

E

E

V

V

K

T

K

E

D

E

Y

K

A

L

D

N

L

I

L

C

R

R

R

E

A

A

D

N

A

A

I

I

F

V

I

E

E

E

L

V

R

K

N

-

F

-

R

K

D

A

E

N

A

L

T

D

G

K

K

D

T

L

W

W

Y

-

D

-

L

-

T

-

S

-

Q
|
Q

A

Y

F

F

T

A

V

V

F

V

L

L

P

D

V

C

K

K

S

A

V

T

G

G

V

V

M

K

G

G

D

D

G

-

R

R

T

E

Y

Y

D

N

Y

W

V

I

V

V

A

A

L

L

R

R

A

M

V

V

Q

K

T

S

S

L

D

D

F

A

M

M

T

T

A

A

D

H

W

V

A

P

E

E

L

I

P

P

Y

F

A

D

L

L

K

K

K

R

V

I

S

S

G

K

R

R

I

I

I

T

N

S

E

E

V

I

R

P

G

N

I

V

N

A

R

R

V

V

T

V

Y

F

D

D

V

I

S

T

S

D

K
|
K

P

P

A

A

T
|
T

I
|
I

E
|
E

W

F

E

E

active site: D33 (= D238), K155 (= K387)
binding xanthosine-5'-monophosphate: R102 (= R307), P178 (= P410), G179 (= G411), P180 (= P412), Q220 (= Q459), K290 (= K530), T294 (= T534), I295 (= I535), E296 (= E536)

7yc6A Crystal structure of d110p mutant of gatase subunit of methanocaldococcus jannaschii gmp synthetase
32% identity, 37% coverage: 6:204/538 of query aligns to 2:181/183 of 7yc6A

query
sites
7yc6A

I

I

L

V

I

I

L

L

D

D

F

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

H

G

V

V

Y

S

S

S

E

K

V

I

H

V

P

P

C

-

D

-

V

-

T

N

D

T

W

P

V

L

R

E

E

E

Y

I

A

E

K

S

D

N

G

K

H

E

L

V

K

K

G

G

V

I

I

I

L

L

S

S

G

G

S

-

H

-

A

G

S

P

V

D

Y

I

E

E

V

K

D

A

D

K

R

N

A

C

P

I

Q

D

A

I

V

A

F

L

E

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

T

L

M

I

A

A

Q

L

Q

A

L

Y

G

G

K

E

V

V

E

-

G

-

S

-

H

-

Q

-

R

-

E

-

F

-

G

-

Y

-

A

-

E

-

V

-

R

-

A

-

R

-

G

G

H

R

T

A

D

A

L

L

L

T

K

K

D

V

I

Y

A

V

D
|
D

V

K

T

E

T

N

P

P

E

L

G

F

H

K

G

N

M

V

-

P

-

R

-

E

L

F

K

N

V

A

W

W

M

A

S

S

H

H

G

K

D

D

K
x
E

V

V

T

K

E

K

L

V

P

P

P

E

G

G

F

F

R

E

L

I

M

L

A

A

S
x
H

T

S

G

D

S

I

C
|
C

P

Q

I

V

A

E

G

A

M

M

A

K

D

H

E

K

A

T

R

K

H

P

F

I

Y

Y

G

G

V

V

Q

Q

F

F

H
|
H

P

P

E

E

V

V

T

A

H

H

T

T

Q

E

Q

Y

G

G

R

N

A

E

I

I

L

L

E

K

R

N

F

F

V

C

L

-

G

K

I

V

C

C

G

G

A

Y

K

K

binding zinc ion: C76 (= C85), D101 (= D126), E123 (≠ K145), E123 (≠ K145), H136 (≠ S158), C140 (= C162), C140 (= C162), H158 (= H180)

8hx8A Crystal structure of 4-amino-4-deoxychorismate synthase from streptomyces venezuelae co-crystallized with chorismate (see paper)
28% identity, 36% coverage: 3:196/538 of query aligns to 3:187/673 of 8hx8A

query
sites
8hx8A

H

H

D

M

K

R

I

T

L

L

I

L

L

I

D

D

F

N

G

Y

S

D

Q

S

V

F

T

T

Q

H

L

N

I

L

A

F

R

Q

R

Y

V

I

R

G

E

E

A

A

H

T

V

G

Y

Q

S

P

E

P

V

V

H

V

-

V

P

P

C

N

D

D

V

A

T

-

D

-

D

D

W

W

V

S

R

R

E

L

Y

P

A

V

K

E

D

D

G

-

H

-

L

F

K

D

G

A

V

I

I

V

L

V

S

S

G

P

S

G

H

P

A

G

S

S

V

P

Y

D

E

R

V

E

D

R

D

D

R

F

-

G

-

I

A

S

P

R

Q

R

A

A

V

I

F

T

E

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

T

G

M

I

A

A

Q

Q

Q

L

L

F

G

G

K

T

V

V

-

G

-

L

-

A

-

P

E

E

G

P

S

M

H

H

Q

G

R

R

E

-

F

-

G

-

Y

V

A

S

E

E

V

V

R

R

A

H

R

T

G

G

H

E

T

-

D

D

L

V

L

F

K

R

D

G

I

L

A

P

D

S

V

P

T

F

T

T

P

-

E

-

G

-

H

-

G

-

M

-

L

-

K

-

V

A

W

V

M

R

S

Y

H

H

G

S

D

L

K

A

V

A

T

T

E

D

L

L

P

P

P

D

G

E

F

L

R

E

L

P

M

L

A

A

S

W

T

S

G

D

S

D

C

G

P

V

I

V

A

M

G

G

M

L

A

R

D

H

E

R

A

E

R

K

H

P

F

L

Y

W

G

G

V

V

Q

Q

F

F

H

H

P

P

E

E

V

S

T
x
I

H

G

T
x
S

Q

D

Q

F

G

G

R

R

A

E

I

I

L

M

E

A

R

N

F

F

binding magnesium ion: I175 (≠ T184), S177 (≠ T186)

Sites not aligning to the query:

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

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)
29% identity, 22% coverage: 79:197/538 of query aligns to 73:185/187 of P00903

query
sites
P00903

V

L

P

P

V

I

L

L

G

G

I

V

C
|
C

Y

L

G

G

M

H

Q

Q

T

A

M

M

A

A

Q

Q

Q

A

L

F

G

G

K

K

V

V

E

V

G

R

S

A

H

A

Q

K

R

V

E

M

F

H

G

G

Y

K

A

T

E

S

V

P

R

I

A

T

R

H

G

N

H

G

T

E

D

G

L

V

L

F

K

R

D

G

I

L

A

A

D

N

V

P

T

L

T

T

P

V

E

T

G

R

H

Y

G

H

M

S

L

L

K

V

V

V

W

-

M

-

S

-

H

-

G

-

D

-

K

E

V

P

T

D

E

S

L

L

P

P

P

A

G

C

F

F

R

D

L

V

M

T

A

A

S

W

T

S

G

E

S

T

C

R

P

E

I

I

A

M

G

G

M

I

A

R

D

H

E

R

A

Q

R

W

H

D

F

L

Y

E

G

G

V

V

Q

Q

F

F

H
|
H

P

P

E
|
E

V

S

T

I

H

L

T

S

Q

E

Q

Q

G

G

R

H

A

Q

I

L

L

L

E

A

R

N

F

F

V

L

C79 (= C85) mutation to S: 10000-fold decrease in catalytic efficiency.
H168 (= H180) mutation to Q: Loss of activity.
E170 (= E182) 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.

Query Sequence

>WP_038216896.1 NCBI__GCF_000745855.1:WP_038216896.1
MSHDKILILDFGSQVTQLIARRVREAHVYSEVHPCDVTDDWVREYAKDGHLKGVILSGSH
ASVYEVDDRAPQAVFELGVPVLGICYGMQTMAQQLGGKVEGSHQREFGYAEVRARGHTDL
LKDIADVTTPEGHGMLKVWMSHGDKVTELPPGFRLMASTGSCPIAGMADEARHFYGVQFH
PEVTHTQQGRAILERFVLGICGAKPDWVMKDHIAEAVEKIREQVGDEEVILGLSGGVDSS
VAAALIHRAIGDQLTCVFVDHGLLRLDEGKMVMEMFAGKLHARVIHVDASEQFLGHLKGV
SDPEQKRKIIGREFVEVFKAEAAKLKAGGAGHKGASFLAQGTIYPDVIESGGAKSKKAVT
IKSHHNVGGLPEQLGLKLLEPLRDLFKDEVRELGVALGLPPEMVYRHPFPGPGLGVRILG
EVKKDYADLLRRADAIFIEELRNFRDEATGKTWYDLTSQAFTVFLPVKSVGVMGDGRTYD
YVVALRAVQTSDFMTADWAELPYALLKKVSGRIINEVRGINRVTYDVSSKPPATIEWE

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