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, 100% coverage: 3:514/514 of query aligns to 7:555/555 of Q8IJR9

query
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Y18 (≠ F14) mutation to F: Slight increase in affinity for glutamine. No defect in glutaminase activity.
H20 (≠ Q16) 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 (≠ R20) 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 (= R21) mutation to L: No effect on glutaminase activity. 1.4-fold decrease in affinity for glutamine.
C89 (= C81) 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 (= Q85) binding L-glutamine
C113 (≠ R105) 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 (vs. gap) 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 (= W130) mutation to F: Slight decrease in affinity for glutamine. Slight increase in glutaminase activity.
N169 (≠ S132) binding L-glutamine; mutation to S: Slight increase in affinity for glutamine. No defect in glutaminase activity.
D172 (= D135) binding L-glutamine; mutation to A: 172-fold decrease in affinity for glutamine. Severe loss of glutaminase activity.
H208 (= H171) binding L-glutamine
Y212 (≠ A175) mutation to W: 2.7-fold decrease in affinity for glutamine. No defect in glutaminase activity.
E213 (≠ H176) 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 (= R298) binding XMP
D371 (= D330) Important for ATPPase activity; mutation to A: Impaired formation of adenyl-XMP intermediate. Slight increase in glutaminase activity.
E374 (= E333) mutation to L: 8.9-fold decrease in affinity for ammonia. Severe loss of glutaminase activity.
K376 (≠ I335) 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 (= K345) mutation to L: Severe loss of ATP pyrophosphatase (ATPPase) activity. 80 percent decrease in glutaminase activity. Impaired GMP formation.
T387 (≠ S346) mutation to A: No effect on ATP pyrophosphatase (ATPPase) activity. 20 percent decrease in glutaminase activity. No effect on GMP formation.
H388 (= H347) 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 (= H348) Important for ATPPase activity; mutation to A: Loss of ATP pyrophosphatase (ATPPase) activity. 67 percent decrease in glutaminase activity. Impaired GMP formation.
N390 (= N349) mutation to A: No effect on ATP pyrophosphatase (ATPPase) activity. Increases glutaminase activity. Loss of GMP formation.
K411 (= K370) mutation to L: 70 percent decrease in glutaminase activity. Loss of GMP formation.
D412 (= D371) mutation to A: 30 percent decrease in glutaminase activity. 7.9-fold decrease in affinity for glutamine.
D413 (≠ E372) mutation to A: 35 percent decrease in glutaminase activity. 3.6-fold decrease in affinity for glutamine.
K415 (≠ R374) mutation to L: Increases glutaminase activity. 4.2-fold decrease in affinity for ATP.
Q476 (= Q435) binding XMP
R539 (= R498) mutation to L: 85 percent decrease in glutaminase activity.
K547 (= K506) binding XMP; mutation to L: 85 percent decrease in glutaminase activity.
I552 (= I511) binding XMP
E553 (= E512) binding XMP; mutation to L: 85 percent decrease in glutaminase activity.
E555 (= E514) 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
49% identity, 99% coverage: 5:514/514 of query aligns to 2:475/475 of 2ywcA

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active site: G51 (= G54), R53 (≠ S56), C78 (= C81), Y79 (= Y82), H164 (= H171), E166 (= E173), D221 (= D229), K343 (= K370)
binding xanthosine-5'-monophosphate: R288 (= R298), P366 (= P393), G367 (= G394), P368 (= P395), Q408 (= Q435), K467 (= K506), T471 (= T510), I472 (= I511), E473 (= E512)

4wioA Crystal structure of the c89a gmp synthetase inactive mutant from plasmodium falciparum in complex with glutamine (see paper)
40% identity, 100% coverage: 3:514/514 of query aligns to 1:525/525 of 4wioA

query
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4wioA

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G

I

V

I

I

L

L

S

S

G

G

G
|
G

P

P

S

Y

S

S

V

V

H

T

D

E

V

A

D

G

A

S

P

P

S

H

V

L

D

K

P

K

A

E

L

V

F

F

A

E

M

Y

G

F

L

L

-

E

-

K

-

I

P

P

V

I

L

F

G

G

I

I

C
x
A

Y
|
Y

G

G

L

M

Q
|
Q

L

E

M

I

A

A

Q

V

L

Q

L

M

G

N

G

G

R

E

V

V

G

K

K

K

A

S

E

K

H

T

R

S

E

E

Y

Y

G

G

R

C

A

T

H

D

L

V

Q

N

I

I

K

L

-

R

-

N

-

D

-

N

-

I

E

N

A

N

I

I

G

T

P

Y

F

C

L

R

P

N

F

F

G

S

A

S

A

A

-

M

-

D

-

L

-

Y

-

S

-

N

-

Y

-

K

-

L

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M

-

N

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-

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-

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-

I

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K

G

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A

D

A

I

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V

V

W

W

M

M

S
x
N

H
|
H

G
x
N

D
|
D

R

E

I

V

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K

M

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P

D

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G

N

F

F

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L

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N

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P

L

L

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A

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G

Y

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S

K

A

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R

Y

N

N

F

I

Y

Y

G

G

V

V

Q

Q

F

Y

H
|
H

L

P

E
|
E

V

V

A

Y

H

E

T

S

P

L

R

D

G

G

A

E

E

L

M

M

L

F

T

Y

A

N

F

F

V

A

R

Y

G

N

V

I

C

C

G

K

C

C

T

K

G

K

D

Q

W

F

T

D

M

P

H

I

S

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Y

Y

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H

D

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L

A

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V

L

A

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N

I

I

R

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A

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Q

Y

V

K

G

H

K

D

G

H

R

Y

V

V

I

I

A

A

L

M

S

S

G

G

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D
|
D

S

S

A

T

V

V

A

A

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A

L

Y

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N

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P

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K

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K

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I

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L

L

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F

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I

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F

F

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K

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K

N

H

N

L

I

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-

I

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D

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I

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F

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L

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Q

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G

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K

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I

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K

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H

H

N

N

V

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G

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L

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M

L

R

K

L

F

Q

K

L

L

V

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

E

T

L

L

G

S

R

R

E

E

L

L

G

N

M

L

P

P

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E

V

I

I

T

R

N

R

R

Q

H

P

P

F

F

P

P

G

G

P

P

G

G

L

L

A

A

I

I

R

R

C

V

L

I

G

G

A

E

V

I

D

N

E

K

H

H

R

K

L

L

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N

V

I

L

L

R

R

R

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A

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D

D

R

D

I

I

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F

M

I

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N

E

D

I

L

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K

D

Q

A

Y

G

G

L

L

Y

Y

G

N

R

Q

L

I

W

S

Q

Q

A

A

F

F

A

A

V

V

L

L

P

-

V

-

R

-

S

-

V

-

G

-

V

-

M

-

G

-

D

-

A

-

R

-

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S

Y

Y

D

D

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Y

T

V

V

C

A

V

L

L

R

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A

A

V

V

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K

S

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A

S

D

S

G

F

M

M

T

T

A

A

D

N

W

W

A

Y

H

Q

I

I

P

P

Y

Y

E

D

V

I

L

L

G

D

R

K

I

I

S

T

T

T

R

R

I

I

I

L

N

S

E

E

V

V

A

K

G

G

I

V

N

N

R

R

V

I

V

L

Y

Y

D

D

I

V

S

S

K

K

P

P

A

A

T

T

I

I

E

E

W

F

E

E

active site: G52 (= G54), A83 (≠ C81), Y84 (= Y82), H197 (= H171), E199 (= E173), D255 (= D229), K393 (= K370)
binding glutamine: Q87 (= Q85), N158 (≠ S132), H159 (= H133), N160 (≠ G134), D161 (= D135), H197 (= H171)

3uowA Crystal structure of pf10_0123, a gmp synthetase from plasmodium falciparum
38% identity, 100% coverage: 3:514/514 of query aligns to 2:517/517 of 3uowA

query
sites
3uowA

E

D

R

K

I

I

L

L

I

V

L

L

D

N

F

F

G

G

S

S

Q

Q

F

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

C

S

E

E

I

T

H

K

P

D

Y

Y

N

G

M

V

A

E

L

L

A

K

E

D

I

I

W

K

A

D

W

M

R

N

P

I

K

K

G

G

I

V

I

I

L

L

S

S

G

G

G
|
G

P

P

S

Y

S

S

V

V

H

T

D

E

V

A

D

G

A

S

P

P

S

H

V

L

D

K

P

K

A

E

L

V

F

F

A

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M

Y

G

F

L

L

-

E

-

K

-

I

P

P

V

I

L

F

G

G

I

I

C
|
C

Y
|
Y

G

G

L

M

Q

Q

L

E

M

I

A

A

Q

V

L

Q

L

M

G

N

G

G

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V

V

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K

K

K

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K

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Y

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G

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A

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D

L

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N

I

I

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L

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N

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D

-

N

-

I

-

N

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I

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-

Y

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C

-

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N

-

F

K

S

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S

A

A

I

M

G

D

P

L

F

Y

L

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P

N

F

Y

G

K

A

L

A

M

G

N

A

C

-

L

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F

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N

-

I

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V

V

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W

M

M

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H

H

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D

D

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M

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P

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N

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F

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L

L

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S

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A

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N

N

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P

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L

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A

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A

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I

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K

A

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Y

N

N

F

I

Y

Y

G

G

V

V

Q

Q

F

Y

H
|
H

L

P

E
|
E

V

V

A

Y

H

E

T

S

P

L

R

D

G

G

A

E

E

L

M

M

L

F

T

Y

A

N

F

F

V

A

R

Y

G

N

V

I

C

C

G

K

C

C

T

K

G

K

D

-

W

F

T

D

M

P

H

I

S

R

Y

Y

V

H

D

E

T

L

A

E

V

L

A

K

T

N

I

I

R

E

A

K

Q

Y

V

K

G

H

K

D

G

H

R

Y

V

V

I

I

A

A

L

M

S

S

G

G

V

I

D
|
D

S

S

A

T

V

V

A

A

V

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

I

I

F

F

V

I

D

D

N

N

G

G

L

L

R

R

F

K

G

N

E

E

A

A

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E

K

N

V

V

A

Y

T

T

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F

F

L

R

K

N

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F

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P

Q

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M

P

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L

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K

V

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D

A

A

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F

F

L

L

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V

N

L

L

A

Q

D

G

V

V

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T

D

D

P

P

E

E

K

Q

K

K

R
|
R

K

K

A

I

I

I

G

G

N

K

L

L

F

F

I

I

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E

I

E

F

F

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K

E

A

S

V

K

N

H

N

L

I

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D

-

I

-

D

-

I

G

N

A

K

D

T

F

F

L

L

A

L

Q

Q

G

G

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T

L

L

Y

Y

P

P

D

D

V

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I

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S

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-

G

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P

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E

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R

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M

L

R

K

L

F

Q

K

L

L

V

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

E

T

L

L

G

S

R

R

E

E

L

L

G

N

M

L

P

P

E

E

V

I

I

T

R

N

R

R

Q

H

P

P

F

F

P
|
P

G
|
G

P
|
P

G

G

L

L

A

A

I

I

R

R

C

V

L

I

G

G

A

E

V

I

D

N

E

K

H

H

R

K

L

L

E

N

V

I

L

L

R

R

R

E

A

V

D

D

R

D

I

I

V

F

M

I

E

N

E

D

I

L

R

K

D

Q

A

Y

G

G

L

L

Y

Y

G

N

R

Q

L

I

W

S

Q
|
Q

A

A

F

F

A

A

V

V

L

L

P

S

V

S

R

K

S

S

V

V

G

-

V

-

M

-

G

-

D

-

A

-

R

-

T

-

Y

Y

D

D

E

Y

T

V

V

C

A

V

L

L

R

R

A

A

V

V

E

K

S

T

A

S

D

S

G

F

M

M

T

T

A

A

D

N

W

W

A

Y

H

Q

I

I

P

P

Y

Y

E

D

V

I

L

L

G

D

R

K

I

I

S

T

T

T

R

R

I

I

I

L

N

S

E

E

V

V

A

K

G

G

I

V

N

N

R

R

V

I

V

L

Y

Y

D

D

I

V

S

S

K
|
K

P

P

A

A

T
|
T

I
|
I

E
|
E

W

F

E

E

active site: G53 (= G54), C84 (= C81), Y85 (= Y82), H198 (= H171), E200 (= E173), D255 (= D229), K381 (= K370)
binding xanthosine-5'-monophosphate: R325 (= R298), P404 (= P393), G405 (= G394), P406 (= P395), Q446 (= Q435), K509 (= K506), T513 (= T510), I514 (= I511), E515 (= E512)

3uowB Crystal structure of pf10_0123, a gmp synthetase from plasmodium falciparum
39% identity, 99% coverage: 4:514/514 of query aligns to 1:477/477 of 3uowB

query
sites
3uowB

R

K

I

I

L

L

I

V

L

L

D

N

F

F

G

G

S

S

Q

Q

F

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

C

S

E

E

I

T

H

K

P

D

Y

Y

N

-

M

-

A

-

L

-

A

K

E

D

I

I

W

K

A

D

W

M

R

N

P

I

K

K

G

G

I

V

I

I

L

L

S

S

G

G

G
|
G

P

P

S

Y

S

S

V

-

H

-

D

-

V

-

D

-

A

-

P

-

S

E

V

V

D

F

P

E

A

Y

L

F

F

L

A

E

M

K

G

K

L

I

P

P

V

I

L

F

G

G

I

I

C
|
C

Y
|
Y

G

G

L

M

Q

Q

L

E

M

I

A

A

-

V

Q

Q

L

M

L

N

G

Y

G

G

R

C

V

T

G

D

-

V

-

N

-

I

K

N

A

I

E

N

H

N

R

I

E

T

Y

Y

G

C

R

A

A

M

H

D

L

L

Q

Y

I

S

K

N

E

Y

A

K

I

L

G

M

P

N

F

C

L

C

P

L

F

F

-

E

G

N

A

I

A

K

G

S

A

D

A

I

E

T

V

V

W

W

M

M

S

N

H

H

G

N

D

D

R

E

I

V

E

T

S

K

M

I

P

P

D

E

G

N

F

F

R

Y

V

L

L

V

A

S

S

S

A

E

N

N

S

C

P

L

L

I

A

C

A

S

I

I

G

Y

D

N

S

K

A

E

R

Y

N

N

F

I

Y

Y

G

G

V

V

Q

Q

F

Y

H
|
H

L

P

E
|
E

V

V

A

Y

H

E

T

S

P

L

R

D

G

G

A

E

E

L

M

M

L

F

T

Y

A

N

F

F

V

A

R

Y

G

N

V

I

C

C

G

K

C

C

T

K

G

F

D

D

W

P

T

I

M

-

H

-

S

R

Y

Y

V

H

D

E

T

L

A

E

V

L

A

K

T

N

I

I

R

E

A

K

Q

Y

V

K

G

H

K

D

G

H

R

Y

V

V

I

I

A

A

L

M

S

S

G

G

V

I

D
|
D

S

S

A

T

V

V

A

A

V

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

I

I

F

F

V

I

D

D

N

N

G

G

L

L

R

R

F

K

G

N

E

E

A

A

E

E

K

N

V

V

A

Y

T

T

V

F

F

L

R

K

N

S

Y

T

F

F

-

P

Q

D

I

M

P

N

L

I

Q

T

V

K

V

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D

D

A

A

R

S

Q

E

R

N

F

F

L

L

D

S

V

N

L

L

A

Q

D

G

V

V

T

T

D

D

P

P

E

E

K

Q

K

K

R
|
R

K

K

A

I

I

I

G

G

N

K

L

L

F

F

I

I

E

E

I

E

F

F

E

E

E

K

E

A

S

V

K

N

H

N

L

I

E

D

G

D

A

I

D

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

I

K

S

K

F

F

K

K

G

-

P

-

S

-

A

-

T

-

I

-

K

-

S

-

H

-

N

-

V

-

G

-

L

-

P

-

E

-

R

-

M

-

R

-

L

-

Q

-

L

L

V

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

E

T

L

L

G

S

R

R

E

E

L

L

G

N

M

L

P

P

E

E

V

I

I

T

R

N

R

R

Q

H

P

P

F

F

P
|
P

G
|
G

P
|
P

G

G

L

L

A

A

I

I

R

R

C

V

L

I

G

G

A

E

V

I

D

N

E

K

H

H

R

K

L

L

E

N

V

I

L

L

R

R

R

E

A

V

D

D

R

D

I

I

V

F

M

I

E

N

E

D

I

L

R

K

D

Q

A

Y

G

G

L

L

Y

Y

G

N

R

Q

L

I

W

S

Q
|
Q

A

A

F

F

A

A

V

V

L

L

P

S

V

S

R

K

S

S

V

V

G

G

V

-

M

-

G

-

D

-

A

-

R

-

T

-

Y

Y

D

D

E

Y

T

V

V

C

A

V

L

L

R

R

A

A

V

V

E

K

S

T

A

S

D

S

G

F

M

M

T

T

A

A

D

N

W

W

A

Y

H

Q

I

I

P

P

Y

Y

E

D

V

I

L

L

G

D

R

K

I

I

S

T

T

T

R

R

I

I

I

L

N

S

E

E

V

V

A

K

G

G

I

V

N

N

R

R

V

I

V

L

Y

Y

D

D

I

V

S

S

K
|
K

P

P

A

A

T
|
T

I
|
I

E
|
E

W

F

E

E

active site: G47 (= G54), C67 (= C81), Y68 (= Y82), H162 (= H171), E164 (= E173), D218 (= D229), K340 (= K370)
binding xanthosine-5'-monophosphate: R288 (= R298), P363 (= P393), G364 (= G394), P365 (= P395), Q405 (= Q435), K469 (= K506), T473 (= T510), I474 (= I511), E475 (= E512)

P49915 GMP synthase [glutamine-hydrolyzing]; GMP synthetase; Glutamine amidotransferase; EC 6.3.5.2 from Homo sapiens (Human) (see paper)
36% identity, 97% coverage: 5:501/514 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

F

Y

T

G

Q

K

L

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I

I

A

D

R

R

V

V

R

R

E

E

A

L

H

F

V

V

Y

Q

C

S

E

E

I

I

H

F

P

P

Y

L

N

E

M

T

A

P

L

A

A

F

E

A

I

I

W

K

A

E

W

Q

R

G

P

F

K

R

G

A

I

I

L

I

S

S

G

G

P

P

S

N

S

S

V

V

H

Y

D

A

V

E

D

D

A

A

P

P

S

W

V

F

D

D

P

P

A

A

L

I

F

F

A

T

M

I

G

G

L

K

P

P

V

V

L

L

G

G

I

I

C
|
C

Y

Y

G

G

L

M

Q

Q

L

M

M

M

A

N

Q

K

L

V

L

F

G

G

R

T

V

V

G

H

K

K

A

K

E

S

H

V

R

R

E

E

Y

D

G

G

R

V

A

F

H

N

L

I

Q

S

I

V

K

D

E

N

A

T

I

C

G

S

P

L

F

F

L

R

P

-

F

-

G

-

A

G

A

L

G

Q

A

K

A

E

E

E

E

V

V

V

W

L

M

L

S

T

H

H

G

G

D

D

R

S

I

V

E

D

S

K

M

V

P

A

D

D

G

G

F

F

R

K

V

V

L

V

A

A

S

R

S

S

A

G

N

N

S

I

P

-

L

V

A

A

A

G

I

I

G

A

D

N

S

E

A

S

R

K

N

K

F

L

Y

Y

G

G

V

A

Q

Q

F

F

H
|
H

L

P

E
|
E

V

V

A

G

H

L

T

T

P

E

R

N

G

G

A

K

E

V

M

I

L

L

T

K

A

N

F

F

V

L

R

Y

G

D

V

I

C

A

G

G

C

C

T

S

G

G

D

T

W

F

T

T

M

V

H

Q

S

N

Y

R

V

E

D

L

T

E

A

C

V

I

A

R

T

E

I

I

R

K

A

E

Q

R

V

V

G

G

K

T

G

S

R

K

V

V

I

L

A

V

A

L

L

L

S

S

G

G

V

V

D

D

S

S

A

T

V

V

A

C

V

T

V

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

I

V

F

H

V

I

D

D

N

N

G

G

L

F

L

M

R

R

F

K

G

R

E

E

A

S

E

Q

K

S

V

V

A

E

T

E

V

A

F

L

R

K

N

K

Y

-

F

L

Q

G

I

I

P

Q

L

V

Q

K

V

V

V

I

D

N

A

A

-

A

-

H

-

S

-

F

-

Y

-

N

-

G

-

T

-

L

-

P

-

I

-

S

-

D

-

E

-

D

-

R

-

T

-

P

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K

R

R

F

I

L

S

D

K

V

T

L

L

A

N

D

M

V

T

T

T

D

S

P

P

E

E

K

E

K

K

R
|
R

K

K

A

I

I

I

G

G

N

D

L

T

F

F

I

V

E

K

I

I

F

A

E

N

E

E

-

V

-

I

-

G

E

E

S

M

K

N

H

L

L

K

E

P

G

E

A

E

D

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

I

A

S

S

F

L

-

V

-

A

K

S

G

G

P

K

S

A

A

E

T

L

I

I

K

K

S

T

H

H

N

N

V

D

G

T

G

E

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L

P

I

E

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M

L

R

R

L

E

Q

E

-

G

-

K

L

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V

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

E

I

L

L

G

G

R

R

E

E

L

L

G

G

M

L

P

P

E

E

V

L

I

V

R

S

R

R

Q

H

P

P

F

F

P

P

G

G

P

P

G

G

L

L

A

A

I

I

R

R

C

V

L

I

G

C

A

A

V

E

D

E

E

P

H

Y

R

I

L

C

E

K

-

D

-

F

-

P

-

E

-

T

-

N

-

I

-

L

-

K

-

I

-

V

-

A

-

D

-

F

-

S

-

A

-

S

-

V

-

K

-

P

-

H

-

T

V

L

L

L

R

Q

R

R

A

V

D

K

R

A

I

C

V

T

M

T

E

E

I

D

R

Q

D

E

A

K

G

L

L

M

-

Q

Y

I

G

T

R

S

L

L

W

H

Q

S

A

L

F

N

A

A

V

F

L

L

P

P

V

I

R

K

S

T

V

V

G

G

V

V

M

Q

G

G

D
|
D

A

C

R

R

T

S

Y

Y

D

S

E

Y

T

V

V

C

A

G

L

I

R

S

A

S

V

K

E

D

S

E

A

-

D

-

G

-

M

-

T

-

A

P

D

D

W

W

A

E

H

S

I

L

P

I

Y

F

E

-

V

-

L

L

G

A

R

R

I

L

S

I

T

P

R

R

I

M

I

C

N

H

E

N

V

V

A

-

G

-

I

-

N

N

R

R

V

V

Y

Y

C104 (= C81) active site, For GATase activity
H190 (= H171) active site, For GATase activity
E192 (= E173) active site, For GATase activity
R337 (= R298) binding XMP
D522 (= D451) 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)
52% identity, 61% coverage: 201:514/514 of query aligns to 5:298/298 of 6jp9A

query
sites
6jp9A

H

K

S

K

Y

F

V

I

D

D

T

E

A

A

V

V

A

E

T

E

I

I

R

K

A

Q

Q

Q

V

I

G

S

K

D

G

R

R

K

V

A

I

I

A

I

A

A

L

L

S

S

G

G

V

V

D
|
D

S

S

A

S

V

V

A

A

V

A

V

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

I

V

F

F

V

V

D

D

N

T

G

G

L

L

L

M

R

R

F

K

G

G

E

E

A

R

E

E

K

E

V

V

A

E

T

K

V

T

F

F

R

R

N

D

Y

K

F

L

Q

G

I

L

P

N

L

L

Q

I

V

V

D

D

A

A

R

K

Q

D

R

R

F

F

L

L

D

N

V

A

L

L

A

K

D

G

V

V

T

T

D

D

P

P

E

E

K

E

K

K

R
|
R

K

K

A

I

I

I

G

G

N

K

L

L

F

F

I

I

E

D

I

V

F

F

E

E

E

I

S

A

K

E

H

D

L

I

E

K

G

-

A

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

-

I

-

S

-

F

-

K

-

G

-

P

-

S

-

A

-

T

-

I

-

K

-

S

-

H

-

H

H

N

N

V

V

G

-

G

A

L

L

P

P

E

H

R

G

M

M

R

V

L

L

Q

E

L

V

V

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

E

L

L

L

G

A

R

K

E

E

L

L

G

G

M

L

P

P

E

D

E

S

V

I

I

V

R

Y

R

R

Q

Q

P

P

F

F

P
|
P

G
|
G

P
|
P

G

G

L

L

A

A

I

V

R

R

C

V

L

L

G

G

A

E

V

V

D

T

E

E

H

E

R

K

L

L

E

N

V

I

L

C

R

R

R

E

A

A

D

N

R

A

I

I

V

V

M

E

E

E

I

V

R

K

D

K

A

A

G

N

L

L

Y

D

G

K

R

D

L

L

W

W

Q
|
Q

A

Y

F

F

A

A

V

V

L

V

L

L

P

D

V

C

R

K

S

A

V

T

G

G

V

V

M

K

G

G

D

D

A

-

R

R

T

E

Y

Y

D

N

E

W

T

I

V

V

A

A

L

L

R

R

A

M

V

V

E

K

S

S

A

L

D

D

G

A

M

M

T

T

A

A

D

H

W

V

A

P

H

E

I

I

P

P

Y

F

E

D

V

L

L

L

G

K

R

R

I

I

S

S

T

K

R

R

I

I

I

T

N

S

E

E

V

I

A

P

G

N

I

V

N

A

R

R

V

V

Y

F

D

D

I

I

S

T

S

D

K
|
K

P

P

A

A

T
|
T

I
|
I

E
|
E

W

F

E

E

active site: D33 (= D229), K155 (= K370)
binding xanthosine-5'-monophosphate: R102 (= R298), P178 (= P393), G179 (= G394), P180 (= P395), Q220 (= Q435), K290 (= K506), T294 (= T510), I295 (= I511), E296 (= E512)

2vxoB Human gmp synthetase in complex with xmp (see paper)
36% identity, 97% coverage: 5:501/514 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

F

Y

T

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I

A

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R

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V

R

R

E

E

A

L

H

F

V

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Q

C

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E

E

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P

P

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N

E

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A

P

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A

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I

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K

A

E

W

Q

R

G

P

F

K

R

G

A

I

I

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S

G

G

G
|
G

P

P

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N

S

S

V

V

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Y

D

A

V

E

D

D

A

A

P

P

S

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V

F

D

D

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P

A

A

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I

F

F

A

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M

I

G

G

L

K

P

P

V

V

L

L

G

G

I

I

C
|
C

Y
|
Y

G

G

L

M

Q

Q

L

M

M

M

A

N

Q

K

L

V

L

F

G

G

R

T

V

V

G

H

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K

A

-

E

-

H

-

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E

S

Y

D

G

G

R

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A

F

H

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I

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K

D

E

N

A

T

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C

G

S

P

-

F

-

L

-

P

L

F

F

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R

A

G

A

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G

Q

A

K

A

E

E

E

E

V

V

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L

M

L

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T

H

H

G

G

D

D

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I

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M

V

P

A

D

D

G

G

F

F

R

K

V

V

L

V

A

A

S

R

S

S

A

G

N

N

S

I

P

-

L

V

A

A

A

G

I

I

G

A

D

N

S

E

A

S

R

K

N

K

F

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Y

G

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A

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Q

F

F

H
|
H

L

P

E
|
E

V

V

A

G

H

L

T

T

P

E

R

N

G

G

A

K

E

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M

I

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A

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F

F

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Y

G

D

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I

C

A

G

G

C

C

T

S

G

G

D

T

W

F

T

T

M

V

H

Q

S

N

Y

R

V

E

D

L

T

E

A

C

V

I

A

R

T

E

I

I

R

K

A

E

Q

R

V

V

G

G

K

T

G

S

R

K

V

V

I

L

A

V

A

L

L

L

S

S

G

G

V

V

D
|
D

S

S

A

T

V

V

A

C

V

T

V

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

I

V

F

H

V

I

D

D

N

N

G

G

L

F

L

M

R

R

F

K

G

R

E

E

A

S

E

Q

K

S

V

V

A

E

T

E

V

A

F

L

R

K

N

K

Y

-

F

L

Q

G

I

I

P

Q

L

V

Q

K

V

V

V

I

D

N

A

A

R

A

Q

H

R

S

F

F

L

Y

D

N

-

G

-

T

-

L

-

P

-

R

-

I

-

S

-

K

V

T

L

L

A

N

D

M

V

T

T

T

D

S

P

P

E

E

K

E

K

K

R
|
R

K

K

A

I

I

I

G

G

N

D

L

T

F

F

I

V

E

K

I

I

F

A

E

N

E

E

-

V

-

I

-

G

E

E

S

M

K

N

H

L

L

K

E

P

G

E

A

E

D

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

I

A

S

S

F

L

-

V

-

A

K

S

G
|
G

P
x
K

S

A

A

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

R

K

M

L

R

R

L

E

Q

E

-

G

-

K

L

V

V

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

E

I

L

L

G

G

R

R

E

E

L

L

G

G

M

L

P

P

E

E

V

L

I

V

R

S

R

R

Q

H

P

P

F

F

P
|
P

G
|
G

P
|
P

G

G

L

L

A

A

I

I

R

R

C

V

L

I

G

C

A

A

V

E

D

E

E

P

H

Y

R

I

L

C

E

K

-

D

-

F

-

P

-

E

-

T

-

N

-

I

-

L

-

K

-

I

-

V

-

A

-

D

-

F

-

S

-

A

-

S

-

V

-

K

-

P

-

H

-

T

V

L

L

L

R

Q

R

R

A

V

D

K

R

A

I

C

V

T

M

T

E

E

I

D

R

Q

D

E

A

K

G

L

L

M

-

Q

Y

I

G

T

R

S

L

L

W

H

Q

S

A

L

F

N

A

A

V

F

L

L

P

P

V

I

R

K

S

T

V

V

G

G

V

V

M

Q

G

G

D

D

A

C

R
|
R

T

S

Y

Y

D

S

E

Y

T

V

V

C

A

G

L

I

R

S

A

S

V

K

E

D

S

E

A

-

D

-

G

-

M

-

T

-

A

P

D

D

W

W

A

E

H

S

I

L

P

I

Y

F

E

-

V

-

L

L

G

A

R

R

I

L

S

I

T

P

R

R

I

M

I

C

N

H

E

N

V

V

A

-

G

-

I

-

N

N

R

R

V

V

Y

Y

active site: G55 (= G54), C82 (= C81), Y83 (= Y82), H165 (= H171), E167 (= E173), D223 (= D229), K381 (= K370)
binding xanthosine-5'-monophosphate: R302 (= R298), G348 (= G339), K349 (≠ P340), P404 (= P393), G405 (= G394), P406 (= P395), R489 (= R453)

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
39% identity, 37% coverage: 5:193/514 of query aligns to 2:179/183 of 7yc6A

query
sites
7yc6A

I

I

L

V

I

I

L

L

D

D

F

N

G

G

S

G

Q

Q

F

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

C

S

E

K

I

I

H

V

P

P

Y

N

N

T

M

T

A

P

L

L

A

E

E

E

I

I

W

E

A

S

W

N

R

K

P

E

-

V

K

K

G

G

I

I

L

L

S

S

G

G

P

P

S

-

V

-

H

-

D

D

V

I

D

E

A

K

P

A

S

K

-

N

-

C

V

I

D

D

P

I

A

A

L

L

F

N

A

A

M

K

G

-

L

L

P

P

V

I

L

L

G

G

I

I

C
|
C

Y

L

G

G

L

H

Q

Q

L

L

M

I

A

A

Q

L

L

A

L

Y

G

G

R

E

V

V

G

G

K

R

A

A

E

A

H

-

R

-

E

-

Y

L

G

T

R

K

A

V

H

Y

L

V

Q
x
D

I

K

K

E

E

N

A

P

I

L

G

F

P

K

F

N

L

V

P

P

-

R

-

E

F

F

G

N

A

A

A

-

G

-

A

-

E

-

V

-

W

W

M

A

S

S

H

H

G

K

D

D

R
x
E

I

V

E

K

S

K

M

V

P

P

D

E

G

G

F

F

R

E

V

I

L

L

A

A

S
x
H

S

S

A

D

N

I

S
x
C

P

Q

L

V

A

E

A

A

I

M

G

K

D

H

S

K

A

T

R

K

N

P

F

I

Y

Y

G

G

V

V

Q

Q

F

F

H
|
H

L

P

E

E

V

V

A

A

H

H

T

T

P

E

R

Y

G

G

A

N

E

E

M

I

L

L

T

K

A

N

F

F

V

C

R

K

G

-

V

V

C

C

G

G

binding zinc ion: C76 (= C81), D101 (≠ Q109), E123 (≠ R136), E123 (≠ R136), H136 (≠ S149), C140 (≠ S153), C140 (≠ S153), H158 (= H171)

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)
30% identity, 30% coverage: 36:189/514 of query aligns to 34:186/187 of P00903

query
sites
P00903

M

L

A

T

L

L

A

A

E

D

I

I

W

D

A

A

W

L

R

K

P

P

K

Q

G

K

I

I

I

V

L

I

S

S

G

P

G

G

P

P

S

C

S

T

V

P

H

-

D

D

V

E

D

A

A

G

P

I

S

S

V

L

D

D

P

V

A

I

L

R

F

H

A

Y

M

A

G

G

-

R

L

L

P

P

V

I

L

L

G

G

I

V

C
|
C

Y

L

G

G

L

H

Q

Q

L

A

M

M

A

A

Q

Q

L

A

L

F

G

G

R

K

V

V

G

V

K

R

A

A

E

A

H

K

R

V

E

M

Y

H

G

G

R

K

A

T

H

S

L

P

Q

I

I

T

K

H

E

N

A

G

I

E

G

G

P

V

F

F

L

-

P

-

F

-

G

-

A

-

A

R

G

G

A

L

A

A

E

N

E

P

V

L

W

T

M

V

S

T

H

R

G

Y

D

H

R

S

I

L

-

V

-

E

-

P

E

D

S

S

M

L

P

P

D

A

G

C

F

F

R

D

V

V

L

T

A

A

S

W

S

S

A

E

N

T

S

R

P

E

L

I

A

M

A

G

I

I

G

R

D

H

S

R

A

Q

R

W

N

D

F

L

Y

E

G

G

V

V

Q

Q

F

F

H
|
H

L

P

E
|
E

V

S

A

I

H

L

T

S

P

E

R

Q

G

G

A

H

E

Q

M

L

L

L

T

A

A

N

F

F

V

L

R

H

C79 (= C81) mutation to S: 10000-fold decrease in catalytic efficiency.
H168 (= H171) mutation to Q: Loss of activity.
E170 (= E173) 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.

8hx8A Crystal structure of 4-amino-4-deoxychorismate synthase from streptomyces venezuelae co-crystallized with chorismate (see paper)
30% identity, 36% coverage: 4:187/514 of query aligns to 5:187/673 of 8hx8A

query
sites
8hx8A

R

R

I

T

L

L

I

L

L

I

D

D

F

N

G

Y

S

D

Q

S

F

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

C

P

E

P

I

V

H

V

P

V

Y

P

N

N

M

D

A

A

L

-

A

-

E

-

I

D

W

W

A

S

W

R

R

L

P

P

-

V

-

E

-

D

-

F

K

D

G

A

I

I

I

V

L

V

S

S

G

P

G

G

P

P

S

G

S

S

V

P

-

D

H

R

D

E

V

R

D

D

A

F

P

G

S

I

V

S

D

R

P

R

A

A

L

I

F

T

A

D

M

S

G

G

L

L

P

P

V

V

L

L

G

G

I

V

C

C

Y

L

G

G

L

H

Q

Q

L

G

M

I

A

A

Q

Q

L

L

L

F

G

G

R

T

V

V

G

G

K

L

A

A

E

P

H

E

R

P

E

M

Y

H

G

G

R

R

A

V

-

S

-

E

-

V

-

R

H

H

L

T

Q

G

I

E

K

D

E

V

A

F

I

R

G

G

P

L

F

P

L

S

P

P

F

F

G

T

A

A

A

V

G

-

A

-

E

-

V

-

W

-

M

R

S

Y

H

H

G

S

D

L

R

A

I

A

E

T

S

D

M

L

P

P

D

D

G

E

F

L

R

E

V

P

L

L

A

A

S

W

S

S

A

D

N

D

S

G

P

V

L

V

A

M

A

G

I

L

G

R

D

H

S

R

A

E

R

K

N

P

F

L

Y

W

G

G

V

V

Q

Q

F

F

H

H

L

P

E

E

V

S

A
x
I

H

G

T
x
S

P

D

R

F

G

G

A

R

E

E

M

I

L

M

T

A

A

N

F

F

binding magnesium ion: I175 (≠ A175), S177 (≠ T177)

Sites not aligning to the query:

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

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)
26% identity, 35% coverage: 4:182/514 of query aligns to 243:413/430 of Q9LVW7

query
sites
Q9LVW7

R

K

I

V

L

I

I

A

L

Y

D

D

F

F

G

G

S

-

Q

-

F

I

T

K

Q

Q

L

N

I

I

A

L

R

R

V

L

R

S

E

S

A

Y

H

G

V

C

Y

Q

C

I

E

T

I

V

H

V

P

P

Y

S

N

T

M

F

A

P

L

A

A

A

E

E

I

A

W

L

A

K

W

M

R

N

P

P

K

D

G

G

I

I

I

L

L

F

S

S

G

N

G

G

P

P

S

G

S

D

V

P

H

S

D

A

V

V

D

P

A

Y

P

-

S

A

V

V

D

E

P

T

A

V

L

K

F

E

A

L

M

L

G

G

-

K

L

V

P

P

V

V

L

Y

G

G

I

I

C

C

Y

M

G

G

L

H

Q

Q

L

L

M

L

A

G

Q

Q

L

A

L

L

G

G

R

K

V

T

G

F

K

K

A

M

E

K

H

F

R

G

E

H

Y

H

G

G

R

G

A

N

H

H

L

-

Q

P

I

V

K

R

E

N

A

-

I

-

G

-

P

-

F

-

L

-

P

-

F

-

G

N

A

R

A

T

G

G

A

Q

A

V

E

E

E

I

V

S

W

A

M

Q

S

N

H

H

G

N

D

Y

R

A

I

V

E

D

-

P

-

A

S

S

M

L

P

P

D

G

G

G

F

V

R

E

V

V

L

T

A

H

S

V

S

N

A

L

N

N

S

D

-

G

P

S

L

C

A

A

A

G

I

L

G

S

D

F

S

P

A

E

R

M

N

N

F

V

Y

M

G

S

V

L

Q

Q

F

Y

H

H

L

P

E

E

V

A

A

S

H

P

T

G

P

P

R
x
H

G

D

A

S

E

D

H410 (≠ R179) mutation to Y: In ven6-1; reticulate leaf phenotype.

Q09794 Multifunctional protein ura1; Pyrimidine-specific carbamoyl phosphate synthase-aspartate carbamoyl transferase; CPSase-ATCase; EC 6.3.5.5; EC 3.5.1.2; EC 6.3.4.16; EC 2.1.3.2 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
26% identity, 35% coverage: 4:184/514 of query aligns to 264:435/2244 of Q09794

query
sites
Q09794

R

R

I

I

L

L

I

V

L

I

D

D

F

V

G

G

S

M

Q

K

F

Y

T

N

Q

Q

L

I

I

R

A

C

R

F

R

L

V

N

R

R

E

G

A

V

H

E

V

L

Y

L

C

V

E

V

I

P

H

W

P

D

Y

Y

N

D

M

F

A

T

L

-

A

K

E

E

I

T

W

Y

A

-

W

-

R

-

P

-

K

D

G

G

I

L

I

F

L

I

S

S

G

N

G

G

P

P

S

G

-

D

-

P

S

S

V

L

H

M

D

D

V

L

D

V

A

V

P

D

S

R

V

V

D

K

P

R

A

V

L

L

F

E

A

S

M

K

G

T

L

V

P

P

V

V

L

F

G

G

I

I

C

C

Y

F

G

G

L

H

Q

Q

L

I

M

M

A

A

Q

R

L

A

G

G

G

A

R

S

V

T

G

T

K

K

A

M

E

K

H

F

R

G

E

N

Y

R

G

G

R

H

A

N

H

-

L

-

Q

-

I

-

K

-

E

-

A

-

I

-

G

-

P

-

F

-

L

I

P

P

F

C

G

T

A

C

-

M

-

I

A

S

G

G

A

R

A

C

E

Y

E

I

V

T

W

S

M

Q

S

N

H

H

G

G

D

Y

R

A

I

V

E

D

-

A

-

S

S

S

M

L

P

S

D

N

G

G

F

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A

F

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S

N

A

A

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N

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D

-

G

P

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A

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D

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Q

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Sites not aligning to the query:

1119 modified: Phosphoserine
1881 modified: Phosphoserine
1885 modified: Phosphoserine

P05990 Multifunctional protein r; Protein rudimentary; EC 6.3.5.5; EC 3.5.1.2; EC 6.3.4.16; EC 2.1.3.2; EC 3.5.2.3 from Drosophila melanogaster (Fruit fly) (see 2 papers)
28% identity, 35% coverage: 4:184/514 of query aligns to 195:366/2224 of P05990

query
sites
P05990

R

R

I

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A

I

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Sites not aligning to the query:

1167 E→K: Severely diminishes UTP inhibition of CPSase; in Su(b).
1883 modified: Phosphoserine
1885 modified: Phosphoserine
1892 modified: Phosphoserine
1894 modified: Phosphoserine

P27708 Multifunctional protein CAD; Carbamoyl phosphate synthetase 2-aspartate transcarbamylase-dihydroorotase; EC 6.3.5.5; EC 3.5.1.2; EC 6.3.4.16; EC 2.1.3.2; EC 3.5.2.3 from Homo sapiens (Human) (see 7 papers)
31% identity, 35% coverage: 4:184/514 of query aligns to 177:349/2225 of P27708

query
sites
P27708

R
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R

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N

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G

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A

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L

L

R177 (= R4) to Q: in a colorectal cancer sample; somatic mutation; dbSNP:rs374122292

Sites not aligning to the query:

1 modified: Initiator methionine, Removed
2 modified: N-acetylalanine
33 M → R: in DEE50; uncertain significance; dbSNP:rs751610198
456 modified: Phosphothreonine; by MAPK1
735 Y → C: in a colorectal cancer sample; somatic mutation
1406 modified: Phosphoserine; by PKA
1471 binding Zn(2+); binding Zn(2+); H→A: No zinc-binding and no catalytic activity.; H→N: Abolishes dihydroorotase activity.
1473 binding Zn(2+); H→A: No zinc-binding and no catalytic activity.
1475 binding (S)-dihydroorotate
1505 binding (S)-dihydroorotate
1512 D→N: No change in catalytic activity.
1556 binding via carbamate group; binding via carbamate group; modified: N6-carboxylysine
1562 T→A: Abolishes dihydroorotase activity.
1563 F→A: Abolishes dihydroorotase activity.
1590 binding Zn(2+); H→A: Abolishes dihydroorotase activity.; H→N: No catalytic activity.
1613 binding Zn(2+); C→S: Reduces dihydroorotase activity.
1614 binding Zn(2+); H→A: Abolishes dihydroorotase activity.
1637 binding Zn(2+); E→T: Abolishes dihydroorotase activity.
1642 H→N: 11.5% of wild-type catalytic activity.
1661 binding (S)-dihydroorotate
1686 binding Zn(2+); D→N: Abolishes dihydroorotase activity.
1690 binding (S)-dihydroorotate; H→N: 3% of wild-type catalytic activity.
1702 binding (S)-dihydroorotate
1789:2225 natural variant: Missing (in DEE50; uncertain significance)
1859 modified: Phosphoserine; by RPS6KB1 and PKA
1873 modified: Phosphoserine; by PKC; in vitro; S→A: Abolishes PMA-induced Thr-456 phosphorylation.
1900 modified: Phosphoserine

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)
23% identity, 36% coverage: 5:189/514 of query aligns to 75:265/276 of Q42565

query
sites
Q42565

I

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L

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N

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G

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x
G

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F

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G150 (= G79) mutation to D: In trp4-1; no visible phenotype under normal growth conditions.
G176 (≠ R101) mutation to E: In wei7-2; insensitive to inhibition of root elongation by ethylene.

Query Sequence

>WP_012536751.1 NCBI__GCF_000021485.1:WP_012536751.1
MQERILILDFGSQFTQLIARRVREAHVYCEIHPYNMALAEIWAWRPKGIILSGGPSSVHD
VDAPSVDPALFAMGLPVLGICYGLQLMAQLLGGRVGKAEHREYGRAHLQIKEAIGPFLPF
GAAGAAEEVWMSHGDRIESMPDGFRVLASSANSPLAAIGDSARNFYGVQFHLEVAHTPRG
AEMLTAFVRGVCGCTGDWTMHSYVDTAVATIRAQVGKGRVIAALSGGVDSAVAVVLIHRA
IGDQLTCIFVDNGLLRFGEAEKVATVFRNYFQIPLQVVDARQRFLDVLADVTDPEKKRKA
IGNLFIEIFEEESKHLEGADFLAQGTLYPDVIESISFKGPSATIKSHHNVGGLPERMRLQ
LVEPLRELFKDEVRELGRELGMPEEVIRRQPFPGPGLAIRCLGAVDEHRLEVLRRADRIV
MEEIRDAGLYGRLWQAFAVLLPVRSVGVMGDARTYDETVALRAVESADGMTADWAHIPYE
VLGRISTRIINEVAGINRVVYDISSKPPATIEWE

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