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)
43% identity, 98% coverage: 10:517/517 of query aligns to 8:555/555 of Q8IJR9

query
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Q8IJR9

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Y18 (≠ V20) mutation to F: Slight increase in affinity for glutamine. No defect in glutaminase activity.
H20 (≠ Q22) 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 (≠ R26) 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 (= R27) mutation to L: No effect on glutaminase activity. 1.4-fold decrease in affinity for glutamine.
C89 (= C87) 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 (= Q91) binding L-glutamine
C113 (≠ R111) 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 (= W133) mutation to F: Slight decrease in affinity for glutamine. Slight increase in glutaminase activity.
N169 (≠ S135) binding L-glutamine; mutation to S: Slight increase in affinity for glutamine. No defect in glutaminase activity.
D172 (= D138) binding L-glutamine; mutation to A: 172-fold decrease in affinity for glutamine. Severe loss of glutaminase activity.
H208 (= H174) binding L-glutamine
Y212 (≠ V178) mutation to W: 2.7-fold decrease in affinity for glutamine. No defect in glutaminase activity.
E213 (≠ H179) 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 (= R301) binding XMP
D371 (= D333) Important for ATPPase activity; mutation to A: Impaired formation of adenyl-XMP intermediate. Slight increase in glutaminase activity.
E374 (= E336) mutation to L: 8.9-fold decrease in affinity for ammonia. Severe loss of glutaminase activity.
K376 (≠ V338) 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 (= K348) mutation to L: Severe loss of ATP pyrophosphatase (ATPPase) activity. 80 percent decrease in glutaminase activity. Impaired GMP formation.
T387 (≠ S349) mutation to A: No effect on ATP pyrophosphatase (ATPPase) activity. 20 percent decrease in glutaminase activity. No effect on GMP formation.
H388 (= H350) 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 (= H351) Important for ATPPase activity; mutation to A: Loss of ATP pyrophosphatase (ATPPase) activity. 67 percent decrease in glutaminase activity. Impaired GMP formation.
N390 (= N352) mutation to A: No effect on ATP pyrophosphatase (ATPPase) activity. Increases glutaminase activity. Loss of GMP formation.
K411 (= K373) mutation to L: 70 percent decrease in glutaminase activity. Loss of GMP formation.
D412 (= D374) mutation to A: 30 percent decrease in glutaminase activity. 7.9-fold decrease in affinity for glutamine.
D413 (≠ E375) mutation to A: 35 percent decrease in glutaminase activity. 3.6-fold decrease in affinity for glutamine.
K415 (≠ R377) mutation to L: Increases glutaminase activity. 4.2-fold decrease in affinity for ATP.
Q476 (= Q438) binding XMP
R539 (= R501) mutation to L: 85 percent decrease in glutaminase activity.
K547 (= K509) binding XMP; mutation to L: 85 percent decrease in glutaminase activity.
I552 (= I514) binding XMP
E553 (= E515) binding XMP; mutation to L: 85 percent decrease in glutaminase activity.
E555 (= E517) 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
48% identity, 98% coverage: 11:517/517 of query aligns to 2:475/475 of 2ywcA

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2ywcA

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active site: G51 (= G60), R53 (≠ S62), C78 (= C87), Y79 (= Y88), H164 (= H174), E166 (= E176), D221 (= D232), K343 (= K373)
binding xanthosine-5'-monophosphate: R288 (= R301), P366 (= P396), G367 (= G397), P368 (= P398), Q408 (= Q438), K467 (= K509), T471 (= T513), I472 (= I514), E473 (= E515)

4wioA Crystal structure of the c89a gmp synthetase inactive mutant from plasmodium falciparum in complex with glutamine (see paper)
40% identity, 98% coverage: 10:517/517 of query aligns to 2:525/525 of 4wioA

query
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4wioA

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V

I

I

L

L

S

S

G

G

G
|
G

P

P

S

Y

S

S

V

V

Y

T

D

E

A

A

D

G

A

S

P

P

H

H

S

L

D

K

A

K

G

E

V

V

Y

F

E

E

L

Y

-

F

-

L

-

E

-

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

M

I

T

A

S

V

Q

Q

L

M

G

N

G

G

K

E

V

V

E

K

R

K

S

S

D

K

K

T

R

S

E

E

F

Y

G

G

R

C

A

T

A

D

M

V

T

N

I

I

-

L

-

R

-

N

-

D

-

N

-

I

-

N

-

I

-

T

-

Y

-

C

-

R

-

N

-

F

D

S

T

A

T

M

D

D

L

L

F

Y

S

S

G

N

L

Y

S

K

G

L

K

M

E

N

E

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

I

V

E

T

Q

K

M

I

P

P

K

E

G

N

F

F

S

Y

A

L

I

V

A

S

H

S

T

S

D

E

N

N

T

C

P

L

A

I

A

C

A

S

M

I

K

Y

D

N

E

K

K

E

R

Y

R

N

L

I

Y

Y

A

G

V

V

Q

Q

F

Y

H
|
H

P

P

E
|
E

V

V

V

Y

H

E

T

S

P

L

K

D

G

G

A

E

E

L

M

M

L

F

G

Y

N

N

F

F

V

A

F

Y

T

N

V

I

C

C

G

K

C

C

Q

K

P

K

I

Q

W

F

T

D

M

P

A

I

N

R

F

Y

I

H

E

E

T

L

E

E

I

L

A

K

A

N

I

I

R

E

E

K

K

Y

V

K

G

H

N

D

G

H

K

Y

V

V

I

I

C

A

A

A

L

M

S

S

G

G

V

I

D
|
D

S

S

S

T

V

V

V

A

A

A

V

A

L

Y

L

T

H

H

K

K

A

I

I

F

G

K

D

E

Q

R

L

F

Q

F

C

G

I

I

F

F

V

I

N

D

N

N

G

G

L

L

R

R

K

K

G

N

E

E

A

A

E

E

K

N

V

V

V

Y

N

T

L

F

F

L

T

K

R

S

H

T

F

F

-

P

K

D

I

M

N

N

L

I

D

T

Y

K

V

I

E

D

A

A

S

S

S

E

R

N

F

F

L

L

D

S

K

N

L

L

K

Q

G

G

I

V

T

T

D

D

P

P

E

E

Q

Q

K

K

R

R

K

K

I

I

G

G

N

K

E

L

F

F

I

I

Y

E

L

E

F

F

E

E

D

-

E

-

A

-

K

K

K

A

I

V

G

N

T

N

V

I

D

D

-

I

-

D

-

I

-

N

-

K

-

T

W

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

T

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

-

D

-

R

-

M

L

K

K

M

F

K

K

L

L

I

F

E

E

P

P

V

F

R

K

E

Y

L

L

F

F

K
|
K

D

D

E

D

V

V

R

K

L

T

L

L

G

S

K

R

E

E

L

L

G

N

L

L

P

P

D

E

E

E

V

I

I

T

H

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

I

I

G

G

E

E

I

I

T

N

A

K

D

H

R

K

L

L

E

N

I

I

L

L

R

R

E

E

S

V

D

D

A

D

I

I

V

F

L

I

D

N

E

D

I

L

R

K

K

Q

A

Y

G

G

L

L

Y

Y

R

N

E

Q

I

I

W

S

Q

Q

S

A

F

F

A

A

V

V

L

L

P

-

V

-

R

-

S

-

V

-

G

-

V

-

M

-

G

-

D

-

A

-

R

-

T

S

Y

Y

D

D

Y

Y

T

V

I

C

A

V

L

L

R

R

A

A

V

V

N

K

S

T

L

S

D

S

G

F

M

M

T

T

A

A

D

N

W

W

V

Y

K

Q

L

I

P

P

Y

Y

E

D

V

I

M

L

G

D

S

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

Q

S

K

K

P

P

A

A

T

T

I

I

E

E

W

F

E

E

active site: G52 (= G60), A83 (≠ C87), Y84 (= Y88), H197 (= H174), E199 (= E176), D255 (= D232), K393 (= K373)
binding glutamine: Q87 (= Q91), N158 (≠ S135), H159 (= H136), N160 (≠ G137), D161 (= D138), H197 (= H174)

3uowA Crystal structure of pf10_0123, a gmp synthetase from plasmodium falciparum
40% identity, 98% coverage: 10:517/517 of query aligns to 3:517/517 of 3uowA

query
sites
3uowA

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

I

L

R

N

E

N

Q

I

S

K

V

I

Y

F

C

S

E

E

I

T

H

K

P

D

Y

Y

N

G

M

V

G

E

L

L

E

K

K

D

I

I

K

K

A

D

F

M

A

N

P

I

Q

K

G

G

I

V

I

I

L

L

S

S

G

G

G
|
G

P

P

S

Y

S

S

V

V

Y

T

D

E

A

A

D

G

A

S

P

P

H

H

S

L

D

K

A

K

G

E

V

V

Y

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

L

E

M

I

T

A

S

V

Q

Q

L

M

G

N

G

G

K

E

V

V

E

K

R

K

S

S

D

K

K

T

R

S

E

E

F

Y

G

G

R

C

A

T

A

D

M

V

T

N

I

I

-

L

-

R

-

N

-

D

-

N

-

I

-

N

-

I

-

T

-

Y

-

C

-

R

-

N

-

F

D

S

T

A

T

M

D

D

L

L

F

Y

S

S

G

N

L

Y

-

K

-

L

-

M

-

N

-

C

-

L

-

F

-

E

-

N

-

I

-

K

S

S

G

D

K

I

E

T

V

V

W

W

M

M

S

N

H

H

G

N

D

D

K

E

I

V

E

T

Q

K

M

I

P

P

K

E

G

N

F

F

S

Y

A

L

I

V

A

S

H

S

T

S

D

E

N

N

T

C

P

L

A

I

A

C

A

S

M

I

K

Y

D

N

E

K

K

E

R

Y

R

N

L

I

Y

Y

A

G

V

V

Q

Q

F

Y

H
|
H

P

P

E
|
E

V

V

V

Y

H

E

T

S

P

L

K

D

G

G

A

E

E

L

M

M

L

F

G

Y

N

N

F

F

V

A

F

Y

T

N

V

I

C

C

G

K

C

C

Q

K

P

K

I

-

W

F

T

D

M

P

A

I

N

R

F

Y

I

H

E

E

T

L

E

E

I

L

A

K

A

N

I

I

R

E

E

K

K

Y

V

K

G

H

N

D

G

H

K

Y

V

V

I

I

C

A

A

A

L

M

S

S

G

G

V

I

D
|
D

S

S

S

T

V

V

V

A

A

A

V

A

L

Y

L

T

H

H

K

K

A

I

I

F

G

K

D

E

Q

R

L

F

Q

F

C

G

I

I

F

F

V

I

N

D

N

N

G

G

L

L

R

R

K

K

G

N

E

E

A

A

E

E

K

N

V

V

V

Y

N

T

L

F

F

L

T

K

R

S

H

T

F

F

-

P

K

D

I

M

N

N

L

I

D

T

Y

K

V

I

E

D

A

A

S

S

S

E

R

N

F

F

L

L

D

S

K

N

L

L

K

Q

G

G

I

V

T

T

D

D

P

P

E

E

Q

Q

K

K

R
|
R

K

K

I

I

G

G

N

K

E

L

F

F

I

I

Y

E

L

E

F

F

E

E

D

-

E

-

A

-

K

K

K

A

I

V

G

N

T

N

V

I

D

D

-

I

-

D

-

I

-

N

-

K

-

T

W

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

T

S

K

-

G

-

P

-

S

-

A

-

V

-

I

-

K

-

S

-

H

-

N

-

V

-

G

-

L

-

P

-

D

-

R

-

M

L

K

K

M

F

K

K

L

L

I

F

E

E

P

P

V

F

R

K

E

Y

L

L

F

F

K
|
K

D

D

E

D

V

V

R

K

L

T

L

L

G

S

K

R

E

E

L

L

G

N

L

L

P

P

D

E

E

E

V

I

I

T

H

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

I

I

G

G

E

E

I

I

T

N

A

K

D

H

R

K

L

L

E

N

I

I

L

L

R

R

E

E

S

V

D

D

A

D

I

I

V

F

L

I

D

N

E

D

I

L

R

K

K

Q

A

Y

G

G

L

L

Y

Y

R

N

E

Q

I

I

W

S

Q
|
Q

S

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

Y

Y

T

V

I

C

A

V

L

L

R

R

A

A

V

V

N

K

S

T

L

S

D

S

G

F

M

M

T

T

A

A

D

N

W

W

V

Y

K

Q

L

I

P

P

Y

Y

E

D

V

I

M

L

G

D

S

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

Q

S

K
|
K

P

P

A

A

T
|
T

I
|
I

E
|
E

W

F

E

E

active site: G53 (= G60), C84 (= C87), Y85 (= Y88), H198 (= H174), E200 (= E176), D255 (= D232), K381 (= K373)
binding xanthosine-5'-monophosphate: R325 (= R301), P404 (= P396), G405 (= G397), P406 (= P398), Q446 (= Q438), K509 (= K509), T513 (= T513), I514 (= I514), E515 (= E515)

3uowB Crystal structure of pf10_0123, a gmp synthetase from plasmodium falciparum
40% identity, 98% coverage: 10:517/517 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

I

L

R

N

E

N

Q

I

S

K

V

I

Y

F

C

S

E

E

I

T

H

K

P

D

Y

Y

N

-

M

-

G

-

L

-

E

K

K

D

I

I

K

K

A

D

F

M

A

N

P

I

Q

K

G

G

I

V

I

I

L

L

S

S

G

G

G
|
G

P

P

-

Y

S

S

S

E

V

V

Y

F

D

E

A

Y

D

-

A

-

P

-

H

-

S

-

D

-

A

-

G

-

V

F

Y

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

L

E

M

I

T

A

S

V

Q

Q

L

M

-

N

-

Y

G

G

G

C

K

T

V

D

E

V

R

N

S

I

D

N

K

I

R

N

E

N

F

I

G

T

R

Y

A

C

A

A

M

M

T

D

I

L

D

Y

D

S

T

N

T

Y

D

K

L

L

F

M

S

N

G

C

L

C

-

L

-

F

-

E

-

N

-

I

-

K

S

S

G

D

K

I

E

T

V

V

W

W

M

M

S

N

H

H

G

N

D

D

K

E

I

V

E

T

Q

K

M

I

P

P

K

E

G

N

F

F

S

Y

A

L

I

V

A

S

H

S

T

S

D

E

N

N

T

C

P

L

A

I

A

C

A

S

M

I

K

Y

D

N

E

K

K

E

R

Y

R

N

L

I

Y

Y

A

G

V

V

Q

Q

F

Y

H
|
H

P

P

E
|
E

V

V

V

Y

H

E

T

S

P

L

K

D

G

G

A

E

E

L

M

M

L

F

G

Y

N

N

F

F

V

A

F

Y

T

N

V

I

C

C

G

K

C

C

Q

K

P

-

I

-

W

F

T

D

M

P

A

I

N

R

F

Y

I

H

E

E

T

L

E

E

I

L

A

K

A

N

I

I

R

E

E

K

K

Y

V

K

G

H

N

D

G

H

K

Y

V

V

I

I

C

A

A

A

L

M

S

S

G

G

V

I

D
|
D

S

S

S

T

V

V

V

A

A

A

V

A

L

Y

L

T

H

H

K

K

A

I

I

F

G

K

D

E

Q

R

L

F

Q

F

C

G

I

I

F

F

V

I

N

D

N

N

G

G

L

L

R

R

K

K

G

N

E

E

A

A

E

E

K

N

V

V

V

Y

N

T

L

F

F

L

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E

active site: G47 (= G60), C67 (= C87), Y68 (= Y88), H162 (= H174), E164 (= E176), D218 (= D232), K340 (= K373)
binding xanthosine-5'-monophosphate: R288 (= R301), P363 (= P396), G364 (= G397), P365 (= P398), Q405 (= Q438), K469 (= K509), T473 (= T513), I474 (= I514), E475 (= E515)

P49915 GMP synthase [glutamine-hydrolyzing]; GMP synthetase; Glutamine amidotransferase; EC 6.3.5.2 from Homo sapiens (Human) (see paper)
36% identity, 97% coverage: 11:514/517 of query aligns to 28:575/693 of P49915

query
sites
P49915

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C104 (= C87) active site, For GATase activity
H190 (= H174) active site, For GATase activity
E192 (= E176) active site, For GATase activity
R337 (= R301) binding XMP
D522 (= D454) binding XMP

Sites not aligning to the query:

610 binding XMP
685 binding XMP
691 binding XMP

2vxoB Human gmp synthetase in complex with xmp (see paper)
36% identity, 97% coverage: 11:514/517 of query aligns to 6:540/658 of 2vxoB

query
sites
2vxoB

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Y

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L

P

I

Y

F

E

-

V

-

M

-

G

-

S

-

I

L

S

A

S

R

R

L

I

I

I

P

N

R

E

M

V

C

K

H

G

N

V

V

N

N

R

R

V

V

Y

Y

D

I

I

F

S

G

-

P

-

V

Q

K

K

E

P

P

A

T

T

D

I

V

active site: G55 (= G60), C82 (= C87), Y83 (= Y88), H165 (= H174), E167 (= E176), D223 (= D232), K381 (= K373)
binding xanthosine-5'-monophosphate: R302 (= R301), G348 (= G342), K349 (≠ P343), P404 (= P396), G405 (= G397), P406 (= P398), R489 (= R456)

Sites not aligning to the query:

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

6jp9A Crsytal structure of a xmp complexed atppase subunit of m. Jannaschii gmp synthetase (see paper)
51% identity, 61% coverage: 205:517/517 of query aligns to 6:298/298 of 6jp9A

query
sites
6jp9A

N

K

F

F

I

I

E

D

T

E

E

A

I

V

A

E

I

I

R

K

E

Q

K

Q

V

I

G

S

N

D

G

R

K

K

V

A

I

I

C

I

A

A

L

L

S

S

G

G

V

V

D
|
D

S

S

V

V

V

A

A

A

V

V

L

L

L

T

H

H

K

K

A

A

I

I

G

G

D

D

Q

K

L

L

Q

T

C

A

I

V

F

F

V

V

N

D

N

T

G

G

L

L

L

M

R

R

K

K

G

G

E

E

A

R

E

E

K

E

V

V

V

E

N

K

L

T

F

F

T

R

R

D

H

K

F

L

K

G

I

L

N

N

L

L

D

I

Y

V

V

V

E

D

A

A

S

K

S

D

R

R

F

F

L

L

D

N

K

A

L

L

K

K

G

G

I

V

T

T

D

D

P

P

E

E

Q

E

K

K

R
|
R

K

K

I

I

G

G

N

K

E

L

F

F

I

I

Y

D

L

V

F

F

E

E

D

E

E

I

A

A

K

E

K

D

I

I

G

K

T

A

V

-

D

E

W

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

-

T

-

K

-

G

-

P

-

S

-

A

-

V

-

I

-

K

-

S

-

H

-

H

H

N

N

V

V

G

A

G

-

L

L

P

P

D

H

R

G

M

M

K

V

M

L

K

E

L

V

I

V

E

E

P

P

V

L

R

R

E

E

L

L

F

Y

K
|
K

D

D

E

E

V

V

R

R

L

L

G

A

K

K

E

E

L

L

G

G

L

L

P

P

D

D

E

S

V

I

I

V

H

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

I

L

G

G

E

E

I

V

T

T

A

E

D

E

R

K

L

L

E

N

I

I

L

C

R

R

E

E

S

A

D

N

A

A

I

I

V

V

L

E

D

E

E

E

I

V

R

K

K

K

A

A

G

N

L

L

Y

D

R

K

E

D

I

L

W

W

Q
|
Q

S

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

Y

W

T

I

I

V

A

A

L

L

R

R

A

M

V

V

N

K

S

S

L

L

D

D

G

A

M

M

T

T

A

A

D

H

W

V

V

P

K

E

L

I

P

P

Y

F

E

D

V

L

M

L

G

K

S

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

Q

D

K
|
K

P

P

A

A

T
|
T

I
|
I

E
|
E

W

F

E

E

active site: D33 (= D232), K155 (= K373)
binding xanthosine-5'-monophosphate: R102 (= R301), P178 (= P396), G179 (= G397), P180 (= P398), Q220 (= Q438), K290 (= K509), T294 (= T513), I295 (= I514), E296 (= E515)

7yc6A Crystal structure of d110p mutant of gatase subunit of methanocaldococcus jannaschii gmp synthetase
38% identity, 36% coverage: 11:196/517 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

V

Y

T

V

Q

H

L

R

I

I

A

H

R

R

R

S

I

L

R

K

E

Y

Q

I

S

G

V

V

Y

S

C

S

E

K

I

I

H

V

P

P

Y

N

N

T

M

T

G

P

L

L

E

E

K

E

I

I

K

E

A

S

F

N

A

K

P

E

-

V

Q

K

G

G

I

I

L

L

S

S

G

G

P

P

S

D

S

I

V

-

Y

-

D

-

A

E

D

K

A

A

P

K

H

N

S

C

D

I

A

D

G

I

V

A

Y

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

L

L

M

I

T

A

S

L

Q

A

L

Y

G

G

K

E

V

V

E

-

R

-

S

-

D

-

K

-

R

-

E

-

F

-

G

G

R

R

A

A

M

L

T

T

-

K

-

V

-

Y

I

V

D
|
D

D

K

T

E

T

N

D

P

L

L

F

F

S

K

G

N

L

V

S

P

G

R

K

E

E

F

E

N

V

A

W

W

M

A

S

S

H

H

G

K

D

D

K
x
E

I

V

E

K

Q

K

M

V

P

P

K

E

G

G

F

F

S

E

A

I

I

L

A

A

H
|
H

T

S

D

D

N

I

T
x
C

P

Q

A

V

A

E

A

A

M

M

K

K

D

H

E

K

K

T

R

K

R

P

L

I

Y

Y

A

G

V

V

Q

Q

F

F

H
|
H

P

P

E

E

V

V

V

A

H

H

T

T

P

E

K

Y

G

G

A

N

E

E

M

I

L

L

G

K

N

N

F

F

V

C

F

-

T

K

V

V

C

C

G

G

binding zinc ion: C76 (= C87), D101 (= D117), E123 (≠ K139), E123 (≠ K139), H136 (= H152), C140 (≠ T156), C140 (≠ T156), H158 (= H174)

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, 29% coverage: 42:191/517 of query aligns to 34:185/187 of P00903

query
sites
P00903

M

L

G

T

L

L

E

A

K

D

I

I

K

D

A

A

F

L

A

K

P

P

Q

Q

G

K

I

I

I

V

L

I

S

S

G

P

G

G

P

P

S

C

S

T

V

P

Y

D

D

E

A

A

D

G

A

I

P

S

H

L

S

D

D

V

A

I

G

R

V

H

Y

Y

E

A

L

G

G

R

V

L

P

P

V

I

L

L

G

G

I

V

C
|
C

Y

L

G

G

M

H

Q

Q

L

A

M

M

T

A

S

Q

Q

A

L

F

G

G

K

K

V

V

E

V

R

R

S

A

D

A

K

K

R

V

E

M

F

H

G

G

R

K

A

T

A

S

M

P

T

I

I

T

D

H

D

N

T

G

T

E

D

G

L

V

F

F

S

R

G

G

L

L

S

A

G

N

K

P

E

L

E

T

V

V

W

T

M

R

S

Y

H

H

G

S

D

L

K

V

I

V

E

E

-

P

-

D

Q

S

M

L

P

P

K

A

G

C

F

F

S

D

A

V

I

T

A

A

H

W

T

S

D

E

N

T

T

R

P

E

A

I

A

M

A

G

M

I

K

R

D

H

E

R

K

Q

R

W

R

D

L

L

Y

E

A

G

V

V

Q

Q

F

F

H
|
H

P

P

E
|
E

V

S

V

I

H

L

T

S

P

E

K

Q

G

G

A

H

E

Q

M

L

L

L

G

A

N

N

F

F

V

L

C79 (= C87) mutation to S: 10000-fold decrease in catalytic efficiency.
H168 (= H174) mutation to Q: Loss of activity.
E170 (= E176) 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)
30% identity, 35% coverage: 11:191/517 of query aligns to 75:264/276 of Q42565

query
sites
Q42565

I

I

L

I

I

V

L

I

D

D

F

N

G

Y

S

D

Q

S

V

F

T

T

Q

Y

L

N

I

L

A

C

R

Q

R

Y

I

M

R

G

E

E

Q

L

S

G

V

C

Y

H

C

F

E

E

I

V

H

Y

P

R

Y

N

N

D

-

E

M

L

G

T

L

V

E

E

K

E

I

L

K

K

A

K

F

K

A

N

P

P

Q

R

G

G

I

V

I

L

L

I

S

S

G

P

G

G

P

P

S

G

S

T

V

P

Y

Q

D

D

A

S

D

G

A

I

P

-

H

-

S

S

D

L

A

Q

G

T

V

V

Y

L

E

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

M

I

T

G

S

E

Q

A

L

F

G

G

K

K

V

I

E

V

R

R

S

S

D

P

-

F

K

G

R

V

E

M

F

H

G
|
G

R

K

A

S

M

M

T

V

I

H

D

Y

D

D

T

E

T

K

-

G

-

E

D

G

L

L

F

F

S

S

G

G

L

L

S

S

G

N

K

P

E

F

E

I

V

V

W

G

M

R

S

Y

H

H

G

S

D

L

K

V

I

I

E

E

Q

K

-

D

-

T

M

F

P

P

K

S

G

D

-

E

F

L

S

E

A

V

I

T

A

A

H

W

T

T

D

E

N

D

T

G

P

L

A

V

A

M

A

A

M

A

K

R

D

H

E

R

K

K

-

Y

R

K

R

H

L

I

Y

Q

A

G

V

V

Q

Q

F

F

H

H

P

P

E

E

V

S

V

I

H

I

T

T

P

T

K

E

G

G

A

K

E

T

M

I

L

V

G

R

N

N

F

F

V

I

G150 (= G85) mutation to D: In trp4-1; no visible phenotype under normal growth conditions.
G176 (= G110) mutation to E: In wei7-2; insensitive to inhibition of root elongation by ethylene.

8hx8A Crystal structure of 4-amino-4-deoxychorismate synthase from streptomyces venezuelae co-crystallized with chorismate (see paper)
28% identity, 26% coverage: 55:190/517 of query aligns to 51:187/673 of 8hx8A

query
sites
8hx8A

I

I

I

V

L

V

S

S

G

P

G

G

P

P

S

G

S

S

V

P

-

D

Y

R

D

E

A

R

D

D

A

F

P

G

H

I

S

S

D

R

A

R

G

A

V

I

Y

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

L

G

M

I

T

A

S

Q

Q

L

L

F

G

G

K

T

V

V

E

G

R

L

S

A

D

P

K

E

R

P

E

M

F

H

G

G

R

R

A

V

A

S

M

E

T

V

I

R

D

H

D

T

T

G

T

E

D

D

L

V

F

F

S

R

G

G

L

L

S

P

G

S

K

P

E

F

E

T

V

A

W

V

M

R

S

Y

H

H

G

S

D

L

K

A

I

A

E

T

Q

D

M

L

P

P

K

D

G

E

F

L

S

E

A

P

I

L

A

A

H

W

T

S

D

D

N

D

T

G

P

V

A

V

A

M

A

G

M

L

K

R

D

H

E

R

K

E

R

K

R

P

L

L

Y

W

A

G

V

V

Q

Q

F

F

H

H

P

P

E

E

V

S

V
x
I

H

G

T
x
S

P

D

K

F

G

G

A

R

E

E

M

I

L

M

G

A

N

N

F

F

binding magnesium ion: I175 (≠ V178), S177 (≠ T180)

Sites not aligning to the query:

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

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)
25% identity, 34% coverage: 11:187/517 of query aligns to 4:183/193 of P00900

query
sites
P00900

I

I

L

L

I

L

L

L

D

D

F

N

G

V

S

D

Q

S

V

F

T

T

Q

Y

L

N

I

L

A

V

R

D

R

Q

I

L

R

R

E

A

Q

S

S

G

V

H

Y

Q

C

V

E

V

I

I

H

Y

P

R

Y

N

N

Q

M

I

G

G

-

A

-

E

-

V

-

I

L

I

E

E

K

R

I

L

K

Q

A

H

F

M

A

E

P

Q

Q

P

G

V

I

L

I

M

L

L

S

S

G

P

G

G

P

P

S

G

S

T

V

P

Y

S

D

E

A

A

D

G

A

C

P

M

H

P

S

E

D

L

A

L

G

Q

V

R

Y

L

E

R

L

G

G

Q

V

L

P

P

V

I

L

I

G

G

I

I

C
|
C

Y

L

G

G

M

H

Q

Q

L

A

M

I

T

V

S

E

Q

A

L

Y

G

G

K

Q

V

V

E

G

R

Q

S

A

D

G

K

E

R

I

E

L

F

H

G

G

R

K

A

A

A

S

M

A

T

I

I

A

D

H

D

D

T

G

T

E

D

G

L

M

F

F

S

A

G

G

L

M

S

A

G

N

K

P

E

L

E

P

V

V

W

A

M

R

S

Y

H

H

G

S

D

L

K

V

I

G

E

S

Q

N

M

I

P

P

K

A

G

D

F

L

S

T

A

V

I

N

A

A

H

R

T

S

D

G

N

E

T

M

P

-

A

V

A

M

A

A

M

V

K

R

D

D

E

D

K

R

R

R

L

V

Y

C

A

G

V

F

Q

Q

F

F

H

H

P

P

E

E

V

S

V

I

H

L

T

T

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G

A

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C84 (= C87) 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)
25% identity, 34% coverage: 11:187/517 of query aligns to 3:182/192 of 1i7qB

query
sites
1i7qB

I

I

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active site: G58 (≠ S62), C83 (= C87), L84 (≠ Y88), H169 (= H174), E171 (= E176)
binding glutamic acid: P55 (≠ G59), G56 (= G60), G58 (≠ S62), C83 (= C87), L84 (≠ Y88), Q87 (= Q91), H132 (= H136), S133 (≠ G137), L134 (≠ D138)

7d54A Crstal structure msgatase with gln (see paper)
34% identity, 19% coverage: 78:177/517 of query aligns to 92:182/242 of 7d54A

query
sites
7d54A

E

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binding glutamine: C101 (= C87), W144 (≠ S135)

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)
26% identity, 36% coverage: 2:185/517 of query aligns to 235:413/430 of Q9LVW7

query
sites
Q9LVW7

S

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x
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D

H410 (≠ K182) mutation to Y: In ven6-1; reticulate leaf phenotype.

O25096 NH(3)-dependent NAD(+) synthetase; EC 6.3.1.5 from Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori) (see paper)
25% identity, 38% coverage: 200:394/517 of query aligns to 9:182/260 of O25096

query
sites
O25096

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31:38 (vs. 226:233, 75% identical) binding ATP
T132 (= T321) binding ATP
K161 (= K373) binding ATP

1xngB Crystal structure of nh3-dependent NAD+ synthetase from helicobacter pylori (see paper)
25% identity, 38% coverage: 200:394/517 of query aligns to 7:180/262 of 1xngB

query
sites
1xngB

I

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M

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R

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x
A

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P

active site: D35 (= D232), E135 (vs. gap)
binding adenosine-5'-triphosphate: G29 (≠ A226), L30 (= L227), S31 (= S228), G33 (= G230), L34 (≠ V231), D35 (= D232), S36 (= S233), M56 (≠ V253), R112 (vs. gap), T130 (= T321), E135 (vs. gap), K159 (= K373)
binding nicotinic acid adenine dinucleotide: R21 (≠ V218), F23 (≠ N220), N106 (= N306), Y117 (= Y310), S120 (vs. gap), L121 (vs. gap), L126 (≠ K317), Y140 (≠ Q327), G141 (= G328), T142 (= T329), D146 (= D333), A150 (≠ S337)

Sites not aligning to the query:

Query Sequence

>WP_012469956.1 NCBI__GCF_000020385.1:WP_012469956.1
MSSTDIHSQKILILDFGSQVTQLIARRIREQSVYCEIHPYNMGLEKIKAFAPQGIILSGG
PSSVYDADAPHSDAGVYELGVPVLGICYGMQLMTSQLGGKVERSDKREFGRAAMTIDDTT
DLFSGLSGKEEVWMSHGDKIEQMPKGFSAIAHTDNTPAAAMKDEKRRLYAVQFHPEVVHT
PKGAEMLGNFVFTVCGCQPIWTMANFIETEIAAIREKVGNGKVICALSGGVDSSVVAVLL
HKAIGDQLQCIFVNNGLLRKGEAEKVVNLFTRHFKINLDYVEASSRFLDKLKGITDPEQK
RKIIGNEFIYLFEDEAKKIGTVDWLAQGTLYPDVIESVSTKGPSAVIKSHHNVGGLPDRM
KMKLIEPVRELFKDEVRLLGKELGLPDEVIHRQPFPGPGLAIRCIGEITADRLEILRESD
AIVLDEIRKAGLYREIWQSFAVLLPVRSVGVMGDARTYDYTIALRAVNSLDGMTADWVKL
PYEVMGSISSRIINEVKGVNRVVYDISQKPPATIEWE

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