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)
40% identity, 100% coverage: 1:522/522 of query aligns to 1:555/555 of Q8IJR9

query
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Y18 (= Y18) mutation to F: Slight increase in affinity for glutamine. No defect in glutaminase activity.
H20 (≠ Q20) 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 (≠ R24) 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 (= R25) 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 (≠ R109) 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 (≠ M175) 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 (= D338) Important for ATPPase activity; mutation to A: Impaired formation of adenyl-XMP intermediate. Slight increase in glutaminase activity.
E374 (= E341) mutation to L: 8.9-fold decrease in affinity for ammonia. Severe loss of glutaminase activity.
K376 (≠ G343) 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 (= K352) mutation to L: Severe loss of ATP pyrophosphatase (ATPPase) activity. 80 percent decrease in glutaminase activity. Impaired GMP formation.
T387 (≠ S353) mutation to A: No effect on ATP pyrophosphatase (ATPPase) activity. 20 percent decrease in glutaminase activity. No effect on GMP formation.
H388 (= H354) 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 (= H355) Important for ATPPase activity; mutation to A: Loss of ATP pyrophosphatase (ATPPase) activity. 67 percent decrease in glutaminase activity. Impaired GMP formation.
N390 (= N356) mutation to A: No effect on ATP pyrophosphatase (ATPPase) activity. Increases glutaminase activity. Loss of GMP formation.
K411 (= K377) mutation to L: 70 percent decrease in glutaminase activity. Loss of GMP formation.
D412 (= D378) mutation to A: 30 percent decrease in glutaminase activity. 7.9-fold decrease in affinity for glutamine.
D413 (≠ E379) mutation to A: 35 percent decrease in glutaminase activity. 3.6-fold decrease in affinity for glutamine.
K415 (≠ R381) mutation to L: Increases glutaminase activity. 4.2-fold decrease in affinity for ATP.
Q476 (= Q442) binding XMP
R539 (= R506) mutation to L: 85 percent decrease in glutaminase activity.
K547 (= K514) binding XMP; mutation to L: 85 percent decrease in glutaminase activity.
I552 (= I519) binding XMP
E553 (= E520) binding XMP; mutation to L: 85 percent decrease in glutaminase activity.
E555 (= E522) mutation to L: 20 percent decrease in glutaminase activity. No effect on GMP formation.

5tw7F Crystal structure of a gmp synthase (glutamine-hydrolyzing) from neisseria gonorrhoeae
46% identity, 99% coverage: 5:522/522 of query aligns to 2:490/490 of 5tw7F

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active site: G55 (= G58), C81 (= C85), Y82 (= Y86), H171 (= H171), E173 (= E173), D229 (= D229), K345 (= K377)
binding magnesium ion: I466 (≠ T498), V469 (= V501), I472 (≠ V504)

4wioA Crystal structure of the c89a gmp synthetase inactive mutant from plasmodium falciparum in complex with glutamine (see paper)
38% identity, 98% coverage: 9:522/522 of query aligns to 3:525/525 of 4wioA

query
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4wioA

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V

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I

I

K

K

A

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N

N

P

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V

V

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L

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G

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|
G

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x
A

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|
Y

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|
Q

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|
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N

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S

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K

K

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A

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T

I

I

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active site: G52 (= G58), A83 (≠ C85), Y84 (= Y86), H197 (= H171), E199 (= E173), D255 (= D229), K393 (= K377)
binding glutamine: Q87 (= Q89), N158 (≠ S132), H159 (= H133), N160 (≠ G134), D161 (= D135), H197 (= H171)

3uowA Crystal structure of pf10_0123, a gmp synthetase from plasmodium falciparum
37% identity, 98% coverage: 9:522/522 of query aligns to 4:517/517 of 3uowA

query
sites
3uowA

V

I

L

L

V

V

V

L

D

N

F

F

G

G

A

S

Q

Q

Y

Y

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V

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G

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|
G

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|
C

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|
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|
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|
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|
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|
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|
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G

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L

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|
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A

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A

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V

L

L

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K

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V

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Q

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G

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Y

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L

L

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K

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M

M

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W

W

T

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D

V

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L

L

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T

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S

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V

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K

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V

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N

R

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L

L

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D

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V

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S

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K
|
K

P

P

G

A

T
|
T

I
|
I

E
|
E

W

F

E

E

active site: G53 (= G58), C84 (= C85), Y85 (= Y86), H198 (= H171), E200 (= E173), D255 (= D229), K381 (= K377)
binding xanthosine-5'-monophosphate: R325 (= R298), P404 (= P400), G405 (= G401), P406 (= P402), Q446 (= Q442), K509 (= K514), T513 (= T518), I514 (= I519), E515 (= E520)

3uowB Crystal structure of pf10_0123, a gmp synthetase from plasmodium falciparum
37% identity, 98% coverage: 9:522/522 of query aligns to 2:477/477 of 3uowB

query
sites
3uowB

V

I

L

L

V

V

V

L

D

N

F

F

G

G

A

S

Q

Q

Y

Y

A

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Q

H

L

L

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I

A

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K

R

R

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R

N

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N

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F

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H

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T

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K

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D

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M

N

N

P

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R

K

A

G

V

V

V

I

L

L

S

S

G

G

G
|
G

P

P

A

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Y

-

A

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D

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A

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L

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D

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F

G

G

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C
|
C

Y
|
Y

G

G

F

M

Q

Q

A

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M

I

A

A

Q

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A

Q

L

M

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N

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Y

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|
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|
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|
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V

I

D

D

H

N

G

G

L

L

R

R

S

K

G

N

E

E

R

A

A

E

Q

N

V

V

Q

Y

R

T

D

-

F

F

V

L

A

K

A

S

T

T

-

F

-

P

G

D

A

M

N

N

L

I

V

T

T

K

V

I

D

D

V

A

A

S

D

E

R

N

F

F

L

L

E

S

A

N

L

L

S

Q

G

G

V

V

T

T

N

D

P

P

E

E

G

Q

K

K

R
|
R

K

K

I

I

G

G

R

K

E

L

F

F

I

I

R

E

A

E

F

F

E

E

G

K

A

A

V

V

R

N

D

N

A

I

L

-

E

-

S

-

Q

-

D

-

G

-

S

D

D

D

V

I

P

N

V

K

E

T

F

F

L

L

V

L

Q

Q

G

G

T

T

L

L

Y

Y

P

P

D

D

V

I

E

E

S

S

G

K

G

-

S

-

G

-

T

-

A

-

N

-

I

-

K

-

S

-

H

-

N

-

V

-

G

-

L

-

P

-

D

-

L

-

K

K

F

F

T

K

L

L

V

F

E

E

P

P

L

F

R

K

L

Y

L

L

F

F

K
|
K

D

D

E

D

V

V

R

K

A

T

V

L

G

S

R

R

E

E

L

L

G

N

L

L

P

P

E

E

I

I

V

T

A

N

R

R

Q

H

P

P

F

F

P
|
P

G
|
G

P
|
P

G

G

L

L

G

A

I

I

R

R

I

V

V

I

G

G

E

E

V

I

T

N

A

K

E

H

R

K

L

L

D

N

T

I

L

L

R

R

R

E

A

V

D

D

A

D

I

I

A

F

R

I

E

N

E

D

L

L

T

K

S

Q

A

Y

G

G

L

L

D

Y

H

N

Q

Q

I

I

W

S

Q
|
Q

C

A

P

F

V

A

V

V

L

L

A

S

D

S

V

-

R

K

S

S

V

V

G

G

V

-

Q

-

G

-

D

-

G

-

R

-

T

-

Y

Y

G

D

H

Y

P

V

I

C

V

V

L

L

R

R

P

A

V

V

S

K

S

T

E

S

D

S

A

F

M

M

T

T

A

A

D

N

W

W

T

Y

R

Q

V

I

P

P

Y

Y

E

D

V

I

L

L

E

D

R

K

I

I

S

T

T

T

R

R

I

I

T

L

N

S

E

E

V

V

R

K

E

G

V

V

N

N

R

R

V

I

V

L

L

Y

D

D

V

V

T

S

S

S

K
|
K

P

P

G

A

T
|
T

I
|
I

E
|
E

W

F

E

E

active site: G47 (= G58), C67 (= C85), Y68 (= Y86), H162 (= H171), E164 (= E173), D218 (= D229), K340 (= K377)
binding xanthosine-5'-monophosphate: R288 (= R298), P363 (= P400), G364 (= G401), P365 (= P402), Q405 (= Q442), K469 (= K514), T473 (= T518), I474 (= I519), E475 (= E520)

6jp9A Crsytal structure of a xmp complexed atppase subunit of m. Jannaschii gmp synthetase (see paper)
50% identity, 62% coverage: 198:522/522 of query aligns to 2:298/298 of 6jp9A

query
sites
6jp9A

W

F

T

D

P

P

A

K

N

K

I

F

A

I

E

D

A

E

L

A

V

V

E

E

Q

E

V

I

R

K

T

Q

Q

Q

I

I

G

S

D

D

G

R

R

K

A

A

I

I

C

I

G

A

L

L

S

S

G

G

V

V

D
|
D

S

S

A

S

V

V

A

A

A

V

L

L

V

T

Q

H

R

K

A

A

I

I

G

G

D

D

R

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

S

K

G

G

E

E

R

R

A

E

Q

E

V

V

Q

E

R

K

D

T

F

F

V

R

A

D

A

K

T

L

G

G

A

L

N

N

L

L

V

I

T

V

V

V

D

D

V

A

A

K

D

D

R

R

F

F

L

L

E

N

A

A

L

L

S

K

G

G

V

V

T

T

N

D

P

P

E

E

G

E

K

K

R
|
R

K

K

I

I

G

G

R

K

E

L

F

F

I

I

R

D

A

V

F

F

E

E

G

-

A

-

V

-

R

-

D

-

A

-

L

-

E

-

S

-

Q

E

D

I

G

A

S

E

D

D

V

I

P

K

V

A

E

E

F

V

L

L

V

V

Q

Q

G

G

T

T

L

I

Y

A

P

P

D

D

V

-

E

-

S

-

G

-

S

-

G

-

T

-

A

-

N

-

I

-

K

-

S

-

H

-

H

H

N

N

V

V

G

-

G

A

L

L

P

P

D

H

D

G

L

M

K

V

F

L

T

E

L

V

V

V

E

E

P

P

L

L

R

R

L

E

L

L

F

Y

K
|
K

D

D

E

E

V

V

R

R

A

L

V

L

G

A

R

K

E

E

L

L

G

G

L

L

P

P

E

D

E

S

I

I

V

V

A

Y

R

R

Q

Q

P

P

F

F

P
|
P

G
|
G

P
|
P

G

G

L

L

G

A

I

V

R

R

I

V

V

L

G

G

E

E

V

V

T

T

A

E

E

E

R

K

L

L

D

N

T

I

L

C

R

R

R

E

A

A

D

N

A

A

I

I

A

V

R

E

E

E

L

V

T

K

S

K

A

A

G

N

L

L

D

D

H

K

Q

D

I

L

W

W

Q
|
Q

C

Y

P

F

V

A

V

V

L

V

L

L

A

-

D

D

V

C

R

K

S

A

V

T

G

G

V

V

Q

K

G

G

D

D

G

-

R

R

T

E

Y

Y

G

N

H

W

P

I

I

V

V

A

L

L

R

R

P

M

V

V

S

K

S

S

E

L

D

D

A

A

M

M

T

T

A

A

D

H

W

V

T

P

R

E

V

I

P

P

Y

F

E

D

V

L

L

L

E

K

R

R

I

I

S

S

T

K

R

R

I

I

T

T

N

S

E

E

V

I

R

P

E

N

V

V

N

A

R

R

V

V

L

F

D

D

V

I

T

T

S

D

K
|
K

P

P

G

A

T
|
T

I
|
I

E
|
E

W

F

E

E

active site: D33 (= D229), K155 (= K377)
binding xanthosine-5'-monophosphate: R102 (= R298), P178 (= P400), G179 (= G401), P180 (= P402), Q220 (= Q442), K290 (= K514), T294 (= T518), I295 (= I519), E296 (= E520)

P49915 GMP synthase [glutamine-hydrolyzing]; GMP synthetase; Glutamine amidotransferase; EC 6.3.5.2 from Homo sapiens (Human) (see paper)
35% identity, 97% coverage: 9:516/522 of query aligns to 28:572/693 of P49915

query
sites
P49915

V

V

L

V

V

I

V

L

D

D

F

A

G

G

A

A

Q

Q

Y

Y

A

G

Q

K

L

V

I

I

A

D

R

R

V

V

R

R

E

E

A

L

R

F

V

V

F

Q

S

S

E

E

V

I

I

F

P

P

H

L

T

E

T

T

S

P

V

A

E

F

E

A

I

I

K

K

A

E

R

Q

N

G

P

F

R

R

A

A

V

I

L

I

S

S

G

G

P

P

A

N

S

S

V

V

Y

Y

A

A

D

E

G

D

A

A

P

P

Q

W

L

F

D

D

P

P

A

A

L

I

F

F

D

T

L

I

D

G

V

K

P

P

V

V

F

L

G

G

I

I

C
|
C

Y

Y

G

G

F

M

Q

Q

A

M

M

M

A

N

Q

K

A

V

L

F

G

G

T

T

V

V

A

H

H

K

T

K

G

S

T

V

S

R

E

E

Y

D

G

G

R

V

T

F

E

N

L

I

K

S

V

V

A

D

G

N

-

T

G

C

Q

S

L

L

H

F

T

R

D

G

L

L

P

Q

E

K

T

E

Q

E

P

V

V

V

W

L

M

L

S

T

H

H

G

G

D

D

A

S

V

V

T

D

A

K

A

V

P

A

E

D

G

G

F

F

E

K

V

V

A

A

T

R

S

S

A

-

G

G

A

N

P

I

V

V

A

A

A

G

F

I

E

A

N

N

R

E

A

S

R

K

L

L

A

Y

G

G

V

A

Q

Q

Y

F

H
|
H

P

P

E
|
E

V

V

M

G

H

L

S

T

P

E

H

N

G

G

Q

K

Q

V

V

I

L

L

S

K

R

N

F

F

L

L

H

Y

E

D

F

I

A

A

G

G

I

C

D

S

A

G

T

T

W

F

T

T

P

V

A

Q

N

N

I

R

A

E

E

L

A

E

L

C

V

I

E

R

Q

E

V

I

R

K

T

E

Q

R

I

V

G

G

D

T

G

S

R

K

A

V

I

L

C

V

G

L

L

L

S

S

G

G

V

V

D

D

S

S

A

T

V

V

A

C

A

T

A

A

L

L

V

L

Q

N

R

R

A

A

I

L

G

N

-

Q

D

E

R

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

S

K

G

R

E

E

R

S

A

Q

Q

S

V

V

Q

E

R

-

D

E

F

A

V

L

A

K

T

L

G

G

A

I

N

Q

L

V

V

K

T

V

V

I

D

N

V

A

A

A

D

H

R

S

F

F

L

Y

-

N

-

G

-

T

-

L

-

P

-

I

-

S

-

D

-

E

-

D

-

R

-

T

-

P

-

R

-

K

-

R

-

I

-

S

E

K

A

T

L

L

S

N

G

M

V

T

T

T

N

S

P

P

E

E

G

E

K

K

R
|
R

K

K

I

I

G

G

R

D

E

T

F

F

I

V

R

K

A

I

F

A

E

N

G

E

A

V

V

I

R

G

D

E

A

M

L

-

E

-

S

-

Q

-

D

-

G

-

S

N

D

L

V

K

P

P

V

E

E

E

-

V

F

F

L

L

V

A

Q

Q

G

G

T

T

L

L

Y

R

P

P

D

D

V

L

V

I

E

E

S

S

G

A

G

S

-

L

-

V

G

A

S

S

G

G

T

K

A

A

N

E

-

L

I

I

K

K

S

T

H

H

N

N

V

D

G

T

G

E

L

L

P

I

D

R

D

K

L

L

K

R

F

E

-

E

-

G

T

K

L

V

V

I

E

E

P

P

L

L

R

K

L

D

L

F

F

H

K

K

D

D

E

E

V

V

R

R

A

I

V

L

G

G

R

R

E

E

L

L

G

G

L

L

P

P

E

E

I

L

V

V

A

S

R

R

Q

H

P

P

F

F

P

P

G

G

P

P

G

G

L

L

G

A

I

I

R

R

I

V

V

I

G

C

-

A

-

E

-

P

-

Y

-

I

-

C

-

K

-

D

-

F

-

P

-

E

-

T

-

N

-

I

-

L

-

K

-

I

-

V

-

A

-

D

-

F

E

S

V

A

T

S

A

V

E

K

R

K

L

P

D

H

T

T

L

L

-

L

R

Q

R

R

A

V

D

K

A

A

I

C

A

T

R

T

E

E

L

D

T

Q

S

E

A

K

G

L

L

M

D

Q

H

I

Q

T

I

S

W

L

Q

H

C

S

P

L

V

N

V

A

L

F

L

L

A

L

D

P

V

I

R

K

S

T

V

V

G

G

V

V

Q

Q

G

G

D
|
D

G

C

R

R

T

S

Y

Y

G

S

H

Y

P

-

I

-

V

-

L

V

R

C

P

G

V

I

S

S

E

K

D

D

A

E

M

-

T

-

A

P

D

D

W

W

T

E

R

S

V

L

P

I

Y

F

E

-

V

-

L

L

E

A

R

R

I

L

S

I

T

P

R

R

I

M

T

C

N

H

E

N

V

V

R

N

E

R

V

V

N

V

R

Y

V

I

V

F

L

G

D

P

V

P

T

V

S

K

K

E

P

P

C104 (= C85) active site, For GATase activity
H190 (= H171) active site, For GATase activity
E192 (= E173) active site, For GATase activity
R337 (= R298) binding XMP
D522 (= D459) 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)
35% identity, 97% coverage: 9:516/522 of query aligns to 6:537/658 of 2vxoB

query
sites
2vxoB

V

V

L

V

V

I

V

L

D

D

F

A

G

G

A

A

Q

Q

Y

Y

A

G

Q

K

L

V

I

I

A

D

R

R

V

V

R

R

E

E

A

L

R

F

V

V

F

Q

S

S

E

E

V

I

I

F

P

P

H

L

T

E

T

T

S

P

V

A

E

F

E

A

I

I

K

K

A

E

R

Q

N

G

P

F

R

R

A

A

V

I

L

I

S

S

G

G

G
|
G

P

P

A

N

S

S

V

V

Y

Y

A

A

D

E

G

D

A

A

P

P

Q

W

L

F

D

D

P

P

A

A

L

I

F

F

D

T

L

I

D

G

V

K

P

P

V

V

F

L

G

G

I

I

C
|
C

Y
|
Y

G

G

F

M

Q

Q

A

M

M

M

A

N

Q

K

A

V

L

F

G

G

T

T

V

V

A

H

H

K

T

K

G

S

T

D

S

G

E

V

Y

F

G

N

R

I

T

S

E

V

L

D

K

N

V

T

A

C

G

S

G

-

Q

-

L

L

H

F

T

R

D

G

L

L

P

Q

E

K

T

E

Q

E

P

V

V

V

W

L

M

L

S

T

H

H

G

G

D

D

A

S

V

V

T

D

A

K

A

V

P

A

E

D

G

G

F

F

E

K

V

V

A

A

T

R

S

S

A

-

G

G

A

N

P

I

V

V

A

A

A

G

F

I

E

A

N

N

R

E

A

S

R

K

L

L

A

Y

G

G

V

A

Q

Q

Y

F

H
|
H

P

P

E
|
E

V

V

M

G

H

L

S

T

P

E

H

N

G

G

Q

K

Q

V

V

I

L

L

S

K

R

N

F

F

L

L

H

Y

E

D

F

I

A

A

G

G

I

C

D

S

A

G

T

T

W

F

T

T

P

V

A

Q

N

N

I

R

A

E

E

L

A

E

L

C

V

I

E

R

Q

E

V

I

R

K

T

E

Q

R

I

V

G

G

D

T

G

S

R

K

A

V

I

L

C

V

G

L

L

L

S

S

G

G

V

V

D
|
D

S

S

A

T

V

V

A

C

A

T

A

A

L

L

V

L

Q

N

R

R

A

A

I

L

G

N

-

Q

D

E

R

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

S

K

G

R

E

E

R

S

A

Q

Q

S

V

V

Q

E

R

-

D

E

F

A

V

L

A

K

T

L

G

G

A

I

N

Q

L

V

V

K

T

V

V

I

D

N

V

A

A

A

D

H

R

S

F

F

L

Y

-

N

-

G

-

T

-

L

-

P

-

R

-

I

-

S

E

K

A

T

L

L

S

N

G

M

V

T

T

T

N

S

P

P

E

E

G

E

K

K

R
|
R

K

K

I

I

G

G

R

D

E

T

F

F

I

V

R

K

A

I

F

A

E

N

G

E

A

V

V

I

R

G

D

E

A

M

L

-

E

-

S

-

Q

-

D

-

G

-

S

N

D

L

V

K

P

P

V

E

E

E

-

V

F

F

L

L

V

A

Q

Q

G

G

T

T

L

L

Y

R

P

P

D

D

V

L

V

I

E

E

S

S

G

A

G

S

-

L

-

V

G

A

S

S

G
|
G

T
x
K

A

A

N

E

-

L

I

I

K

K

S

T

H

H

N

N

V

D

G

T

G

E

L

L

P

I

D

R

D

K

L

L

K

R

F

E

-

E

-

G

T

K

L

V

V

I

E

E

P

P

L

L

R

K

L

D

L

F

F

H

K
|
K

D

D

E

E

V

V

R

R

A

I

V

L

G

G

R

R

E

E

L

L

G

G

L

L

P

P

E

E

I

L

V

V

A

S

R

R

Q

H

P

P

F

F

P
|
P

G
|
G

P
|
P

G

G

L

L

G

A

I

I

R

R

I

V

V

I

G

C

-

A

-

E

-

P

-

Y

-

I

-

C

-

K

-

D

-

F

-

P

-

E

-

T

-

N

-

I

-

L

-

K

-

I

-

V

-

A

-

D

-

F

E

S

V

A

T

S

A

V

E

K

R

K

L

P

D

H

T

T

L

L

-

L

R

Q

R

R

A

V

D

K

A

A

I

C

A

T

R

T

E

E

L

D

T

Q

S

E

A

K

G

L

L

M

D

Q

H

I

Q

T

I

S

W

L

Q

H

C

S

P

L

V

N

V

A

L

F

L

L

A

L

D

P

V

I

R

K

S

T

V

V

G

G

V

V

Q

Q

G

G

D

D

G

C

R
|
R

T

S

Y

Y

G

S

H

Y

P

-

I

-

V

-

L

V

R

C

P

G

V

I

S

S

E

K

D

D

A

E

M

-

T

-

A

P

D

D

W

W

T

E

R

S

V

L

P

I

Y

F

E

-

V

-

L

L

E

A

R

R

I

L

S

I

T

P

R

R

I

M

T

C

N

H

E

N

V

V

R

N

E

R

V

V

N

V

R

Y

V

I

V

F

L

G

D

P

V

P

T

V

S

K

K

E

P

P

active site: G55 (= G58), C82 (= C85), Y83 (= Y86), H165 (= H171), E167 (= E173), D223 (= D229), K381 (= K377)
binding xanthosine-5'-monophosphate: R302 (= R298), G348 (= G347), K349 (≠ T348), P404 (= P400), G405 (= G401), P406 (= P402), R489 (= R461)

Sites not aligning to the query:

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

7yc6A Crystal structure of d110p mutant of gatase subunit of methanocaldococcus jannaschii gmp synthetase
35% identity, 34% coverage: 9:187/522 of query aligns to 2:174/183 of 7yc6A

query
sites
7yc6A

V

I

L

V

V

I

V

L

D

D

F

N

G

G

A

G

Q

Q

Y

Y

A

V

Q

H

L

R

I

I

A

H

R

R

R

S

V

L

R

K

E

Y

A

I

R

G

V

V

F

S

S

S

E

K

V

I

I

V

P

P

H

N

T

T

S

P

V

L

E

E

I

I

K

E

A

S

-

N

R

K

N

E

P

V

R

K

A

G

V

I

L

L

S

S

G

G

P

P

A

D

S

I

V

E

Y

K

A

A

D

K

G

N

A

C

P

-

Q

-

L

I

D

D

P

I

A

A

L

L

F

-

D

N

L

A

D

K

V

L

P

P

V

I

F

L

G

G

I

I

C
|
C

Y

L

G

G

F

H

Q

Q

A

L

M

I

A

A

Q

L

A

A

L

Y

G

G

T

E

V

V

A

G

H

R

T

A

G

A

-

L

T

T

S

K

E

V

Y

Y

G

V

R
x
D

T

K

E

E

L

-

K

-

V

-

A

-

G

-

G

N

Q

P

L

L

H

F

T

K

D

N

L

V

P

P

E

R

T

E

Q

F

P

N

V

A

W

W

M

A

S

S

H

H

G

K

D

D

A
x
E

V

V

T

K

A

K

A

V

P

P

E

E

G

G

F

F

E

E

V

I

V

L

A

A

T
x
H

S

S

A

D

G

I

A
x
C

P

Q

V

V

A

E

A

A

F

M

E

K

N

H

R

K

A

T

R

K

R

P

L

I

A

Y

G

G

V

V

Q

Q

Y

F

H
|
H

P

P

E

E

V

V

M

A

H

H

S

T

P

E

H

Y

G

G

Q

N

Q

E

V

I

L

L

S

K

R

N

F

F

binding zinc ion: C76 (= C85), D101 (≠ R109), E123 (≠ A136), E123 (≠ A136), H136 (≠ T149), C140 (≠ A153), C140 (≠ A153), 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)
33% identity, 29% coverage: 41:189/522 of query aligns to 35:186/187 of P00903

query
sites
P00903

S

T

V

L

E

A

E

D

I

I

K

D

A

A

R

L

N

K

P

P

R

Q

A

K

V

I

V

V

L

I

S

S

G

P

G

G

P

P

A

C

S

T

V

P

Y

-

A

-

D

-

G

-

A

-

P

-

Q

-

L

-

D

D

P

E

A

A

L

G

F

I

D

S

L

L

D

D

V

V

-

I

-

R

-

H

-

Y

-

A

-

G

-

R

-

L

P

P

V

I

F

L

G

G

I

V

C
|
C

Y

L

G

G

F

H

Q

Q

A

A

M

M

A

A

Q

Q

A

A

L

F

G

G

T

K

V

V

A

V

H

R

T

A

G

A

T

K

S

V

E

M

Y

H

G

G

R

K

T

T

E

S

L

P

K

I

V

T

A

H

G

N

G

G

Q

E

-

G

L

V

H

F

T

R

D

G

L

L

P

A

E

N

T

P

Q

L

P

T

V

V

W

T

M

R

S

Y

H

H

G

S

D

L

A

V

V

V

-

E

-

P

T

D

A

S

A

L

P

P

E

A

G

C

F

F

E

D

V

V

V

T

A

A

T

W

S

S

A

E

G

T

A

R

P

E

V

I

A

M

A

G

F

I

E

R

N

H

R

R

A

Q

R

W

R

D

L

L

A

E

G

G

V

V

Q

Q

Y

F

H
|
H

P

P

E
|
E

V

S

M

I

H

L

S

S

P

E

H

Q

G

G

Q

H

Q

Q

V

L

L

L

S

A

R

N

F

F

L

L

H

H

C79 (= C85) 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, 29% coverage: 35:187/522 of query aligns to 33:187/673 of 8hx8A

query
sites
8hx8A

V

V

I

V

P

P

H

N

T

D

T

A

S

D

V

W

E

S

E

R

I

L

K

P

A

V

R

E

N

D

P

F

R

D

A

A

V

I

V

V

L

V

S

S

G

P

G

G

P

P

A

-

S

-

V

-

Y

-

A

-

D

-

G

G

A

S

P

P

Q

D

L

R

D

E

P

R

-

D

-

F

-

G

-

I

-

S

-

R

A

A

L

I

F

T

D

D

L

S

D

G

V

L

P

P

V

V

F

L

G

G

I

V

C

C

Y

L

G

G

F

H

Q

Q

A

G

M

I

A

A

Q

Q

A

L

L

F

G

G

T

T

V

V

A

G

H

L

T

A

G

P

T

E

S

P

E

M

Y

H

G

G

R

R

-

V

T

S

E

E

L

V

K

R

V

H

A

T

G

G

G

E

Q

D

L

V

H

F

T

R

D

G

L

L

P

P

E

S

T

P

Q

F

P

T

V

A

W

V

M

R

S

Y

H

H

G

S

D

L

A

A

V

A

T

T

A

D

A

L

P

P

E

D

G

E

F

L

E

E

V

P

V

L

A

A

T

W

S

S

A

D

G

D

A

G

P

V

V

V

A

M

A

G

F

L

E

R

N

H

R

R

A

E

R

K

R

P

L

L

A

W

G

G

V

V

Q

Q

Y

F

H

H

P

P

E

E

V

S

M
x
I

H

G

S
|
S

P

D

H

F

G

G

Q

R

Q

E

V

I

L

M

S

A

R

N

F

F

binding magnesium ion: I175 (≠ M175), S177 (= S177)

Sites not aligning to the query:

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

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)
27% identity, 35% coverage: 8:188/522 of query aligns to 74:264/276 of Q42565

query
sites
Q42565

P

P

V

I

L

I

V

V

V

I

D

D

F

N

G

Y

A

D

Q

S

Y

F

A

T

Q

Y

L

N

I

L

A

C

R

Q

R

Y

V

M

R

G

E

E

A

L

R

G

V

C

F

H

S

F

E

E

V

V

I

Y

P

R

H

N

-

D

T

E

T

L

S

T

V

V

E

E

I

L

K

K

A

K

R

K

N

N

P

P

R

R

A

G

V

V

V

L

L

I

S

S

G

P

G

G

P

P

A

G

S

T

V

P

Y

Q

A

D

D

S

G

G

A

I

P

S

Q

L

L

Q

D

T

P

V

A

L

L

E

F

L

D

G

L

P

D

L

V

V

P

P

V

L

F

F

G
|
G

I

V

C

C

Y

M

G

G

F

L

Q

Q

A

C

M

I

A

G

Q

E

A

A

L

F

G

G

T

K

V

I

A

V

H

R

T

S

-

P

-

F

-

G

-

V

-

M

-

H

G
|
G

T

K

S

S

E

S

Y

M

G

V

R

H

T

Y

E

D

L

E

K

K

V

G

A

E

G

E

G

G

Q

-

L

L

H

F

T

S

D

G

L

L

P

S

E

N

T

P

Q

F

P

I

V

V

W

G

M

R

S

Y

H

H

G

S

D

L

A

V

V

I

-

E

-

K

-

D

T

T

A

F

A

P

P

S

E

D

G

E

F

L

E

E

V

V

V

T

A

A

-

W

T

T

S

E

A

D

G

G

A

L

P

V

V

M

A

A

F

R

E

H

N

R

R

K

A

Y

R

K

R

H

L

I

A

Q

G

G

V

V

Q

Q

Y

F

H

H

P

P

E

E

V

S

M

I

H

I

S

T

P

T

H

E

G

G

Q

K

Q

T

V

I

L

V

S

R

R

N

F

F

L

I

G150 (= G83) mutation to D: In trp4-1; no visible phenotype under normal growth conditions.
G176 (= G103) mutation to E: In wei7-2; insensitive to inhibition of root elongation by ethylene.

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)
28% identity, 30% coverage: 31:188/522 of query aligns to 30:187/193 of P00900

query
sites
P00900

V

I

F

Y

S

R

E

N

V

Q

I

I

P

G

H

A

T

E

T

V

S

I

V

I

E

E

E

R

I

L

K

Q

A

H

R

M

N

E

P

Q

R

P

A

V

V

L

V

M

L

L

S

S

G

P

G

G

P

P

A

G

S

T

V

P

Y

S

A

E

D

A

G

G

A

C

-

M

P

P

Q

E

L

L

D

L

P

Q

A

R

L

L

F

R

D

G

L

-

D

Q

V

L

P

P

V

I

F

I

G

G

I

I

C
|
C

Y

L

G

G

F

H

Q

Q

A

A

M

I

A

V

Q

E

A

A

L

Y

G

G

T

Q

V

V

A

G

H

Q

T

A

G

G

T

E

S

I

E

L

Y

H

G

G

R

K

T

A

E

S

L

A

K

I

V

A

A

H

G

D

G

G

Q

E

-

G

L

M

H

F

T

A

D

G

L

M

P

A

E

N

T

P

Q

L

P

P

V

V

W

A

M

R

S

Y

H

H

G

S

D

L

A

V

V

G

T

S

A

N

A

I

P

P

E

A

G

D

F

L

E

T

V

V

V

N

A

A

T

R

S

S

A

-

G

G

A

E

P

M

V

V

A

M

A

A

F

V

E

R

N

D

R

D

A

R

R

R

L

V

A

C

G

G

V

F

Q

Q

Y

F

H

H

P

P

E

E

V

S

M

I

H

L

S

T

P

T

H

H

G

G

Q

A

Q

R

V

L

L

L

S

E

R

Q

F

T

L

L

C84 (= C85) 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)
28% identity, 30% coverage: 31:188/522 of query aligns to 29:186/192 of 1i7qB

query
sites
1i7qB

V

I

F

Y

S

R

E

N

V

Q

I

I

P

G

H

A

T

E

T

V

S

I

V

I

E

E

E

R

I

L

K

Q

A

H

R

M

N

E

P

Q

R

P

A

V

V

L

V

M

L

L

S

S

G
x
P

G
|
G

P

P

A
x
G

S

T

V

P

Y

S

A

E

D

A

G

G

A

C

-

M

P

P

Q

E

L

L

D

L

P

Q

A

R

L

L

F

R

D

G

L

-

D

Q

V

L

P

P

V

I

F

I

G

G

I

I

C
|
C

Y
x
L

G

G

F

H

Q
|
Q

A

A

M

I

A

V

Q

E

A

A

L

Y

G

G

T

Q

V

V

A

G

H

Q

T

A

G

G

T

E

S

I

E

L

Y

H

G

G

R

K

T

A

E

S

L

A

K

I

V

A

A

H

G

D

G

G

Q

E

-

G

L

M

H

F

T

A

D

G

L

M

P

A

E

N

T

P

Q

L

P

P

V

V

W

A

M

R

S

Y

H
|
H

G
x
S

D
x
L

A

V

V

G

T

S

A

N

A

I

P

P

E

A

G

D

F

L

E

T

V

V

V

N

A

A

T

-

S

R

A

F

G

G

A

E

P

M

V

V

A

M

A

A

F

V

E

R

N

D

R

D

A

R

R

R

L

V

A

C

G

G

V

F

Q

Q

Y

F

H
|
H

P

P

E
|
E

V

S

M

I

H

L

S

T

P

T

H

H

G

G

Q

A

Q

R

V

L

L

L

S

E

R

Q

F

T

L

L

active site: G58 (≠ A60), C83 (= C85), L84 (≠ Y86), H169 (= H171), E171 (= E173)
binding glutamic acid: P55 (≠ G57), G56 (= G58), G58 (≠ A60), C83 (= C85), L84 (≠ Y86), Q87 (= Q89), H132 (= H133), S133 (≠ G134), L134 (≠ D135)

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)
31% identity, 33% coverage: 9:179/522 of query aligns to 244:410/430 of Q9LVW7

query
sites
Q9LVW7

V

V

L

I

V

A

V

Y

D

D

F

F

G

G

A

I

Q

K

Y

-

A

-

Q

Q

L

N

I

I

A

L

R

R

V

L

R

S

E

S

A

Y

R

G

V

C

F

Q

S

I

E

T

V

V

I

V

P

P

H

S

T

T

T

F

S

P

V

A

E

A

E

E

I

A

K

L

A

K

R

M

N

N

P

P

R

D

A

G

V

I

V

L

L

F

S

S

G

N

G

G

P

P

A

G

S

D

V

P

Y

S

A

A

D

-

G

-

A

V

P

P

Q

Y

L

A

D

V

P

E

A

T

L

V

F

K

D

E

L

L

-

L

-

G

D

K

V

V

P

P

V

V

F

Y

G

G

I

I

C

C

Y

M

G

G

F

H

Q

Q

A

L

M

L

A

G

Q

Q

A

A

L

L

G

G

T

-

V

-

A

-

H

K

T

T

G

F

T

K

S

M

E

K

Y

F

G

G

R

H

T

-

E

-

L

-

K

-

V

-

A

H

G

G

Q

N

L

H

H

P

T

V

D

R

L

N

P

N

E

R

T

T

Q

G

P

Q

V

V

W

E

M

I

S

S

-

A

-

Q

-

N

H

H

G

N

D

Y

A

A

V

V

T

D

A

P

A

A

-

S

-

L

P

P

E

G

G

G

F

V

E

E

V

V

V

T

A

H

T

V

S

N

A

L

G

N

-

D

A

G

P

S

V

C

A

A

A

G

F

L

E

S

N

F

R

P

A

E

R

M

R

N

L

V

A

M

G

S

V

L

Q

Q

Y

Y

H

H

P

P

E

E

V

A

M

S

H

P

S

G

P

P

H
|
H

H410 (= H179) mutation to Y: In ven6-1; reticulate leaf phenotype.

1ce8B Carbamoyl phosphate synthetase from escherichis coli with complexed with the allosteric ligand imp (see paper)
32% identity, 20% coverage: 2:108/522 of query aligns to 186:291/379 of 1ce8B

query
sites
1ce8B

E

E

S

D

A

E

T

L

P

P

R

F

P

H

V

V

L

V

V

A

V

Y

D

D

F

F

G

G

A

A

Q

K

Y

R

A

N

Q

I

L

L

I

R

A

M

R

L

R

V

V

D

R

R

E

G

A

C

R

R

V

L

F

-

S

-

E

T

V

I

I

V

P

P

H

A

T

Q

T

T

S

S

V

A

E

E

E

D

I

V

K

L

A

K

R

M

N

N

P

P

R

D

A

G

V

I

V

F

L

L

S

S

G

N

G

G

P

P

A

G

S

D

-

P

V

A

Y

P

A

C

D

D

G

Y

A

A

P

I

Q

T

L

A

D

I

P

Q

A

K

L

F

F

L

D

E

L

T

D

D

V

I

P

P

V

V

F

F

G

G

I

I

C
|
C

Y

L

G

G

F

H

Q

Q

A

L

M

L

A

A

Q

L

A

A

L

S

G

G

G

A

T

K

V

T

A

V

H

K

T

M

G

K

T

F

S

G

E

H

Y

H

G

G

active site: C268 (= C85)

Sites not aligning to the query:

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

P0A6F1 Carbamoyl phosphate synthase small chain; Carbamoyl phosphate synthetase glutamine chain; EC 6.3.5.5 from Escherichia coli (strain K12) (see paper)
32% identity, 20% coverage: 2:108/522 of query aligns to 187:292/382 of P0A6F1

query
sites
P0A6F1

E

E

S

D

A

E

T

L

P

P

R

F

P

H

V

V

L

V

V

A

V

Y

D

D

F

F

G

G

A

A

Q

K

Y

R

A

N

Q

I

L

L

I

R

A

M

R

L

R

V

V

D

R

R

E

G

A

C

R

R

V

L

F

-

S

-

E

T

V

I

I

V

P

P

H

A

T

Q

T

T

S

S

V

A

E

E

E

D

I

V

K

L

A

K

R

M

N

N

P

P

R

D

A

G

V

I

V

F

L

L

S

S

G

N

G
|
G

P

P

A
x
G

S

D

-

P

V

A

Y

P

A

C

D

D

G

Y

A

A

P

I

Q

T

L

A

D

I

P

Q

A

K

L

F

F

L

D

E

L

T

D

D

V

I

P

P

V

V

F

F

G

G

I

I

C

C

Y
x
L

G

G

F

H

Q
|
Q

A

L

M

L

A

A

Q

L

A

A

L

S

G

G

G

A

T

K

V

T

A

V

H

K

T

M

G

K

T

F

S

G

E

H

Y

H

G

G

G241 (= G58) binding L-glutamine
G243 (≠ A60) binding L-glutamine
L270 (≠ Y86) binding L-glutamine
Q273 (= Q89) binding L-glutamine

Sites not aligning to the query:

47 binding L-glutamine
311 binding L-glutamine
313 binding L-glutamine
314 binding L-glutamine

1c3oB Crystal structure of the carbamoyl phosphate synthetase: small subunit mutant c269s with bound glutamine (see paper)
31% identity, 20% coverage: 2:108/522 of query aligns to 186:291/379 of 1c3oB

query
sites
1c3oB

E

E

S

D

A

E

T

L

P

P

R

F

P

H

V

V

L

V

V

A

V

Y

D

D

F

F

G

G

A

A

Q
x
K

Y

R

A

N

Q

I

L

L

I

R

A

M

R

L

R

V

V

D

R

R

E

G

A

C

R

R

V

L

F

-

S

-

E

T

V

I

I

V

P

P

H

A

T

Q

T

T

S

S

V

A

E

E

E

D

I

V

K

L

A

K

R

M

N

N

P

P

R

D

A

G

V

I

V

F

L

L

S

S

G
x
N

G
|
G

P

P

A
x
G

S

D

-

P

V

A

Y

P

A

C

D

D

G

Y

A

A

P

I

Q

T

L

A

D

I

P

Q

A

K

L

F

F

L

D

E

L

T

D

D

V

I

P

P

V

V

F

F

G

G

I

I

C
x
S

Y
x
L

G

G

F

H

Q

Q

A

L

M

L

A

A

Q

L

A

A

L

S

G

G

G

A

T

K

V

T

A

V

H

K

T

M

G

K

T

F

S

G

E

H

Y

H

G

G

active site: K201 (≠ Q17), S268 (≠ C85)
binding glutamine: N239 (≠ G57), G240 (= G58), G242 (≠ A60), S268 (≠ C85), L269 (≠ Y86)

Sites not aligning to the query:

active site: 352, 354
binding glutamine: 46, 310, 311, 312, 313

Query Sequence

>WP_011778773.1 NCBI__GCF_000015305.1:WP_011778773.1
MESATPRPVLVVDFGAQYAQLIARRVREARVFSEVIPHTTSVEEIKARNPRAVVLSGGPA
SVYADGAPQLDPALFDLDVPVFGICYGFQAMAQALGGTVAHTGTSEYGRTELKVAGGQLH
TDLPETQPVWMSHGDAVTAAPEGFEVVATSAGAPVAAFENRARRLAGVQYHPEVMHSPHG
QQVLSRFLHEFAGIDATWTPANIAEALVEQVRTQIGDGRAICGLSGGVDSAVAAALVQRA
IGDRLTCVFVDHGLLRSGERAQVQRDFVAATGANLVTVDVADRFLEALSGVTNPEGKRKI
IGREFIRAFEGAVRDALESQDGSDVPVEFLVQGTLYPDVVESGGGSGTANIKSHHNVGGL
PDDLKFTLVEPLRLLFKDEVRAVGRELGLPEEIVARQPFPGPGLGIRIVGEVTAERLDTL
RRADAIAREELTSAGLDHQIWQCPVVLLADVRSVGVQGDGRTYGHPIVLRPVSSEDAMTA
DWTRVPYEVLERISTRITNEVREVNRVVLDVTSKPPGTIEWE

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