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)
45% identity, 100% coverage: 2:511/511 of query aligns to 6:555/555 of Q8IJR9

query
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Y18 (= Y14) 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 (= W127) mutation to F: Slight decrease in affinity for glutamine. Slight increase in glutaminase activity.
N169 (≠ S129) binding L-glutamine; mutation to S: Slight increase in affinity for glutamine. No defect in glutaminase activity.
D172 (= D132) binding L-glutamine; mutation to A: 172-fold decrease in affinity for glutamine. Severe loss of glutaminase activity.
H208 (= H168) binding L-glutamine
Y212 (≠ S172) mutation to W: 2.7-fold decrease in affinity for glutamine. No defect in glutaminase activity.
E213 (≠ H173) 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 (= R295) binding XMP
D371 (= D327) Important for ATPPase activity; mutation to A: Impaired formation of adenyl-XMP intermediate. Slight increase in glutaminase activity.
E374 (= E330) mutation to L: 8.9-fold decrease in affinity for ammonia. Severe loss of glutaminase activity.
K376 (≠ V332) 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 (= K342) mutation to L: Severe loss of ATP pyrophosphatase (ATPPase) activity. 80 percent decrease in glutaminase activity. Impaired GMP formation.
T387 (= T343) mutation to A: No effect on ATP pyrophosphatase (ATPPase) activity. 20 percent decrease in glutaminase activity. No effect on GMP formation.
H388 (= H344) 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 (= H345) Important for ATPPase activity; mutation to A: Loss of ATP pyrophosphatase (ATPPase) activity. 67 percent decrease in glutaminase activity. Impaired GMP formation.
N390 (= N346) mutation to A: No effect on ATP pyrophosphatase (ATPPase) activity. Increases glutaminase activity. Loss of GMP formation.
K411 (= K367) mutation to L: 70 percent decrease in glutaminase activity. Loss of GMP formation.
D412 (= D368) mutation to A: 30 percent decrease in glutaminase activity. 7.9-fold decrease in affinity for glutamine.
D413 (≠ E369) mutation to A: 35 percent decrease in glutaminase activity. 3.6-fold decrease in affinity for glutamine.
K415 (≠ R371) mutation to L: Increases glutaminase activity. 4.2-fold decrease in affinity for ATP.
Q476 (= Q432) binding XMP
R539 (= R495) mutation to L: 85 percent decrease in glutaminase activity.
K547 (= K503) binding XMP; mutation to L: 85 percent decrease in glutaminase activity.
I552 (= I508) binding XMP
E553 (= E509) binding XMP; mutation to L: 85 percent decrease in glutaminase activity.
E555 (= E511) mutation to L: 20 percent decrease in glutaminase activity. No effect on GMP formation.

4wioA Crystal structure of the c89a gmp synthetase inactive mutant from plasmodium falciparum in complex with glutamine (see paper)
43% identity, 99% coverage: 5:511/511 of query aligns to 3:525/525 of 4wioA

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active site: G52 (= G54), A83 (≠ C81), Y84 (= Y82), H197 (= H168), E199 (= E170), D255 (= D226), K393 (= K367)
binding glutamine: Q87 (= Q85), N158 (≠ S129), H159 (= H130), N160 (≠ A131), D161 (= D132), H197 (= H168)

3uowA Crystal structure of pf10_0123, a gmp synthetase from plasmodium falciparum
42% identity, 100% coverage: 2:511/511 of query aligns to 1:517/517 of 3uowA

query
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3uowA

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G

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G

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active site: G53 (= G54), C84 (= C81), Y85 (= Y82), H198 (= H168), E200 (= E170), D255 (= D226), K381 (= K367)
binding xanthosine-5'-monophosphate: R325 (= R295), P404 (= P390), G405 (= G391), P406 (= P392), Q446 (= Q432), K509 (= K503), T513 (= T507), I514 (= I508), E515 (= E509)

3uowB Crystal structure of pf10_0123, a gmp synthetase from plasmodium falciparum
43% identity, 99% coverage: 5:511/511 of query aligns to 2:477/477 of 3uowB

query
sites
3uowB

I

I

V

L

I

V

L

L

D

N

F

F

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G

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Q

Q

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Y

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G

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|
G

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|
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L

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K

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K

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G

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N

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D

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|
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A

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E

W

F

E

E

active site: G47 (= G54), C67 (= C81), Y68 (= Y82), H162 (= H168), E164 (= E170), D218 (= D226), K340 (= K367)
binding xanthosine-5'-monophosphate: R288 (= R295), P363 (= P390), G364 (= G391), P365 (= P392), Q405 (= Q432), K469 (= K503), T473 (= T507), I474 (= I508), E475 (= E509)

6jp9A Crsytal structure of a xmp complexed atppase subunit of m. Jannaschii gmp synthetase (see paper)
61% identity, 61% coverage: 199:511/511 of query aligns to 6:298/298 of 6jp9A

query
sites
6jp9A

N

K

F

F

L

I

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E

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A

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|
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|
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P

R

E

L

I

P

P

Y

F

D

D

L

L

D

K

T

R

I

I

M

S

R

K

R

R

I

I

I

T

N

S

E

E

V

I

K

P

G

N

V

V

N

A

R

R

V

V

Y

F

D

D

I

I

S

T

S

D

K
|
K

P

P

A

A

T
|
T

I
|
I

E
|
E

W

F

E

E

active site: D33 (= D226), K155 (= K367)
binding xanthosine-5'-monophosphate: R102 (= R295), P178 (= P390), G179 (= G391), P180 (= P392), Q220 (= Q432), K290 (= K503), T294 (= T507), I295 (= I508), E296 (= E509)

P49915 GMP synthase [glutamine-hydrolyzing]; GMP synthetase; Glutamine amidotransferase; EC 6.3.5.2 from Homo sapiens (Human) (see paper)
40% identity, 97% coverage: 4:498/511 of query aligns to 27:562/693 of P49915

query
sites
P49915

G

A

I

V

V

V

I

I

L

L

D

D

F

A

G

G

S

A

Q

Q

Y

Y

T

G

Q

K

L

V

I

I

A

D

R

R

I

V

R

R

E

E

L

L

H

F

I

V

Y

Q

S

S

E

E

I

I

L

F

P

P

Y

L

N

E

T

T

P

P

V

A

E

F

E

A

I

I

L

K

K

E

H

Q

N

G

P

F

K

R

G

A

I

I

F

I

S

S

G

G

P

P

A

N

S

S

V

V

Y

Y

E

A

K

E

D

D

A

A

P

P

K

W

P

F

D

D

E

P

R

A

V

I

Y

F

D

T

L

I

G

G

L

K

P

P

I

V

L

L

G

G

I

I

C
|
C

Y

Y

G

G

L

M

Q

Q

L

M

I

M

T

N

H

K

H

V

F

F

G

G

E

T

V

V

V

H

K

K

A

K

D

S

K

V

H

R

E

E

Y

D

G

G

R

V

A

F

E

N

I

I

Q

S

V

V

L

D

N

N

H

T

E

C

D

S

L

L

F

F

Y

R

E

G

I

L

P

Q

E

K

F

E

T

E

H

V

V

V

W

L

M

L

S

T

H

H

A

G

D

D

K

S

V

V

V

D

K

K

L

V

P

A

Q

D

G

G

F

F

E

K

V

V

L

V

A

A

R

R

S

S

F

G

N

N

A

I

P

-

Y

V

A

A

A

G

V

I

R

A

N

N

K

E

E

S

K

K

I

L

W

Y

G

G

V

A

Q

Q

F

F

H
|
H

P

P

E
|
E

V

V

S

G

H

L

T

T

L

E

L

N

G

G

K

K

E

V

I

I

L

L

K

K

N

N

F

F

A

L

V

Y

R

D

I

I

C

A

G

G

C

C

K

S

Q

G

D

T

W

F

T

T

M

V

G

Q

N

N

F

R

L

E

M

L

E

E

E

C

I

I

V

R

K

E

I

I

R

K

Q

E

T

R

V

V

G

G

N

T

K

S

K

K

A

V

I

L

C

V

A

L

L

L

S

S

G

G

V

V

D

D

S

S

S

T

V

V

A

C

A

T

V

A

L

L

V

L

H

N

N

R

A

A

I

L

G

N

-

Q

D

E

N

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

K

K

G

R

E

E

R

S

E

Q

Q

S

V

V

E

E

K

E

T

A

F

L

R

K

D

-

N

K

F

L

H

G

I

I

P

Q

L

V

I

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

R

R

E

K

R

R

F

I

L

S

N

K

A

T

L

L

K

N

G

M

I

T

T

T

D

S

P

P

E

E

Q

E

K

K

R
|
R

K

K

I

I

G

G

N

D

L

T

F

F

I

V

-

K

-

I

-

A

-

N

E

E

V

V

F

I

E

G

E

E

E

M

A

N

K

L

K

K

L

P

K

E

D

E

V

V

E

-

F

F

L

L

V

A

Q

Q

G

G

T

T

L

L

Y

R

P

P

D

D

V

L

I

I

E

E

S

S

V

A

S

S

V

L

-

V

-

A

K

S

G

G

P

K

S

A

A

E

V

L

I

I

K

K

T

T

H

H

N

N

V

D

G

T

G

E

L

L

P

I

E

R

R

K

M

L

N

R

L

E

-

E

-

G

K

K

L

V

I

I

E

E

P

P

L

L

R

K

E

D

L

F

F

H

K

K

D

D

E

E

V

V

R

R

E

I

L

L

G

G

K

R

E

E

L

L

G

G

L

L

P

P

D

E

E

E

I

L

I

V

Y

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

V

V

I

I

G

C

E

A

-

E

-

P

-

Y

-

I

-

C

-

K

-

D

-

F

-

P

V

E

T

T

Q

N

E

N

S

I

L

L

D

K

I

I

L

V

R

A

E

D

A

F

D

S

A

A

I

S

V

V

-

K

-

P

-

H

-

T

-

L

L

L

E

Q

E

R

I

V

K

K

K

A

A

C

G

T

L

T

Y

E

K

E

D

D

-

Q

-

E

-

K

-

L

-

M

-

Q

-

I

-

T

-

S

L

L

W

H

Q

S

S

L

F

N

A

A

V

F

L

L

P

P

I

I

H

K

T

T

V

V

G

G

V

V

M

Q

G

G

D
|
D

Y

C

R

R

T

S

Y

Y

E

S

K

Y

V

V

I

C

A

G

V

I

R

S

A

S

V

K

E

D

S

E

S

-

D

-

G

-

M

-

T

-

A

P

D

D

W

W

A

E

R

S

L

L

P

I

Y

F

D

-

L

-

D

-

T

-

I

L

M

A

R

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

C104 (= C81) active site, For GATase activity
H190 (= H168) active site, For GATase activity
E192 (= E170) active site, For GATase activity
R337 (= R295) binding XMP
D522 (= D448) 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)
41% identity, 97% coverage: 4:498/511 of query aligns to 5:527/658 of 2vxoB

query
sites
2vxoB

G

A

I

V

V

V

I

I

L

L

D

D

F

A

G

G

S

A

Q

Q

Y

Y

T

G

Q

K

L

V

I

I

A

D

R

R

I

V

R

R

E

E

L

L

H

F

I

V

Y

Q

S

S

E

E

I

I

L

F

P

P

Y

L

N

E

T

T

P

P

V

A

E

F

E

A

I

I

L

K

K

E

H

Q

N

G

P

F

K

R

G

A

I

I

F

I

S

S

G

G

G
|
G

P

P

A

N

S

S

V

V

Y

Y

E

A

K

E

D

D

A

A

P

P

K

W

P

F

D

D

E

P

R

A

V

I

Y

F

D

T

L

I

G

G

L

K

P

P

I

V

L

L

G

G

I

I

C
|
C

Y
|
Y

G

G

L

M

Q

Q

L

M

I

M

T

N

H

K

H

V

F

F

G

G

E

T

V

V

V

-

K

-

A

-

D

H

K

K

H

K

E

S

Y

D

G

G

R

V

A

F

E

N

I

I

Q

S

V

V

L

D

N

N

H

T

E

C

D

S

L

L

F

F

Y

R

E

G

I

L

P

Q

E

K

F

E

T

E

H

V

V

V

W

L

M

L

S

T

H

H

A

G

D

D

K

S

V

V

V

D

K

K

L

V

P

A

Q

D

G

G

F

F

E

K

V

V

L

V

A

A

R

R

S

S

F

G

N

N

A

I

P

-

Y

V

A

A

A

G

V

I

R

A

N

N

K

E

E

S

K

K

I

L

W

Y

G

G

V

A

Q

Q

F

F

H
|
H

P

P

E
|
E

V

V

S

G

H

L

T

T

L

E

L

N

G

G

K

K

E

V

I

I

L

L

K

K

N

N

F

F

A

L

V

Y

R

D

I

I

C

A

G

G

C

C

K

S

Q

G

D

T

W

F

T

T

M

V

G

Q

N

N

F

R

L

E

M

L

E

E

E

C

I

I

V

R

K

E

I

I

R

K

Q

E

T

R

V

V

G

G

N

T

K

S

K

K

A

V

I

L

C

V

A

L

L

L

S

S

G

G

V

V

D
|
D

S

S

S

T

V

V

A

C

A

T

V

A

L

L

V

L

H

N

N

R

A

A

I

L

G

N

-

Q

D

E

N

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

K

K

G

R

E

E

R

S

E

Q

Q

S

V

V

E

E

K

E

T

A

F

L

R

K

D

-

N

K

F

L

H

G

I

I

P

Q

L

V

I

K

V

V

V

I

D

N

A

A

R

A

E

H

R

S

F

F

L

Y

N

N

A

G

-

T

-

L

-

P

-

R

-

I

-

S

-

K

-

T

L

L

K

N

G

M

I

T

T

T

D

S

P

P

E

E

Q

E

K

K

R
|
R

K

K

I

I

G

G

N

D

L

T

F

F

I

V

-

K

-

I

-

A

-

N

E

E

V

V

F

I

E

G

E

E

E

M

A

N

K

L

K

K

L

P

K

E

D

E

V

V

E

-

F

F

L

L

V

A

Q

Q

G

G

T

T

L

L

Y

R

P

P

D

D

V

L

I

I

E

E

S

S

V

A

S

S

V

L

-

V

-

A

K

S

G
|
G

P
x
K

S

A

A

E

V

L

I

I

K

K

T

T

H

H

N

N

V

D

G

T

G

E

L

L

P

I

E

R

R

K

M

L

N

R

L

E

-

E

-

G

K

K

L

V

I

I

E

E

P

P

L

L

R

K

E

D

L

F

F

H

K
|
K

D

D

E

E

V

V

R

R

E

I

L

L

G

G

K

R

E

E

L

L

G

G

L

L

P

P

D

E

E

E

I

L

I

V

Y

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

V

V

I

I

G

C

E

A

-

E

-

P

-

Y

-

I

-

C

-

K

-

D

-

F

-

P

V

E

T

T

Q

N

E

N

S

I

L

L

D

K

I

I

L

V

R

A

E

D

A

F

D

S

A

A

I

S

V

V

-

K

-

P

-

H

-

T

-

L

L

L

E

Q

E

R

I

V

K

K

K

A

A

C

G

T

L

T

Y

E

K

E

D

D

-

Q

-

E

-

K

-

L

-

M

-

Q

-

I

-

T

-

S

L

L

W

H

Q

S

S

L

F

N

A

A

V

F

L

L

P

P

I

I

H

K

T

T

V

V

G

G

V

V

M

Q

G

G

D

D

Y

C

R
|
R

T

S

Y

Y

E

S

K

Y

V

V

I

C

A

G

V

I

R

S

A

S

V

K

E

D

S

E

S

-

D

-

G

-

M

-

T

-

A

P

D

D

W

W

A

E

R

S

L

L

P

I

Y

F

D

-

L

-

D

-

T

-

I

L

M

A

R

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

active site: G55 (= G54), C82 (= C81), Y83 (= Y82), H165 (= H168), E167 (= E170), D223 (= D226), K381 (= K367)
binding xanthosine-5'-monophosphate: R302 (= R295), G348 (= G336), K349 (≠ P337), P404 (= P390), G405 (= G391), P406 (= P392), R489 (= R450)

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
44% identity, 37% coverage: 5:192/511 of query aligns to 2:181/183 of 7yc6A

query
sites
7yc6A

I

I

V

V

I

I

L

L

D

D

F

N

G

G

S

G

Q

Q

Y

Y

T

V

Q

H

L

R

I

I

A

H

R

R

R

S

I

L

R

K

E

Y

L

I

H

G

I

V

Y

S

S

S

E

K

I

I

L

V

P

P

Y

N

N

T

T

T

P

P

V

L

E

E

I

I

L

E

K

S

H

N

N

K

P

E

-

V

K

K

G

G

I

I

F

L

S

S

G

G

P

P

A

D

S

I

V

E

Y

K

E

A

K

K

D

N

A

C

P

-

K

-

P

-

D

I

E

D

R

I

V

A

Y

L

D

N

L

A

G

K

L

L

P

P

I

I

L

L

G

G

I

I

C
|
C

Y

L

G

G

L

H

Q

Q

L

L

I

I

T

A

H

L

H

A

F

Y

G

G

E

E

V

V

V

G

K

R

A

A

D

-

K

-

H

-

E

-

Y

-

G

A

R

L

A

T

E

K

I

V

Q

Y

V

V

L
x
D

N

K

H

E

E

N

D

P

L

L

F

F

Y

K

E

N

I

V

P

P

E

R

F

E

T

F

H

N

V

A

W

W

M

A

S

S

H

H

A

K

D

D

K
x
E

V

V

V

K

K

K

L

V

P

P

Q

E

G

G

F

F

E

E

V

I

L

L

A

A

R
x
H

S

S

F

D

N

I

A
x
C

P

Q

Y

V

A

E

A

A

V

M

R

K

N

H

K

K

E

T

K

K

K

P

I

I

W

Y

G

G

V

V

Q

Q

F

F

H
|
H

P

P

E

E

V

V

S

A

H

H

T

T

L

E

L

Y

G

G

K

N

E

E

I

I

L

L

K

K

N

N

F

F

A

C

V

-

R

K

I

V

C

C

G

G

C

Y

K

K

binding zinc ion: C76 (= C81), D101 (≠ L111), E123 (≠ K133), E123 (≠ K133), H136 (≠ R146), C140 (≠ A150), C140 (≠ A150), H158 (= H168)

8hx8A Crystal structure of 4-amino-4-deoxychorismate synthase from streptomyces venezuelae co-crystallized with chorismate (see paper)
36% identity, 29% coverage: 37:184/511 of query aligns to 44:187/673 of 8hx8A

query
sites
8hx8A

P

P

V

V

E

E

E

D

I

F

L

-

K

-

H

-

N

-

P

-

K

D

G

A

I

I

I

V

F

V

S

S

G

P

G

G

P

P

A

G

S

S

V

P

-

D

Y

R

E

E

K

R

D

D

A

F

P

G

K

I

P

S

D

R

E

R

R

A

V

I

Y

T

D

D

L

S

G

G

L

L

P

P

I

V

L

L

G

G

I

V

C

C

Y

L

G

G

L

H

Q

Q

L

G

I

I

T

A

H

Q

H

L

F

F

G

G

E

T

V

V

V

G

K

L

A

A

D

P

K

E

H

P

E

M

Y

H

G

G

R

R

A

V

E

S

I

E

Q

V

V

R

L

H

N

T

H

G

E

E

D

D

L

V

F

F

Y

R

E

G

I

L

P

P

E

S

F

P

T

F

H

T

V

A

W

V

M

R

S

Y

H

H

A

S

D

L

K

A

V

A

V

T

K

D

L

L

P

P

Q

D

G

E

F

L

E

E

V

P

L

L

A

A

R

W

S

S

F

D

N

D

A

G

P

V

Y

V

A

M

A

G

V

L

R

R

N

H

K

R

E

E

K

K

K

P

I

L

W

W

G

G

V

V

Q

Q

F

F

H

H

P

P

E

E

V

S

S
x
I

H

G

T
x
S

L

D

L

F

G

G

K

R

E

E

I

I

L

M

K

A

N

N

F

F

binding magnesium ion: I175 (≠ S172), S177 (≠ T174)

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)
31% identity, 36% coverage: 2:184/511 of query aligns to 72:263/276 of Q42565

query
sites
Q42565

H

H

Q

G

G

P

I

I

V

I

I

V

L

I

D

D

F

N

G

Y

S

D

Q

S

Y

F

T

T

Q

Y

L

N

I

L

A

C

R

Q

R

Y

I

M

R

G

E

E

L

L

H

G

I

C

Y

H

S

F

E

E

I

V

L

Y

P

R

Y

N

N

D

T

E

-

L

P

T

V

V

E

E

I

L

L

K

K

K

H

K

N

N

P

P

K

R

G

G

I

V

I

L

F

I

S

S

G

P

G

G

P

P

A

G

S

T

V

-

Y

-

E

P

K

Q

D

D

A

S

P

G

K

I

P

S

D

L

E

Q

R

T

V

V

Y

L

D

E

L

L

G

G

-

P

-

L

L

V

P

P

I

L

L

F

G
|
G

I

V

C

C

Y

M

G

G

L

L

Q

Q

L

C

I

I

T

G

H

E

H

A

F

F

G

G

E

K

V

I

V

V

K

R

A

S

D

P

-

F

K

G

H

V

E

M

Y

H

G
|
G

R

K

A

S

E

S

I

M

Q

V

V

H

L

Y

N

D

H

E

-

K

-

G

-

E

E

E

D

G

L

L

F

F

Y

S

E

G

I

L

P

S

E

N

F

P

T

F

H

I

V

V

W

G

M

R

S

Y

H

H

A

S

D

L

K

V

V

I

V

E

K

K

-

D

-

T

L

F

P

P

Q

S

G

D

-

E

F

L

E

E

V

V

L

T

A

A

R

W

S

T

F

E

N

D

A

G

P

L

Y

V

A

M

A

A

V

A

R

R

N

H

K

R

E

K

-

Y

K

K

K

H

I

I

W

Q

G

G

V

V

Q

Q

F

F

H

H

P

P

E

E

V

S

S

I

H

I

T

T

L

T

L

E

G

G

K

K

E

T

I

I

L

V

K

R

N

N

F

F

G150 (= G79) mutation to D: In trp4-1; no visible phenotype under normal growth conditions.
G176 (= G104) mutation to E: In wei7-2; insensitive to inhibition of root elongation by ethylene.

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)
34% identity, 28% coverage: 46:187/511 of query aligns to 44:187/187 of P00903

query
sites
P00903

P

P

K

Q

G

K

I

I

I

V

F

I

S

S

G

P

G

G

P

P

A

C

S

T

V

P

Y

D

E

E

K

A

D

G

A

I

P

S

K

L

P

D

D

V

E

I

R

R

V

H

Y

Y

D

A

L

G

G

R

L

L

P

P

I

I

L

L

G

G

I

V

C
|
C

Y

L

G

G

L

H

Q

Q

L

A

I

M

T

A

H

Q

H

A

F

F

G

G

E

K

V

V

K

R

A

A

D

A

K

K

H

V

E

M

Y

H

G

G

R

K

A

T

E

S

I

P

Q

I

V

T

L

H

N

N

H

G

E

E

D

G

L

V

F

F

Y

R

E

G

I

L

P

A

E

N

F

P

T

L

H

T

V

V

W

T

M

R

S

Y

H

H

A

S

D

L

K

V

V

V

V

E

-

P

-

D

K

S

L

L

P

P

Q

A

G

C

F

F

E

D

V

V

L

T

A

A

R

W

S

S

F

E

N

T

A

R

P

E

Y

I

A

M

A

G

V

I

R

R

N

H

K

R

E

Q

K

W

K

D

I

L

W

E

G

G

V

V

Q

Q

F

F

H
|
H

P

P

E
|
E

V

S

S

I

H

L

T

S

L

E

L

Q

G

G

K

H

E

Q

I

L

L

L

K

A

N

N

F

F

A

L

V

H

R

R

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

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)
32% identity, 33% coverage: 5:172/511 of query aligns to 244:406/430 of Q9LVW7

query
sites
Q9LVW7

I

V

V

I

I

A

L

Y

D

D

F

F

G

G

S

I

Q

K

Y

-

T

-

Q

Q

L

N

I

I

A

L

R

R

I

L

R

S

E

S

L

Y

H

G

I

C

Y

Q

S

I

E

T

I

V

L

V

P

P

Y

S

N

T

T

F

P

P

V

A

E

A

E

E

I

A

L

L

K

K

H

M

N

N

P

P

K

D

G

G

I

I

I

L

F

F

S

S

G

N

G

G

P

P

A

G

S

D

V

-

Y

-

E

P

K

S

D

A

A

V

P

P

K

Y

P

A

D

V

E

E

R

T

V

V

Y

K

D

E

L

L

-

L

-

G

G

K

L

V

P

P

I

V

L

Y

G

G

I

I

C

C

Y

M

G

G

L

H

Q

Q

L

L

I

L

T

G

H

Q

H

A

F

L

G

G

E

K

V

T

V

F

K

K

A

M

D

K

K

F

H

G

E

H

Y

H

G

G

R

-

A

G

E

N

I

H

Q

P

V

V

L

R

N

N

H

N

E

R

D

T

L

G

F

Q

Y

V

E

E

I

I

P

S

E

A

F

Q

T

N

H

H

V

-

W

-

M

-

S

N

H

Y

A

A

D

V

K

D

V

P

V

A

K

S

L

L

P

P

Q

G

G

G

F

V

E

E

V

V

L

T

A

H

R

V

S

N

F

L

N

N

-

D

A

G

P

S

Y

C

A

A

A

G

V

L

R

S

N

F

K

P

E

E

K

M

K

N

I

V

W

M

G

S

V

L

Q

Q

F

Y

H

H

P

P

E

E

V

A

S

S

Sites not aligning to the query:

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

1i7qB Anthranilate synthase from s. Marcescens (see paper)
27% identity, 35% coverage: 5:183/511 of query aligns to 3:184/192 of 1i7qB

query
sites
1i7qB

I

I

V

L

I

L

L

L

D

D

F

N

G

V

S

D

Q

S

Y

F

T

T

Q

Y

L

N

I

L

A

V

R

D

R

Q

I

L

R

R

-

A

-

S

-

G

-

H

E

Q

L

V

H

V

I

I

Y

Y

S

R

E

N

I

Q

L

I

P

G

Y

A

N

E

T

V

P

I

V

I

E

E

E

R

I

L

L

Q

K

H

H

M

N

E

P

Q

K

P

G

V

I

L

I

M

F

L

S

S

G
x
P

G
|
G

P

P

A
x
G

S

T

V

P

Y

S

E

E

K

A

D

G

A

C

-

M

P

P

K

E

P

L

D

L

E

Q

R

R

V

L

Y

R

D

G

L

Q

G

-

L

L

P

P

I

I

L

I

G

G

I

I

C
|
C

Y
x
L

G

G

L

H

Q
|
Q

L

A

I

I

T

V

H

E

H

A

F

Y

G

G

E

Q

V

V

V

G

K

Q

A

A

D

G

K

E

H

I

E

L

Y

H

G

G

R

K

A

A

E

S

I

A

Q

I

V

A

L

H

N

D

H

G

E

E

D

G

L

M

F

F

Y

A

E

G

I

M

P

A

E

N

F

P

T

L

H

P

V

V

W

A

M

R

S

Y

H
|
H

A
x
S

D
x
L

K

V

V

G

V

S

K

N

L

I

P

P

Q

A

G

D

F

L

E

T

V

V

L

N

A

A

R

R

S

-

F

F

N

G

A

E

P

M

Y

V

A

M

A

A

V

V

R

R

N

D

K

D

E

R

K

R

I

V

W

C

G

G

V

F

Q

Q

F

F

H
|
H

P

P

E
|
E

V

S

S

I

H

L

T

T

L

T

L

H

G

G

K

A

E

R

I

L

L

L

K

E

N

Q

active site: G58 (≠ A56), C83 (= C81), L84 (≠ Y82), H169 (= H168), E171 (= E170)
binding glutamic acid: P55 (≠ G53), G56 (= G54), G58 (≠ A56), C83 (= C81), L84 (≠ Y82), Q87 (= Q85), H132 (= H130), S133 (≠ A131), L134 (≠ D132)

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)
27% identity, 35% coverage: 5:183/511 of query aligns to 4:185/193 of P00900

query
sites
P00900

I

I

V

L

I

L

L

L

D

D

F

N

G

V

S

D

Q

S

Y

F

T

T

Q

Y

L

N

I

L

A

V

R

D

R

Q

I

L

R

R

-

A

-

S

-

G

-

H

E

Q

L

V

H

V

I

I

Y

Y

S

R

E

N

I

Q

L

I

P

G

Y

A

N

E

T

V

P

I

V

I

E

E

E

R

I

L

L

Q

K

H

H

M

N

E

P

Q

K

P

G

V

I

L

I

M

F

L

S

S

G

P

G

G

P

P

A

G

S

T

V

P

Y

S

E

E

K

A

D

G

A

C

-

M

P

P

K

E

P

L

D

L

E

Q

R

R

V

L

Y

R

D

G

L

Q

G

-

L

L

P

P

I

I

L

I

G

G

I

I

C
|
C

Y

L

G

G

L

H

Q

Q

L

A

I

I

T

V

H

E

H

A

F

Y

G

G

E

Q

V

V

V

G

K

Q

A

A

D

G

K

E

H

I

E

L

Y

H

G

G

R

K

A

A

E

S

I

A

Q

I

V

A

L

H

N

D

H

G

E

E

D

G

L

M

F

F

Y

A

E

G

I

M

P

A

E

N

F

P

T

L

H

P

V

V

W

A

M

R

S

Y

H

H

A

S

D

L

K

V

V

G

V

S

K

N

L

I

P

P

Q

A

G

D

F

L

E

T

V

V

L

N

A

A

R

R

S

S

F

G

N

E

A

M

P

-

Y

V

A

M

A

A

V

V

R

R

N

D

K

D

E

R

K

R

I

V

W

C

G

G

V

F

Q

Q

F

F

H

H

P

P

E

E

V

S

S

I

H

L

T

T

L

T

L

H

G

G

K

A

E

R

I

L

L

L

K

E

N

Q

C84 (= C81) active site, Nucleophile; for GATase activity

Sites not aligning to the query:

1 modified: Initiator methionine, Removed

P0A6F1 Carbamoyl phosphate synthase small chain; Carbamoyl phosphate synthetase glutamine chain; EC 6.3.5.5 from Escherichia coli (strain K12) (see paper)
28% identity, 33% coverage: 5:172/511 of query aligns to 194:357/382 of P0A6F1

query
sites
P0A6F1

I

V

V

V

I

A

L

Y

D

D

F

F

G

G

S

A

Q

K

Y

R

T

N

Q

-

L

-

I

I

A

L

R

R

R

M

I

L

R

V

E

D

L

R

H

G

I

C

Y

R

S

L

E

T

I

I

L

V

P

P

Y

A

N

Q

T

T

P

S

V

A

E

E

E

D

I

V

L

L

K

K

H

M

N

N

P

P

K

D

G

G

I

I

I

F

F

L

S

S

G

N

G
|
G

P

P

A
x
G

S

D

V

P

Y

A

E

P

K

C

D

D

-

Y

A

A

P

I

K

T

P

A

D

I

E

Q

R

K

V

F

Y

L

D

E

L

T

G

D

L

I

P

P

I

V

L

F

G

G

I

I

C

C

Y
x
L

G

G

L

H

Q
|
Q

L

L

I

L

T

A

H

L

H

A

F

S

G

G

G

A

E

K

V

T

V

V

K

K

A

M

D

K

K

F

H

G

E

H

Y

H

G

G

R

G

A

-

E

-

I

-

Q

-

V

-

L

-

N

N

H

H

-

P

-

V

E

K

D

D

L

V

F

E

Y

K

E

N

I

V

P

V

E

M

F

I

T

T

H

A

V

Q

W
x
N

M

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S
x
G

H
x
F

A

A

D

V

K

D

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V

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L

P

P

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A

G

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S

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G241 (= G54) binding L-glutamine
G243 (≠ A56) binding L-glutamine
L270 (≠ Y82) binding L-glutamine
Q273 (= Q85) binding L-glutamine
N311 (≠ W127) binding L-glutamine
G313 (≠ S129) binding L-glutamine
F314 (≠ H130) binding L-glutamine

Sites not aligning to the query:

47 binding L-glutamine

1ce8B Carbamoyl phosphate synthetase from escherichis coli with complexed with the allosteric ligand imp (see paper)
28% identity, 33% coverage: 5:172/511 of query aligns to 193:356/379 of 1ce8B

query
sites
1ce8B

I

V

V

V

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Y

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-

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A

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C
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C

Y

L

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G

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Q

L

L

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A

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L

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A

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V

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Y

H

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G

A

-

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-

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-

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-

N

N

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H

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P

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K

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A

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V

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L

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P

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A

G

N

F

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V

V

L

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A

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S

-

L

F

F

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active site: C268 (= C81), H352 (= H168), E354 (= E170)

Sites not aligning to the query:

binding L-ornithine: 119, 122

1c3oB Crystal structure of the carbamoyl phosphate synthetase: small subunit mutant c269s with bound glutamine (see paper)
27% identity, 33% coverage: 5:172/511 of query aligns to 193:356/379 of 1c3oB

query
sites
1c3oB

I

V

V

V

I

A

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Y

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D

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F

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x
K

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-

L

-

I

I

A

L

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E

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N

G
|
G

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x
G

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A

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D

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Y

A

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D

E

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P

I

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x
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x
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L

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G

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H

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-

I

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-

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N

N

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H

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-

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D

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x
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A

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D

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L

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P

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A

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active site: K201 (≠ Q13), S268 (≠ C81), H352 (= H168), E354 (= E170)
binding glutamine: N239 (≠ G53), G240 (= G54), G242 (≠ A56), S268 (≠ C81), L269 (≠ Y82), N310 (≠ W127), H311 (≠ M128), G312 (≠ S129), F313 (≠ H130)

Sites not aligning to the query:

binding glutamine: 46

Query Sequence

>WP_012673904.1 NCBI__GCF_000021545.1:WP_012673904.1
MHQGIVILDFGSQYTQLIARRIRELHIYSEILPYNTPVEEILKHNPKGIIFSGGPASVYE
KDAPKPDERVYDLGLPILGICYGLQLITHHFGGEVVKADKHEYGRAEIQVLNHEDLFYEI
PEFTHVWMSHADKVVKLPQGFEVLARSFNAPYAAVRNKEKKIWGVQFHPEVSHTLLGKEI
LKNFAVRICGCKQDWTMGNFLMEEIVKIRQTVGNKKAICALSGGVDSSVAAVLVHNAIGD
NLTCIFVDNGLLRKGEREQVEKTFRDNFHIPLIVVDARERFLNALKGITDPEQKRKIIGN
LFIEVFEEEAKKLKDVEFLVQGTLYPDVIESVSVKGPSAVIKTHHNVGGLPERMNLKLIE
PLRELFKDEVRELGKELGLPDEIIYRQPFPGPGLAIRVIGEVTQESLDILREADAIVLEE
IKKAGLYKDLWQSFAVLLPIHTVGVMGDYRTYEKVIAVRAVESSDGMTADWARLPYDLLD
TIMRRIINEVKGVNRVVYDISSKPPATIEWE

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