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, 99% coverage: 7:521/521 of query aligns to 7:555/555 of Q8IJR9

query
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Q8IJR9

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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
C113 (≠ H109) 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 (= W136) mutation to F: Slight decrease in affinity for glutamine. Slight increase in glutaminase activity.
N169 (≠ S138) binding ; mutation to S: Slight increase in affinity for glutamine. No defect in glutaminase activity.
D172 (= D141) binding ; mutation to A: 172-fold decrease in affinity for glutamine. Severe loss of glutaminase activity.
H208 (= H177) binding
Y212 (≠ T181) mutation to W: 2.7-fold decrease in affinity for glutamine. No defect in glutaminase activity.
E213 (≠ H182) 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 (= R304) binding
D371 (= D336) Important for ATPPase activity; mutation to A: Impaired formation of adenyl-XMP intermediate. Slight increase in glutaminase activity.
E374 (= E339) mutation to L: 8.9-fold decrease in affinity for ammonia. Severe loss of glutaminase activity.
K376 (≠ A341) 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
R539 (= R505) mutation to L: 85 percent decrease in glutaminase activity.
K547 (= K513) binding ; mutation to L: 85 percent decrease in glutaminase activity.
I552 (= I518) binding
E553 (= E519) binding ; mutation to L: 85 percent decrease in glutaminase activity.
E555 (= E521) mutation to L: 20 percent decrease in glutaminase activity. No effect on GMP formation.

2ywcA Crystal structure of gmp synthetase from thermus thermophilus in complex with xmp
47% identity, 98% coverage: 9:521/521 of query aligns to 2:475/475 of 2ywcA

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2ywcA

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active site: G51 (= G58), R53 (≠ E60), C78 (= C85), Y79 (= Y86), H164 (= H177), E166 (= E179), D221 (= D235), K343 (= K377)
binding xanthosine-5'-monophosphate: R288 (= R304), P366 (= P400), G367 (= G401), P368 (= P402), Q408 (= Q442), K467 (= K513), T471 (= T517), I472 (= I518), E473 (= E519)

4wioA Crystal structure of the c89a gmp synthetase inactive mutant from plasmodium falciparum in complex with glutamine (see paper)
38% identity, 99% coverage: 7:521/521 of query aligns to 1:525/525 of 4wioA

query
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4wioA

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G

I

V

I

I

L

L

S

S

G

G

G
|
G

P

P

E

Y

S

S

T

V

T

T

L

E

P

A

G

G

A

S

P

P

A

H

A

L

P

K

Q

K

E

E

V

V

F

F

D

E

-

Y

-

F

-

L

-

E

S

K

G

K

L

I

P

P

V

I

F

F

G

G

I

I

C
x
A

Y
|
Y

G

G

M

M

Q
|
Q

T

E

L

I

A

A

A

V

Q

Q

L

M

G

N

G

G

E

E

T

V

E

K

A

K

A

S

D

K

Q

T

R

S

E

E

F

Y

G

G

H

C

A

T

E

D

V

V

N

N

I

I

V

L

A

R

P

N

D

D

A

N

L

I

-

N

-

I

-

T

-

Y

-

C

-

R

-

N

F

F

S

S

G

S

L

A

S

M

D

D

H

L

P

Y

G

S

E

N

A

Y

K

K

L

L

-

M

-

N

-

E

-

C

-

L

-

F

-

E

-

N

-

I

-

K

-

S

-

D

-

I

-

T

N

T

V

V

W

W

M

M

S
x
N

H
|
H

G
x
N

D
|
D

H

E

V

V

S

T

K

K

A

I

P

P

P

E

G

N

F

F

T

Y

I

L

T

V

A

S

T

S

D

E

R

N

I

C

P

L

V

I

A

C

A

S

M

I

A

Y

N

N

E

K

D

E

K

Y

R

N

W

I

Y

Y

G

G

V

V

Q

Q

F

Y

H
|
H

P

P

E
|
E

V

V

T

Y

H

E

T

S

L

L

Q

D

G

G

Q

E

A

L

L

M

L

F

R

Y

R

N

F

F

V

A

V

Y

D

N

V

I

C

C

G

K

C

C

E

K

T

K

L

Q

W

F

T

D

A

P

A

I

N

R

I

Y

I

H

E

E

D

L

Q

E

I

L

A

K

R

N

V

I

R

E

E

K

Q

Y

V

K

G

H

D

D

D

H

D

Y

V

V

I

I

L

A

G

A

L

M

S

S

G

G

V

I

D
|
D

S

S

S

T

V

V

V

A

A

A

L

Y

L

T

H

H

K

K

A

I

I

F

G

K

D

E

K

R

L

F

T

F

C

G

V

I

F

F

V

I

D

D

T

N

G

G

L

L

R

R

W

K

Q

N

E

E

G

A

D

E

Q

N

V

V

M

Y

A

T

M

F

F

L

A

K

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S

H

T

M

F

-

P

G

D

V

M

K

N

V

I

I

T

R

K

V

I

N

D

A

A

A

S

D

E

R

N

Y

F

F

L

A

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K

N

L

L

E

Q

G

G

V

V

S

T

D

D

P

P

E

E

A

Q

K

K

R

R

K

K

I

I

G

G

N

K

L

L

F

F

V

I

D

E

I

E

F

F

D

E

E

K

E

A

S

V

N

N

K

N

L

I

S

D

-

I

-

D

-

I

N

N

A

K

K

T

W

F

L

L

A

L

Q

Q

G

G

T

T

I

L

Y

Y

P

P

D

D

V

I

I

I

E

E

S

S

A

K

G

C

S

S

K

K

T

-

G

N

K

L

A

S

H

D

V

T

I

I

K

K

S

T

H

H

N

N

V

-

G

-

L

-

P

-

E

-

H

-

M

L

K

K

L

F

G

K

L

L

V

F

E

E

P

P

L

F

R

K

E

Y

L

L

F

F

K
|
K

D

D

E

D

V

V

R

K

R

T

L

L

G

S

V

R

E

E

L

L

G

N

L

L

P

P

R

E

S

E

M

I

V

T

Y

N

R

R

H

H

P

P

F

F

P

P

G

G

P

P

G

G

L

L

G

A

V

I

R

R

I

V

L

I

G

G

E

E

V

I

K

N

R

K

E

H

Y

K

A

L

E

N

L

I

L

L

A

R

K

E

A

V

D

D

A

D

I

I

F

F

I

I

E

N

E

D

L

L

R

K

K

Q

A

Y

D

G

L

L

Y

Y

D

N

K

Q

T

I

S

S

Q

Q

A

A

F

F

A

A

V

V

F

L

L

L

P

-

V

-

K

-

S

-

V

-

G

-

V

-

G

-

D

-

A

-

R

-

A

S

Y

Y

E

D

W

Y

V

V

I

C

A

V

L

L

R

R

A

A

V

V

E

K

T

T

I

S

D

S

F

F

M

M

T

T

A

A

H

N

W

W

A

Y

H

Q

L

I

P

P

Y

Y

E

D

F

I

L

L

G

D

T

K

V

I

S

T

N

T

R

R

I

I

I

L

N

S

E

E

L

V

R

K

G

G

V

V

S

N

R

R

V

I

V

L

Y

Y

D

D

I

V

S

S

G

S

K

K

P

P

A

A

T

T

I

I

E

E

W

F

E

E

active site: G52 (= G58), A83 (≠ C85), Y84 (= Y86), H197 (= H177), E199 (= E179), D255 (= D235), K393 (= K377)
binding glutamine: Q87 (= Q89), N158 (≠ S138), H159 (= H139), N160 (≠ G140), D161 (= D141), H197 (= H177)

3uowA Crystal structure of pf10_0123, a gmp synthetase from plasmodium falciparum
37% identity, 99% coverage: 7:521/521 of query aligns to 2:517/517 of 3uowA

query
sites
3uowA

D

D

K

K

I

I

L

L

I

V

L

L

D

N

F

F

G

G

A

S

Q

Q

Y

Y

T

F

Q

H

L

L

I

I

A

V

R

K

R

R

I

L

R

N

E

N

L

I

G

K

V

I

Y

F

C

S

E

E

I

T

W

K

A

D

W

Y

D

G

H

V

N

E

P

L

A

K

D

D

I

I

A

K

G

D

F

M

G

N

A

I

K

K

G

G

I

V

I

I

L

L

S

S

G

G

G
|
G

P

P

E

Y

S

S

T

V

T

T

L

E

P

A

G

G

A

S

P

P

A

H

A

L

P

K

Q

K

E

E

V

V

F

F

D

E

-

Y

-

F

-

L

-

E

S

K

G

K

L

I

P

P

V

I

F

F

G

G

I

I

C
|
C

Y
|
Y

G

G

M

M

Q

Q

T

E

L

I

A

A

A

V

Q

Q

L

M

G

N

G

G

E

E

T

V

E

K

A

K

A

S

D

K

Q

T

R

S

E

E

F

Y

G

G

H

C

A

T

E

D

V

V

N

N

I

I

V

L

A

R

P

N

D

D

A

N

L

I

-

N

-

I

-

T

-

Y

-

C

-

R

-

N

F

F

S

S

G

S

L

A

S

M

D

D

H

L

P

Y

G

S

E

N

A

Y

K

K

L

L

-

M

-

N

-

C

-

L

-

F

-

E

-

N

-

I

-

K

-

S

-

D

-

I

-

T

N

T

V

V

W

W

M

M

S

N

H

H

G

N

D

D

H

E

V

V

S

T

K

K

A

I

P

P

P

E

G

N

F

F

T

Y

I

L

T

V

A

S

T

S

D

E

R

N

I

C

P

L

V

I

A

C

A

S

M

I

A

Y

N

N

E

K

D

E

K

Y

R

N

W

I

Y

Y

G

G

V

V

Q

Q

F

Y

H
|
H

P

P

E
|
E

V

V

T

Y

H

E

T

S

L

L

Q

D

G

G

Q

E

A

L

L

M

L

F

R

Y

R

N

F

F

V

A

V

Y

D

N

V

I

C

C

G

K

C

C

E

K

T

K

L

-

W

F

T

D

A

P

A

I

N

R

I

Y

I

H

E

E

D

L

Q

E

I

L

A

K

R

N

V

I

R

E

E

K

Q

Y

V

K

G

H

D

D

D

H

D

Y

V

V

I

I

L

A

G

A

L

M

S

S

G

G

V

I

D
|
D

S

S

S

T

V

V

V

A

A

A

L

Y

L

T

H

H

K

K

A

I

I

F

G

K

D

E

K

R

L

F

T

F

C

G

V

I

F

F

V

I

D

D

T

N

G

G

L

L

R

R

W

K

Q

N

E

E

G

A

D

E

Q

N

V

V

M

Y

A

T

M

F

F

L

A

K

E

S

H

T

M

F

-

P

G

D

V

M

K

N

V

I

I

T

R

K

V

I

N

D

A

A

A

S

D

E

R

N

Y

F

F

L

A

S

K

N

L

L

E

Q

G

G

V

V

S

T

D

D

P

P

E

E

A

Q

K

K

R
|
R

K

K

I

I

G

G

N

K

L

L

F

F

V

I

D

E

I

E

F

F

D

E

E

K

E

A

S

V

N

N

K

N

L

I

S

D

-

I

-

D

-

I

N

N

A

K

K

T

W

F

L

L

A

L

Q

Q

G

G

T

T

I

L

Y

Y

P

P

D

D

V

I

I

I

E

E

S

S

A

K

G

C

S

S

K

-

T

-

G

-

K

-

A

-

H

-

V

-

I

-

K

-

S

-

H

-

N

-

V

-

G

-

L

-

P

-

E

-

H

-

M

L

K

K

L

F

G

K

L

L

V

F

E

E

P

P

L

F

R

K

E

Y

L

L

F

F

K
|
K

D

D

E

D

V

V

R

K

R

T

L

L

G

S

V

R

E

E

L

L

G

N

L

L

P

P

R

E

S

E

M

I

V

T

Y

N

R

R

H

H

P

P

F

F

P
|
P

G
|
G

P
|
P

G

G

L

L

G

A

V

I

R

R

I

V

L

I

G

G

E

E

V

I

K

N

R

K

E

H

Y

K

A

L

E

N

L

I

L

L

A

R

K

E

A

V

D

D

A

D

I

I

F

F

I

I

E

N

E

D

L

L

R

K

K

Q

A

Y

D

G

L

L

Y

Y

D

N

K

Q

T

I

S

S

Q
|
Q

A

A

F

F

A

A

V

V

F

L

L

L

P

S

V

S

K

K

S

S

V

V

G

-

V

-

G

-

D

-

A

-

R

-

A

-

Y

Y

E

D

W

Y

V

V

I

C

A

V

L

L

R

R

A

A

V

V

E

K

T

T

I

S

D

S

F

F

M

M

T

T

A

A

H

N

W

W

A

Y

H

Q

L

I

P

P

Y

Y

E

D

F

I

L

L

G

D

T

K

V

I

S

T

N

T

R

R

I

I

I

L

N

S

E

E

L

V

R

K

G

G

V

V

S

N

R

R

V

I

V

L

Y

Y

D

D

I

V

S

S

G

S

K
|
K

P

P

A

A

T
|
T

I
|
I

E
|
E

W

F

E

E

active site: G53 (= G58), C84 (= C85), Y85 (= Y86), H198 (= H177), E200 (= E179), D255 (= D235), K381 (= K377)
binding xanthosine-5'-monophosphate: R325 (= R304), P404 (= P400), G405 (= G401), P406 (= P402), Q446 (= Q442), K509 (= K513), T513 (= T517), I514 (= I518), E515 (= E519)

3uowB Crystal structure of pf10_0123, a gmp synthetase from plasmodium falciparum
36% identity, 99% coverage: 8:521/521 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

A

S

Q

Q

Y

Y

T

F

Q

H

L

L

I

I

A

V

R

K

R

R

I

L

R

N

E

N

L

I

G

K

V

I

Y

F

C

S

E

E

I

T

W

K

A

D

W

Y

D

-

H

-

N

-

P

-

A

K

D

D

I

I

A

K

G

D

F

M

G

N

A

I

K

K

G

G

I

V

I

I

L

L

S

S

G

G

G
|
G

P

P

E

Y

S

S

T

E

T

V

L

F

P

-

G

-

A

-

P

-

A

-

P

-

Q

E

E

Y

V

F

F

L

D

E

S

K

G

K

L

I

P

P

V

I

F

F

G

G

I

I

C
|
C

Y
|
Y

G

G

M

M

Q

Q

T

E

L

I

A

A

A

V

Q

Q

L

M

G

N

G

-

E

-

T

-

E

-

A

-

D

-

Q

-

R

-

E

-

F

Y

G

G

H

C

A

T

E

D

V

V

N

N

I

I

V

N

A

I

P

N

D

N

A

I

L

T

F

Y

S

C

G

A

L

M

S

D

D

L

H

Y

P

S

G

N

E

Y

A

K

K

L

L

M

N

N

-

C

-

L

-

F

-

E

-

N

-

I

-

K

-

S

-

D

-

I

-

T

V

V

W

W

M

M

S

N

H

H

G

N

D

D

H

E

V

V

S

T

K

K

A

I

P

P

P

E

G

N

F

F

T

Y

I

L

T

V

A

S

T

S

D

E

R

N

I

C

P

L

V

I

A

C

A

S

M

I

A

Y

N

N

E

K

D

E

K

Y

R

N

W

I

Y

Y

G

G

V

V

Q

Q

F

Y

H
|
H

P

P

E
|
E

V

V

T

Y

H

E

T

S

L

L

Q

D

G

G

Q

E

A

L

L

M

L

F

R

Y

R

N

F

F

V

A

V

Y

D

N

V

I

C

C

G

K

C

C

E

K

T

-

L

-

W

F

T

D

A

P

A

I

N

R

I

Y

I

H

E

E

D

L

Q

E

I

L

A

K

R

N

V

I

R

E

E

K

Q

Y

V

K

G

H

D

D

D

H

D

Y

V

V

I

I

L

A

G

A

L

M

S

S

G

G

V

I

D
|
D

S

S

S

T

V

V

V

A

A

A

L

Y

L

T

H

H

K

K

A

I

I

F

G

K

D

E

K

R

L

F

T

F

C

G

V

I

F

F

V

I

D

D

T

N

G

G

L

L

R

R

W

K

Q

N

E

E

G

A

D

E

Q

N

V

V

M

Y

A

T

M

F

F

L

A

K

E

S

H

T

M

F

-

P

G

D

V

M

K

N

V

I

I

T

R

K

V

I

N

D

A

A

A

S

D

E

R

N

Y

F

F

L

A

S

K

N

L

L

E

Q

G

G

V

V

S

T

D

D

P

P

E

E

A

Q

K

K

R
|
R

K

K

I

I

G

G

N

K

L

L

F

F

V

I

D

E

I

E

F

F

D

E

E

K

E

A

S

V

N

N

K

N

L

I

S

D

-

D

-

I

N

N

A

K

K

T

W

F

L

L

A

L

Q

Q

G

G

T

T

I

L

Y

Y

P

P

D

D

V

I

I

I

E

E

S

S

A

K

G

-

S

-

K

-

T

-

G

-

K

-

A

-

H

-

V

-

I

-

K

-

S

-

H

-

N

-

V

-

G

-

L

-

P

-

E

-

H

-

M

-

K

K

L

F

G

K

L

L

V

F

E

E

P

P

L

F

R

K

E

Y

L

L

F

F

K
|
K

D

D

E

D

V

V

R

K

R

T

L

L

G

S

V

R

E

E

L

L

G

N

L

L

P

P

R

E

S

E

M

I

V

T

Y

N

R

R

H

H

P

P

F

F

P
|
P

G
|
G

P
|
P

G

G

L

L

G

A

V

I

R

R

I

V

L

I

G

G

E

E

V

I

K

N

R

K

E

H

Y

K

A

L

E

N

L

I

L

L

A

R

K

E

A

V

D

D

A

D

I

I

F

F

I

I

E

N

E

D

L

L

R

K

K

Q

A

Y

D

G

L

L

Y

Y

D

N

K

Q

T

I

S

S

Q
|
Q

A

A

F

F

A

A

V

V

F

L

L

L

P

S

V

S

K

K

S

S

V

V

G

G

V

-

G

-

D

-

A

-

R

-

A

-

Y

Y

E

D

W

Y

V

V

I

C

A

V

L

L

R

R

A

A

V

V

E

K

T

T

I

S

D

S

F

F

M

M

T

T

A

A

H

N

W

W

A

Y

H

Q

L

I

P

P

Y

Y

E

D

F

I

L

L

G

D

T

K

V

I

S

T

N

T

R

R

I

I

I

L

N

S

E

E

L

V

R

K

G

G

V

V

S

N

R

R

V

I

V

L

Y

Y

D

D

I

V

S

S

G

S

K
|
K

P

P

A

A

T
|
T

I
|
I

E
|
E

W

F

E

E

active site: G47 (= G58), C67 (= C85), Y68 (= Y86), H162 (= H177), E164 (= E179), D218 (= D235), K340 (= K377)
binding xanthosine-5'-monophosphate: R288 (= R304), P363 (= P400), G364 (= G401), P365 (= P402), Q405 (= Q442), K469 (= K513), T473 (= T517), I474 (= I518), E475 (= E519)

6jp9A Crsytal structure of a xmp complexed atppase subunit of m. Jannaschii gmp synthetase (see paper)
50% identity, 61% coverage: 203:521/521 of query aligns to 1:298/298 of 6jp9A

query
sites
6jp9A

L

M

W

F

T

D

A

P

A

K

N

K

I

F

I

I

E

D

D

E

Q

A

I

V

A

E

R

E

V

I

R

K

E

Q

Q

Q

V

I

G

S

D

D

D

R

D

K

V

A

I

I

L

I

G

A

L

L

S

S

G

G

V

V

D
|
D

S

S

V

V

V

A

A

A

A

V

L

L

L

T

H

H

K

K

A

A

I

I

G

G

D

D

K

K

L

L

T

T

C

A

V

V

F

F

V

V

D

D

T

T

G

G

L

L

L

M

R

R

W

K

Q

G

E

E

G

R

D

E

Q

E

V

V

M

E

A

K

M

T

F

F

A

R

E

D

H

K

M

L

G

G

V

L

K

N

V

L

I

I

R

V

V

V

N

D

A

A

A

K

D

D

R

R

Y

F

F

L

A

N

K

A

L

L

E

K

G

G

V

V

S

T

D

D

P

P

E

E

A

E

K

K

R
|
R

K

K

I

I

G

G

N

K

L

L

F

F

V

I

D

D

I

V

F

F

D

E

E

E

E

I

S

A

N

E

K

D

L

I

S

-

N

K

A

A

K

E

W

V

L

L

A

V

Q

Q

G

G

T

T

I

I

Y

A

P

P

D

D

V

-

I

-

E

-

S

-

A

-

G

-

S

-

K

-

T

-

G

-

K

-

A

-

H

-

V

-

I

-

K

-

S

-

H

-

H

H

N

N

V

V

G

-

G

A

L

L

P

P

E

H

H

G

M

M

K

V

L

L

G

E

L

V

V

V

E

E

P

P

L

L

R

R

E

E

L

L

F

Y

K
|
K

D

D

E

E

V

V

R

R

R

L

L

L

G

A

V

K

E

E

L

L

G

G

L

L

P

P

R

D

S

S

M

I

V

V

Y

Y

R

R

H

Q

P

P

F

F

P
|
P

G
|
G

P
|
P

G

G

L

L

G

A

V

V

R

R

I

V

L

L

G

G

E

E

V

V

K

T

R

E

E

E

Y

K

A

L

E

N

L

I

L

C

A

R

K

E

A

A

D

N

A

A

I

I

F

V

I

E

E

E

L

V

R

K

K

K

A

A

D

N

L

L

Y

D

D

K

K

D

T

L

S

W

Q
|
Q

A

Y

F

F

A

A

V

V

F

V

L

L

P

D

V

C

K

K

S

A

V

T

G

G

V

V

V

K

G

G

D

D

A

-

R

R

A

E

Y

Y

E

N

W

W

V

I

I

V

A

A

L

L

R

R

A

M

V

V

E

K

T

S

I

L

D

D

F

A

M

M

T

T

A

A

H

H

W

V

A

P

H

E

L

I

P

P

Y

F

E

D

F

L

L

L

G

K

T

R

V

I

S

S

N

K

R

R

I

I

I

T

N

S

E

E

L

I

R

P

G

N

V

V

S

A

R

R

V

V

Y

F

D

D

I

I

S

T

G

D

K
|
K

P

P

A

A

T
|
T

I
|
I

E
|
E

W

F

E

E

active site: D33 (= D235), K155 (= K377)
binding xanthosine-5'-monophosphate: R102 (= R304), P178 (= P400), G179 (= G401), P180 (= P402), Q220 (= Q442), K290 (= K513), T294 (= T517), I295 (= I518), E296 (= E519)

P49915 GMP synthase [glutamine-hydrolyzing]; GMP synthetase; Glutamine amidotransferase; EC 6.3.5.2 from Homo sapiens (Human) (see paper)
36% identity, 97% coverage: 9:514/521 of query aligns to 28:567/693 of P49915

query
sites
P49915

I

V

L

V

I

I

L

L

D

D

F

A

G

G

A

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

G

F

V

V

Y

Q

C

S

E

E

I

I

W

F

A

P

W

L

D

E

H

T

N

P

P

A

A

F

D

A

I

I

A

K

G

E

F

Q

G

G

A

F

K

R

G

A

I

I

L

I

S

S

G

G

P

P

E

N

S

S

T

V

T

Y

L

A

P

E

G

D

A

A

P

P

A

W

A

F

P

D

Q

P

E

A

V

I

F

F

D

T

S

I

G

G

L

K

P

P

V

V

F

L

G

G

I

I

C
|
C

Y

Y

G

G

M

M

Q

Q

T

M

L

M

A

N

A

K

Q

V

L

F

G

G

E

T

T

V

E

H

A

K

D

S

Q

V

R

R

E

E

F

D

G

G

H

V

A

F

E

N

V

I

N

S

I

V

V

D

A

N

P

T

D

C

A

S

L

L

F

F

S

R

G

G

L

L

S

-

D

-

H

-

P

-

G

-

E

Q

A

K

K

E

L

E

N

V

V

V

W

L

M

L

S

T

H

H

G

G

D

D

H

S

V

V

S

D

K

K

A

V

P

A

P

D

G

G

F

F

T

K

I

V

T

V

A

A

T

R

T

S

D

G

R

N

I

I

P

-

V

V

A

A

A

G

M

I

A

A

N

N

E

E

D

S

K

K

R

K

W

L

Y

Y

G

G

V

A

Q

Q

F

F

H
|
H

P

P

E
|
E

V

V

T

G

H

L

T

T

L

E

Q

N

G

G

Q

K

A

V

L

I

L

L

R

K

R

N

F

F

V

L

V

Y

D

D

V

I

C

A

G

G

C

C

E

S

T

G

L

T

W

F

T

T

A

V

A

Q

N

N

I

R

I

E

E

L

D

E

Q

C

I

I

A

R

R

E

V

I

R

K

E

E

Q

R

V

V

G

G

D

T

D

S

D

K

V

V

I

L

L

V

G

L

L

L

S

S

G

G

V

V

D

D

S

S

S

T

V

V

V

C

A

T

A

A

L

L

H

N

K

R

A

A

I

L

G

N

-

Q

D

E

K

Q

L

V

T

I

C

A

V

V

F

H

V

I

D

D

T

N

G

G

L

F

L

M

R

R

W

K

Q

R

E

E

G

S

D

Q

Q

S

V

V

M

E

A

E

M

A

F

L

A

-

E

K

H

K

M

L

G

G

V

I

K

Q

V

V

I

K

R

V

V

I

N

N

A

A

D

H

R

S

Y

F

F

Y

-

N

-

G

-

T

-

L

-

P

-

I

-

S

-

D

-

E

-

D

-

R

-

T

-

P

-

R

-

K

-

R

-

I

-

S

A

K

K

T

L

L

E

N

G

M

V

T

S

T

D

S

P

P

E

E

A

E

K

K

R
|
R

K

K

I

I

G

G

N

D

L

T

F

F

V

V

D

K

I

I

F

A

D

N

E

E

-

V

-

I

-

G

E

E

S

M

N

N

K

L

L

K

S

P

N

E

A

E

K

V

W

F

L

L

A

A

Q

Q

G

G

T

T

I

L

Y

R

P

P

D

D

V

L

I

I

E

E

S

S

A

A

G

S

-

L

S

V

K

A

T

S

G

G

K

K

A

A

H

E

V

L

I

I

K

K

S

T

H

H

N

N

V

D

G

T

G

E

L

L

P

I

E

R

H

K

M

L

K

R

L

E

-

E

-

G

G

K

L

V

V

I

E

E

P

P

L

L

R

K

E

D

L

F

F

H

K

K

D

D

E

E

V

V

R

R

R

I

L

L

G

G

V

R

E

E

L

L

G

G

L

L

P

P

R

E

S

E

M

L

V

V

Y

S

R

R

H

H

P

P

F

F

P

P

G

G

P

P

G

G

L

L

G

A

V

I

R

R

I

V

L

I

-

C

-

A

-

E

-

P

-

Y

-

I

-

C

-

K

-

D

-

F

-

P

-

E

-

T

-

N

-

I

-

L

-

K

-

I

-

V

-

A

-

D

-

F

-

S

G

A

E

S

V

V

K

K

R

K

E

P

Y

H

A

T

E

-

L

L

A

Q

K

R

A

V

D

K

A

A

I

C

F

T

I

T

E

E

L

D

R

Q

K

E

A

K

D

L

L

M

Y

Q

D

I

K

T

T

S

S

L

Q

H

A

S

F

L

A

N

V

A

F

F

-

L

L

L

P

P

V

I

K

K

S

T

V

V

G

G

V

V

V

Q

G

G

D
|
D

A

C

R

R

A

S

Y

Y

E

S

W

Y

V

V

I

C

A

G

L

I

R

S

A

S

V

K

E

D

T

E

I

P

D

D

F

-

M

-

T

-

A

-

H

-

W

W

A

E

H

S

L

L

P

I

Y

-

E

-

F

F

L

L

G

A

T

R

V

L

S

I

N

P

R

R

I

M

I

C

N

H

E

-

L

-

R

-

G

N

V

V

S

N

R

R

V

V

Y

Y

D

-

I

I

S

F

G

G

K

P

P

P

C104 (= C85) active site, For GATase activity
H190 (= H177) active site, For GATase activity
E192 (= E179) active site, For GATase activity
R337 (= R304) binding
D522 (= D458) binding

Sites not aligning to the query:

610 binding
685 binding
691 binding

2vxoB Human gmp synthetase in complex with xmp (see paper)
36% identity, 97% coverage: 9:514/521 of query aligns to 6:532/658 of 2vxoB

query
sites
2vxoB

I

V

L

V

I

I

L

L

D

D

F

A

G

G

A

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

G

F

V

V

Y

Q

C

S

E

E

I

I

W

F

A

P

W

L

D

E

H

T

N

P

P

A

A

F

D

A

I

I

A

K

G

E

F

Q

G

G

A

F

K

R

G

A

I

I

L

I

S

S

G

G

G
|
G

P

P

E

N

S

S

T

V

T

Y

L

A

P

E

G

D

A

A

P

P

A

W

A

F

P

D

Q

P

E

A

V

I

F

F

D

T

S

I

G

G

L

K

P

P

V

V

F

L

G

G

I

I

C
|
C

Y
|
Y

G

G

M

M

Q

Q

T

M

L

M

A

N

A

K

Q

V

L

F

G

G

E

-

T

-

E

-

A

T

A

V

D

H

Q

K

R

K

E

S

F

D

G

G

H

V

A

F

E

N

V

I

N

S

I

V

V

D

A

N

P

T

D

C

A

S

L

L

F

F

S

R

G

G

L

L

S

-

D

-

H

-

P

-

G

-

E

Q

A

K

K

E

L

E

N

V

V

V

W

L

M

L

S

T

H

H

G

G

D

D

H

S

V

V

S

D

K

K

A

V

P

A

P

D

G

G

F

F

T

K

I

V

T

V

A

A

T

R

T

S

D

G

R

N

I

I

P

-

V

V

A

A

A

G

M

I

A

A

N

N

E

E

D

S

K

K

R

K

W

L

Y

Y

G

G

V

A

Q

Q

F

F

H
|
H

P

P

E
|
E

V

V

T

G

H

L

T

T

L

E

Q

N

G

G

Q

K

A

V

L

I

L

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K

R

N

F

F

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L

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Y

D

D

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I

C

A

G

G

C

C

E

S

T

G

L

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F

T

T

A

V

A

Q

N

N

I

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I

E

E

L

D

E

Q

C

I

I

A

R

R

E

V

I

R

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E

E

Q

R

V

V

G

G

D

T

D

S

D

K

V

V

I

L

L

V

G

L

L

L

S

S

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D
|
D

S

S

S

T

V

V

V

C

A

T

A

A

L

L

H

N

K

R

A

A

I

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G

N

-

Q

D

E

K

Q

L

V

T

I

C

A

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F

H

V

I

D

D

T

N

G

G

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F

L

M

R

R

W

K

Q

R

E

E

G

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D

Q

Q

S

V

V

M

E

A

E

M

A

F

L

A

-

E

K

H

K

M

L

G

G

V

I

K

Q

V

V

I

K

R

V

V

I

N

N

A

A

D

H

R

S

Y

F

F

Y

-

N

-

G

-

T

-

L

-

P

-

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-

I

-

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A

K

K

T

L

L

E

N

G

M

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T

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T

D

S

P

P

E

E

A

E

K

K

R
|
R

K

K

I

I

G

G

N

D

L

T

F

F

V

V

D

K

I

I

F

A

D

N

E

E

-

V

-

I

-

G

E

E

S

M

N

N

K

L

L

K

S

P

N

E

A

E

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F

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L

A

A

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Q

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T

I

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Y

R

P

P

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D

V

L

I

I

E

E

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S

A

A

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-

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|
G

K
|
K

A

A

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E

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I

I

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K

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H

N

N

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D

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E

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G

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S

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G

P
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P

G

G

L

L

G

A

V

I

R

R

I

V

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I

-

C

-

A

-

E

-

P

-

Y

-

I

-

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-

D

-

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-

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-

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-

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-

N

-

I

-

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-

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-

I

-

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-

A

-

D

-

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-

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G

A

E

S

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V

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P

Y

H

A

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E

-

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L

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A

A

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E

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E

A

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D

L

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M

Y

Q

D

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S

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H

A

S

F

L

A

N

V

A

F

F

-

L

L

L

P

P

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I

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K

S

T

V

V

G

G

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Q

G

G

D

D

A

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R
|
R

A

S

Y

Y

E

S

W

Y

V

V

I

C

A

G

L

I

R

S

A

S

V

K

E

D

T

E

I

P

D

D

F

-

M

-

T

-

A

-

H

-

W

W

A

E

H

S

L

L

P

I

Y

-

E

-

F

F

L

L

G

A

T

R

V

L

S

I

N

P

R

R

I

M

I

C

N

H

E

-

L

-

R

-

G

N

V

V

S

N

R

R

V

V

Y

Y

D

-

I

I

S

F

G

G

K

P

P

P

active site: G55 (= G58), C82 (= C85), Y83 (= Y86), H165 (= H177), E167 (= E179), D223 (= D235), K381 (= K377)
binding xanthosine-5'-monophosphate: R302 (= R304), G348 (= G346), K349 (= K347), P404 (= P400), G405 (= G401), P406 (= P402), R489 (= R460)

Sites not aligning to the query:

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

7yc6A Crystal structure of d110p mutant of gatase subunit of methanocaldococcus jannaschii gmp synthetase
39% identity, 37% coverage: 9:199/521 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

A

G

Q

Q

Y

Y

T

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I

I

A

H

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I

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K

E

Y

L

I

G

G

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V

Y

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C

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I

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V

A

P

W

N

D

T

H

T

N

P

P

L

A

E

D

E

I

I

-

E

A

S

G

N

F

K

G

E

A

V

K

K

G

G

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S

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G

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P

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S

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A

A

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I

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A

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D

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S

A

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K

L

L

P

P

V

I

F

L

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G

I

I

C
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C

Y

L

G

G

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H

Q

Q

T

L

L

I

A

A

A

L

Q

A

L

Y

G

G

E

E

T

V

E

-

A

-

D

-

Q

-

R

-

E

-

F

-

G

G

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R

A

A

E

A

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L

N

T

I

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V

A

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D
|
D

A

K

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E

F

N

S

P

G

L

L

F

S

K

D

N

H

V

P

P

G

R

E

E

A

-

K

-

L

F

N

N

V

A

W

W

M

A

S

S

H

H

G

K

D

D

H
x
E

V

V

S

K

K

K

A

V

P

P

P

E

G

G

F

F

T

E

I

I

T

L

A

A

T
x
H

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x
C

P

Q

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V

A

E

A

A

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M

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Y

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G

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|
H

P

P

E

E

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V

T

A

H

H

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T

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E

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Y

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G

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A

E

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R

N

F

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-

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C

D

K

V

V

C

C

G

G

binding zinc ion: C76 (= C85), D101 (= D118), E123 (≠ H142), E123 (≠ H142), H136 (≠ T155), C140 (≠ I159), C140 (≠ I159), H158 (= H177)

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, 36% coverage: 9:194/521 of query aligns to 75:264/276 of Q42565

query
sites
Q42565

I

I

L

I

I

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L

I

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D

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A

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G

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P

-

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P

V

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F

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G
|
G

I

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C

C

Y

M

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G

M

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Q

T

C

L

I

A

G

A

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Q

A

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G

G

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T

I

E

V

A

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A

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P

Q

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R

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A
x
G

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S

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P

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D

D

-

E

-

K

-

G

-

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A

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A

A

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W

T

T

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D

D

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G

I

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V

M

A

A

M

R

A

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N

R

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D

Y

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K

R

H

W

I

Y

Q

G

G

V

V

Q

Q

F

F

H

H

P

P

E

E

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I

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T

L

T

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E

G

G

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K

A

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L

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R

R

R

N

F

F

V

I

G150 (= G83) mutation to D: In trp4-1; no visible phenotype under normal growth conditions.
G176 (≠ A110) 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)
25% identity, 36% coverage: 9:194/521 of query aligns to 2:185/187 of P00903

query
sites
P00903

I

I

L

L

I

L

L

I

D

D

F

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A

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Y

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I

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C

E

E

L

L

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A

Y

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A

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W

N

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A

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A

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D

I

I

A

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A

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A

P

K

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K

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G

P

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T

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A

G

G

A

I

P

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A

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Y

D

A

S

G

G

R

L

L

P

P

V

I

F

L

G

G

I

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C
|
C

Y

L

G

G

M

H

Q

Q

T

A

L

M

A

A

A

Q

Q

A

L

F

G

G

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T

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E

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A

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A

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A

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M

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G

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K

A

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A

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P

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E

A

G

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F

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G

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L

S

A

D

N

H

P

P

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G

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E

V

A

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R

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Y

N

H

V

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W

L

M

V

S

V

H

E

G

P

D

D

H

S

V

L

S

-

K

-

A

-

P

P

P

A

G

C

F

F

T

D

I

V

T

T

A

A

T

W

T

S

D

E

R

T

I

R

P

E

V

I

A

M

A

G

M

I

A

R

N

H

E

R

D

Q

K

W

R

D

W

L

Y

E

G

G

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V

Q

Q

F

F

H
|
H

P

P

E
|
E

V

S

T

I

H

L

T

S

L

E

Q

Q

G

G

Q

H

A

Q

L

L

R

A

R

N

F

F

V

L

C79 (= C85) mutation to S: 10000-fold decrease in catalytic efficiency.
H168 (= H177) mutation to Q: Loss of activity.
E170 (= E179) 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.

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)
29% identity, 27% coverage: 53:192/521 of query aligns to 52:185/193 of P00900

query
sites
P00900

I

L

I

M

L

L

S

S

G

P

G

G

P

P

E

G

S

T

T

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T

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P

A

G

G

A

C

P

M

A

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A

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L

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F

L

D

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G

Q

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C
|
C

Y

L

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A

E

Q

A

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Q

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-

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A

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A

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I

A

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I

A

A

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D

-

G

-

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A

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F

S

A

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G

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M

S

A

D

N

H

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P

-

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-

E

-

A

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K

P

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P

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A

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Y

H

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H

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V

G

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N

A

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T

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A

A

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D

G

R

E

I

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P

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V

V

A

M

A

A

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A

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N

D

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D

D

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C

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G

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F

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Q

F

F

H

H

P

P

E

E

V

S

T

I

H

L

T

T

L

T

Q

H

G

G

Q

A

A

R

L

L

R

E

R

Q

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)
29% identity, 27% coverage: 53:192/521 of query aligns to 51:184/192 of 1i7qB

query
sites
1i7qB

I

L

I

M

L

L

S

S

G
x
P

G
|
G

P

P

E
x
G

S

T

T

P

T

S

L

E

P

A

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G

A

C

P

M

A

P

A

E

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L

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L

E

Q

V

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F

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D

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G

Q

L

L

P

P

V

I

F

I

G

G

I

I

C
|
C

Y
x
L

G

G

M

H

Q
|
Q

T

A

L

I

A

V

A

E

Q

A

L

Y

G

G

E

Q

T

V

E

G

A

Q

A

A

D

G

Q

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R

-

E

E

F

I

G

L

H

H

A

G

E

K

V

A

N

S

I

A

V

I

A

A

P

H

D

D

-

G

-

E

A

G

L

M

F

F

S

A

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G

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M

S

A

D

N

H

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P

-

G

-

E

-

A

-

K

P

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L

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W

A

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R

S

Y

H
|
H

G
x
S

D
x
L

H

V

V

G

S

S

K

N

A

I

P

P

P

A

G

D

F

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A

A

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A

M

A

A

M

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A

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N

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E

D

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C

G

G

V

F

Q

Q

F

F

H
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H

P

P

E
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E

V

S

T

I

H

L

T

T

L

T

Q

H

G

G

Q

A

A

R

L

L

R

E

R

Q

active site: G58 (≠ E60), C83 (= C85), L84 (≠ Y86), H169 (= H177), E171 (= E179)
binding glutamic acid: P55 (≠ G57), G56 (= G58), G58 (≠ E60), C83 (= C85), L84 (≠ Y86), Q87 (= Q89), H132 (= H139), S133 (≠ G140), L134 (≠ D141)

P08955 Multifunctional protein CAD; Carbamoyl phosphate synthetase 2-aspartate transcarbamylase-dihydroorotase; EC 6.3.5.5; EC 3.5.1.2; EC 6.3.4.16; EC 2.1.3.2; EC 3.5.2.3 from Mesocricetus auratus (Golden hamster) (see paper)
28% identity, 33% coverage: 8:179/521 of query aligns to 177:338/2225 of P08955

query
sites
P08955

K

R

I

I

L

C

I

A

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L

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D

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C

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G

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Y

Y

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I

-

A

-

R

R

R

C

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C

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Q

L

L

G

G

V

A

Y

E

C

V

E

T

I

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A

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W

W

D

N

H

H

N

-

P

-

A

-

D

E

I

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Q

G

K

A

Y

K

D

G

G

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I

F

L

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S

G

N

G

G

P

P

-

G

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D

S

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A

T

S

L

Y

P

P

G

G

A

V

P

V

A

A

A

T

P

L

Q

N

E

R

V

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F

L

D

S

-

E

-

P

S

N

G

P

L

R

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P

V

V

F

F

G

G

I

I

C

C

Y

L

G

G

M

H

Q

Q

T

L

L

L

A

A

A

L

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A

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G

G

G

A

E

K

T

T

E

Y

A

K

A

M

D

R

Q

Y

R

G

E

N

F

R

G

G

H

H

A

N

E

Q

V

-

N

-

I

-

V

-

A

-

P

-

D

P

A

C

L

L

F

L

S

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G

G

L

T

S

-

D

-

H

-

P

-

G

G

E

R

A

C

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F

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L

N

T

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S

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-

M

Q

S

N

H

H

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G

D

F

H

A

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V

-

D

-

A

S

D

K

S

A

L

P

P

P

A

G

G

F

W

T

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-

P

I

L

T

F

A

T

T

N

T

A

D

N

R

D

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C

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N

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E

A

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M

I

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N

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E

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D

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Y

F

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V

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Q

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F

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H

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P

E

E

Sites not aligning to the query:

1406 modified: Phosphoserine; by PKA; S→A: No effect on enzyme kinetics.; S→D: Increases CPSase activity and reduces sensitivity to feedback inhibition by UTP.

3fijA Crystal structure of a uncharacterized protein lin1909
33% identity, 20% coverage: 75:180/521 of query aligns to 85:201/224 of 3fijA

query
sites
3fijA

F

L

D

D

S

A

G

G

L

K

P

P

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I

F

F

G

A

I

I

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C

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M

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A

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G

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E

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A

A

A

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x
H

-

L

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R

-

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-

E

E

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F

L

G

G

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A
x
H

E

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N

D

I

I

V

E

A

P

P

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A

E

L

L

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-

S

-

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-

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A

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K

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H

H

H

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P

G

N

E

K

A

K

K

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L

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N

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x
S

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H
|
H

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H

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S

K

K

K

A

L

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A

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P

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A

A

-

R

T

T

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D

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x
E

A

A

A

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M

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A

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W

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Y

-

L

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P

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L

binding manganese (ii) ion: H123 (vs. gap), H134 (≠ A110), S156 (≠ V135), H158 (= H139), E181 (≠ V161)

P0A6F1 Carbamoyl phosphate synthase small chain; Carbamoyl phosphate synthetase glutamine chain; EC 6.3.5.5 from Escherichia coli (strain K12) (see paper)
27% identity, 33% coverage: 9:181/521 of query aligns to 194:357/382 of P0A6F1

query
sites
P0A6F1

I

V

L

V

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L

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D

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F

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G
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G

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x
G

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T

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Q

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F

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L

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A

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N

I

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x
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G

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x
F

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G241 (= G58) binding
G243 (vs. gap) binding
L270 (≠ Y86) binding
Q273 (= Q89) binding
N311 (≠ S138) binding
G313 (= G140) binding
F314 (≠ D141) binding

Sites not aligning to the query:

47 binding

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, 20% coverage: 8:109/521 of query aligns to 243:339/430 of Q9LVW7

query
sites
Q9LVW7

K

K

I

V

L

I

I

A

L

Y

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D

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F

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G

A

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A

A

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A

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S

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A

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A

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K

E

E

V

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F

L

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K

G

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P

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Y

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G

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I

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C

Y

M

G

G

M

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Q

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L

L

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A

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Q

A

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G

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F

A

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K

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K

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F

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G

H

H

Sites not aligning to the query:

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

1ce8B Carbamoyl phosphate synthetase from escherichis coli with complexed with the allosteric ligand imp (see paper)
27% identity, 33% coverage: 9:181/521 of query aligns to 193:356/379 of 1ce8B

query
sites
1ce8B

I

V

L

V

I

A

L

Y

D

D

F

F

G

G

A

A

Q

K

Y

R

T

N

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-

L

-

I

I

A

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I

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E

D

L

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Y

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N

S

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A

A

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D

I

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A

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M

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A

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K

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S

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G

G

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P

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G

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A

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A

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F

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C

Y

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L

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A

A

A

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A

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-

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K

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F

F

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H

A

H

E

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G

N

N

I

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V

-

A

-

P

-

D

-

A

-

L

-

F

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-

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S

-

D

-

H

H

P

P

-

V

G

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E

D

A

V

K

E

L

K

N

N

V

V

W

V

M

M

-

I

-

T

-

A

-

Q

S

N

H

H

G

G

D

F

H

A

V

V

S

D

K

E

A

A

P

T

P

L

G

P

F

A

T

N

I

L

T

R

A

V

T

T

T

H

D

K

R

S

I

L

-

F

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D

-

G

P

T

V

L

A

Q

A

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M

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A

H

N

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D

D

K

K

R

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A

Y

F

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Q

F

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H
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H

P

P

E
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E

V

A

T

S

active site: C268 (= C85), H352 (= H177), E354 (= E179)

Sites not aligning to the query:

binding L-ornithine: 119, 122

Query Sequence

>WP_057506705.1 NCBI__GCF_001431535.1:WP_057506705.1
MTNIHTDKILILDFGAQYTQLIARRIRELGVYCEIWAWDHNPADIAGFGAKGIILSGGPE
STTLPGAPAAPQEVFDSGLPVFGICYGMQTLAAQLGGETEAADQREFGHAEVNIVAPDAL
FSGLSDHPGEAKLNVWMSHGDHVSKAPPGFTITATTDRIPVAAMANEDKRWYGVQFHPEV
THTLQGQALLRRFVVDVCGCETLWTAANIIEDQIARVREQVGDDDVILGLSGGVDSSVVA
ALLHKAIGDKLTCVFVDTGLLRWQEGDQVMAMFAEHMGVKVIRVNAADRYFAKLEGVSDP
EAKRKIIGNLFVDIFDEESNKLSNAKWLAQGTIYPDVIESAGSKTGKAHVIKSHHNVGGL
PEHMKLGLVEPLRELFKDEVRRLGVELGLPRSMVYRHPFPGPGLGVRILGEVKREYAELL
AKADAIFIEELRKADLYDKTSQAFAVFLPVKSVGVVGDARAYEWVIALRAVETIDFMTAH
WAHLPYEFLGTVSNRIINELRGVSRVVYDISGKPPATIEWE

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