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, 98% coverage: 10:526/526 of query aligns to 8:555/555 of Q8IJR9

query
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Y18 (= Y20) mutation to F: Slight increase in affinity for glutamine. No defect in glutaminase activity.
H20 (≠ Q22) mutation to A: Slight decrease in affinity for glutamine. 1.8-fold increase in affinity for ATP. Slight increase in affinity for XMP. Moderate reduction in glutaminase activity.
K24 (≠ R26) mutation to L: 50 percent decrease in glutaminase activity. 5.3-fold decrease in affinity for glutamine. 1.7-fold increase in affinity for ATP. 2.8-fold decrease in affinity for XMP.
R25 (= R27) mutation to L: No effect on glutaminase activity. 1.4-fold decrease in affinity for glutamine.
C89 (= C87) mutation to A: Loss of glutaminase activity, however, glutamine binding is not affected. In presence of exogenous ammonia, the amination of XMP to produce GMP is normal. 2.3-fold decrease in affinity for ATP and 1.8-fold decrease in affinity for XMP. 2.9-fold decrease in affinity for ATP and 1.9-fold decrease in affinity for XMP; when associated with A-113.
Q93 (= Q91) binding L-glutamine
C113 (≠ Y111) 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 (≠ G134) 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 (= W141) mutation to F: Slight decrease in affinity for glutamine. Slight increase in glutaminase activity.
N169 (≠ S143) binding L-glutamine; mutation to S: Slight increase in affinity for glutamine. No defect in glutaminase activity.
D172 (= D146) binding L-glutamine; mutation to A: 172-fold decrease in affinity for glutamine. Severe loss of glutaminase activity.
H208 (= H182) binding L-glutamine
Y212 (≠ T186) mutation to W: 2.7-fold decrease in affinity for glutamine. No defect in glutaminase activity.
E213 (≠ H187) 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 (= R309) binding XMP
D371 (= D341) Important for ATPPase activity; mutation to A: Impaired formation of adenyl-XMP intermediate. Slight increase in glutaminase activity.
E374 (= E344) mutation to L: 8.9-fold decrease in affinity for ammonia. Severe loss of glutaminase activity.
K376 (≠ A346) 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 (= K357) mutation to L: Severe loss of ATP pyrophosphatase (ATPPase) activity. 80 percent decrease in glutaminase activity. Impaired GMP formation.
T387 (≠ S358) mutation to A: No effect on ATP pyrophosphatase (ATPPase) activity. 20 percent decrease in glutaminase activity. No effect on GMP formation.
H388 (= H359) 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 (= H360) Important for ATPPase activity; mutation to A: Loss of ATP pyrophosphatase (ATPPase) activity. 67 percent decrease in glutaminase activity. Impaired GMP formation.
N390 (= N361) mutation to A: No effect on ATP pyrophosphatase (ATPPase) activity. Increases glutaminase activity. Loss of GMP formation.
K411 (= K382) mutation to L: 70 percent decrease in glutaminase activity. Loss of GMP formation.
D412 (= D383) mutation to A: 30 percent decrease in glutaminase activity. 7.9-fold decrease in affinity for glutamine.
D413 (≠ E384) mutation to A: 35 percent decrease in glutaminase activity. 3.6-fold decrease in affinity for glutamine.
K415 (≠ R386) mutation to L: Increases glutaminase activity. 4.2-fold decrease in affinity for ATP.
Q476 (= Q447) binding XMP
R539 (= R510) mutation to L: 85 percent decrease in glutaminase activity.
K547 (= K518) binding XMP; mutation to L: 85 percent decrease in glutaminase activity.
I552 (= I523) binding XMP
E553 (= E524) binding XMP; mutation to L: 85 percent decrease in glutaminase activity.
E555 (= E526) 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)
37% identity, 98% coverage: 10:526/526 of query aligns to 2:525/525 of 4wioA

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active site: G52 (= G60), A83 (≠ C87), Y84 (= Y88), H197 (= H182), E199 (= E184), D255 (= D240), K393 (= K382)
binding glutamine: Q87 (= Q91), N158 (≠ S143), H159 (= H144), N160 (≠ G145), D161 (= D146), H197 (= H182)

3uowA Crystal structure of pf10_0123, a gmp synthetase from plasmodium falciparum
37% identity, 98% coverage: 10:526/526 of query aligns to 3:517/517 of 3uowA

query
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3uowA

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active site: G53 (= G60), C84 (= C87), Y85 (= Y88), H198 (= H182), E200 (= E184), D255 (= D240), K381 (= K382)
binding xanthosine-5'-monophosphate: R325 (= R309), P404 (= P405), G405 (= G406), P406 (= P407), Q446 (= Q447), K509 (= K518), T513 (= T522), I514 (= I523), E515 (= E524)

3uowB Crystal structure of pf10_0123, a gmp synthetase from plasmodium falciparum
37% identity, 98% coverage: 10:526/526 of query aligns to 1:477/477 of 3uowB

query
sites
3uowB

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active site: G47 (= G60), C67 (= C87), Y68 (= Y88), H162 (= H182), E164 (= E184), D218 (= D240), K340 (= K382)
binding xanthosine-5'-monophosphate: R288 (= R309), P363 (= P405), G364 (= G406), P365 (= P407), Q405 (= Q447), K469 (= K518), T473 (= T522), I474 (= I523), E475 (= E524)

P49915 GMP synthase [glutamine-hydrolyzing]; GMP synthetase; Glutamine amidotransferase; EC 6.3.5.2 from Homo sapiens (Human) (see paper)
35% identity, 98% coverage: 11:523/526 of query aligns to 28:575/693 of P49915

query
sites
P49915

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A

V

V

F

H

V

I

D

D

H

N

G

G

L

F

L

M

R

R

Y

K

K

R

E

E

G

S

D

Q

Q

S

V

V

-

E

M

E

A

A

M

L

F

K

A

K

E

L

N

G

M

I

G

Q

L

V

R

K

V

V

I

I

R

N

A

A

-

A

-

H

-

S

-

F

-

Y

-

N

-

G

-

T

-

L

-

P

-

I

-

S

-

D

-

E

-

D

-

R

D

T

V

P

E

R

E

K

R

R

F

I

M

S

A

K

A

T

L

L

A

N

G

M

E

T

T

T

D

S

P

P

E

E

K

E

K

K

R
|
R

K

K

I

I

G

G

H

D

E

T

F

F

I

V

-

K

-

I

-

A

-

N

E

E

V

V

F

I

D

G

A

E

E

M

S

N

T

L

K

K

L

P

Q

E

G

E

V

V

K

-

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

K

E

V

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

M

L

-

R

-

E

D

E

M

G

S

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

K

I

L

L

G

G

V

R

A

E

L

L

G

G

L

L

P

P

Y

E

N

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

E

P

Y

H

A

T

D

L

I

L

L

Q

R

R

L

V

A

K

D

A

N

C

I

T

Y

T

I

E

E

E

E

D

L

Q

V

E

K

K

W

L

E

M

L

Q

Y

I

D

T

K

S

T

L

S

H

Q

S

A

L

F

N

T

A

V

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

R

S

Y

Y

D

S

Y

Y

V

V

V

C

A

G

L

I

R

S

A

S

V

K

E

D

T

E

I

P

D

D

F

-

M

-

T

-

A

-

R

-

W

W

A

E

H

S

L

L

P

I

Y

-

E

-

F

F

L

L

E

A

H

R

V

L

S

I

G

P

R

R

I

M

I

C

N

H

E

N

I

V

P

N

R

R

I

V

S

V

R

Y

V

I

V

F

Y

G

D

P

I

P

S

V

S

K

K

E

P

P

A

T

T

D

I

V

C104 (= C87) active site, For GATase activity
H190 (= H182) active site, For GATase activity
E192 (= E184) active site, For GATase activity
R337 (= R309) binding XMP
D522 (= D463) 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, 98% coverage: 11:523/526 of query aligns to 6:540/658 of 2vxoB

query
sites
2vxoB

I

V

L

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

I

L

G

F

V

V

Y

Q

C

S

E

E

V

I

E

F

P

P

W

L

D

E

I

T

D

P

A

A

K

F

D

A

V

I

E

K

A

E

F

Q

G

G

A

F

R

R

G

A

I

I

L

I

S

S

G

G

G
|
G

P

P

E

N

T

S

V

V

T

Y

G

A

E

E

D

D

S

A

P

P

V

W

A

F

P

D

D

P

I

A

V

I

F

F

Q

T

L

I

G

G

V

K

P

P

V

V

L

L

G

G

I

I

C
|
C

Y
|
Y

G

G

M

M

Q

Q

T

M

M

M

A

N

E

K

Q

V

L

F

G

G

K

T

V

V

I

H

S

K

T

S

E

D

H

-

E

-

Y

-

G

G

Y

V

A

F

Q

N

V

I

R

S

A

V

H

D

G

N

H

T

T

C

K

S

L

L

L

F

G

R

E

G

I

L

E

Q

D

K

E

E

V

E

T

V

P

-

E

-

G

-

Y

-

G

-

M

-

L

-

D

-

V

V

W

L

M

L

S

T

H

H

G

G

D

D

R

S

V

V

E

D

S

K

M

V

P

A

D

D

G

G

F

F

K

K

L

V

M

V

A

A

S

R

T

S

P

G

S

N

C

I

P

-

I

V

A

A

G

G

M

I

A

A

N

N

E

E

D

S

K

K

N

K

F

L

Y

Y

G

G

I

A

Q

Q

F

F

H
|
H

P

P

E
|
E

V

V

T

G

H

L

T

T

K

E

Q

N

G

G

L

K

R

V

M

I

L

L

E

K

R

N

F

F

V

L

I

Y

T

D

L

I

C

A

G

G

C

C

Q

S

K

G

L

T

W

F

T

T

T

V

E

Q

N

N

I

R

I

E

E

L

D

E

S

C

V

I

K

R

K

E

V

I

R

K

E

E

L

R

V

V

G

G

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T

D

S

Q

K

V

V

M

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

Q

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

Y

K

K

R

E

E

G

S

D

Q

Q

S

V

V

-

E

M

E

A

A

M

L

F

K

A

K

E

L

N

G

M

I

G

Q

L

V

R

K

V

V

I

I

R

N

A

A

-

A

-

H

-

S

-

F

-

Y

-

N

-

G

-

T

D

T

V

T

E

L

E

P

R

R

F

I

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A

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A

T

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L

A

N

G

M

E

T

T

T

D

S

P

P

E

E

K

E

K

K

R
|
R

K

K

I

I

G

G

H

D

E

T

F

F

I

V

-

K

-

I

-

A

-

N

E

E

V

V

F

I

D

G

A

E

E

M

S

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T

L

K

K

L

P

Q

E

G

E

V

V

K

-

W

F

L

L

A

A

Q

Q

G

G

T

T

I

L

Y

R

P

P

D

D

V

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I

I

E

E

S

S

A

A

G

S

-

L

S

V

K

A

T

S

G
|
G

K
|
K

A

A

K

E

V

L

I

I

K

K

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T

H

H

N

N

V

D

G

T

G

E

L

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M

L

-

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-

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K

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I

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E

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P

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|
K

D

D

E

E

V

V

R

R

K

I

L

L

G

G

V

R

A

E

L

L

G

G

L

L

P

P

Y

E

N

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

E

P

Y

H

A

T

D

L

I

L

L

Q

R

R

L

V

A

K

D

A

N

C

I

T

Y

T

I

E

E

E

E

D

L

Q

V

E

K

K

W

L

E

M

L

Q

Y

I

D

T

K

S

T

L

S

H

Q

S

A

L

F

N

T

A

V

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

R

S

Y

Y

D

S

Y

Y

V

V

V

C

A

G

L

I

R

S

A

S

V

K

E

D

T

E

I

P

D

D

F

-

M

-

T

-

A

-

R

-

W

W

A

E

H

S

L

L

P

-

Y

-

E

I

F

F

L

L

E

A

H

R

V

L

S

I

G

P

R

R

I

M

I

C

N

H

E

N

I

V

P

N

R

R

I

V

S

V

R

Y

V

I

V

F

Y

G

D

P

I

P

S

V

S

K

K

E

P

P

A

T

T

D

I

V

active site: G55 (= G60), C82 (= C87), Y83 (= Y88), H165 (= H182), E167 (= E184), D223 (= D240), K381 (= K382)
binding xanthosine-5'-monophosphate: R302 (= R309), G348 (= G351), K349 (= K352), P404 (= P405), G405 (= G406), P406 (= P407), R489 (= R465)

Sites not aligning to the query:

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

6jp9A Crsytal structure of a xmp complexed atppase subunit of m. Jannaschii gmp synthetase (see paper)
47% identity, 61% coverage: 208:526/526 of query aligns to 1:298/298 of 6jp9A

query
sites
6jp9A

L

M

W

F

T

D

T

P

E

K

N

K

I

F

I

I

E

D

D

E

S

A

V

V

K

E

V

I

R

K

E

Q

L

Q

V

I

G

S

S

D

D

R

Q

K

V

A

M

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

Q

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

Y

K

K

G

E

E

G

R

D

E

Q

E

V

V

M

E

A

K

M

T

F

F

A

R

E

D

N

K

M

L

G

G

L

L

R

N

V

L

I

I

R

V

A

V

D

D

V

A

E

K

E

D

R

R

F

F

M

L

A

N

A

A

L

L

A

K

G

G

E

V

T

T

D

D

P

P

E

E

K

E

K

K

R
|
R

K

K

I

I

G

G

H

K

E

L

F

F

I

I

E

D

V

V

F

F

D

E

A

E

E

I

S

A

T

E

K

D

L

I

Q

K

G

A

V

-

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

-

K

-

V

-

I

-

K

-

S

-

H

-

H

H

N

N

V

V

G

-

G

A

L

L

P

P

D

H

D

G

M

M

D

V

M

L

S

E

L

V

I

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

K

L

L

L

G

A

V

K

A

E

L

L

G

G

L

L

P

P

Y

D

N

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

K

E

E

E

Y

K

A

L

D

N

I

I

L

C

R

R

L

E

A

A

D

N

N

A

I

I

Y

V

I

E

E

E

L

V

V

K

K

K

W

A

E

N

L

L

Y

D

D

K

K

D

T

L

S

W

Q
|
Q

A

Y

F

F

T

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

R

E

Y

Y

D

N

Y

W

V

I

V

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

R

H

W

V

A

P

H

E

L

I

P

P

Y

F

E

D

F

L

L

L

E

K

H

R

V

I

S

S

G

K

R

R

I

I

I

T

N

S

E

E

I

I

P

P

R

N

I

V

S

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 (= D240), K155 (= K382)
binding xanthosine-5'-monophosphate: R102 (= R309), P178 (= P405), G179 (= G406), P180 (= P407), Q220 (= Q447), K290 (= K518), T294 (= T522), I295 (= I523), E296 (= E524)

7yc6A Crystal structure of d110p mutant of gatase subunit of methanocaldococcus jannaschii gmp synthetase
35% identity, 37% coverage: 11:204/526 of query aligns to 2:179/183 of 7yc6A

query
sites
7yc6A

I

I

L

V

I

I

L

L

D

D

F

N

G

G

S

G

Q

Q

Y

Y

T

V

Q

H

L

R

I

I

A

H

R

R

R

S

I

L

R

K

E

Y

I

I

G

G

V

V

Y

S

C

S

E

K

V

I

E

V

P

P

W

N

D

T

I

T

D

P

A

L

K

E

D

E

V

I

E

E

A

S

F

N

G

K

-

E

A

V

R

K

G

G

I

I

L

L

S

S

G

G

P

P

E

D

T

I

V

-

T

-

G

-

E

E

D

K

S

A

P

K

V

N

A

C

P

I

D

D

I

I

V

A

F

L

Q

N

L

A

G

K

V

L

P

P

V

I

L

L

G

G

I

I

C
|
C

Y

L

G

G

M

H

Q

Q

T

L

M

I

A

A

E

L

Q

A

L

Y

G

G

K

E

V

V

I

-

S

-

T

-

E

-

H

-

E

-

Y

-

G

G

Y

R

A

A

Q

A

V

L

R

-

A

-

H

-

G

-

H

-

T

T

K

K

L

V

L

Y

G

V

E
x
D

I

K

E

E

D

N

E

P

V

L

T

F

P

K

E

N

G

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Y

P

G

R

M

E

L

F

D

N

V

A

W

W

M

A

S

S

H

H

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x
E

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V

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K

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P

P

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E

G

G

F

F

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M

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x
H

T

S

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D

S

I

C
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C

P

Q

I

V

A

E

G

A

M

M

A

K

N

H

E

K

D

T

K

K

N

P

F

I

Y

Y

G

G

I

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Q

Q

F

F

H
|
H

P

P

E

E

V

V

T

A

H

H

T

T

K

E

Q

Y

G

G

L

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R

E

M

I

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L

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K

R

N

F

F

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I

-

T

K

L

V

C

C

G

G

binding zinc ion: C76 (= C87), D101 (≠ E125), E123 (≠ R147), E123 (≠ R147), H136 (≠ S160), C140 (= C164), C140 (= C164), H158 (= H182)

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)
26% identity, 36% coverage: 11:199/526 of query aligns to 2:185/187 of P00903

query
sites
P00903

I

I

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L

I

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L

I

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G

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-

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G

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C

Y

L

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Q

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M

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A

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G

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A

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N

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P

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G

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Y

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G

H

M

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L

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D

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W

-

M

-

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-

H

-

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I

I

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G

M

I

A

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H
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H

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E

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Q

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F

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L

C79 (= C87) mutation to S: 10000-fold decrease in catalytic efficiency.
H168 (= H182) mutation to Q: Loss of activity.
E170 (= E184) mutation to A: 150-fold decrease in catalytic efficiency.; mutation to D: 4-fold decrease in catalytic efficiency.; mutation E->K,Q: Loss of activity.

Q42565 Anthranilate synthase beta subunit 1, chloroplastic; Anthranilate synthase component 2-1; Anthranilate synthase, glutamine amidotransferase component 2-1; Protein TRYPTOPHAN BIOSYNTHESIS 4; Protein WEAK ETHYLENE INSENSITIVE 7; EC 4.1.3.27 from Arabidopsis thaliana (Mouse-ear cress) (see 2 papers)
27% identity, 36% coverage: 11:199/526 of query aligns to 75:264/276 of Q42565

query
sites
Q42565

I

I

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I

I

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L

I

D

D

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E

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-

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G

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-

L

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G

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V

C

C

Y

M

G

G

M

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Q

Q

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M

I

A

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E

Q

A

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K

V

I

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-

E

-

H

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P

Y

F

G

G

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|
G

H

K

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E

-

I

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E

Y

D

D

E

E

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E

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A

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Y

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K

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R

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F

F

V

I

G150 (= G85) mutation to D: In trp4-1; no visible phenotype under normal growth conditions.
G176 (= G118) mutation to E: In wei7-2; insensitive to inhibition of root elongation by ethylene.

Q09794 Multifunctional protein ura1; Pyrimidine-specific carbamoyl phosphate synthase-aspartate carbamoyl transferase; CPSase-ATCase; EC 6.3.5.5; EC 3.5.1.2; EC 6.3.4.16; EC 2.1.3.2 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
29% identity, 34% coverage: 10:186/526 of query aligns to 264:426/2244 of Q09794

query
sites
Q09794

R

R

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I

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W

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-

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S

D

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-

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L

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A

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S

N

T

A

P

N

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D

C

G

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S

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G

M

I

A

Y

N

N

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D

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Q

F

F

H

H

P

P

E

E

V

S

T

T

Sites not aligning to the query:

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

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: 10:184/526 of query aligns to 177:338/2225 of P08955

query
sites
P08955

R

R

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A

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A

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I

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D

-

A

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H

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A

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Q

-

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-

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A

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A

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Q

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F

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H

P

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.

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)
28% identity, 34% coverage: 9:186/526 of query aligns to 242:406/430 of Q9LVW7

query
sites
Q9LVW7

H

Y

R

K

I

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L

I

I

A

L

Y

D

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V

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I

F

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A

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A

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A

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G

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E

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Q

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A

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N

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H

P

P

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E

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A

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S

Sites not aligning to the query:

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

8hx8A Crystal structure of 4-amino-4-deoxychorismate synthase from streptomyces venezuelae co-crystallized with chorismate (see paper)
27% identity, 36% coverage: 10:198/526 of query aligns to 5:187/673 of 8hx8A

query
sites
8hx8A

R

R

I

T

L

L

I

L

L

I

D

D

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I

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D

S

D

C

G

P

V

I

V

A

M

G

G

M

L

A

R

N

H

E

R

D

E

K

K

N

P

F

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Y

W

G

G

I

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Q

Q

F

F

H

H

P

P

E

E

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S

T
x
I

H

G

T
x
S

K

D

Q

F

G

G

L

R

R

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M

I

L

M

E

A

R

N

F

F

binding magnesium ion: I175 (≠ T186), S177 (≠ T188)

Sites not aligning to the query:

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

P27708 Multifunctional protein CAD; Carbamoyl phosphate synthetase 2-aspartate transcarbamylase-dihydroorotase; EC 6.3.5.5; EC 3.5.1.2; EC 6.3.4.16; EC 2.1.3.2; EC 3.5.2.3 from Homo sapiens (Human) (see 7 papers)
29% identity, 33% coverage: 10:184/526 of query aligns to 177:338/2225 of P27708

query
sites
P27708

R
|
R

I

I

L

L

I

A

L

L

D

D

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G

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Y

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N

Q

Q

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I

-

A

-

R

R

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I

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R

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A

Y

E

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W

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D

-

H

-

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D

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Y

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-

F

-

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-

A

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-

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N

G

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G

T

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A

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A

Y

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T

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L

G

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R

-

V

-

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-

E

-

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N

-

P

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R

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P

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V

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F

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G

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I

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A

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-

I

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-

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T

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Y

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G

Y

N

A

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Q

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R

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P

-

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T

A

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A

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N

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E

N

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N

P

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Q

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F

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H

P

P

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E

R177 (= R10) to Q: in a colorectal cancer sample; somatic mutation; dbSNP:rs374122292

Sites not aligning to the query:

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

P07259 Multifunctional protein URA2; Pyrimidine-specific carbamoyl phosphate synthase-aspartate carbamoyl transferase; CPSase-ATCase; EC 6.3.5.5; EC 3.5.1.2; EC 6.3.4.16; EC 2.1.3.2 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see paper)
24% identity, 44% coverage: 10:239/526 of query aligns to 228:449/2214 of P07259

query
sites
P07259

R

R

I

I

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L

I

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L

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-

R

R

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F

R

I

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G

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E

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W

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D

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-

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I

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L

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S

G

N

G

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P

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D

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G

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T

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L

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A

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G

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T

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G

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M

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A

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C

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P

P

I

L

A

F

G

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M

N

A

A

N

N

E

D

D

D

K

S

N

N

-

E

-

G

-

I

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Y

-

H

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E

-

L

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F

Y

Y

F

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Q

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F

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T

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T

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T

R

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M

F

L

L

E

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R

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F

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A

C

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Q

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K

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T

T

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Q

-

V

-

L

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K

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P

-

I

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A

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F

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-

G

N

G

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E

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V

V

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K

K

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E

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A

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K

Q

V

V

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M

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L

L

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G

L

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S

S

G

G

V

L

Sites not aligning to the query:

1857 modified: Phosphoserine; by PKA

1ce8B Carbamoyl phosphate synthetase from escherichis coli with complexed with the allosteric ligand imp (see paper)
25% identity, 33% coverage: 11:186/526 of query aligns to 193:356/379 of 1ce8B

query
sites
1ce8B

I

V

L

V

I

A

L

Y

D

D

F

F

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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

I

R

G

G

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C

Y

R

C

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I

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V

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P

W

A

D

Q

I

T

D

S

A

A

K

E

D

D

V

V

E

L

A

K

F

M

G

N

A

P

R

D

G

G

I

I

I

F

L

L

S

S

G

N

G

G

P

P

E

-

T

-

V

-

T

-

G

G

E

D

D

P

S

A

P

P

-

C

-

D

-

Y

-

A

-

I

V

T

A

A

P

I

D

Q

I

K

V

F

F

L

Q

E

L

T

G

D

V

I

P

P

V

V

L

F

G

G

I

I

C
|
C

Y

L

G

G

M

H

Q

Q

T

L

M

L

A

A

E

L

Q

A

L

S

G

G

G

A

K

K

V

T

I

V

S

-

T

-

E

K

H

M

E

K

Y

F

G

G

Y

H

A

-

Q

-

V

-

R

-

A

-

H

H

G

G

H

G

T

N

K

H

L

P

L

V

G

K

E

D

I

V

E

E

D

K

E

N

V

V

T

-

P

-

E

-

G

-

Y

-

G

-

M

V

L

M

D

I

V

T

W

A

M

Q

S

N

H

H

G

G

D

F

R

A

V

V

E

D

-

E

-

A

S

T

M

L

P

P

D

A

G

N

F

L

K

R

L

V

M

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-

H

A

K

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S

T

L

P

F

S

D

C

G

P

T

I

L

A

Q

G

G

M

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A

H

N

R

E

T

D

D

K

K

N

P

F

A

Y

F

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S

I

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Q

F

G

H
|
H

P

P

E
|
E

V

A

T

S

active site: C268 (= C87), H352 (= H182), E354 (= E184)

Sites not aligning to the query:

binding L-ornithine: 119, 122

Query Sequence

>WP_019556800.1 NCBI__GCF_000381085.1:WP_019556800.1
MTQANIHDHRILILDFGSQYTQLIARRIREIGVYCEVEPWDIDAKDVEAFGARGIILSGG
PETVTGEDSPVAPDIVFQLGVPVLGICYGMQTMAEQLGGKVISSTEHEYGYAQVRAHGHT
KLLGEIEDEVTPEGYGMLDVWMSHGDRVESMPDGFKLMASTPSCPIAGMANEDKNFYGIQ
FHPEVTHTKQGLRMLERFVITLCGCQKLWTTENIIEDSVKKVRELVGSDQVMLGLSGGVD
SSVVAALLHKAIGDQLTCVFVDHGLLRYKEGDQVMAMFAENMGLRVIRADVEERFMAALA
GETDPEKKRKIIGHEFIEVFDAESTKLQGVKWLAQGTIYPDVIESAGSKTGKAKVIKSHH
NVGGLPDDMDMSLIEPLRELFKDEVRKLGVALGLPYNMVYRHPFPGPGLGVRILGEVKKE
YADILRLADNIYIEELVKWELYDKTSQAFTVFLPVKSVGVVGDARRYDYVVALRAVETID
FMTARWAHLPYEFLEHVSGRIINEIPRISRVVYDISSKPPATIEWE

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