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)
30% identity, 96% coverage: 5:186/189 of query aligns to 8:229/555 of Q8IJR9

query
sites
Q8IJR9

K

K

I

I

L

L

V

V

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L

N

N

N

F

Y

G

G

S

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Q

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x
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H

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C

Y18 (≠ F15) mutation to F: Slight increase in affinity for glutamine. No defect in glutaminase activity.
H20 (= H17) 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 (≠ R21) 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 (≠ A22) mutation to L: No effect on glutaminase activity. 1.4-fold decrease in affinity for glutamine.
C89 (= C79) 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 (= Q83) binding L-glutamine
C113 (≠ E103) 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 (= W125) mutation to F: Slight decrease in affinity for glutamine. Slight increase in glutaminase activity.
N169 (≠ S127) binding L-glutamine; mutation to S: Slight increase in affinity for glutamine. No defect in glutaminase activity.
D172 (= D130) binding L-glutamine; mutation to A: 172-fold decrease in affinity for glutamine. Severe loss of glutaminase activity.
H208 (= H166) binding L-glutamine
Y212 (≠ S170) mutation to W: 2.7-fold decrease in affinity for glutamine. No defect in glutaminase activity.
E213 (≠ H171) 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.

Sites not aligning to the query:

336 binding XMP
371 Important for ATPPase activity; D→A: Impaired formation of adenyl-XMP intermediate. Slight increase in glutaminase activity.
374 E→L: 8.9-fold decrease in affinity for ammonia. Severe loss of glutaminase activity.
376 K→L: 20 percent decrease in glutaminase activity. 4.4-fold decrease in affinity for glutamine. 1.8-fold decrease in affinity for XMP.
386 K→L: Severe loss of ATP pyrophosphatase (ATPPase) activity. 80 percent decrease in glutaminase activity. Impaired GMP formation.
387 T→A: No effect on ATP pyrophosphatase (ATPPase) activity. 20 percent decrease in glutaminase activity. No effect on GMP formation.
388 Important for ATPPase activity; H→A: Moderate decrease in ATP pyrophosphatase (ATPPase) activity. Reduces 49 percent decrease in glutaminase activity. Impaired GMP formation.
389 Important for ATPPase activity; H→A: Loss of ATP pyrophosphatase (ATPPase) activity. 67 percent decrease in glutaminase activity. Impaired GMP formation.
390 N→A: No effect on ATP pyrophosphatase (ATPPase) activity. Increases glutaminase activity. Loss of GMP formation.
411 K→L: 70 percent decrease in glutaminase activity. Loss of GMP formation.
412 D→A: 30 percent decrease in glutaminase activity. 7.9-fold decrease in affinity for glutamine.
413 D→A: 35 percent decrease in glutaminase activity. 3.6-fold decrease in affinity for glutamine.
415 K→L: Increases glutaminase activity. 4.2-fold decrease in affinity for ATP.
476 binding XMP
539 R→L: 85 percent decrease in glutaminase activity.
547 binding XMP; K→L: 85 percent decrease in glutaminase activity.
552 binding XMP
553 binding XMP; E→L: 85 percent decrease in glutaminase activity.
555 E→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)
30% identity, 96% coverage: 5:186/189 of query aligns to 2:218/525 of 4wioA

query
sites
4wioA

K

K

I

I

L

L

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V

V

L

N

N

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F

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Q

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H

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D

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C

active site: G52 (= G55), A83 (≠ C79), Y84 (≠ L80), H197 (= H166), E199 (= E168)
binding glutamine: Q87 (= Q83), N158 (≠ S127), H159 (= H128), N160 (≠ A129), D161 (= D130), H197 (= H166)

Sites not aligning to the query:

active site: 255, 393

P00903 Aminodeoxychorismate synthase component 2; ADC synthase; ADCS; 4-amino-4-deoxychorismate synthase component 2; Aminodeoxychorismate synthase, glutamine amidotransferase component; EC 2.6.1.85 from Escherichia coli (strain K12) (see paper)
34% identity, 94% coverage: 6:183/189 of query aligns to 2:185/187 of P00903

query
sites
P00903

I

I

L

L

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C79 (= C79) mutation to S: 10000-fold decrease in catalytic efficiency.
H168 (= H166) mutation to Q: Loss of activity.
E170 (= E168) 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.

3uowB Crystal structure of pf10_0123, a gmp synthetase from plasmodium falciparum
33% identity, 96% coverage: 5:186/189 of query aligns to 1:183/477 of 3uowB

query
sites
3uowB

K

K

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L

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Y

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Y

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W

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E

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C

active site: G47 (= G55), C67 (= C79), Y68 (≠ L80), H162 (= H166), E164 (= E168)

Sites not aligning to the query:

active site: 218, 340
binding xanthosine-5'-monophosphate: 288, 363, 364, 365, 405, 469, 473, 474, 475

8hx8A Crystal structure of 4-amino-4-deoxychorismate synthase from streptomyces venezuelae co-crystallized with chorismate (see paper)
30% identity, 96% coverage: 2:182/189 of query aligns to 2:187/673 of 8hx8A

query
sites
8hx8A

R

R

E

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D

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S
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x
S

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K

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E

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A

N

N

F

F

binding magnesium ion: I175 (≠ S170), S177 (≠ T172)

Sites not aligning to the query:

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

2vxoB Human gmp synthetase in complex with xmp (see paper)
33% identity, 94% coverage: 6:183/189 of query aligns to 6:182/658 of 2vxoB

query
sites
2vxoB

I

V

L

V

V

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D

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G

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D

A

I

I

L

K

A

E

E

Q

E

G

P

F

D

R

G

A

L

I

I

I

L

I

S

S

G

G

G
|
G

P

P

E

N

M

S

E

V

R

Y

A

A

-

E

-

D

G

A

L

P

C

W

F

F

D

D

-

P

Y

A

V

I

R

F

E

T

I

I

D

G

I

K

P

P

I

V

L

L

G

G

I

I

C
|
C

L
x
Y

G

G

H

M

Q

Q

A

M

I

M

A

N

L

K

A

V

Y

F

G

G

H

T

V

V

H

H

S

K

G

K

K

S

K

D

G

G

G

V

Y

F

A

-

E

-

I

-

E

N

I

I

E

S

V

V

I

D

E

N

E

T

D

C

D

S

I

L

L

F

R

R

G

G

L

L

G

Q

P

K

K

E

I

E

T

V

V

V

W

L

A

L

S

T

H

H

A

G

D

D

E

S

V

V

A

D

I

K

L

V

P

A

E

D

G

G

F

F

I

K

H

V

L

V

A

A

R

R

S

S

D

G

I

N

C

I

E

-

I

V

E

A

A

G

M

I

R

A

H

N

P

E

T

S

K

K

P

K

I

L

Y

Y

G

G

V

A

Q

Q

W

F

H
|
H

P

P

E
|
E

V

V

S

G

H

L

T

T

K

E

K

N

G

G

D

K

E

V

L

I

L

L

T

K

N

N

F

F

F

L

active site: G55 (= G55), C82 (= C79), Y83 (≠ L80), H165 (= H166), E167 (= E168)

Sites not aligning to the query:

active site: 223, 381
binding xanthosine-5'-monophosphate: 302, 348, 349, 404, 405, 406, 489, 575, 610, 650, 654, 655, 656

P49915 GMP synthase [glutamine-hydrolyzing]; GMP synthetase; Glutamine amidotransferase; EC 6.3.5.2 from Homo sapiens (Human) (see paper)
32% identity, 94% coverage: 6:183/189 of query aligns to 28:207/693 of P49915

query
sites
P49915

I

V

L

V

V

I

V

L

N

D

N

A

Y

G

G

A

Q

Q

F

Y

C

G

H

K

L

V

I

I

H

D

R

R

A

R

V

V

R

R

D

E

L

L

D

F

M

V

D

Q

T

S

K

E

I

I

I

F

P

P

N

L

V

E

T

T

P

P

I

A

E

F

D

A

I

I

L

K

A

E

E

Q

E

G

P

F

D

R

G

A

L

I

I

I

L

I

S

S

G

G

P

P

E

N

M

S

E

V

R

Y

A

A

-

E

-

D

G

A

L

P

C

W

F

F

D

D

-

P

Y

A

V

I

R

F

E

T

I

I

D

G

I

K

P

P

I

V

L

L

G

G

I

I

C
|
C

L

Y

G

G

H

M

Q

Q

A

M

I

M

A

N

L

K

A

V

Y

F

G

G

H

T

V

V

H

H

S

K

G

K

K

S

K

V

G

R

G

E

Y

D

A

G

E

V

I

F

E

N

I

I

E

S

V

V

I

D

E

N

E

T

D

C

D

S

I

L

L

F

R

R

G

G

L

L

G

Q

P

K

K

E

I

E

T

V

V

V

W

L

A

L

S

T

H

H

A

G

D

D

E

S

V

V

A

D

I

K

L

V

P

A

E

D

G

G

F

F

I

K

H

V

L

V

A

A

R

R

S

S

D

G

I

N

C

I

E

-

I

V

E

A

A

G

M

I

R

A

H

N

P

E

T

S

K

K

P

K

I

L

Y

Y

G

G

V

A

Q

Q

W

F

H
|
H

P

P

E
|
E

V

V

S

G

H

L

T

T

K

E

K

N

G

G

D

K

E

V

L

I

L

L

T

K

N

N

F

F

F

L

C104 (= C79) active site, For GATase activity
H190 (= H166) active site, For GATase activity
E192 (= E168) active site, For GATase activity

Sites not aligning to the query:

337 binding XMP
522 binding XMP
610 binding XMP
685 binding XMP
691 binding XMP

1ce8B Carbamoyl phosphate synthetase from escherichis coli with complexed with the allosteric ligand imp (see paper)
30% identity, 90% coverage: 19:189/189 of query aligns to 204:376/379 of 1ce8B

query
sites
1ce8B

I

I

H

L

R

R

A

M

V

L

R

V

D

D

L

R

D

G

M

C

D

R

T

L

K

T

I

I

I

V

P

P

N

A

V

Q

T

T

P

S

I

A

E

E

D

D

I

V

L

L

A

K

E

M

E

N

P

P

D

D

G

G

L

I

I

F

L

L

S

S

G

N

G

G

P

P

-

G

-

D

-

P

-

A

E

P

M

C

E

D

R

Y

A

A

G

I

L

T

C

A

F

I

D

Q

Y

K

V

F

R

L

E

E

I

T

D

D

I

I

P

P

I

V

L

F

G

G

I

I

C
|
C

L

L

G

G

H

H

Q

Q

A

L

I

L

A

A

L

L

A

A

Y

S

G

G

G

A

H

K

V

T

H

V

S

K

G

M

K

K

K

F

G

G

G

H

Y

H

-

G

A

G

E

N

I

H

E

P

I

V

E

K

V

D

I

V

E

E

E

K

D

N

D

V

I

V

L

M

R

-

G

-

L

-

G

-

P

-

K

-

I

I

T

T

V

A

W

Q

A

N

-

H

S

G

H

F

A

A

D

V

E

D

V

E

A

A

I

T

L

L

P

P

E

A

G

N

F

L

-

R

-

V

I

T

H

H

L

K

A

S

R

L

S

F

D

D

I

-

C

G

E

T

I

L

E

Q

A

G

M

I

R

H

H

R

P

T

T

D

K

K

P

P

I

A

Y

F

G

S

V

F

Q

Q

W

G

H
|
H

P

P

E
|
E

V

A

S

S

-

P

H

G

T

P

K

H

K

D

G

A

D

A

E

P

L

L

L

F

T

D

N

H

F

F

F

I

E

E

V

L

C

I

D

E

R

Q

Y

Y

active site: C268 (= C79), H352 (= H166), E354 (= E168)

Sites not aligning to the query:

binding L-ornithine: 119, 122

P0A6F1 Carbamoyl phosphate synthase small chain; Carbamoyl phosphate synthetase glutamine chain; EC 6.3.5.5 from Escherichia coli (strain K12) (see paper)
30% identity, 90% coverage: 19:189/189 of query aligns to 205:377/382 of P0A6F1

query
sites
P0A6F1

I

I

H

L

R

R

A

M

V

L

R

V

D

D

L

R

D

G

M

C

D

R

T

L

K

T

I

I

I

V

P

P

N

A

V

Q

T

T

P

S

I

A

E

E

D

D

I

V

L

L

A

K

E

M

E

N

P

P

D

D

G

G

L

I

I

F

L

L

S

S

G

N

G
|
G

P

P

-
x
G

-

D

-

P

-

A

E

P

M

C

E

D

R

Y

A

A

G

I

L

T

C

A

F

I

D

Q

Y

K

V

F

R

L

E

E

I

T

D

D

I

I

P

P

I

V

L

F

G

G

I

I

C

C

L
|
L

G

G

H

H

Q
|
Q

A

L

I

L

A

A

L

L

A

A

Y

S

G

G

G

A

H

K

V

T

H

V

S

K

G

M

K

K

K

F

G

G

G

H

Y

H

-

G

A

G

E

N

I

H

E

P

I

V

E

K

V

D

I

V

E

E

E

K

D

N

D

V

I

V

L

M

R

-

G

-

L

-

G

-

P

-

K

-

I

I

T

T

V

A

W

Q

A
x
N

-

H

S
x
G

H
x
F

A

A

D

V

E

D

V

E

A

A

I

T

L

L

P

P

E

A

G

N

F

L

-

R

-

V

I

T

H

H

L

K

A

S

R

L

S

F

D

D

I

-

C

G

E

T

I

L

E

Q

A

G

M

I

R

H

H

R

P

T

T

D

K

K

P

P

I

A

Y

F

G

S

V

F

Q

Q

W

G

H

H

P

P

E

E

V

A

S

S

-

P

H

G

T

P

K

H

K

D

G

A

D

A

E

P

L

L

L

F

T

D

N

H

F

F

F

I

E

E

V

L

C

I

D

E

R

Q

Y

Y

G241 (= G55) binding L-glutamine
G243 (vs. gap) binding L-glutamine
L270 (= L80) binding L-glutamine
Q273 (= Q83) binding L-glutamine
N311 (≠ A126) binding L-glutamine
G313 (≠ S127) binding L-glutamine
F314 (≠ H128) binding L-glutamine

Sites not aligning to the query:

47 binding L-glutamine

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)
25% identity, 97% coverage: 6:188/189 of query aligns to 75:269/276 of Q42565

query
sites
Q42565

I

I

L

I

V

V

V

I

N

D

N

N

Y

Y

G

D

Q

S

F

F

C

T

H

Y

L

N

I

L

H

C

R

Q

A

Y

V

M

R

G

D

E

L

L

D

G

M

C

D

H

T

F

K

E

I

V

I

Y

P

R

N

N

-

D

V

E

T

L

P

T

I

V

E

E

D

E

I

L

L

K

A

K

E

K

E

N

P

P

D

R

G

G

L

V

I

L

L

I

S

S

G

P

G

G

P

P

E

G

M

T

-

P

E

Q

R

D

A

S

G

G

L

I

C

S

F

L

D

Q

Y

T

V

V

R

L

E

E

I

L

D

G

-

P

-

L

I

V

P

P

I

L

L

F

G
|
G

I

V

C

C

L

M

G

G

H

L

Q

Q

A

C

I

I

A

G

L

E

A

A

Y

F

G

G

H

K

V

I

H

V

S

R

G

S

K

P

-

F

-

G

-

V

-

M

K

H

G
|
G

G

K

Y

S

A

S

E

M

I

V

E

H

I

Y

E

D

V

E

I

K

E

G

E

E

D

E

D

G

I

L

L

F

R

S

G

G

L

L

G

S

P

N

K

P

I

F

T

I

V

V

W

G

A

R

S

Y

H

H

A

S

-

L

-

V

D

I

E

E

V

K

A

D

I

T

L

F

P

P

E

S

G

D

F

E

I

L

H

E

L

V

-

T

A

A

R

W

S

T

D

E

I

D

C

G

E

L

I

V

E

M

A

A

M

A

R

R

H

H

P

R

T

K

-

Y

K

K

P

H

I

I

Y

Q

G

G

V

V

Q

Q

W

F

H

H

P

P

E

E

V

S

S

I

H

I

T

T

K

T

K

E

G

G

D

K

E

T

L

I

L

V

T

R

N

N

F

F

F

I

E

K

V

I

C

V

D

E

R

K

G150 (= G77) mutation to D: In trp4-1; no visible phenotype under normal growth conditions.
G176 (= G99) mutation to E: In wei7-2; insensitive to inhibition of root elongation by ethylene.

P07258 Carbamoyl phosphate synthase arginine-specific small chain; CPS; CPSase; CPSase-arg; Arginine-specific carbamoyl phosphate synthetase, glutamine chain; Carbamoyl phosphate synthase A; CPS-A; Glutamine-dependent carbamoyl phosphate synthetase; EC 6.3.5.5 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see paper)
32% identity, 90% coverage: 19:189/189 of query aligns to 197:373/411 of P07258

query
sites
P07258

I

I

H

I

R

R

A

C

V

L

R

V

D

K

L

R

D

G

M

A

D

N

T

V

K

T

I

V

I

F

P

P

N

Y

V

D

T

Y

P

R

I

I

E

Q

D

D

I

V

L

-

A

A

E

S

E

E

P

F

D

D

G

G

L

I

I

F

L

L

S

S

G

N

G

G

P

P

-

G

E

N

M

P

E

E

R

L

A

C

G

Q

L

A

C

T

F

I

D

S

Y

N

V

V

R

R

E

E

I

L

-

L

-

N

-

P

-

V

-

Y

-

D

D

C

I

I

P

P

I

I

L

F

G

G

I

I

C
|
C

L

L

G

G

H

H

Q

Q

A

L

I

L

A

A

L

L

A

A

Y

S

G

G

G

A

H

S

V

T

H

H

S

K

G

L

K

K

K

Y

G

G

G

N

Y

R

A

A

E

-

I

-

E

-

I

-

E

H

V

N

I

I

E

P

E

A

D

M

D

D

I

L

L

T

R

T

G

G

L

Q

G

C

P

H

K

I

I

T

T

S

V

Q

W

N

A
x
H

S

G

H

Y

A

A

D

V

E

D

V

P

A

E

I

T

L

L

P

P

E

K

G

D

-

Q

-

W

-

K

-

P

-

Y

F

F

I

V

H

N

L

L

A

N

-

D

R

K

S

S

D

N

I

-

C

-

E

-

I

-

E

E

A

G

M

M

R

I

H

H

P

L

T

Q

K

R

P

P

I

I

Y

F

G

S

V

T

Q

Q

W

F

H
|
H

P

P

E

E

V

A

S

-

H

-

T

-

K

-

K

K

G

G

D

G

E

P

L

L

L

D

T

T

-

A

-

I

-

L

-

F

-

D

N

K

F

F

E

D

V

N

C

I

D

E

R

K

Y

Y

C264 (= C79) mutation to D: Abolishes glutamine-dependent CPSase activity.
H307 (≠ A126) mutation to D: Abolishes glutamine-dependent CPSase activity.
H349 (= H166) mutation to D: Abolishes glutamine-dependent CPSase activity.

1c3oB Crystal structure of the carbamoyl phosphate synthetase: small subunit mutant c269s with bound glutamine (see paper)
29% identity, 90% coverage: 19:189/189 of query aligns to 204:376/379 of 1c3oB

query
sites
1c3oB

I

I

H

L

R

R

A

M

V

L

R

V

D

D

L

R

D

G

M

C

D

R

T

L

K

T

I

I

I

V

P

P

N

A

V

Q

T

T

P

S

I

A

E

E

D

D

I

V

L

L

A

K

E

M

E

N

P

P

D

D

G

G

L

I

I

F

L

L

S

S

G
x
N

G
|
G

P

P

-
x
G

-

D

-

P

-

A

E

P

M

C

E

D

R

Y

A

A

G

I

L

T

C

A

F

I

D

Q

Y

K

V

F

R

L

E

E

I

T

D

D

I

I

P

P

I

V

L

F

G

G

I

I

C
x
S

L
|
L

G

G

H

H

Q

Q

A

L

I

L

A

A

L

L

A

A

Y

S

G

G

G

A

H

K

V

T

H

V

S

K

G

M

K

K

K

F

G

G

G

H

Y

H

-

G

A

G

E

N

I

H

E

P

I

V

E

K

V

D

I

V

E

E

E

K

D

N

D

V

I

V

L

M

R

-

G

-

L

-

G

-

P

-

K

-

I

I

T

T

V

A

W

Q

A
x
N

-
x
H

S
x
G

H
x
F

A

A

D

V

E

D

V

E

A

A

I

T

L

L

P

P

E

A

G

N

F

L

-

R

-

V

I

T

H

H

L

K

A

S

R

L

S

F

D

D

I

-

C

G

E

T

I

L

E

Q

A

G

M

I

R

H

H

R

P

T

T

D

K

K

P

P

I

A

Y

F

G

S

V

F

Q

Q

W

G

H
|
H

P

P

E
|
E

V

A

S

S

-

P

H

G

T

P

K

H

K

D

G

A

D

A

E

P

L

L

L

F

T

D

N

H

F

F

F

I

E

E

V

L

C

I

D

E

R

Q

Y

Y

active site: S268 (≠ C79), H352 (= H166), E354 (= E168)
binding glutamine: N239 (≠ G54), G240 (= G55), G242 (vs. gap), S268 (≠ C79), L269 (= L80), N310 (≠ A126), H311 (vs. gap), G312 (≠ S127), F313 (≠ H128)

Sites not aligning to the query:

active site: 201
binding glutamine: 46

8hx9A Crystal structure of 4-amino-4-deoxychorismate synthase from streptomyces venezuelae with chorismate (see paper)
26% identity, 96% coverage: 2:182/189 of query aligns to 1:144/632 of 8hx9A

query
sites
8hx9A

R

R

E

H

L

M

K

R

I

T

L

L

V

L

V

I

N

D

N

N

Y

Y

G

D

Q

S

F

F

C

T

H

H

L

N

I

L

H

F

R

Q

A

Y

V

I

R

G

D

E

L

A

D

T

M

G

D

Q

T

P

K

P

I

V

-

V

P

P

N

N

V

D

T

A

P

D

I

W

E

S

D

R

I

L

L

P

A

V

E

E

E

D

P

F

D

D

G

A

L

I

I

V

L

V

S

S

G

-

P

-

E

-

M

-

E

P

R

R

A

A

G

-

L

-

C

-

F

-

D

-

Y

-

V

I

R

T

E

D

I

S

D

G

I

L

P

P

I

V

L

L

G

G

I

V

C

C

L

L

G

M

H

H

Q

-

A

-

I

-

A

-

L

-

A

-

Y

-

G

-

G

G

H

R

V

V

H

S

S

E

G

V

K

R

K

H

G

T

G

G

Y

-

A

-

E

-

I

-

E

-

I

-

E

-

V

-

I

-

E

-

D

E

D

D

I

V

L

F

R

R

G

G

L

L

G

P

P

S

K

P

I

F

T

T

V

A

W

V

A

R

S

Y

H

H

A

-

D

D

E

E

V

L

A

E

I

-

L

-

P

-

E

-

G

-

F

-

I

-

H

P

L

L

A

A

R

W

S

S

D

D

I

D

C

G

E

V

I

V

E

M

A

G

M

L

R

R

H

H

P

R

T

E

K

K

P

P

I

L

Y

W

G

G

V

V

Q

Q

W

F

H

H

P

P

E

E

V

S

S

I

H

G

T
x
S

K
x
D

K

F

G

G

D

R

E

E

L

I

L

M

T

A

N

N

F

F

binding magnesium ion: S134 (≠ T172), D135 (≠ K173)

Sites not aligning to the query:

binding (3R,4R)-3-[(1-carboxyethenyl)oxy]-4-hydroxycyclohexa-1,5-diene-1-carboxylic acid: 453, 454, 455, 456, 547, 570, 590, 603, 604, 605, 606, 619, 623
binding tryptophan: 189, 190, 191, 199, 201, 419, 420, 421, 574, 575

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)
30% identity, 92% coverage: 6:179/189 of query aligns to 4:183/193 of P00900

query
sites
P00900

I

I

L

L

V

L

N

D

N

N

Y

V

G

D

Q

S

F

F

C

T

H

Y

L

N

I

L

H

V

R

D

A

Q

V

L

R

R

D

A

L

S

D

G

M

H

D

Q

T

V

K

V

I

I

I

Y

P

R

N

N

V

Q

T

I

P

G

I

A

E

E

D

V

I

I

L

I

-

E

-

R

-

L

-

Q

-

H

A

M

E

E

E

Q

P

P

D

V

G

-

L

L

I

M

L

L

S

S

G

P

G

G

P

P

E

G

M

T

E

P

R

S

A

E

G

A

L

G

C

C

F

M

D

P

Y

E

V

L

R

L

E

Q

I

R

-

L

-

R

-

G

D

Q

I

L

P

P

I

I

L

I

G

G

I

I

C
|
C

L

L

G

G

H

H

Q

Q

A

A

I

I

A

V

L

E

A

A

Y

Y

G

G

H

Q

V

V

H

-

S

-

G

G

K

Q

K

A

G

G

G

E

Y

I

A

L

E

H

I

G

E

K

I

A

E

S

V

A

I

I

E

A

E

H

D

D

-

G

-

E

D

G

I

M

L

F

R

A

G

G

L

M

G

A

P

N

K

P

I

L

T

P

V

V

W

A

A

R

S

Y

H

H

A

S

D

L

E

V

V

G

A

S

I

N

L

I

P

P

E

A

G

D

F

L

I

T

H

V

L

N

A

A

R

R

S

S

D

G

I

E

C

M

E

-

I

V

E

M

A

A

M

V

R

R

H

D

P

D

T

R

K

R

P

R

I

V

Y

C

G

G

V

F

Q

Q

W

F

H

H

P

P

E

E

V

S

S

I

H

L

T

T

K

T

K

H

G

G

D

A

E

R

L

L

C84 (= C79) active site, Nucleophile; for GATase activity

Sites not aligning to the query:

1 modified: Initiator methionine, Removed

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)
30% identity, 74% coverage: 44:183/189 of query aligns to 211:353/2225 of P08955

query
sites
P08955

A

S

E

Q

E

K

P

Y

D

D

G

G

L

L

I

F

L

L

S

S

G

N

G

G

P

P

-

G

-

D

E

P

M

A

E

S

R

Y

A

P

G

G

L

V

C

V

F

A

D

T

Y

L

V

N

R

R

E

V

I

L

D

S

-

E

-

P

-

N

-

P

I

R

P

P

I

V

L

F

G

G

I

I

C

C

L

L

G

G

H

H

Q

Q

A

L

I

L

A

A

L

L

A

A

Y

I

G

G

G

A

H

K

V

T

H

Y

S

K

G

M

K

R

K

Y

G

G

G

N

Y

R

A

G

E

H

I

-

E

-

I

-

E

-

V

-

I

-

E

N

E

Q

D

P

D

C

I

L

L

L

R

V

G

G

L

T

G

G

P

R

K

C

I

F

T

L

V

T

W

S

A

Q

S

N

H

H

-

G

-

F

A

A

D

V

E

D

V

A

A

D

I

S

L

L

P

P

E

A

G

G

F

W

I

T

H

P

L

L

-

F

A

T

R

N

S

A

D

N

I

D

C

C

E

S

I

N

E

E

A

G

M

I

R

V

H

H

P

D

T

S

K

L

P

P

I

F

Y

F

G

S

V

V

Q

Q

W

F

H

H

P

P

E

E

V

H

S

R

H

A

T

G

K

P

K

S

G

D

D

M

E

E

L

L

T

F

N

D

F

V

F

F

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.

Query Sequence

>WP_011024463.1 NCBI__GCF_000007345.1:WP_011024463.1
MRELKILVVNNYGQFCHLIHRAVRDLDMDTKIIPNVTPIEDILAEEPDGLILSGGPEMER
AGLCFDYVREIDIPILGICLGHQAIALAYGGHVHSGKKGGYAEIEIEVIEEDDILRGLGP
KITVWASHADEVAILPEGFIHLARSDICEIEAMRHPTKPIYGVQWHPEVSHTKKGDELLT
NFFEVCDRY

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