SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing WP_013010467.1 NCBI__GCF_000025725.1:WP_013010467.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.

Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures

Found 20 (the maximum) hits to proteins with known functional sites (download)

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)
43% identity, 97% coverage: 1:180/186 of query aligns to 1:186/187 of P00903

query
sites
P00903

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C79 (= C75) mutation to S: 10000-fold decrease in catalytic efficiency.
H168 (= H162) mutation to Q: Loss of activity.
E170 (= E164) 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)
37% identity, 97% coverage: 2:181/186 of query aligns to 75:266/276 of Q42565

query
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Q42565

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G150 (= G73) mutation to D: In trp4-1; no visible phenotype under normal growth conditions.
G176 (= G98) mutation to E: In wei7-2; insensitive to inhibition of root elongation by ethylene.

P00900 Anthranilate synthase component 2; AS; ASII; Anthranilate synthase, GATase component; Anthranilate synthase, glutamine amidotransferase component; EC 4.1.3.27 from Serratia marcescens (see 3 papers)
36% identity, 96% coverage: 2:179/186 of query aligns to 4:187/193 of P00900

query
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P00900

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C84 (= C75) 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)
36% identity, 96% coverage: 2:179/186 of query aligns to 3:186/192 of 1i7qB

query
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1i7qB

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active site: G58 (≠ S50), C83 (= C75), L84 (= L76), H169 (= H162), E171 (= E164)
binding glutamic acid: P55 (= P47), G56 (= G48), G58 (≠ S50), C83 (= C75), L84 (= L76), Q87 (= Q79), H132 (= H125), S133 (= S126), L134 (= L127)

8hx8A Crystal structure of 4-amino-4-deoxychorismate synthase from streptomyces venezuelae co-crystallized with chorismate (see paper)
37% identity, 96% coverage: 3:181/186 of query aligns to 7:190/673 of 8hx8A

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8hx8A

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binding magnesium ion: I175 (= I166), S177 (= S168)

Sites not aligning to the query:

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

7yc6A Crystal structure of d110p mutant of gatase subunit of methanocaldococcus jannaschii gmp synthetase
29% identity, 98% coverage: 1:183/186 of query aligns to 1:179/183 of 7yc6A

query
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7yc6A

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binding zinc ion: C76 (= C75), D101 (≠ T106), E123 (≠ A128), E123 (≠ A128), H136 (≠ A140), C140 (≠ G144), C140 (≠ G144), H158 (= H162)

8hx9A Crystal structure of 4-amino-4-deoxychorismate synthase from streptomyces venezuelae with chorismate (see paper)
32% identity, 96% coverage: 3:181/186 of query aligns to 6:147/632 of 8hx9A

query
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8hx9A

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K

-

D

D

A

A

N

D

-

W

-

S

-

R

-

L

-

P

-

V

-

E

E

D

Y

F

Q

D

G

A

I

I

I

V

L

V

S

S

P

P

G

-

P

-

S

-

N

-

P

R

A

A

N

I

S

T

G

D

S

S

T

G

L

L

E

-

Y

-

L

-

D

-

K

-

Y

-

A

-

G

-

R

-

T

-

P

P

I

V

F

L

G

G

V

V

C

C

L

L

G

-

M

-

Q

-

S

-

I

-

G

-

H

-

Y

-

L

-

G

-

Y

-

E

-

V

-

R

-

A

-

K

-

S

-

V

-

M

M

H

H

G

G

K

R

V

V

D

S

N

E

I

V

K

R

L

H

T

T

G

G

D

E

S

D

K

-

I

V

L

F

S

R

G

G

V

L

K

P

D

S

D

P

F

F

A

T

T

A

V

V

R

R

Y

Y

H

H

S

-

L

-

A

-

V

-

A

-

P

-

E

D

E

E

M

L

I

E

I

P

A

L

K

A

A

W

S

S

A

D

D

D

G

G

E

V

C

V

M

M

A

G

I

L

E

R

D

H

D

R

S

E

K

K

L

P

L

L

Y

W

G

G

V

V

Q

Q

F

F

H

H

P

P

E

E

S

S

I

I

L

G

S
|
S

E
x
D

H

F

G

G

D

R

S

E

I

I

V

M

K

A

N

N

F

F

M

R

N

D

I

L

binding magnesium ion: S134 (= S168), D135 (≠ E169)

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

1gpmA Escherichia coli gmp synthetase complexed with amp and pyrophosphate (see paper)
27% identity, 85% coverage: 29:186/186 of query aligns to 39:204/501 of 1gpmA

query
sites
1gpmA

I

V

R

T

N

E

T

A

E

Q

Y

I

K

R

D

D

A

F

N

N

E

P

Y

-

Q

S

G

G

I

I

L

L

S

S

P

G

G
|
G

P

P

-

E

-

S

S

T

N

T

P

E

A

E

N

N

S

S

G

P

S

R

T

A

L

P

E

Q

Y

Y

L

V

D

-

K

-

Y

F

A

E

G

A

R

G

T

V

P

P

I

V

F

F

G

G

V

V

C
|
C

L
x
Y

G

G

M

M

Q

Q

S

T

I

M

G

A

H

M

Y

Q

L

L

G

G

Y

G

E

H

V

V

R

E

R

A

A

S

K

N

S

E

V

R

M

E

H

F

G

G

K

Y

V

A

D

-

N

Q

I

V

K

E

L

V

T

V

G

N

D

D

S

S

K

A

I

L

L

V

S

R

G

G

V

I

K

E

D

D

D

A

F

L

A

T

T

A

-

D

-

G

-

K

-

P

-

L

-

D

-

V

-

W

V

M

R

S

Y

H

H

G

S

D

L

K

A

V

V

T

A

A

A

I

P

P

E

S

E

D

M

F

I

I

I

T

A

V

K

A

A

S

S

T

A

E

D

S

G

C

E

P

C

F

M

A

A

I

I

M

E

A

D

N

D

E

S

E

K

K

L

R

L

F

Y

Y

G

G

V

V

Q

Q

F

F

H
|
H

P

P

E
|
E

S

V

I

T

L

H

S

T

E

R

H

Q

G

G

D

M

S

R

I

M

V

L

K

E

N

R

F

F

M

V

-

R

N

D

I

I

C

C

G

Q

V

C

E

E

A

A

active site: G57 (= G48), C84 (= C75), Y85 (≠ L76), H179 (= H162), E181 (= E164)

Sites not aligning to the query:

active site: 237, 357
binding adenosine monophosphate: 231, 232, 233, 258, 313
binding pyrophosphate 2-: 233, 235, 236, 237, 238, 357

2ywcA Crystal structure of gmp synthetase from thermus thermophilus in complex with xmp
29% identity, 78% coverage: 41:185/186 of query aligns to 44:187/475 of 2ywcA

query
sites
2ywcA

Q

Q

G

A

I

L

I

I

L

L

S

S

P

G

G
|
G

P

P

S
x
R

N

S

P

V

A

F

N

D

S

P

G

D

S

A

T

P

L

R

E

P

Y

D

L

P

D

R

K

L

Y

F

A

S

G

S

R

G

T

L

P

P

I

L

F

L

G

G

V

I

C
|
C

L
x
Y

G

G

M

M

Q

Q

S

L

I

L

G

A

H

Q

Y

E

L

L

G

G

Y

G

E

R

V

V

R

E

R

R

A

A

K

G

S

R

V

A

M

E

H

Y

G

G

K

K

V

A

D

L

N

L

I

T

K

R

L

H

T

E

G

G

D

-

S

-

K

P

I

L

L

F

S

R

G

G

V

L

K

E

D

G

D

E

F

V

A

Q

T

V

V

W

R

M

Y

S

H

H

S

Q

L

D

A

A

V

V

A

T

A

A

P

P

E

P

-

G

M

W

I

R

I

V

A

V

K

A

A

E

S

T

A

E

D

E

G

N

E

P

C

V

M

A

A

A

I

I

E

A

D

S

D

P

S

D

K

G

L

R

L

A

Y

Y

G

G

V

V

Q

Q

F

F

H
|
H

P

P

E
|
E

S

V

I

A

L

H

S

T

E

P

H

K

G

G

D

M

S

Q

I

I

V

L

K

E

N

N

F

F

M

L

N

E

I

L

C

A

G

G

V

V

E

K

active site: G51 (= G48), R53 (≠ S50), C78 (= C75), Y79 (≠ L76), H164 (= H162), E166 (= E164)

Sites not aligning to the query:

active site: 221, 343
binding xanthosine-5'-monophosphate: 288, 366, 367, 368, 408, 467, 471, 472, 473

3uowA Crystal structure of pf10_0123, a gmp synthetase from plasmodium falciparum
28% identity, 97% coverage: 3:182/186 of query aligns to 4:219/517 of 3uowA

query
sites
3uowA

L

I

M

L

V

V

D

L

N

N

Y

F

D

G

S

S

F

Q

T

Y

Y

F

N

H

L

L

V

I

A

V

L

K

F

-

R

R

L

L

N

N

G

N

A

I

K

K

V

I

D

F

V

S

-

E

-

T

-

K

-

D

-

Y

-

G

I

V

R

E

N

L

T

K

E

D

Y

I

K

K

D

D

A

M

N

N

E

-

Y

I

Q

K

G

G

I

V

I

I

L

L

S

S

P

G

G
|
G

P

P

S

Y

N

S

P

V

A

T

N

E

S

A

G

G

S

S

-

P

-

H

-

L

-

K

-

E

T

V

L

F

E

E

Y

Y

L

F

D

-

K

-

Y

L

A

E

G

K

R

K

T

I

P

P

I

I

F

F

G

G

V

I

C
|
C

L
x
Y

G

G

M

M

Q

Q

S

E

I

I

G

A

H

V

Y

Q

L

M

G

N

Y

G

E

E

V

V

R

K

A

S

K

K

S

T

V

S

M

E

H

Y

G

G

-

C

-

T

-

D

-

V

-

N

-

I

-

L

K

R

V

N

D

D

N

N

I

I

K

N

-

N

-

I

-

T

-

Y

-

C

-

R

-

N

-

F

-

S

-

A

-

M

-

D

L

L

T

Y

G

S

D

N

S

Y

K

K

I

L

L

M

S

N

-

C

-

L

-

F

-

E

G

N

V

I

K

K

D

S

D

D

F

I

A

T

T

T

V

V

-

W

-

M

R

N

Y

H

H

N

S

D

L

E

A

V

V

T

A

K

A

I

P

P

E

E

E

N

M

F

I

Y

I

L

A

V

K

S

A

S

S

S

A

E

D

N

G

C

E

L

C

I

M

C

A

S

I

I

E

Y

D

N

D

K

S

E

K

Y

L

N

L

I

Y

Y

G

G

V

V

Q

Q

F

Y

H
|
H

P

P

E
|
E

S

V

I

Y

L

E

S

S

E

L

H

D

G

G

D

E

S

L

I

M

V

F

K

Y

N

N

F

F

-

A

M

Y

N

N

I

I

C

C

active site: G53 (= G48), C84 (= C75), Y85 (≠ L76), H198 (= H162), E200 (= E164)

Sites not aligning to the query:

active site: 255, 381
binding xanthosine-5'-monophosphate: 325, 404, 405, 406, 446, 509, 513, 514, 515

Q8IJR9 GMP synthase [glutamine-hydrolyzing]; PfGMPS; Glutamine amidotransferase; Guanosine monophosphate synthetase; EC 6.3.5.2 from Plasmodium falciparum (isolate 3D7) (see 3 papers)
27% identity, 97% coverage: 3:182/186 of query aligns to 9:229/555 of Q8IJR9

query
sites
Q8IJR9

L

I

M

L

V

V

D

L

N

N

Y

F

D

G

S

S

F

Q

T
x
Y

Y

F

N
x
H

L

L

V

I

A

V

L
x
K

F

-

R
|
R

L

L

N

N

G

N

A

I

K

K

V

I

D

F

V

S

-

E

-

T

-

K

-

D

-

Y

-

G

I

V

R

E

N

L

T

K

E

D

Y

I

K

K

D

D

A

M

N

N

E

-

Y

I

Q

K

G

G

I

V

I

I

L

L

S

S

P

G

G

G

P

P

S

Y

N

S

P

V

A

T

N

E

S

A

G

G

S

S

-

P

-

H

-

L

-

K

-

E

T

V

L

F

E

E

Y

Y

L

F

D

-

K

-

Y

L

A

E

G

K

R

K

T

I

P

P

I

I

F

F

G

G

V

I

C
|
C

L

Y

G

G

M

M

Q
|
Q

S

E

I

I

G

A

H

V

Y

Q

L

M

G

N

Y

G

E

E

V

V

R

K

A

S

K

K

S

T

V

S

M

E

H

Y

G

G

K
x
C

V

T

D

D

-

V

-

N

-

I

-

L

-

R

-

N

-

D

-

N

-

I

-

N

-

I

-

T

-

Y

-

C

-

R

-

N

-

F

-

G

-

D

-

S

-

A

-

M

-

D

-

L

-

Y

-

S

N

N

I

Y

K

K

L

L

T

M

G

N

D

E

S

T

K

C

I

C

L

L

-

F

S

E

G

N

V

I

K
|
K

D

S

D

D

F

I

A

T

T

T

V

V

-
x
W

-

M

R
x
N

Y

H

H

N

S
x
D

L

E

A

V

V

T

A

K

A

I

P

P

E

E

E

N

M

F

I

Y

I

L

A

V

K

S

A

S

S

S

A

E

D

N

G

C

E

L

C

I

M

C

A

S

I

I

E

Y

D

N

D

K

S

E

K

Y

L

N

L

I

Y

Y

G

G

V

V

Q

Q

F

Y

H
|
H

P

P

E

E

S

V

I
x
Y

L
x
E

S

S

E

L

H

D

G

G

D

E

S

L

I

M

V

F

K

Y

N

N

F

F

-

A

M

Y

N

N

I

I

C

C

Y18 (≠ T12) mutation to F: Slight increase in affinity for glutamine. No defect in glutaminase activity.
H20 (≠ N14) 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 (≠ L18) 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 (= R20) mutation to L: No effect on glutaminase activity. 1.4-fold decrease in affinity for glutamine.
C89 (= C75) 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 (= Q79) binding L-glutamine
C113 (≠ K99) 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 (= K116) 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 (vs. gap) mutation to F: Slight decrease in affinity for glutamine. Slight increase in glutaminase activity.
N169 (≠ R123) binding L-glutamine; mutation to S: Slight increase in affinity for glutamine. No defect in glutaminase activity.
D172 (≠ S126) binding L-glutamine; mutation to A: 172-fold decrease in affinity for glutamine. Severe loss of glutaminase activity.
H208 (= H162) binding L-glutamine
Y212 (≠ I166) mutation to W: 2.7-fold decrease in affinity for glutamine. No defect in glutaminase activity.
E213 (≠ L167) 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.

P49915 GMP synthase [glutamine-hydrolyzing]; GMP synthetase; Glutamine amidotransferase; EC 6.3.5.2 from Homo sapiens (Human) (see paper)
29% identity, 75% coverage: 40:179/186 of query aligns to 69:207/693 of P49915

query
sites
P49915

Y

F

Q

R

G

A

I

I

L

I

S

S

P

G

G

G

P

P

S

N

N

S

P

V

A

Y

N

A

S

E

G

D

S

A

T

P

L

W

E

F

Y

D

L

P

D

A

K

I

Y

F

A

T

G

I

R

G

T

K

P

P

I

V

F

L

G

G

V

I

C
|
C

L

Y

G

G

M

M

Q

Q

S

M

I

M

G

N

H

K

Y

V

L

F

G

G

Y

G

E

T

V

V

R

H

R

K

A

-

K

K

S

S

V

V

M

R

H

E

G

D

K

G

V

V

D

F

N

N

I

I

K

S

L

V

T

D

G

N

D

T

S

C

K

S

I

L

L

F

S

R

G

G

V

L

K

Q

D

K

D

E

F

E

A

V

T

V

V

L

R

L

Y

T

H

H

S

G

L

D

A

S

V

V

A

D

A

K

P

V

E

A

E

D

M

G

I

F

I

K

A

V

K

V

A

A

S

R

A

S

D

G

G

N

E

I

C

V

M

A

A

G

I

I

E

A

D

N

D

E

S

S

K

K

L

K

L

L

Y

Y

G

G

V

A

Q

Q

F

F

H
|
H

P

P

E
|
E

S

V

I

G

L

L

S

T

E

E

H

N

G

G

D

K

S

V

I

I

V

L

K

K

N

N

F

F

M

L

C104 (= C75) active site, For GATase activity
H190 (= H162) active site, For GATase activity
E192 (= E164) 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

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, 83% coverage: 11:164/186 of query aligns to 185:338/2225 of P27708

query
sites
P27708

F

L

T

K

Y

Y

N

N

L

Q

V

I

A

R

L

C

F

L

R

C

L

Q

N

R

G

G

A

A

K

E

V

V

D

T

V

V

I

V

R

P

N

W

T

D

E

H

Y

A

K

L

D

D

A

S

N

Q

E

E

Y

Y

Q

E

G

G

I

L

I

F

L

L

S

S

P

N

G

G

P

P

S

G

N

D

P

P

A

A

N

S

S

Y

G

P

S

S

T

V

L

V

E

S

Y

T

L

L

D

S

K

R

Y

V

A

L

G

S

R

E

T

P

-

N

-

P

-

R

P

P

I

V

F

F

G

G

V

I

C

C

L

L

G

G

M

H

Q

Q

S

L

I

L

G

A

H

L

Y

A

L

I

G

G

Y

A

E

K

V

T

R

Y

R

K

A

M

K

R

S

Y

V

G

M

N

H

R

G

G

K

H

V

N

D

Q

N

P

I

C

K

L

L

L

T

V

G

G

D

S

S

G

K

R

I

C

L

-

S

-

G

-

V

-

K

-

D

-

F

F

A

L

T

T

V

S

R

Q

Y

N

H

H

S

G

L

F

A

A

V

V

-

E

-

T

-

D

A

S

A

L

P

P

E

A

E

D

M

W

I

A

I

P

A

L

K

F

A

T

S

N

A

A

-

N

D

D

G

G

E

S

C

N

M

E

A

G

I

I

E

V

D

H

D

N

S

S

K

L

L

P

L

F

Y

F

G

S

V

V

Q

Q

F

F

H

H

P

P

E

E

Sites not aligning to the query:

1 modified: Initiator methionine, Removed
2 modified: N-acetylalanine
33 M → R: in DEE50; uncertain significance; dbSNP:rs751610198
177 R → Q: in a colorectal cancer sample; somatic mutation; dbSNP:rs374122292
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

3uowB Crystal structure of pf10_0123, a gmp synthetase from plasmodium falciparum
29% identity, 97% coverage: 3:182/186 of query aligns to 2:183/477 of 3uowB

query
sites
3uowB

L

I

M

L

V

V

D

L

N

N

Y

F

D

G

S

S

F

Q

T

Y

Y

F

N

H

L

L

V

I

A

V

L

K

F

-

R

R

L

L

N

N

G

N

A

I

K

K

V

I

D

-

V

F

I

S

R

E

N

T

T

K

E

D

Y

Y

K

K

D

D

A

I

N

K

E

D

Y

M

-

N

-

I

Q

K

G

G

I

V

I

I

L

L

S

S

P

G

G
|
G

P

P

S

Y

N

-

P

-

A

-

N

-

S

-

G

S

S

E

T

V

L

F

E

E

Y

Y

L

F

D

-

K

-

Y

L

A

E

G

K

R

K

T

I

P

P

I

I

F

F

G

G

V

I

C
|
C

L
x
Y

G

G

M

M

Q

Q

S

E

I

I

G

A

H

V

Y

Q

L

M

G

N

Y

Y

E

G

V

C

R

T

-

D

-

V

-

N

-

I

R

N

A

I

K

N

S

N

V

I

M

T

H

Y

G

C

K

A

V

M

D

D

-

L

-

Y

-

S

N

N

I

Y

K

K

L

L

T

M

G

-

D

N

S

C

K

C

I

L

L

F

S

E

G

N

V

I

K

K

D

S

D

D

F

I

A

T

T

T

V

V

-

W

-

M

R

N

Y

H

H

N

S

D

L

E

A

V

V

T

A

K

A

I

P

P

E

E

E

N

M

F

I

Y

I

L

A

V

K

S

A

S

S

S

A

E

D

N

G

C

E

L

C

I

M

C

A

S

I

I

E

Y

D

N

D

K

S

E

K

Y

L

N

L

I

Y

Y

G

G

V

V

Q

Q

F

Y

H
|
H

P

P

E
|
E

S

V

I

Y

L

E

S

S

E

L

H

D

G

G

D

E

S

L

I

M

V

F

K

Y

N

N

F

F

-

A

M

Y

N

N

I

I

C

C

active site: G47 (= G48), C67 (= C75), Y68 (≠ L76), H162 (= H162), E164 (= E164)

Sites not aligning to the query:

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

5tw7F Crystal structure of a gmp synthase (glutamine-hydrolyzing) from neisseria gonorrhoeae
29% identity, 78% coverage: 41:185/186 of query aligns to 48:195/490 of 5tw7F

query
sites
5tw7F

Q

K

G

G

I

I

L

L

S

S

P

G

G
|
G

P

P

S

N

N

S

P

-

A

-

N

-

S

-

G

-

S

-

T

-

L

-

E

V

Y

Y

L

E

D

S

K

D

Y

Y

A

Q

G

A

R

D

T

T

-

G

-

I

-

F

-

D

-

L

-

G

-

I

P

P

I

V

F

L

G

G

V

I

C
|
C

L
x
Y

G

G

M

M

Q

Q

S

F

I

M

G

A

H

H

Y

H

L

L

G

G

Y

G

E

E

V

V

R

Q

R

P

A

G

K

N

S

Q

V

R

M

E

H

F

G

G

K

Y

V

A

D

-

N

Q

I

V

K

K

L

-

T

T

G

I

D

D

S

S

K

G

I

L

L

T

S

R

G

G

V

I

K

Q

D

D

-

A

-

P

-

N

-

T

F

L

A

D

T

V

V

W

R

M

Y

S

H

H

S

G

L

D

A

K

V

V

A

S

A

K

-

L

P

P

E

D

E

G

M

F

I

A

I

V

A

I

K

G

A

D

S

T

A

P

D

S

G

C

E

P

C

I

M

A

A

M

I

M

E

E

D

N

D

T

S

E

K

K

L

Q

L

F

Y

Y

G

G

V

I

Q

Q

F

F

H
|
H

P

P

E
|
E

S

V

I

T

L

H

S

T

E

K

H

Q

G

G

D

R

S

A

I

L

V

L

K

N

N

R

F

F

-

V

M

L

N

D

I

I

C

C

G

G

V

A

E

Q

active site: G55 (= G48), C81 (= C75), Y82 (≠ L76), H171 (= H162), E173 (= E164)

Sites not aligning to the query:

active site: 229, 345
binding magnesium ion: 466, 469, 472

4wioA Crystal structure of the c89a gmp synthetase inactive mutant from plasmodium falciparum in complex with glutamine (see paper)
27% identity, 97% coverage: 3:182/186 of query aligns to 3:218/525 of 4wioA

query
sites
4wioA

L

I

M

L

V

V

D

L

N

N

Y

F

D

G

S

S

F

Q

T

Y

Y

F

N

H

L

L

V

I

A

V

L

K

F

-

R

R

L

L

N

N

G

N

A

I

K

K

V

I

D

F

V

S

-

E

-

T

-

K

-

D

-

Y

-

G

I

V

R

E

N

L

T

K

E

D

Y

I

K

K

D

D

A

M

N

N

E

-

Y

I

Q

K

G

G

I

V

I

I

L

L

S

S

P

G

G
|
G

P

P

S

Y

N

S

P

V

A

T

N

E

S

A

G

G

S

S

-

P

-

H

-

L

-

K

-

E

T

V

L

F

E

E

Y

Y

L

F

D

-

K

-

Y

L

A

E

G

K

R

K

T

I

P

P

I

I

F

F

G

G

V

I

C
x
A

L
x
Y

G

G

M

M

Q
|
Q

S

E

I

I

G

A

H

V

Y

Q

L

M

G

N

Y

G

E

E

V

V

R

K

A

S

K

K

S

T

V

S

M

E

H

Y

G

G

K

C

V

T

D

D

-

V

-

N

-

I

-

L

-

R

-

N

-

D

-

N

-

I

-

N

-

I

-

T

-

Y

-

C

-

R

-

N

-

F

-

S

-

A

-

M

-

D

-

L

-

Y

-

S

N

N

I

Y

K

K

L

L

T

M

G

N

D

E

S

C

K

-

I

L

L

F

S

E

G

N

V

I

K

K

D

S

D

D

F

I

A

T

T

T

V

V

-

W

-

M

R
x
N

Y
x
H

H
x
N

S
x
D

L

E

A

V

V

T

A

K

A

I

P

P

E

E

E

N

M

F

I

Y

I

L

A

V

K

S

A

S

S

S

A

E

D

N

G

C

E

L

C

I

M

C

A

S

I

I

E

Y

D

N

D

K

S

E

K

Y

L

N

L

I

Y

Y

G

G

V

V

Q

Q

F

Y

H
|
H

P

P

E
|
E

S

V

I

Y

L

E

S

S

E

L

H

D

G

G

D

E

S

L

I

M

V

F

K

Y

N

N

F

F

-

A

M

Y

N

N

I

I

C

C

active site: G52 (= G48), A83 (≠ C75), Y84 (≠ L76), H197 (= H162), E199 (= E164)
binding glutamine: Q87 (= Q79), N158 (≠ R123), H159 (≠ Y124), N160 (≠ H125), D161 (≠ S126), H197 (= H162)

Sites not aligning to the query:

active site: 255, 393

2vxoB Human gmp synthetase in complex with xmp (see paper)
27% identity, 75% coverage: 40:179/186 of query aligns to 47:182/658 of 2vxoB

query
sites
2vxoB

Y

F

Q

R

G

A

I

I

L

I

S

S

P

G

G
|
G

P

P

S

N

N

S

P

V

A

Y

N

A

S

E

G

D

S

A

T

P

L

W

E

F

Y

D

L

P

D

A

K

I

Y

F

A

T

G

I

R

G

T

K

P

P

I

V

F

L

G

G

V

I

C
|
C

L
x
Y

G

G

M

M

Q

Q

S

M

I

M

G

N

H

K

Y

V

L

F

G

G

Y

-

E

-

V

-

R

-

A

-

K

-

S

G

V

T

M

V

H

H

G

K

K

K

V

S

D

D

-

G

-

V

-

F

N

N

I

I

K

S

L

V

T

D

G

N

D

T

S

C

K

S

I

L

L

F

S

R

G

G

V

L

K

Q

D

K

D

E

F

E

A

V

T

V

V

L

R

L

Y

T

H

H

S

G

L

D

A

S

V

V

A

D

A

K

P

V

E

A

E

D

M

G

I

F

I

K

A

V

K

V

A

A

S

R

A

S

D

G

G

N

E

I

C

V

M

A

A

G

I

I

E

A

D

N

D

E

S

S

K

K

L

K

L

L

Y

Y

G

G

V

A

Q

Q

F

F

H
|
H

P

P

E
|
E

S

V

I

G

L

L

S

T

E

E

H

N

G

G

D

K

S

V

I

I

V

L

K

K

N

N

F

F

M

L

active site: G55 (= G48), C82 (= C75), Y83 (≠ L76), H165 (= H162), E167 (= E164)

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

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, 83% coverage: 11:164/186 of query aligns to 185:338/2225 of P08955

query
sites
P08955

F

L

T

K

Y

Y

N

N

L

Q

V

I

A

R

L

C

F

L

R

C

L

Q

N

L

G

G

A

A

K

E

V

V

D

T

V

V

I

V

R

P

N

W

T

N

E

H

Y

E

K

L

D

D

A

S

N

Q

E

K

Y

Y

Q

D

G

G

I

L

I

F

L

L

S

S

P

N

G

G

P

P

S

G

N

D

P

P

A

A

N

S

S

Y

G

P

S

G

T

V

L

V

E

A

Y

T

L

L

D

N

K

R

Y

V

A

L

G

S

R

E

T

P

-

N

-

P

-

R

P

P

I

V

F

F

G

G

V

I

C

C

L

L

G

G

M

H

Q

Q

S

L

I

L

G

A

H

L

Y

A

L

I

G

G

Y

A

E

K

V

T

R

Y

R

K

A

M

K

R

S

Y

V

G

M

N

H

R

G

G

K

H

V

N

D

Q

N

P

I

C

K

L

L

L

T

V

G

G

D

T

S

G

K

R

I

C

L

-

S

-

G

-

V

-

K

-

D

-

F

F

A

L

T

T

V

S

R

Q

Y

N

H

H

S

G

L

F

A

A

V

V

A

D

A

A

-

D

-

S

-

L

P

P

E

A

E

G

M

W

I

T

I

P

A

L

K

F

A

T

S

N

A

A

-

N

D

D

G

C

E

S

C

N

M

E

A

G

I

I

E

V

D

H

D

D

S

S

K

L

L

P

L

F

Y

F

G

S

V

V

Q

Q

F

F

H

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)
24% identity, 75% coverage: 42:181/186 of query aligns to 285:422/430 of Q9LVW7

query
sites
Q9LVW7

G

G

I

I

I

L

L

F

S

S

P

N

G

G

P

P

S

G

N

D

P

P

A

S

N

A

S

V

G

P

S

Y

T

A

L

V

E

E

Y

T

L

V

D

K

K

E

Y

L

A

L

G

G

R

K

T

V

P

P

I

V

F

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G

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H

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A

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|
H

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H410 (= H170) mutation to Y: In ven6-1; reticulate leaf phenotype.

P20054 Multifunctional protein pyr1-3; 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 Dictyostelium discoideum (Social amoeba)
27% identity, 84% coverage: 27:183/186 of query aligns to 227:384/2225 of P20054

query
sites
P20054

D

D

V

V

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R

A

N

N

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E

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N

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A

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A

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Sites not aligning to the query:

1 modified: N-acetylmethionine

Query Sequence

>WP_013010467.1 NCBI__GCF_000025725.1:WP_013010467.1
MFLMVDNYDSFTYNLVALFRLNGAKVDVIRNTEYKDANEYQGIILSPGPSNPANSGSTLE
YLDKYAGRTPIFGVCLGMQSIGHYLGYEVRRAKSVMHGKVDNIKLTGDSKILSGVKDDFA
TVRYHSLAVAAPEEMIIAKASADGECMAIEDDSKLLYGVQFHPESILSEHGDSIVKNFMN
ICGVEA

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