SitesBLAST

P00968 Carbamoyl phosphate synthase large chain; Carbamoyl phosphate synthetase ammonia chain; EC 6.3.4.16; EC 6.3.5.5 from Escherichia coli (strain K12) (see 6 papers)
45% identity, 92% coverage: 1:971/1058 of query aligns to 1:971/1073 of P00968

query
sites
P00968

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M1 (= M1) modified: Initiator methionine, Removed
R129 (= R129) binding ATP
R169 (= R169) binding ATP
G175 (= G175) binding ATP
G176 (= G176) binding ATP
E208 (≠ R208) binding ATP
L210 (≠ I210) binding ATP
E215 (= E215) binding ATP
G241 (= G241) binding ATP
I242 (= I242) binding ATP
H243 (= H243) binding ATP
Q285 (= Q284) binding ATP; binding Mn(2+)
E299 (= E298) binding ATP; binding Mn(2+); binding Mn(2+)
N301 (= N300) binding Mn(2+)
R715 (= R711) binding ATP
H754 (≠ A749) binding ATP
L756 (≠ Y751) binding ATP
E761 (= E755) binding ATP
G786 (= G780) binding ATP
V787 (= V781) binding ATP
H788 (= H782) binding ATP
S789 (= S783) binding ATP
Q829 (= Q823) binding ATP; binding Mn(2+)
E841 (= E835) binding ATP; binding Mn(2+); binding Mn(2+)
N843 (= N837) binding Mn(2+)

Q42601 Carbamoyl phosphate synthase arginine-specific large chain, chloroplastic; CPS; CPSase; Ammonium-dependent carbamoyl phosphate synthetase; Arginine-specific carbamoyl phosphate synthetase, ammonia chain; Glutamine-dependent carbamoyl phosphate synthetase; Protein VENOSA 3; EC 6.3.4.16; EC 6.3.5.5 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
46% identity, 91% coverage: 5:972/1058 of query aligns to 96:1077/1187 of Q42601

query
sites
Q42601

T

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P149 (≠ E58) mutation to L: In ven3-2; reduced plant size and reticulate leaf phenotype.
G587 (= G492) mutation to E: In ven3-3; reticulate leaf phenotype.
A844 (≠ Q737) mutation to T: In ven3-4; reduced plant size and reticulate leaf phenotype.
P1014 (≠ A905) mutation to L: In ven3-1; reticulate leaf phenotype.

1t36A Crystal structure of e. Coli carbamoyl phosphate synthetase small subunit mutant c248d complexed with uridine 5'-monophosphate (see paper)
45% identity, 92% coverage: 1:971/1058 of query aligns to 1:956/1058 of 1t36A

query
sites
1t36A

M

M

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R

P

L

V

Y

I

G

G

T

T

T

S

M

P

D

D

T

A

I

I

D

D

Q

R

L

A

E

E

D

D

R

R

G

E

R

R

F

F

Y

Q

D

H

F

A

M

V

K

E

S

R

V

L

N

K

V

L

P

K

H

Q

I

P

P

A

G

N

V

A

T

T

V

V

Y

T

D

A

E

I

V

E

G

M

L

A

V

V

E

E

Q

K

A

A

E

K

K

E

I

I

G

G

Y

Y

P

P

V

L

L

V

R
|
R

P

P

S

A

Y

-

V

-

I

-

G

-

Q

-

G

-

M
|
M

V

E

I

I

I

V

T

Y

S

D

R

E

E

A

E

D

M

L

V

R

D

R

Y

Y

V

F

N

Q

N

T

Q

-

D

-

Q

-

S

-

I

-

V

-

F

-

P

A

I

V

L

L

I

L

D

D

A

H

Y
x
F

Y
x
L

-

D

P

D

G

A

V

V

E
|
E

I

V

E

D

V

V

D

D

A

A

L

I

T

C

D
|
D

G

G

E

E

D

M

I

V

L

L

I

I

P

G

G

G

M

I

F

M

E

E

H

H

I

I

E
|
E

K

Q

A
|
A

G
|
G

V
|
V

H
|
H

S

S

G

G

D
|
D

S

S

M

A

A

C

V

S

T

L

P

P

P

A

F

Y

S

T

L

L

K

S

E

Q

E

E

V

I

K

Q

Q

D

T

V

V

M

Y

R

E

Q

Y

Q

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N

Q

K

K

I

L

A

A

K

F

G

E

M

L

D

Q

F

V

K

R

G

G

I

L

F

M

N

N

I

V

Q
|
Q

F

F

V

A

L

V

Y

K

N

N

H

N

Q

E

L

V

Y

Y

V

L

I

I

E
|
E

I

V

N
|
N

P

P

R

R

A

A

S

A

R
|
R

T

T

V

V

P

P

I

F

L

V

S

S

K

K

V

A

T

T

G

G

L

V

N

P

M

L

V

A

E

K

T

V

T

A

V

A

Q

R

L

V

L

M

L

A

G

G

Q

K

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S

L

L

R

A

N

E

L

Q

G

G

L

V

P

T

T

K

G

E

H

V

L

I

P

P

E

P

T

-

N

-

Y

Y

T

S

V

V

K

K

A
x
E

P

V

I

V

F

L

S

P

Y

F

S

N

K

K

L

F

A
x
P

G

G

L

V

D

D

P

P

I

L

L
|
L

E

G

A
x
P

E

E

M

M

K

R

S

S

T

T

G

G

E

E

L

V

I

M

S

G

I

V

G

G

N

R

T

T

V

F

E

A

D

E

A

A

M

F

K

A

K

K

A

A

F

Q

A

L

W

G

S

S

E

N

G

S

Q

T

I

M

P

-

L

-

Y

-

R

K

Q

K

K

H

G

G

L

R

I

A

F

L

V

L

N

S

I

V

A

R

E

E

E

G

E

D

L
x
K

A

E

E

R

F

V

R

V

P

D

L

L

V

A

K

A

K

K

M

L

S

L

E

K

L

Q

G

G

F

F

T

E

I

L

active site: R129 (= R129), R169 (= R169), M174 (≠ L174), G176 (= G176), K202 (≠ T202), E215 (= E215), H243 (= H243), N283 (= N282), Q285 (= Q284), E299 (= E298), N301 (= N300), R303 (= R302), S307 (= S306), D338 (≠ P337), G507 (≠ N503), K634 (≠ Q630), R715 (= R711), E746 (= E755), D754 (= D763), Q814 (= Q823), E826 (= E835), N828 (= N837), R833 (= R842), P886 (≠ A897)
binding adenosine-5'-diphosphate: R129 (= R129), I167 (= I167), R169 (= R169), M174 (≠ L174), G175 (= G175), G176 (= G176), E208 (≠ R208), L210 (≠ I210), I211 (≠ A211), E215 (= E215), M240 (≠ V240), G241 (= G241), I242 (= I242), H243 (= H243), Q285 (= Q284), I298 (= I297), E299 (= E298), T376 (= T374), R715 (= R711), M718 (= M721), F740 (≠ Y750), L741 (≠ Y751), E746 (= E755), A770 (= A779), G771 (= G780), V772 (= V781), H773 (= H782), E826 (= E835), P894 (≠ A905)
binding manganese (ii) ion: Q285 (= Q284), E299 (= E298), E299 (= E298), N301 (= N300), Q814 (= Q823), E826 (= E835)
binding L-ornithine: E768 (= E777), D776 (= D785), E877 (≠ A888), L892 (= L903)
binding phosphate ion: M174 (≠ L174), G175 (= G175), H243 (= H243), E299 (= E298), N301 (= N300), R303 (= R302), R306 (= R305)
binding uridine-5'-monophosphate: K939 (≠ L954)

Sites not aligning to the query:

binding L-ornithine: 1026, 1027
binding uridine-5'-monophosphate: 959, 961, 962, 978, 1000, 1001, 1002, 1011, 1014

1c3oA Crystal structure of the carbamoyl phosphate synthetase: small subunit mutant c269s with bound glutamine (see paper)
45% identity, 92% coverage: 1:971/1058 of query aligns to 1:956/1058 of 1c3oA

query
sites
1c3oA

M

M

P

P

R

K

I

R

T

T

S

D

I

I

S

K

S

S

V

I

L

L

V

I

I

L

G

G

S

A

G

G

P

P

I

I

V

V

I

I

G

G

Q

Q

A

A

A

C

E

E

F

F

D

D

Y

Y

A

S

G

G

T

A

Q

Q

A

A

C

C

L

K

A

A

L

L

K

R

E

E

G

G

I

Y

R

R

V

V

I

I

L

L

V

V

N

N

N

S

N

N

P

P

A

A

T

T

V

I

M

M

T

T

D

D

E

P

A

E

C

M

A

A

D

D

V

A

V

T

Y

Y

F

I

E

E

P

P

L

I

T

H

V

W

E

E

S

V

I

V

E

R

K

K

I

I

Q

E

K

K

E

E

Q

R

P

P

D

D

G

A

L

V

L

L

A

P

T

T

L

M

G

G

Q

Q

T

T

G

A

L

L

N

N

L

C

A

A

F

L

A

E

L

L

H

E

K

R

A

Q

N

G

I

V

L

L

D

E

K

E

Y

F

N

G

V

V

H

T

L

M

L

I

G

G

T

A

P

T

I

A

E

D

S

A

I

I

M

D

K

K

G

A

E

E

D

D

R
|
R

E

R

F

F

R

D

D

V

L

A

M

M

N

K

E

K

L

I

N

G

E

L

P

E

V

T

P

A

E

R

S

S

Q

G

I

I

V

A

S

H

T

T

E

M

E

E

A

E

A

A

V

L

K

A

F

V

A

A

N

A

S

D

V

V

G

G

Y

F

P

P

I

C

I
|
I

I

I

R
|
R

P

P

A

S

Y

F

T

T

L
x
M

G
|
G

A

S

G

G

I

I

A

A

D

Y

D

N

E

R

K

E

E

E

L

F

R

E

Y

E

I

I

V

C

K

A

G

R

G

G

L

L

A

D

Q

L

S

S

P

P

I

T

T
x
K

Q

E

C

L

L

L

I

I

E

D

R

E

S

S

I
x
L

A
x
I

G

G

F

W

K

K

E
|
E

I

Y

E

E

Y

M

E

E

V

V

M

V

R

R

D

D

A

K

N

N

D

D

T

N

C

C

I

I

T

I

V

V

C

C

N

S

M

I

E

E

N

N

I

F

D

D

P

A

V
x
M

G
|
G

I

I

H
|
H

T
|
T

G

G

D

D

S

S

I

I

V

T

V

V

A

A

P

P

S

A

Q

Q

T

T

L

L

T

T

D

D

V

K

E

E

Y

Y

Q

Q

M

I

L

M

R

R

S

N

A

A

S

S

V

M

K

A

I

V

I

L

R

R

A

E

L

I

G

G

I

V

-

E

V

T

G

G

C

S

N
|
N

I

V

Q
|
Q

F

F

A

A

L

V

D

N

P

P

N

K

S

N

K

G

Q

R

Y

L

Y

I

L

V

I
|
I

E
|
E

V

M

N
|
N

P

P

R
|
R

V

V

S

S

R
|
R

S
|
S

S

S

A

A

L

L

A

A

S

S

K

K

A

A

T

T

G

G

Y

F

P

P

I

I

A

A

R

K

M

V

A

A

K

K

L

L

S

A

I

V

G

G

Y

Y

H

T

L

L

H

D

E

E

L

L

L

M

N

N

P
x
D

V

I

T

T

-

G

G

G

H

R

T

T

Y

P

A

A

S

S

F

F

E

E

P

P

A

S

L

I

D

D

Y

Y

V

V

V

T

K

K

F

I

P

P

R

R

W

F

P

N

F

F

D

E

K

K

F

F

T

A

Q

G

A

A

D

N

R

D

K

R

L

L

G

T

T
|
T

Q

Q

M

M

K

K

A

S

T

V

G

G

E

E

V

V

M

M

A

A

I

I

E

G

R

R

N

T

L

Q

E

Q

S

E

G

S

I

L

Q

Q

K

K

A

A

V

L

R

R

S

G

L

L

E

E

I

V

K

G

T

A

D

T

G

G

L

F

S

D

F

-

P

P

A

K

L

V

K

S

K

L

W

D

G

D

D

P

E

E

E

A

L

L

W

T

E

K

V

I

-

R

-

E

V

L

K

K

K

D

A

A

D

G

D

A

R

D

R

R

F

I

F

W

A

Y

I

I

L

A

E

D

L

A

L

F

R

R

R

A

G

G

I

L

T

S

V

V

D

D

T

G

I

V

H

F

E

N

E

L

T

T

M

N

I

I

N

D

L

R

F

W

F

F

L

L

Y

V

S

Q

F

I

K

E

H

E

L

L

I

V

D

R

L

L

E

E

Q

E

E

K

I

V

T

A

N

E

S

V

S

G

L

I

E

T

L

G

V

L

S

N

E

A

A

D

D

F

L

L

I

R

K

Q

Y

L

K

K

R

R

F

K

G

G

F

F

S

A

D

D

Q

A

W

R

I

L

S

A

Q

K

V

L

W

A

N
x
G

V

V

S

R

L

E

H

A

D

E

V

I

R

R

E

K

K

L

R

R

K

D

A

Q

Y

Y

G

D

I

L

L

H

P

P

S

V

Y

Y

K

K

M
x
R

V

V

D

D

T

T

C

C

A

A

E

E

F

F

T
x
A

A
x
T

N

D

T

T

A

A

Y

Y

Y

M

Y

Y

S

S

S

T

W

Y

H

E

G

E

E

E

H

C

D

E

V

A

D
x
N

V

P

S

S

S

T

N

D

K

R

K

E

K

K

I

I

L

M

I

V

V

L

G

G

S

G

G

G

P

P

I

N

R

R

I

I

G

G

Q

Q

G

G

I

I

E

E

F

F

D

D

Y

Y

C

C

S

C

V

V

H

H

G

A

A

S

I

L

S

A

L

L

K

R

K

E

L

D

G

G

Y

Y

E

E

A

T

I

I

I

M

M

V

N

N

N

C

N

N

P

P

E

E

T

T

V

V

S

S

T

T

D

D

Y

Y

E

D

M

T

A

S

D

D

R

R

L

L

Y

Y

F

F

E

E

P

P

L

V

T

T

V

L

E

E

D

D

V

V

L

L

N

E

V

I

V

V

E

R

L

I

E

E

Q
x
K

I

P

E

K

G

G

V

V

I

I

V

V

Q

Q

L

Y

G

G

Q

Q

T

T

A

P

I

L

S

K

L

L

V

A

Q

R

G

A

L

L

E

E

E

A

A

A

G

G

V

V

R

P

L

V

Y

I

G

G

T

T

T

S

M

P

D

D

T

A

I

I

D

D

Q

R

L

A

E

E

D

D

R

R

G

E

R

R

F

F

Y

Q

D

H

F

A

M

V

K

E

S

R

V

L

N

K

V

L

P

K

H

Q

I

P

P

A

G

N

V

A

T

T

V

V

Y

T

D

A

E

I

V

E

G

M

L

A

V

V

E

E

Q

K

A

A

E

K

K

E

I

I

G

G

Y

Y

P

P

V

L

L

V

R
|
R

P

P

S

A

Y

-

V

-

I

-

G

-

Q

-

G

-

M
|
M

V

E

I

I

I

V

T

Y

S

D

R

E

E

A

E

D

M

L

V

R

D

R

Y

Y

V

F

N

Q

N

T

Q

-

D

-

Q

-

S

-

I

-

V

-

F

-

P

A

I

V

L

L

I

L

D

D

A

H

Y
x
F

Y
x
L

-

D

P

D

G

A

V

V

E
|
E

I

V

E

D

V

V

D

D

A

A

L

I

T

C

D
|
D

G

G

E

E

D

M

I

V

L

L

I

I

P

G

G

G

M

I

F

M

E

E

H

H

I

I

E
|
E

K

Q

A
|
A

G
|
G

V
|
V

H
|
H

S
|
S

G

G

D
|
D

S

S

M

A

A

C

V

S

T

L

P

P

P

A

F

Y

S

T

L

L

K

S

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Q

E

E

V

I

K

Q

Q

D

T

V

V

M

Y

R

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Q

Y

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V

N

Q

K

K

I

L

A

A

K

F

G

E

M

L

D

Q

F

V

K

R

G

G

I

L

F

M

N

N

I

V

Q
|
Q

F

F

V

A

L

V

Y

K

N

N

H

N

Q

E

L

V

Y

Y

V

L

I

I

E
|
E

I

V

N
|
N

P

P

R

R

A

A

S

A

R
|
R

T

T

V

V

P

P

I

F

L

V

S

S

K

K

V

A

T

T

G

G

L

V

N

P

M

L

V

A

E

K

T

V

T

A

V

A

Q

R

L

V

L

M

L

A

G

G

Q

K

S

S

L

L

R

A

N

E

L

Q

G

G

L

V

P

T

T

K

G

E

H

V

L

I

P

P

E

P

T

-

N

-

Y

Y

T

S

V

V

K

K

A
x
E

P

V

I

V

F

L

S

P

Y

F

S

N

K

K

L

F

A
x
P

G

G

L

V

D

D

P

P

I

L

L
|
L

E

G

A

P

E

E

M

M

K

R

S

S

T

T

G

G

E

E

L

V

I

M

S

G

I

V

G

G

N

R

T

T

V

F

E

A

D

E

A

A

M

F

K

A

K

K

A

A

F

Q

A

L

W

G

S

S

E

N

G

S

Q

T

I

M

P

-

L

-

Y

-

R

K

Q

K

K

H

G

G

L

R

I

A

F

L

V

L

N

S

I

V

A

R

E

E

E

G

E

D

L

K

A

E

E

R

F

V

R

V

P

D

L

L

V

A

K

A

K

K

M

L

S

L

E

K

L

Q

G

G

F

F

T

E

I

L

active site: R129 (= R129), R169 (= R169), M174 (≠ L174), G176 (= G176), K202 (≠ T202), E215 (= E215), H243 (= H243), N283 (= N282), Q285 (= Q284), E299 (= E298), N301 (= N300), R303 (= R302), S307 (= S306), D338 (≠ P337), G507 (≠ N503), K634 (≠ Q630), R715 (= R711), E746 (= E755), D754 (= D763), Q814 (= Q823), E826 (= E835), N828 (= N837), R833 (= R842), P886 (≠ A897)
binding adenosine-5'-diphosphate: R129 (= R129), I167 (= I167), R169 (= R169), M174 (≠ L174), G176 (= G176), L210 (≠ I210), I211 (≠ A211), E215 (= E215), M240 (≠ V240), G241 (= G241), H243 (= H243), T244 (= T244), Q285 (= Q284), I298 (= I297), E299 (= E298), T376 (= T374), R715 (= R711), M718 (= M721), F740 (≠ Y750), L741 (≠ Y751), E746 (= E755), A770 (= A779), G771 (= G780), V772 (= V781), H773 (= H782), S774 (= S783), E826 (= E835)
binding glutamine: R528 (≠ M524), A537 (≠ T533), T538 (≠ A534), N554 (≠ D550)
binding manganese (ii) ion: Q285 (= Q284), E299 (= E298), E299 (= E298), N301 (= N300), Q814 (= Q823), E826 (= E835)
binding L-ornithine: E768 (= E777), D776 (= D785), E877 (≠ A888), L892 (= L903)
binding phosphate ion: M174 (≠ L174), G175 (= G175), H243 (= H243), E299 (= E298), N301 (= N300), R303 (= R302), R306 (= R305)

Sites not aligning to the query:

binding L-ornithine: 1026, 1027

1ce8A Carbamoyl phosphate synthetase from escherichis coli with complexed with the allosteric ligand imp (see paper)
44% identity, 92% coverage: 1:971/1058 of query aligns to 1:956/1058 of 1ce8A

query
sites
1ce8A

M

M

P

P

R

K

I

R

T

T

S

D

I

I

S

K

S

S

V

I

L

L

V

I

I

L

G

G

S

A

G

G

P

P

I

I

V

V

I

I

G

G

Q

Q

A

A

A

C

E

E

F

F

D

D

Y

Y

A

S

G

G

T

A

Q

Q

A

A

C

C

L

K

A

A

L

L

K

R

E

E

G

G

I

Y

R

R

V

V

I

I

L

N

V

V

N

N

N

S

N

N

P

P

A

A

T

T

V

I

M

M

T

T

D

D

E

P

A

E

C

M

A

A

D

D

V

A

V

T

Y

Y

F

I

E

E

P

P

L

I

T

H

V

W

E

E

S

V

I

V

E

R

K

K

I

I

Q

E

K

K

E

E

Q

R

P

P

D

D

G

A

L

V

L

L

A

P

T

T

L

M

G

G

Q

Q

T

T

G

A

L

L

N

N

L

C

A

A

F

L

A

E

L

L

H

E

K

R

A

Q

N

G

I

V

L

L

D

E

K

E

Y

F

N

G

V

V

H

T

L

M

L

I

G

G

T

A

P

T

I

A

E

D

S

A

I

I

M

D

K

K

G

A

E

E

D

D

R
|
R

E

R

F

F

R

D

D

V

L

A

M

M

N

K

E

K

L

I

N

G

E

L

P

E

V

T

P

A

E

R

S

S

Q

G

I

I

V

A

S

H

T

T

E

M

E

E

A

E

A

A

V

L

K

A

F

V

A

A

N

A

S

D

V

V

G

G

Y

F

P

P

I

C

I
|
I

I

I

R
|
R

P

P

A

S

Y

F

T

T

L
x
M

G
|
G

A

S

G

G

I

I

A

A

D

Y

D

N

E

R

K

E

E

E

L

F

R

E

Y

E

I

I

V

C

K

A

G

R

G

G

L

L

A

D

Q

L

S

S

P

P

I

T

T
x
K

Q

E

C

L

L

L

I

I

E

D

R

E

S

S

I
x
L

A
x
I

G

G

F

W

K

K

E
|
E

I

Y

E

E

Y

M

E

E

V

V

M

V

R

R

D

D

A

K

N

N

D

D

T

N

C

C

I

I

T

I

V

V

C

C

N

S

M

I

E

E

N

N

I

F

D

D

P

A

V
x
M

G
|
G

I
|
I

H
|
H

T

T

G

G

D

D

S

S

I

I

V

T

V

V

A

A

P

P

S

A

Q

Q

T

T

L

L

T

T

D

D

V

K

E

E

Y

Y

Q

Q

M

I

L

M

R

R

S

N

A

A

S

S

V

M

K

A

I

V

I

L

R

R

A

E

L

I

G

G

I

V

-

E

V

T

G

G

C

S

N
|
N

I

V

Q
|
Q

F

F

A

A

L

V

D

N

P

P

N

K

S

N

K

G

Q

R

Y

L

Y

I

L

V

I
|
I

E
|
E

V

M

N
|
N

P

P

R
|
R

V

V

S

S

R
|
R

S
|
S

S

S

A

A

L

L

A

A

S

S

K

K

A

A

T

T

G

G

Y

F

P

P

I

I

A

A

R

K

M

V

A

A

K

K

L

L

S

A

I

V

G

G

Y

Y

H

T

L

L

H

D

E

E

L

L

L

M

N

N

P
x
D

V

I

T

T

-

G

G

G

H

R

T

T

Y

P

A

A

S

S

F

F

E

E

P

P

A

S

L

I

D

D

Y

Y

V

V

V

T

K

K

F

I

P

P

R

R

W

F

P

N

F

F

D

E

K

K

F

F

T

A

Q

G

A

A

D

N

R

D

K

R

L

L

G

T

T
|
T

Q

Q

M

M

K

K

A

S

T

V

G

G

E

E

V

V

M

M

A

A

I

I

E

G

R

R

N

T

L

Q

E

Q

S

E

G

S

I

L

Q

Q

K

K

A

A

V

L

R

R

S

G

L

L

E

E

I

V

K

G

T

A

D

T

G

G

L

F

S

D

F

-

P

P

A

K

L

V

K

S

K

L

W

D

G

D

D

P

E

E

E

A

L

L

W

T

E

K

V

I

-

R

-

E

V

L

K

K

K

D

A

A

D

G

D

A

R

D

R

R

F

I

F

W

A

Y

I

I

L

A

E

D

L

A

L

F

R

R

R

A

G

G

I

L

T

S

V

V

D

D

T

G

I

V

H

F

E

N

E

L

T

T

M

N

I

I

N

D

L

R

F

W

F

F

L

L

Y

V

S

Q

F

I

K

E

H

E

L

L

I

V

D

R

L

L

E

E

Q

E

E

K

I

V

T

A

N

E

S

V

S

G

L

I

E

T

L

G

V

L

S

N

E

A

A

D

D

F

L

L

I

R

K

Q

Y

L

K

K

R

R

F

K

G

G

F

F

S

A

D

D

Q

A

W

R

I

L

S

A

Q

K

V

L

W

A

N
x
G

V

V

S

R

L

E

H

A

D

E

V

I

R

R

E

K

K

L

R

R

K

D

A

Q

Y

Y

G

D

I

L

L

H

P

P

S

V

Y

Y

K

K

M
x
R

V

V

D

D

T

T

C

C

A

A

E

E

F

F

T
x
A

A
x
T

N

D

T

T

A

A

Y

Y

Y

M

Y

Y

S

S

S

T

W

Y

H

E

G

E

E

E

H

C

D
x
E

V

A

D
x
N

V

P

S

S

S

T

N

D

K

R

K

E

K

K

I

I

L

M

I

V

V

L

G

G

S

G

G

G

P

P

I

N

R

R

I

I

G

G

Q

Q

G

G

I

I

E

E

F

F

D

D

Y

Y

C

C

S

C

V

V

H

H

G

A

A

S

I

L

S

A

L

L

K

R

K

E

L

D

G

G

Y

Y

E

E

A

T

I

I

I

M

M

V

N

N

N

C

N

N

P

P

E

E

T

T

V

V

S

S

T

T

D

D

Y

Y

E

D

M

T

A

S

D

D

R

R

L

L

Y

Y

F

F

E

E

P

P

L

V

T

T

V

L

E

E

D

D

V

V

L

L

N

E

V

I

V

V

E

R

L

I

E

E

Q
x
K

I

P

E

K

G

G

V

V

I

I

V

V

Q

Q

L

Y

G

G

Q

Q

T

T

A

P

I

L

S

K

L

L

V

A

Q

R

G

A

L

L

E

E

E

A

A

A

G

G

V

V

R

P

L

V

Y

I

G

G

T

T

T

S

M

P

D

D

T

A

I

I

D

D

Q

R

L

A

E

E

D

D

R

R

G

E

R

R

F

F

Y

Q

D

H

F

A

M

V

K

E

S

R

V

L

N

K

V

L

P

K

H

Q

I

P

P

A

G

N

V

A

T

T

V

V

Y

T

D

A

E

I

V

E

G

M

L

A

V

V

E

E

Q

K

A

A

E

K

K

E

I

I

G

G

Y

Y

P

P

V

L

L

V

R
|
R

P

P

S

A

Y

-

V

-

I

-

G

-

Q

-

G

-

M

M

V

E

I

I

I

V

T

Y

S

D

R

E

E

A

E

D

M

L

V

R

D

R

Y

Y

V

F

N

Q

N

T

Q

-

D

-

Q

-

S

-

I

-

V

-

F

-

P

A

I

V

L

L

I

L

D

D

A

H

Y
x
F

Y
x
L

-

D

P

D

G

A

V

V

E
|
E

I

V

E

D

V

V

D

D

A

A

L

I

T

C

D
|
D

G

G

E

E

D

M

I

V

L

L

I

I

P

G

G

G

M

I

F

M

E

E

H

H

I

I

E
|
E

K

Q

A
|
A

G
|
G

V
|
V

H
|
H

S
|
S

G

G

D
|
D

S

S

M

A

A

C

V

S

T

L

P

P

P

A

F

Y

S

T

L

L

K

S

E

Q

E

E

V

I

K

Q

Q

D

T

V

V

M

Y

R

E

Q

Y

Q

T

V

N

Q

K

K

I

L

A

A

K

F

G

E

M

L

D

Q

F

V

K

R

G

G

I

L

F

M

N

N

I

V

Q
|
Q

F

F

V

A

L

V

Y

K

N

N

H

N

Q

E

L

V

Y

Y

V

L

I

I

E
|
E

I

V

N
|
N

P

P

R

R

A

A

S

A

R
|
R

T

T

V

V

P

P

I

F

L

V

S

S

K

K

V

A

T

T

G

G

L

V

N

P

M

L

V

A

E

K

T

V

T

A

V

A

Q

R

L

V

L

M

L

A

G

G

Q

K

S

S

L

L

R

A

N

E

L

Q

G

G

L

V

P

T

T

K

G

E

H

V

L

I

P

P

E

P

T

-

N

-

Y

Y

T

S

V

V

K

K

A
x
E

P

V

I

V

F

L

S

P

Y

F

S

N

K

K

L

F

A
x
P

G

G

L

V

D

D

P

P

I

L

L
|
L

E

G

A

P

E

E

M

M

K

R

S

S

T

T

G

G

E

E

L

V

I

M

S

G

I

V

G

G

N

R

T

T

V

F

E

A

D

E

A

A

M

F

K

A

K

K

A

A

F

Q

A

L

W

G

S

S

E

N

G

S

Q

T

I

M

P

-

L

-

Y

-

R

K

Q

K

K

H

G

G

L

R

I

A

F

L

V

L

N
x
S

I

V

A

R

E

E

E

G

E

D

L
x
K

A

E

E

R

F

V

R

V

P

D

L

L

V

A

K

A

K

K

M

L

S

L

E

K

L

Q

G

G

F

F

T

E

I

L

active site: R129 (= R129), R169 (= R169), M174 (≠ L174), G176 (= G176), K202 (≠ T202), E215 (= E215), H243 (= H243), N283 (= N282), Q285 (= Q284), E299 (= E298), N301 (= N300), R303 (= R302), S307 (= S306), D338 (≠ P337), G507 (≠ N503), K634 (≠ Q630), R715 (= R711), E746 (= E755), D754 (= D763), Q814 (= Q823), E826 (= E835), N828 (= N837), R833 (= R842), P886 (≠ A897)
binding adenosine-5'-diphosphate: R129 (= R129), I167 (= I167), R169 (= R169), M174 (≠ L174), G176 (= G176), L210 (≠ I210), I211 (≠ A211), E215 (= E215), M240 (≠ V240), G241 (= G241), I242 (= I242), H243 (= H243), Q285 (= Q284), I298 (= I297), E299 (= E298), T376 (= T374), R715 (= R711), F740 (≠ Y750), L741 (≠ Y751), E746 (= E755), A770 (= A779), G771 (= G780), V772 (= V781), H773 (= H782), S774 (= S783), E826 (= E835)
binding inosinic acid: S933 (≠ N948), K939 (≠ L954)
binding manganese (ii) ion: M174 (≠ L174), Q285 (= Q284), E299 (= E298), E299 (= E298), N301 (= N300), Q814 (= Q823), E826 (= E835)
binding L-ornithine: R528 (≠ M524), A537 (≠ T533), T538 (≠ A534), E552 (≠ D548), N554 (≠ D550), E768 (= E777), D776 (= D785), E877 (≠ A888), L892 (= L903)
binding phosphate ion: M174 (≠ L174), G175 (= G175), H243 (= H243), E299 (= E298), N301 (= N300), R303 (= R302), R306 (= R305)

Sites not aligning to the query:

binding inosinic acid: 959, 961, 962, 978, 979, 986, 1000, 1001, 1002, 1010, 1011, 1013
binding L-ornithine: 1025, 1026, 1027

1a9xA Carbamoyl phosphate synthetase: caught in the act of glutamine hydrolysis (see paper)
44% identity, 92% coverage: 1:971/1058 of query aligns to 1:956/1058 of 1a9xA

query
sites
1a9xA

M

M

P

P

R

K

I

R

T

T

S

D

I

I

S

K

S

S

V

I

L

L

V

I

I

L

G

G

S

A

G

G

P

P

I

I

V

V

I

I

G

G

Q

Q

A

A

A

C

E

E

F

F

D

D

Y

Y

A

S

G

G

T

A

Q

Q

A

A

C

C

L

K

A

A

L

L

K

R

E

E

G

G

I

Y

R

R

V

V

I

I

L

N

V

V

N

N

N

S

N

N

P

P

A

A

T

T

V

I

M

M

T

T

D

D

E

P

A

E

C

M

A

A

D

D

V

A

V

T

Y

Y

F

I

E

E

P

P

L

I

T

H

V

W

E

E

S

V

I

V

E

R

K

K

I

I

Q

E

K

K

E

E

Q

R

P

P

D

D

G

A

L

V

L

L

A

P

T

T

L

M

G

G

Q

Q

T

T

G

A

L

L

N

N

L

C

A

A

F

L

A

E

L

L

H

E

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|
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|
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active site: K202 (≠ T202), D338 (≠ P337), G507 (≠ N503), K634 (≠ Q630), D754 (= D763), P886 (≠ A897)
binding adenosine-5'-diphosphate: R129 (= R129), I167 (= I167), R169 (= R169), M174 (≠ L174), G175 (= G175), G176 (= G176), L210 (≠ I210), E215 (= E215), M240 (≠ V240), G241 (= G241), I242 (= I242), H243 (= H243), T244 (= T244), Q285 (= Q284), I298 (= I297), E299 (= E298), T376 (= T374), R715 (= R711), M718 (= M721), F740 (≠ Y750), L741 (≠ Y751), E746 (= E755), A770 (= A779), G771 (= G780), V772 (= V781), H773 (= H782), E826 (= E835)
binding manganese (ii) ion: Q285 (= Q284), E299 (= E298), E299 (= E298), N301 (= N300), Q814 (= Q823), E826 (= E835)
binding L-ornithine: E768 (= E777), D776 (= D785), E877 (≠ A888), L892 (= L903)
binding phosphate ion: G175 (= G175), H243 (= H243), E299 (= E298), N301 (= N300), R303 (= R302), R306 (= R305)

Sites not aligning to the query:

binding L-ornithine: 1025, 1026, 1027

P05990 Multifunctional protein r; Protein rudimentary; 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 Drosophila melanogaster (Fruit fly) (see 2 papers)
43% identity, 92% coverage: 1:971/1058 of query aligns to 402:1356/2224 of P05990

query
sites
P05990

M

M

P

P

R

R

I

-

T

-

S

-

I

-

S

-

S

K

V

V

L

L

V

I

I

L

G

G

S

S

G

G

P

G

I

L

V

S

I

I

G

G

Q

Q

A

A

A

G

E

E

F

F

D

D

Y

Y

A

S

G

G

T

S

Q

Q

A

A

C

I

L

K

A

A

L

M

K

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E

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G

N

I

I

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T

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L

L

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N

N

N

P

N

N

P

I

A

A

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T

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M

Q

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A

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C

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A

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Y

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K

Q

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K

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N

G

G

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L

L

A

L

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T

L

F

G

G

Q

Q

T

T

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A

L

L

N

N

L

C

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E1167 (= E774) mutation to K: Severely diminishes UTP inhibition of CPSase; in Su(b).

Sites not aligning to the query:

1883 modified: Phosphoserine
1885 modified: Phosphoserine
1892 modified: Phosphoserine
1894 modified: Phosphoserine

Q8C196 Carbamoyl-phosphate synthase [ammonia], mitochondrial; Carbamoyl-phosphate synthetase I; CPSase I; EC 6.3.4.16 from Mus musculus (Mouse) (see 2 papers)
41% identity, 93% coverage: 7:993/1058 of query aligns to 422:1414/1500 of Q8C196

query
sites
Q8C196

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K1291 (≠ L871) modified: N6-acetyllysine; alternate; modified: N6-succinyllysine; alternate

Sites not aligning to the query:

44 modified: N6-acetyllysine; alternate; modified: N6-succinyllysine; alternate
287 modified: N6-acetyllysine; alternate; modified: N6-succinyllysine; alternate

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)
42% identity, 91% coverage: 7:971/1058 of query aligns to 404:1358/2225 of P20054

query
sites
P20054

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Sites not aligning to the query:

1 modified: N-acetylmethionine

P07756 Carbamoyl-phosphate synthase [ammonia], mitochondrial; Carbamoyl-phosphate synthetase I; CPSase I; EC 6.3.4.16 from Rattus norvegicus (Rat) (see 2 papers)
41% identity, 93% coverage: 7:993/1058 of query aligns to 422:1414/1500 of P07756

query
sites
P07756

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S537 (≠ P119) modified: carbohydrate, O-linked (GlcNAc) serine; alternate
S1331 (= S909) modified: carbohydrate, O-linked (GlcNAc) serine
T1332 (= T910) modified: carbohydrate, O-linked (GlcNAc) threonine
T1391 (= T970) mutation to V: 400-fold increase in the activation constant of NAG. 3-fold decrease in the reaction rate at saturation of NAG.
T1394 (≠ E973) mutation to A: 900-fold increase in the activation constant of NAG. 3-fold decrease in the reaction rate at saturation of NAG.
W1410 (= W989) mutation to K: 60-fold increase in the activation constant of NAG.

Sites not aligning to the query:

1437 N→D: 70-fold increase in the activation constant of NAG.
1440 N→D: 110-fold increase in the activation constant of NAG. Modifies the specificity for the activator: Binds Phe-NAG considerably better than NAG.

P03965 Carbamoyl phosphate synthase arginine-specific large chain; CPS; CPSase; CPSase-arg; Ammonium-dependent carbamoyl phosphate synthetase; Arginine-specific carbamoyl phosphate synthetase, ammonia chain; Carbamoyl phosphate synthase A; CPS-A; Glutamine-dependent carbamoyl phosphate synthetase; EC 6.3.4.16; EC 6.3.5.5 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see paper)
42% identity, 96% coverage: 4:1015/1058 of query aligns to 25:1035/1118 of P03965

query
sites
P03965

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L229 (≠ I210) mutation to G: Abolishes ammonia-dependent ATPase activity.
H262 (= H243) mutation to N: No effect.
D265 (= D246) mutation D->A,E,N: Reduces ammonia-dependent ATPase activity 17-58 fold.
I316 (= I297) mutation I->G,S,H: Reduces ammonia-dependent ATPase activity 17-64 fold.
H807 (= H782) mutation to N: No effect.
D810 (= D785) mutation D->A,E,N: Abolishes ammonia-dependent ATPase activity.

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)
43% identity, 92% coverage: 2:971/1058 of query aligns to 434:1390/2214 of P07259

query
sites
P07259

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Sites not aligning to the query:

1857 modified: Phosphoserine; by PKA

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)
41% identity, 98% coverage: 10:1050/1058 of query aligns to 477:1530/2244 of Q09794

query
sites
Q09794

V

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S1119 (≠ T661) modified: Phosphoserine

Sites not aligning to the query:

1881 modified: Phosphoserine
1885 modified: Phosphoserine

P31327 Carbamoyl-phosphate synthase [ammonia], mitochondrial; Carbamoyl-phosphate synthetase I; CPSase I; EC 6.3.4.16 from Homo sapiens (Human) (see 22 papers)
40% identity, 93% coverage: 7:993/1058 of query aligns to 422:1414/1500 of P31327

query
sites
P31327

I

V

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I

L

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A
|
A

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A438 (= A23) to P: in CPS1D; almost complete loss of enzyme activity; dbSNP:rs772497399
K453 (= K38) modified: N6-glutaryllysine; alternate
K458 (≠ R43) modified: N6-glutaryllysine; alternate
K527 (≠ D109) modified: N6-glutaryllysine; alternate
G530 (≠ N112) to V: found in a patient with VACTERL syndrome and postsurgical PHN; uncertain significance; dbSNP:rs1250316045
K532 (≠ H114) modified: N6-glutaryllysine; alternate
T544 (≠ G126) to M: in CPS1D; almost complete loss of enzyme activity; approximately 60-fold increase in the apparent Km for bicarbonate and approximately 4-fold respective decrease and increase in the apparent Vmax and Km for ammonia; dbSNP:rs121912592
K553 (≠ L135) modified: N6-glutaryllysine; alternate
Q678 (= Q262) to P: in CPS1D; results in a poor enzyme expression and solubility; hampers correct enzyme folding
K728 (= K312) modified: N6-glutaryllysine
K757 (≠ H341) modified: N6-glutaryllysine; alternate
K772 (= K356) modified: N6-glutaryllysine; alternate
P774 (= P358) to L: in CPS1D; the enzyme is inactive
K793 (= K377) modified: N6-glutaryllysine; alternate
K811 (= K395) modified: N6-glutaryllysine; alternate
K841 (≠ E422) modified: N6-glutaryllysine; alternate
L843 (≠ V424) to S: in CPS1D; associated in cis with E-875; causes 70% decrease of enzyme activity; significant decrease in protein yield
R850 (= R431) to C: in CPS1D; moderate decrease in protein yield and partial loss of enzyme activity; dbSNP:rs1015051007; to H: in CPS1D; partial loss of enzyme activity; dbSNP:rs767694281
K856 (≠ E437) modified: N6-glutaryllysine; alternate
K869 (≠ E450) modified: N6-glutaryllysine
T871 (= T452) to P: in CPS1D; significant decrease in protein yield and enzyme activity
K875 (≠ L456) modified: N6-glutaryllysine; alternate; to E: associated in cis with S-843 in a patient with carbamoyl-phosphate synthase deficiency; does not affect enzyme activity; significant decrease in protein yield and thermal stability; dbSNP:rs147062907
K889 (≠ Q470) modified: N6-glutaryllysine; alternate
K892 (≠ T473) modified: N6-glutaryllysine; alternate
K905 (≠ I486) modified: N6-glutaryllysine
K908 (= K489) modified: N6-glutaryllysine; alternate
G911 (= G492) to E: in CPS1D; significant decrease in protein yield and enzyme activity; dbSNP:rs1388955593; to V: in CPS1D; significant decrease in protein yield and enzyme activity
S913 (= S494) to L: in CPS1D; significant decrease in protein yield and partial loss of enzyme activity; dbSNP:rs754706559
D914 (= D495) to G: in CPS1D; significant decrease in protein yield and enzyme activity; to H: in CPS1D; significant decrease in protein yield and enzyme activity; dbSNP:rs765484849
K915 (≠ Q496) modified: N6-glutaryllysine; alternate
S918 (= S499) to P: in CPS1D; significant decrease in protein yield and enzyme activity
K919 (≠ Q500) modified: N6-glutaryllysine; alternate
R932 (= R513) to T: in CPS1D; significant decrease in protein yield and partial loss of enzyme activity
I937 (= I518) to N: in CPS1D; associated with R-401; significant decrease in protein yield and enzyme activity; dbSNP:rs760714614
A949 (= A530) to T: in CPS1D; partial loss of enzyme activity and significant decrease in thermal stability; dbSNP:rs537170841
L958 (≠ Y539) to P: in CPS1D; significant decrease in protein yield and enzyme activity
Y959 (= Y540) to C: in CPS1D; significant decrease in protein yield and thermal stability; partial loss of enzyme activity; dbSNP:rs1191587211
Y962 (≠ W543) to C: in CPS1D; significant decrease in protein yield and partial loss of enzyme activity; dbSNP:rs955666400
G964 (= G545) to D: in CPS1D; significant decrease in protein yield and enzyme activity; dbSNP:rs534815243
I986 (= I568) to T: in CPS1D; associated with V-304; dbSNP:rs1553516442
G987 (= G569) to C: in CPS1D; may affect splicing; dbSNP:rs1553516443
K1074 (≠ R656) modified: N6-glutaryllysine; alternate
K1150 (≠ D732) modified: N6-glutaryllysine
K1168 (≠ A749) modified: N6-glutaryllysine; alternate
K1183 (≠ D763) modified: N6-glutaryllysine; alternate
I1215 (≠ L795) to V: in CPS1D; uncertain significance; dbSNP:rs141373204
K1224 (≠ Y804) modified: N6-glutaryllysine
I1254 (= I834) to F: in CPS1D; uncertain significance
F1266 (≠ I846) to S: in dbSNP:rs1047886
M1283 (≠ L863) to L: in dbSNP:rs1047887
K1356 (≠ Q934) modified: N6-glutaryllysine; alternate
K1360 (= K942) modified: N6-glutaryllysine; alternate
LIGI 1363:1366 (≠ FVNI 946:949) natural variant: Missing (in CPS1D; uncertain significance)
G1376 (≠ P959) to S: no functional consequences; no negative effect on protein stability, enzyme activity and thermal stability; dbSNP:rs140578009
A1378 (≠ V961) to T: in CPS1D; significant reduction in thermal stability; dbSNP:rs1245373037
L1381 (≠ M964) to S: in CPS1D; significant loss of protein stability
T1406 (= T985) to N: probable risk factor for PHN; dbSNP:rs1047891
P1411 (≠ I990) to L: in CPS1D; modestly decreases enzyme activity; dbSNP:rs1202306773

Sites not aligning to the query:

55 modified: N6-glutaryllysine; alternate
123 S → F: in CPS1D; modestly decreases enzyme activity; S → Y: in CPS1D; uncertain significance
171 modified: N6-glutaryllysine; alternate
174 R → W: in CPS1D; uncertain significance; dbSNP:rs1553509661
176 modified: N6-glutaryllysine
207 modified: N6-glutaryllysine; alternate
210 modified: N6-glutaryllysine; alternate
214 modified: N6-glutaryllysine; alternate
219 modified: N6-glutaryllysine; alternate
228 modified: N6-glutaryllysine; alternate
237 modified: N6-glutaryllysine
280 modified: N6-glutaryllysine; alternate
304 A → V: in CPS1D; associated with T-986; dbSNP:rs775920437
307 modified: N6-glutaryllysine; alternate
310 modified: N6-glutaryllysine; alternate
337 H → R: in CPS1D; modestly decreases enzyme activity; dbSNP:rs28940283
344 T → A: no negative effect on protein stability, enzyme activity and thermal stability; dbSNP:rs1047883
355 N → D: in CPS1D; around 80% decrease in enzyme activity; significant reduction in thermal stability; approximately 4-fold decrease in the apparent Vmax for ATP, bicarbonate and ammonia; dbSNP:rs1472190012
389 Y → C: in CPS1D; around 40% decrease in enzyme activity; significant loss of thermal stability
390 L → R: in CPS1D; significant loss of protein stability
401 G → R: in CPS1D; uncertain significance; associated with N-937 in a patient; dbSNP:rs760895692
402 modified: N6-glutaryllysine; alternate
412 modified: N6-glutaryllysine; alternate
1443 T → A: in CPS1D; almost complete loss of enzyme activity; approximately 10-fold decrease in the apparent Vmax for bicarbonate, ammonia and ATP; decreased affinity for NAG
1453 R → Q: in CPS1D; the enzyme is inactive; R → W: in CPS1D; the enzyme is inactive; dbSNP:rs933813349
1479 modified: N6-glutaryllysine; alternate
1486 modified: N6-glutaryllysine; alternate
1491 Y → H: in CPS1D; triggers a large decrease in the apparent affinity for N-acetyl-L-glutamate (NAG); dbSNP:rs1553519513

Q18990 Multifunctional protein pyr-1; 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 Caenorhabditis elegans (see 3 papers)
42% identity, 91% coverage: 10:971/1058 of query aligns to 393:1352/2198 of Q18990

query
sites
Q18990

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Sites not aligning to the query:

1602 H→Q: In cu8; probable loss of dihydroorotase activity. Severe late stage embryonic lethality in 50% of animals. The few surviving mutants have a shorter and thicker pharyngeal isthmus, an abnormal knobbed tail, mild egg-laying defects, moderate fluid accumulation in the coelom and a slower growth. Actin and intermediate filaments are disorganized in the pharynx. Moderate reduction in heparan sulfate levels and increased levels of chondroitin sulfate. In an umps-1 zu456 mutant background, prevents the formation of abnormally enlarged gut granules in embryos. Complete embryonic lethality in a rnst-2 qx245 mutant background.

5douD Crystal structure of human carbamoyl phosphate synthetase i (cps1), ligand-bound form (see paper)
40% identity, 93% coverage: 7:993/1058 of query aligns to 380:1355/1430 of 5douD

query
sites
5douD

I

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active site: R505 (= R129), R545 (= R169), N576 (≠ T202), E589 (= E215), H617 (= H243), N656 (= N282), Q658 (= Q284), E672 (= E298), N674 (= N300), R676 (= R302), S680 (= S306), G880 (≠ N503), A1006 (≠ Q630), R1087 (= R711), E1116 (= E755), K1124 (≠ D763), Q1184 (= Q823), E1196 (= E835), N1198 (= N837), R1203 (= R842), R1260 (≠ A897)
binding adenosine-5'-diphosphate: R505 (= R129), M543 (≠ I167), R545 (= R169), L550 (= L174), G551 (= G175), G552 (= G176), E581 (= E207), S583 (= S209), V584 (≠ I210), T585 (≠ A211), E589 (= E215), M614 (≠ V240), G615 (= G241), V616 (≠ I242), H617 (= H243), Q658 (= Q284), I671 (= I297), E672 (= E298), L1085 (= L709), F1110 (≠ Y750), V1111 (≠ Y751), E1116 (= E755), A1140 (= A779), V1142 (= V781), H1143 (= H782), S1144 (= S783), Q1184 (= Q823), L1186 (≠ V825), I1195 (= I834), E1196 (= E835)
binding magnesium ion: Q658 (= Q284), E672 (= E298), E672 (= E298), N674 (= N300)
binding n-acetyl-l-glutamate: I1307 (= I949), Q1308 (≠ A950), T1332 (= T970), A1334 (≠ V972), T1335 (≠ E973), W1351 (= W989)
binding phosphate ion: L550 (= L174), G551 (= G175), H617 (= H243), E672 (= E298), N674 (= N300), R676 (= R302), R679 (= R305)

Sites not aligning to the query:

active site: 252, 335, 337
binding n-acetyl-l-glutamate: 1379, 1384, 1385, 1386, 1390

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)
41% identity, 91% coverage: 10:971/1058 of query aligns to 396:1342/2225 of P08955

query
sites
P08955

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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.

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)
41% identity, 91% coverage: 10:971/1058 of query aligns to 396:1342/2225 of P27708

query
sites
P27708

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T456 (= T70) modified: Phosphothreonine; by MAPK1
Y735 (= Y352) to C: in a colorectal cancer sample; somatic mutation

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
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

6w2jA Cps1 bound to allosteric inhibitor h3b-374 (see paper)
40% identity, 93% coverage: 7:993/1058 of query aligns to 377:1344/1422 of 6w2jA

query
sites
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active site: Q651 (= Q284), E665 (= E298), N667 (= N300), S673 (= S306), G869 (≠ N503), A995 (≠ Q630), K1113 (≠ D763), R1249 (≠ A897)
binding (2-fluoranyl-4-methoxy-phenyl)-[(3~{R},5~{R})-4-(2-fluoranyl-4-methoxy-phenyl)carbonyl-3,5-dimethyl-piperazin-1-yl]methanone: D605 (= D238), M607 (≠ V240), V615 (≠ I248), P725 (= P358), R726 (= R359), W727 (= W360), D730 (= D363), F732 (= F365), F756 (≠ I393), L760 (≠ V397), C763 (≠ L400), H764 (≠ E401), S795 (≠ D429), R797 (= R431), I798 (≠ F432)

Sites not aligning to the query:

binding zinc ion: 273, 293, 295, 320

Query Sequence

>WP_078430316.1 NCBI__GCF_002019605.1:WP_078430316.1
MPRITSISSVLVIGSGPIVIGQAAEFDYAGTQACLALKEEGIRVILVNNNPATVMTDEAC
ADVVYFEPLTVESIEKIIQKEQPDGLLATLGGQTGLNLAFALHKANILDKYNVHLLGTPI
ESIMKGEDREEFRDLMNELNEPVPESQIVSTEEAAVKFANSVGYPIIIRPAYTLGGAGGG
IADDEKELRYIVKGGLAQSPITQCLIERSIAGFKEIEYEVMRDANDTCITVCNMENIDPV
GIHTGDSIVVAPSQTLTDVEYQMLRSASVKIIRALGIVGGCNIQFALDPNSKQYYLIEVN
PRVSRSSALASKATGYPIARMAAKLSIGYHLHELLNPVTGHTYASFEPALDYVVVKFPRW
PFDKFTQADRKLGTQMKATGEVMAIERNLESGIQKAVRSLEIKTDGLSFPALKKWGDEEL
WEVVKKADDRRFFAILELLRRGITVDTIHEETMINLFFLYSFKHLIDLEQEITNSSLELV
SEADLIKYKRFGFSDQWISQVWNVSLHDVREKRKAYGILPSYKMVDTCAAEFTANTAYYY
SSWHGEHDVDVSSNKKKILIVGSGPIRIGQGIEFDYCSVHGAISLKKLGYEAIIMNNNPE
TVSTDYEMADRLYFEPLTVEDVLNVVELEQIEGVIVQLGGQTAISLVQGLEEAGVRLYGT
TMDTIDQLEDRGRFYDFMKSVNVPHIPGVTVYDEVGLVEQAEKIGYPVLLRPSYVIGGQG
MVIITSREEMVDYVNNQDQSIVFPILIDAYYPGVEIEVDALTDGEDILIPGMFEHIEKAG
VHSGDSMAVTPPFSLKEEVKQTVYEYTNKIAKGMDFKGIFNIQFVLYNHQLYVIEINPRA
SRTVPILSKVTGLNMVETTVQLLLGQSLRNLGLPTGHLPETNYYTVKAPIFSYSKLAGLD
PILEAEMKSTGELISIGNTVEDAMKKAFAWSEGQIPPLYRQKGLIFVNIAEEELAEFRPL
VKKMSELGFTIVEENQLLSDSRPLTFNEWIDQEDAVAYISIPKKGYKTWKEQRQQALKNR
VTVITEMTTLSMMLNSINGNADEVVSIQEWMHRTKSSV

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