SitesBLAST

6pnzA The structure of the aspartate transcarbamoylase trimer from staphylococcus aureus complexed with pala at 2.27 resolution.
38% identity, 93% coverage: 17:312/320 of query aligns to 3:288/293 of 6pnzA

query
sites
6pnzA

H

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A

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binding n-(phosphonacetyl)-l-aspartic acid: S48 (= S66), T49 (= T67), R50 (= R68), T51 (= T69), S75 (= S93), K78 (= K96), R100 (= R118), H127 (= H148), Q130 (= Q151), R160 (= R181), V161 (= V182), R210 (= R236), Q212 (= Q238), P252 (= P276), A253 (≠ G277)

4bjhB Crystal structure of the aquifex reactor complex formed by dihydroorotase (h180a, h232a) with dihydroorotate and aspartate transcarbamoylase with n-(phosphonacetyl)-l-aspartate (pala) (see paper)
39% identity, 93% coverage: 18:315/320 of query aligns to 4:289/291 of 4bjhB

query
sites
4bjhB

L

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active site: R47 (= R68), T48 (= T69), K75 (= K96), R97 (= R118), H126 (= H148), Q129 (= Q151)
binding n-(phosphonacetyl)-l-aspartic acid: S45 (= S66), T46 (= T67), R47 (= R68), T48 (= T69), R97 (= R118), H126 (= H148), R159 (= R181), V160 (= V182), R213 (= R236), Q215 (= Q238), P250 (= P276), G251 (= G277)

3d6nB Crystal structure of aquifex dihydroorotase activated by aspartate transcarbamoylase (see paper)
39% identity, 93% coverage: 18:315/320 of query aligns to 4:289/291 of 3d6nB

query
sites
3d6nB

L

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active site: R47 (= R68), T48 (= T69), K75 (= K96), R97 (= R118), H126 (= H148), Q129 (= Q151)
binding citrate anion: T48 (= T69), R97 (= R118), H126 (= H148), R159 (= R181), V160 (= V182), R213 (= R236), G251 (= G277)

5g1nE Aspartate transcarbamoylase domain of human cad bound to pala (see paper)
36% identity, 94% coverage: 17:318/320 of query aligns to 7:306/307 of 5g1nE

query
sites
5g1nE

H

H

L

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active site: R57 (= R68), T58 (= T69), K85 (= K96), R106 (= R118), H134 (= H148), Q137 (= Q151), T227 (≠ L235), P266 (= P276), G292 (= G304)
binding n-(phosphonacetyl)-l-aspartic acid: S55 (= S66), T56 (= T67), R57 (= R68), T58 (= T69), S82 (= S93), K85 (= K96), R106 (= R118), H134 (= H148), R167 (= R181), T168 (≠ V182), R228 (= R236), Q230 (= Q238), P266 (= P276), M267 (≠ G277)

P27708 CAD protein; EC 6.3.5.5; EC 2.1.3.2; EC 3.5.2.3 from Homo sapiens (Human) (see 7 papers)
36% identity, 94% coverage: 17:317/320 of query aligns to 1925:2223/2225 of P27708

query
sites
P27708

H
|
H

L
x
I

L
|
L

S
|
S

I
x
V

E
x
Q

G
x
Q

L
x
F

P
x
T

R
x
K

D
|
D

I
x
Q

V
x
M

T
x
S

H
|
H

I
x
L

L
x
F

D
x
N

T
x
V

A
|
A

A
x
H

N
x
T

F
x
L

V
x
R

S
x
M

V
x
M

N
x
V

D
x
Q

R
x
K

E
|
E

V

-

K
x
R

K
x
S

V
x
L

P
x
D

L
x
I

L
|
L

R
x
K

G
|
G

K
|
K

S
x
V

V
x
M

F
x
A

N
x
S

L
x
M

F
|
F

F
x
Y

E
|
E

N
x
V

S
|
S

T
|
T

R
|
R

T
|
T

R
x
S

T
x
S

F
|
F

E
x
A

I
x
A

A
|
A

A
x
M

K
x
A

R
|
R

L
|
L

S
x
G

A
x
G

D
x
A

V
|
V

L
|
L

N
x
S

L
x
F

D
x
S

I
x
E

A
|
A

R
x
T

S
|
S

A
x
V

S
x
Q

K
|
K

G
|
G

E
|
E

S
|
S

L
|
L

L
x
A

D
|
D

T
x
S

I
x
V

A
x
Q

N
x
T

L
x
M

S
|
S

A
x
C

M
x
Y

A

-

A
|
A

D
|
D

L
x
V

F
x
V

V
|
V

V
x
L

R
|
R

H
|
H

S
x
P

E
x
Q

S
x
P

G
|
G

A
|
A

P
x
V

Y
x
E

L
|
L

I
x
A

A
|
A

Q
x
K

H
|
H

V
x
C

A

-

P

-

H
x
R

V
x
R

H
x
P

V
|
V

I
|
I

N
|
N

A
|
A

G
|
G

D
|
D

G
|
G

R
x
V

H
x
G

A
x
E

H
|
H

P
|
P

T
|
T

Q
|
Q

G
x
A

L
|
L

D
|
D

M
x
I

Y
x
F

T
|
T

I
|
I

R
|
R

H
x
E

Y
x
E

K
x
L

K
x
G

D
x
T

F
x
V

S
x
N

N
x
G

L
x
M

T
|
T

V
x
I

A
x
T

I
x
M

V
|
V

G
|
G

D
|
D

V
x
L

L
x
K

H
|
H

S
x
G

R
|
R

V
x
T

A
x
V

R
x
H

S
|
S

D

-

I
x
L

H
x
A

G
x
C

L
|
L

T
x
L

T
|
T

L
x
Q

G
x
Y

C
x
R

A
x
V

E
x
S

V
x
L

R
|
R

V
x
Y

V
|
V

G
x
A

P
|
P

R
x
P

T
x
S

L
|
L

-
x
R

-
x
M

-
x
P

-
x
T

V
|
V

P
x
R

S
x
A

D
x
F

M
x
V

A
|
A

Q
x
S

M
x
R

G
|
G

V
x
T

R
x
K

V
x
Q

-
x
E

C
x
F

H
x
E

T
x
S

L
x
I

E
|
E

G
x
A

I
x
L

K
x
P

D
|
D

A
x
T

D
|
D

V
|
V

V
x
L

I
x
Y

M
|
M

L
x
T

R
|
R

L
x
I

Q
|
Q

N
x
K

E
|
E

R
|
R

M
x
F

S
x
G

G

-

A

-

L

-

P

-

S
|
S

S
x
T

Q
|
Q

E
|
E

Y
|
Y

F
x
E

K
x
A

S
x
C

F
|
F

G
|
G

-
x
Q

-
x
F

-
x
I

L
|
L

T
|
T

Q
x
P

E
x
H

K
x
I

L
x
M

Q
x
T

L
x
R

A
|
A

K
|
K

P
x
K

D
x
K

A
x
M

I
x
V

V
|
V

M
|
M

H
|
H

P
|
P

G
x
M

P
|
P

I

-

N

-

R
|
R

G
x
V

V
x
N

E
|
E

I
|
I

D
x
S

S
x
V

A
x
E

V
|
V

V
x
D

D
x
S

G
x
D

K
x
P

Q
x
R

S
x
A

V
x
A

I
x
Y

L
x
F

P
x
R

Q
|
Q

V
x
A

T
x
E

F
x
N

G
|
G

I
x
M

A
x
Y

V
x
I

R
|
R

M
|
M

A
|
A

V
x
L

M
x
L

S
x
A

I
x
T

V
|
V

A
x
L

G
|
G

Sites not aligning to the query:

1 modified: Initiator methionine, Removed
2 modified: N-acetylalanine
33 M → R: in DEE50; unknown pathological 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 ; binding ; H→A: No zinc-binding and no catalytic activity.; H→N: Abolishes dihydroorotase activity.
1473 binding ; H→A: No zinc-binding and no catalytic activity.
1475 binding
1505 binding
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 ; H→A: Abolishes dihydroorotase activity.; H→N: No catalytic activity.
1613 binding ; C→S: Reduces dihydroorotase activity.
1614 binding ; H→A: Abolishes dihydroorotase activity.
1637 binding ; E→T: Abolishes dihydroorotase activity.
1642 H→N: 11.5% of wild-type catalytic activity.
1661 binding
1686 binding ; binding ; D→N: Abolishes dihydroorotase activity.
1690 binding ; H→N: 3% of wild-type catalytic activity.
1789:2225 natural variant: Missing (in DEE50; unknown pathological 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

P08955 CAD protein; EC 6.3.5.5; EC 2.1.3.2; EC 3.5.2.3 from Mesocricetus auratus (Golden hamster) (see paper)
36% identity, 94% coverage: 17:317/320 of query aligns to 1925:2223/2225 of P08955

query
sites
P08955

H

H

L

I

L

L

S

S

I

V

E

K

G

Q

L

F

P

T

R

K

D

D

I

Q

V

M

T

S

H

H

I

L

L

F

D

N

T

V

A

A

A

H

N

T

F

L

V

R

S

M

V

M

N

V

D

Q

R

K

E

E

V

-

K

R

K

S

V

L

P

D

L

I

L

L

R

K

G

G

K

K

S

V

V

M

F

A

N

S

L

M

F

F

F

Y

E

E

N

V

S

S

T

T

R

R

T

T

R

S

T

S

F

F

E

A

I

A

A

A

A

M

K

A

R

R

L

L

S

G

A

G

D

A

V

V

L

L

N

S

L

F

D

S

I

E

A

A

R

T

S

S

A

V

S

Q

K

K

G

G

E

E

S

S

L

L

L

A

D

D

T

S

I

V

A

Q

N

T

L

M

S

S

A

C

M

Y

A

-

A

A

D

D

L

V

F

V

V

V

V

L

R

R

H

H

S

P

E

Q

S

P

G

G

A

A

P

V

Y

E

L

L

I

A

A

A

Q

K

H

H

V

C

A

-

P

-

H

R

V

R

H

P

V

V

I

I

N

N

A

A

G

G

D

D

G

G

R

V

H

G

A

E

H

H

P

P

T

T

Q

Q

G

A

L

L

D

D

M

I

Y

F

T

T

I

I

R

R

H

E

Y

E

K

L

K

G

D

T

F

V

S

N

N

G

L

M

T

T

V

I

A

T

I

M

V

V

G

G

D

D

V

L

L

K

H

H

S

G

R

R

V

T

A

V

R

H

S

S

D

-

I

L

H

A

G

C

L

L

T

L

T

T

L

Q

G

Y

C

R

A

V

E

S

V

L

R

R

V

Y

V

V

G

A

P

P

R

P

T

S

L

L

-

R

-

M

-

P

-

S

V

V

P

W

S

D

D

F

M

V

A

A

Q

S

M

R

G

G

V

T

R

K

V

Q

-

E

C

F

H

E

T

S

L

I

E

E

G

A

I

L

K

P

D

D

A

T

D

D

V

V

V

L

I

Y

M

M

L

T

R

R

L

I

Q

Q

N

K

E

E

R

R

M

F

S

G

G

-

A

-

L

-

P

-

S

S

S

T

Q

Q

E

E

Y

Y

F

E

K

A

S

C

F

F

G

G

-

Q

-

F

-

I

L

L

T

T

Q

P

E

H

K

I

L

M

Q

T

L

R

A

A

K

K

P

K

D

K

A

M

I

V

V

V

M

M

H

H

P

P

G

M

P

P

I

-

N

-

R

R

G

V

V

N

E

E

I

I

D

S

S

V

A

E

V

V

V

D

D

S

G

D

K

P

Q

R

S

A

V

A

I

Y

L

F

P

R

Q

Q

V

A

T

E

F

N

G

G

I

M

A

Y

V

I

R

R

M

M

A

A

V

L

M

L

S

A

I

T

V

V

A

L

G

G

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.

3e2pA Catalytic subunit of m. Jannaschii aspartate transcarbamoylase in an orthorhombic crystal form (see paper)
35% identity, 95% coverage: 17:320/320 of query aligns to 3:305/306 of 3e2pA

query
sites
3e2pA

H

H

L

L

L

I

S

S

I

M

E

K

G

D

L

I

P

G

R

K

D

E

I

E

V

I

T

L

H

E

I

I

L

L

D

D

T

E

A

A

A

R

N

K

F

M

V

E

S

E

V

L

N

L

D

N

R

T

E

K

V

-

K

R

K

P

V

L

P

K

L

L

R

E

G

G

K

K

S

I

V

L

F

A

N

T

L

V

F

F

F

Y

E

E

N

P

S

S

T

T

R
|
R

T
|
T

R

R

T

L

T

S

F

F

E

E

I

T

A

A

A

M

K
|
K

R

R

L

L

S

G

A

G

D

E

V
|
V

L

I

N

T

L

M

-

T

D

D

I

L

A

K

R

S

S

S

A

V

S

A

K
|
K

G

G

E

E

S

S

L

L

L

I

D

D

T

T

I

I

A

R

N

V

L

I

S

S

A

G

M

Y

A

A

A

-

D

D

L

I

F

I

V

V

V

L

R
|
R

H

H

S

P

E

S

S

E

G

G

A

A

P

A

Y

R

L

L

I

A

A

S

Q

E

H

Y

V

-

A

-

P

S

H

Q

V

V

H

P

V

I

I

I

N

N

A

A

G

G

D

D

G

G

R

S

H

N

A

Q

H
|
H

P

P

T

T

Q
|
Q

G

T

L

L

D

D

M

L

Y

Y

T

T

I

I

R

M

H

R

Y

E

K

I

K

G

D

R

F

I

S

D

N

G

L

I

T

K

V

I

A

A

I

F

V

V

G

G

D

D

V

L

L

K

H

Y

S

G

R

R

V

T

A

V

R

H

S

S

D

L

I

V

H

Y

G

A

L

L

T

S

T

L

L

F

G

E

C

N

A

V

E

E

V

M

R

Y

V

F

V

V

G

S

P

P

R

K

T

E

L

L

-

R

V

L

P

P

S

K

D

D

M

I

A

I

Q

E

-

D

-

L

-

K

-

A

-

K

-

N

M

I

G

K

V

F

R

Y

V

E

C

K

H

E

T

S

L

L

E

D

G

L

I

D

K

D

D

D

A

I

D

D

V

V

V

L

I

Y

M

V

L
x
T

R

R

L

I

Q

Q

N

K

E

E

R

R

M

-

S

-

G

-

A

-

L

-

L

F

P

P

S

D

S

P

Q

N

E

E

Y

Y

F

E

K

K

-

V

-

K

-

G

S

S

F

Y

G

K

L

I

T

K

Q

R

E

E

K

Y

L

V

Q

E

L

G

A

K

K

K

P

-

D

-

A

F

I

I

V

I

M

M

H

H

P
|
P

G

L

P

P

I

-

N

-

R

R

G

V

V

D

E

E

I

I

D

D

S

Y

A

D

V

V

V

D

D

D

G

L

K

P

Q

Q

S

A

V

K

I

Y

L

F

P

K

Q

Q

V

S

T

F

F

Y

G
|
G

I

I

A

P

V

V

R

R

M

M

A

A

V

I

M

L

-

K

S

K

I

L

V

I

A

E

G

D

N

N

E

E

A

G

active site: R53 (= R68), T54 (= T69), K82 (= K96), R103 (= R118), H131 (= H148), Q134 (= Q151), T225 (≠ L235), P262 (= P276), G288 (= G304)
binding sulfate ion: K63 (= K78), V69 (= V84)

1ml4A The pala-liganded aspartate transcarbamoylase catalytic subunit from pyrococcus abyssi (see paper)
35% identity, 94% coverage: 18:317/320 of query aligns to 7:305/307 of 1ml4A

query
sites
1ml4A

L

V

L

I

S

S

I

I

E

R

G

D

L

F

P

S

R

K

D

E

I

D

V

I

T

E

H

T

I

V

L

L

D

A

T

T

A

A

A

E

N

R

F

L

V

-

S

-

V

-

N

-

D

E

R

R

E

E

V

L

K

K

-

E

-

K

-

G

K

Q

V

L

P

E

L

Y

L

A

R

K

G

G

K

K

S

I

V

L

F

A

N

T

L

L

F

F

E

E

N

P

S
|
S

T
|
T

R
|
R

T
|
T

R

R

T

L

T

S

F

F

E

E

I

S

A

A

A

M

K

H

R

R

L

L

S

G

A

G

D

A

V

V

L

I

N

G

L

F

-

A

D

E

I

A

A

S

R

T

S

S

A

V

S

K

K
|
K

G

G

E

E

S

S

L

L

L

R

D

D

T

T

I

I

A

K

N

T

L

V

S

E

A

Q

M

Y

A

-

A

C

D

D

L

V

F

I

V

V

V

I

R
|
R

H

H

S

P

E

K

S

E

G

G

A

A

P

A

Y

R

L

L

I

A

A

A

Q

E

H

-

V

-

A

V

P

A

H

E

V

V

H

P

V

V

I

I

N

N

A

A

G

G

D

D

G

G

R

S

H

N

A

Q

H
|
H

P

P

T

T

Q
|
Q

G

T

L

L

D

D

M

L

Y

Y

T

T

I

I

R

K

H

K

Y

E

K

F

K

G

D

R

F

I

S

D

N

G

L

L

T

K

V

I

A

G

I

L

V

L

G

G

D

D

V

L

L

K

H

Y

S

G

R
|
R

V
x
T

A

V

R

H

S

S

D

L

I

A

H

E

G

A

L

L

T

T

T

F

L

Y

G

D

C

V

A

-

E

E

V

L

R

Y

V

L

V

I

G

S

P

P

R

E

T

L

L

L

-

R

-

M

-

P

-

R

-

H

V

I

P

V

S

E

D

E

M

L

A

R

Q

E

M

K

G

G

V

M

R

K

V

V

C

V

H

E

-

T

T

T

L

L

E

E

E

D

G

V

I

I

K

G

D

K

A

L

D

D

V

V

V

L

I

Y

M

V

L
x
T

R
|
R

L

I

Q
|
Q

N

K

E

E

R

R

M

-

S

-

G

-

A

-

L

-

L

F

P

P

S

D

S

E

Q

Q

E

E

Y

Y

F

L

K

K

-

V

-

K

-

G

S

S

F

Y

G

Q

L

V

T

N

Q

L

E

K

K

V

L

L

Q

E

L

K

A

A

K

K

P

D

D

E

A

L

I

R

V

I

M

M

H

H

P
|
P

G
x
L

P
|
P

I

-

N

-

R

R

G

V

V

D

E

E

I

I

D

H

S

P

A

E

V

V

V

D

D

N

G

T

K

K

Q

H

S

A

V

I

I

Y

L

F

P

R

Q

Q

V

V

T

F

F

N

G
|
G

I

V

A

P

V

V

R

R

M

M

A

A

V

L

M

L

S

A

I

L

V

V

A

L

G

G

active site: R56 (= R68), T57 (= T69), K85 (= K96), R106 (= R118), H134 (= H148), Q137 (= Q151), T227 (≠ L235), P266 (= P276), G292 (= G304)
binding n-(phosphonacetyl)-l-aspartic acid: S54 (= S66), T55 (= T67), R56 (= R68), T57 (= T69), R106 (= R118), H134 (= H148), Q137 (= Q151), R167 (= R181), T168 (≠ V182), R228 (= R236), Q230 (= Q238), P266 (= P276), L267 (≠ G277), P268 (= P278)

5g1pA Aspartate transcarbamoylase domain of human cad bound to carbamoyl phosphate (see paper)
34% identity, 94% coverage: 17:318/320 of query aligns to 4:291/292 of 5g1pA

query
sites
5g1pA

H

H

L

I

L

L

S

S

I

V

E

Q

G

Q

L

F

P

T

R

K

D

D

I

Q

V

M

T

S

H

H

I

L

L

F

D

N

T

V

A

A

A

H

N

T

F

L

V

R

S

M

V

M

N

V

D

Q

R

K

E

E

V

-

K

R

K

S

V

L

P

D

L

I

L

L

R

K

G

G

K

K

S

V

V

M

F

A

N

S

L

M

F

F

F

Y

E

E

N

V

S
|
S

T
|
T

R
|
R

T
|
T

R

S

T

S

F

F

E

A

I

A

A

A

A

M

K

A

R

R

L

L

S

G

A

G

D

A

V

V

L

L

N

S

L

F

D

S

I

E

A

A

R

T

S

S

A

V

S

Q

K
|
K

G

G

E

E

S

S

L

L

L

A

D

D

T

S

I

V

A

Q

N

T

L

M

S

S

A

C

M

Y

A

-

A

A

D

D

L

V

F

V

V

V

V

L

R
|
R

H

H

S

P

E

Q

S

P

G

G

A

A

P

V

Y

E

L

L

I

A

A

A

Q

K

H

H

V

C

A

-

P

-

H

R

V

R

H

P

V

V

I

I

N

N

A

A

G

G

D

D

G

G

R

V

H

G

A

E

H
|
H

P

P

T

T

Q
|
Q

G

A

L

L

D

D

M

I

Y

F

T

T

I

I

R

R

H

E

Y

E

K

L

K

G

D

T

F

V

S

N

N

G

L

M

T

T

V

I

A

T

I

M

V

V

G

G

D

D

V

L

L

K

H

H

S

G

R

R

V

T

A

V

R

H

S

S

D

-

I

L

H

A

G

C

L

L

T

L

T

T

L

Q

G

Y

C

R

A

V

E

S

V

L

R

R

V

Y

V

V

G

A

P

P

-

P

-

S

-

L

-

R

-

M

-

P

-

T

-

V

R

R

T

A

L

F

V

V

P

A

S

S

D

G

M

T

A

K

Q

Q

M

-

G

-

V

-

R

E

V

E

C

F

H

E

T

S

L

I

E

E

G

A

I

L

K

P

D

D

A

T

D

D

V

V

V

L

I

Y

M

M

L
x
T

R

R

L

I

Q

Q

N

K

E

E

R

R

M

F

S

-

G

-

A

-

L

-

P

-

S

-

Q

-

E

-

Y

-

F

-

K

-

S

Q

F

F

G

I

L

L

T

T

Q

P

E

H

K

I

L

M

Q

T

L

R

A

A

K

K

P

K

D

K

A

M

I

V

V

V

M

M

H

H

P
|
P

G
x
M

P

P

I

-

N

-

R

R

G

V

V

N

E

E

I

I

D

S

S

V

A

E

V

V

V

D

D

S

G

D

K

P

Q

R

S

A

V

A

I

Y

L

F

P

R

Q

Q

V

A

T

E

F

N

G
|
G

I

M

A

Y

V

I

R

R

M

M

A

A

V

L

M

L

S

A

I

T

V

V

A

L

G

G

N

R

active site: R54 (= R68), T55 (= T69), K82 (= K96), R103 (= R118), H131 (= H148), Q134 (= Q151), T223 (≠ L235), P251 (= P276), G277 (= G304)
binding phosphoric acid mono(formamide)ester: S52 (= S66), T53 (= T67), R54 (= R68), T55 (= T69), R103 (= R118), H131 (= H148), Q134 (= Q151), P251 (= P276), M252 (≠ G277)

P05990 CAD protein; Protein rudimentary; EC 6.3.5.5; EC 2.1.3.2; EC 3.5.2.3 from Drosophila melanogaster (Fruit fly) (see 2 papers)
34% identity, 94% coverage: 17:317/320 of query aligns to 1919:2218/2224 of P05990

query
sites
P05990

H

H

L

I

L

L

S

A

I

V

E

D

G

M

L

F

P

N

R

K

D

D

I

H

V

L

T

N

H

D

I

I

L

F

D

N

T

L

A

A

A

Q

-

L

N

K

F

L

V

R

S

G

V

T

N

K

D

D

R

R

E

P

V

V

K

D

K

E

V

-

P

-

L

L